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Human Metabolome Database Version 2.5

 

Showing metabocard for Cyclic AMP (HMDB00058)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-07 11:41:00
Accession Number HMDB00058
Secondary Accession Numbers Not Available
Common Name Cyclic AMP
Description Cyclic AMP is an adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH. cAMP is synthesized from ATP by adenylate cyclase. Adenylate cyclase is located at the cell membranes. Adenylate cyclase is activated by the hormones glucagon and adrenaline and by G protein. Liver adenylate cyclase responds more strongly to glucagon, and muscle adenylate cyclase responds more strongly to adrenaline. cAMP decomposition into AMP is catalyzed by the enzyme phosphodiesterase.
Synonyms
  1. Cyclic AMP
  2. 3'5'-cyclic AMP
  3. 6-(6-Amino-9H-purin-9-yl)tetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinine-2,7-diol 2-oxide
  4. Acrasin
  5. Adenosine 3',5'-cyclic monophosphate
  6. Adenosine 3',5'-cyclic phosphate
  7. Adenosine 3',5'-cyclophosphate
  8. Adenosine 3',5'-monophosphate
  9. Adenosine 3,5'-cyclic monophosphorate
  10. Adenosine 3,5'-cyclic monophosphoric acid
  11. Adenosine cyclic monophosphate
  12. Cyclic 3',5'-AMP
  13. Cyclic 3',5'-adenylate
  14. Cyclic 3',5'-adenylic acid
  15. Cyclic adenosine 3',5'-phosphate
  16. adenosine cyclic-monophosphate
  17. adenosine-cyclic-phosphate
  18. adenosine-cyclic-phosphoric-acid
  19. cAMP
Chemical IUPAC Name cyclic 3',5'-(hydrogen phosphate)Adenosine
Chemical Formula C10H12N5O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Second messenger
  • Component of Purine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 329.206
Monoisotopic Molecular Weight 329.052521
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@@H]2COP(O)(=O)O[C@H]2[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC2COP(O)(=O)OC2C1O
KEGG Compound ID C00575 Link Image
BioCyc ID CAMP Link Image
BiGG ID 1484809 Link Image
Wikipedia Link Cyclic AMP Link Image
NuGOwiki Link HMDB00058 Link Image
Metagene Link HMDB00058 Link Image
METLIN ID 5120 Link Image
PubChem Compound 6076 Link Image
PubChem Substance 820438 Link Image
ChEBI ID 17489 Link Image
CAS Registry Number 60-92-4
InChI Identifier InChI=1/C10H12N5O6P/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7-4(20-10)1-19-22(17,18)21-7/h2-4,6-7,10,16H,1H2,(H,17,18)(H2,11,12,13)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Genieser, H. G.; Butt, E.; Bottin, U.; Dostmann, W.; Jastorff, B. Synthesis of the 3',5'-cyclic phosphates from unprotected nucleosides. Synthesis (1989), (1), 53-4.
Melting Point (Experimental) 219-220 oC
Experimental Water Solubility 4 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 136.0 mg/mL [MEYLAN,WM et al. (1996)]; 3.58 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity -2.96 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.29 [Predicted by ALOGPS]; -2.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • golgi apparatus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 0.0085 +/- 0.0005 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Biofluid CSF
Value 0.020 +/- 0.004 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.024 (0.022-0.026) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.021 +/- 0.008 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 0.020 (0.016-0.024) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.020+/- 0.004 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid Urine
Value 0.22 +/- 0.055 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Raij K, Harkonen M: Determination of cyclic adenosine 3',5'-monophosphate in urine. Scand J Clin Lab Invest. 1976 Mar;36(2):161-8. [PubMed Link Image]
Biofluid Urine
Value 0.38 +/- 0.14 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Daniels CK, Zhang L, Musser B, Vestal RE: A solid-phase radioimmunoassay for cyclic AMP. J Pharmacol Toxicol Methods. 1994 Feb;31(1):41-6. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.0077 +/- 0.0003 uM
Age Adult:>18 yrs old
Sex Male
Condition Headache
Comments Not Available
References
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Biofluid CSF
Value 0.0110 +/- 0.0028 uM
Age Adult:>18 yrs old
Sex Both
Condition Idiopathic polyneuritis
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.00860 (0.00620-0.0110) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypoxic-ischemic encephalopathy
Comments Moderate to severe Hypoxic-ischemic encephalopathy
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.014 (0.012-0.017) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypoxic-ischemic encephalopathy
Comments Mild Hypoxic-ischemic encephalopathy
References
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Biofluid CSF
Value 0.034 (0.021-0.046) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments serious meningitis
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.011 (0.0082-0.014) uM
Age Adult:>18 yrs old
Sex Both
Condition Idiopathic polyneuritis
Comments Not Available
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid CSF
Value 0.033 +/- 0.012 uM
Age Adult:>18 yrs old
Sex N/A
Condition Meningitis
Comments Serious case.
References
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Biofluid Urine
Value 0.24 +/- 0.028 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Chronic renal failure
Comments Not Available
References
  • Dimitrakov D, Kumchev E, Lyutakova E, Ledzhev I, Nikolov D, Tsekov V: Cyclic adenosine monophosphate (cAMP) levels in predialysis patients with chronic renal failure. Folia Med (Plovdiv). 1997;39(1):29-33. [PubMed Link Image]
Associated Disorders
Condition References
Chronic renal failure
  • Dimitrakov D, Kumchev E, Lyutakova E, Ledzhev I, Nikolov D, Tsekov V: Cyclic adenosine monophosphate (cAMP) levels in predialysis patients with chronic renal failure. Folia Med (Plovdiv). 1997;39(1):29-33. [PubMed Link Image]
Headache
  • Kruuse C, Frandsen E, Schifter S, Thomsen LL, Birk S, Olesen J: Plasma levels of cAMP, cGMP and CGRP in sildenafil-induced headache. Cephalalgia. 2004 Jul;24(7):547-53. [PubMed Link Image]
Hypoxic-ischemic encephalopathy
  • Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
Idiopathic polyneuritis
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
Meningitis
  • Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Imashuku S, Todo S, Nakajima F: [Intra-aortic prostaglandin E1 infusion in the treatment of advanced neuroblastoma] Gan To Kagaku Ryoho. 1983 Sep;10(9):1936-43. [PubMed Link Image]
  2. Wine JJ, Joo NS: Submucosal glands and airway defense. Proc Am Thorac Soc. 2004;1(1):47-53. [PubMed Link Image]
  3. Onali P, Strada SJ, Chang L, Epstein PM, Hersh EM, Thompson WJ: Purification and characterization of high-affinity cyclic adenosine 5'-monophosphate phosphodiesterases from human acute myelogenous leukemic cells. Cancer Res. 1985 Mar;45(3):1384-91. [PubMed Link Image]
  4. Rademaker MT, Charles CJ, Lewis LK, Yandle TG, Cooper GJ, Coy DH, Richards AM, Nicholls MG: Beneficial hemodynamic and renal effects of adrenomedullin in an ovine model of heart failure. Circulation. 1997 Sep 16;96(6):1983-90. [PubMed Link Image]
  5. Mashayekhi F, Aghahoseini F, Rezaie A, Zamani MJ, Khorasani R, Abdollahi M: Alteration of cyclic nucleotides levels and oxidative stress in saliva of human subjects with periodontitis. J Contemp Dent Pract. 2005 Nov 15;6(4):46-53. [PubMed Link Image]
  6. Sugo T, Tachimoto H, Chikatsu T, Murakami Y, Kikukawa Y, Sato S, Kikuchi K, Nagi T, Harada M, Ogi K, Ebisawa M, Mori M: Identification of a lysophosphatidylserine receptor on mast cells. Biochem Biophys Res Commun. 2006 Mar 24;341(4):1078-87. Epub 2006 Jan 25. [PubMed Link Image]
  7. Watanabe K, Beinborn M, Nagamatsu S, Ishida H, Takahashi S: Menetrier's disease in a patient with Helicobacter pylori infection is linked to elevated glucagon-like peptide-2 activity. Scand J Gastroenterol. 2005 Apr;40(4):477-81. [PubMed Link Image]
  8. Naef A, Keller HU: A short transient increase in cyclic adenosine 3', 5'-monophosphate levels of neutrophil granulocytes following exposure to chemotactic factors. Adv Exp Med Biol. 1982;141:39-48. [PubMed Link Image]
  9. Kukreja SC, Shevrin DH, Wimbiscus SA, Ebeling PR, Danks JA, Rodda CP, Wood WI, Martin TJ: Antibodies to parathyroid hormone-related protein lower serum calcium in athymic mouse models of malignancy-associated hypercalcemia due to human tumors. J Clin Invest. 1988 Nov;82(5):1798-802. [PubMed Link Image]
  10. Wickenheisser JK, Nelson-DeGrave VL, McAllister JM: Human ovarian theca cells in culture. Trends Endocrinol Metab. 2006 Mar;17(2):65-71. Epub 2006 Feb 7. [PubMed Link Image]
  11. Fouassier L, Chinet T, Robert B, Carayon A, Balladur P, Mergey M, Paul A, Poupon R, Capeau J, Barbu V, Housset C: Endothelin-1 is synthesized and inhibits cyclic adenosine monophosphate- dependent anion secretion by an autocrine/paracrine mechanism in gallbladder epithelial cells. J Clin Invest. 1998 Jun 15;101(12):2881-8. [PubMed Link Image]
  12. Carceles MD, Ribo AR, Davalos R, Martinez T, Hernandez J: Effect of diazepam on adenosine 3',5'-cyclic monophosphate (cAMP) plasma levels in anesthetized patients. Clin Ther. 2004 May;26(5):737-43. [PubMed Link Image]
  13. Chu MS, Chang CF, Yang CC, Bau YC, Ho LL, Hung SC: Signalling pathway in the induction of neurite outgrowth in human mesenchymal stem cells. Cell Signal. 2006 Apr;18(4):519-30. Epub 2005 Aug 11. [PubMed Link Image]
  14. Rudman D, O'Brien MS, McKinney AS, Hoffman JC Jr, Patterson JH: Observations on the cyclic nucleotide concentrations in human cerebrospinal fluid. J Clin Endocrinol Metab. 1976 Jun;42(6):1088-97. [PubMed Link Image]
  15. Machen TE: Innate immune response in CF airway epithelia: hyperinflammatory? Am J Physiol Cell Physiol. 2006 Aug;291(2):C218-30. [PubMed Link Image]
  16. Lerche A, Svenson M, Wiik A: Cerebrospinal fluid levels of cyclic nucleotides in meningitis and idiopathic polyneuritis. Acta Neurol Scand. 1984 Mar;69(3):168-75. [PubMed Link Image]
  17. Ruppert D, Weithmann KU: HL 725, an extremely potent inhibitor of platelet phosphodiesterase and induced platelet aggregation in vitro. Life Sci. 1982 Nov 8;31(19):2037-43. [PubMed Link Image]
  18. Tanaka Y, Horinouchi T, Koike K: New insights into beta-adrenoceptors in smooth muscle: distribution of receptor subtypes and molecular mechanisms triggering muscle relaxation. Clin Exp Pharmacol Physiol. 2005 Jul;32(7):503-14. [PubMed Link Image]
  19. Fischer JA, Bourne HR, Dambacher MA, Tschopp F, De Meyer R, Devogelaer JP, Werder EA, Nagant De Deuxchaisnes C: Pseudohypoparathyroidism: inheritance and expression of deficient receptor-cyclase coupling protein activity. Clin Endocrinol (Oxf). 1983 Dec;19(6):747-54. [PubMed Link Image]
  20. Liu H, Chang L, Chen Y, Xia S, Zhang X: Clinical implication of the changes of cAMP, TXA2 and PGI2 in CSF of asphyxiated newborns. J Huazhong Univ Sci Technolog Med Sci. 2003;23(2):195-7, 200. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Histone acetyltransferase p300
  2. CREB-binding protein
  3. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  4. Hormone-sensitive lipase
  5. Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  6. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
  7. High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
  8. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
  9. cGMP-inhibited 3',5'-cyclic phosphodiesterase B
  10. High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
  11. cGMP-inhibited 3',5'-cyclic phosphodiesterase A
  12. cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
  13. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
  14. cAMP-specific 3',5'-cyclic phosphodiesterase 4B
  15. cAMP-specific 3',5'-cyclic phosphodiesterase 7B
  16. High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
  17. cGMP-dependent 3',5'-cyclic phosphodiesterase
  18. High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
  19. cAMP-specific 3',5'-cyclic phosphodiesterase 4C
  20. cAMP-specific 3',5'-cyclic phosphodiesterase 4D
  21. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  22. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
  23. cAMP-specific 3',5'-cyclic phosphodiesterase 4A
  24. cGMP-specific 3',5'-cyclic phosphodiesterase
  25. Adenylate cyclase type 7
  26. Adenylate cyclase type 6
  27. Adenylate cyclase type 5
  28. Adenylate cyclase type 8
  29. Adenylate cyclase type 9
  30. Adenylate cyclase type 3
  31. Adenylate cyclase type 1
  32. Adenylate cyclase type 2
  33. Cytochrome P450 17A1
  34. Cyclic nucleotide-gated cation channel alpha 3
  35. Cyclic nucleotide-gated cation channel beta 3
  36. Rap guanine nucleotide exchange factor 2
  37. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
  38. cAMP-dependent protein kinase, gamma-catalytic subunit
  39. cAMP-dependent protein kinase, alpha-catalytic subunit
  40. Serine/threonine-protein kinase PRKY
  41. cAMP-dependent protein kinase, beta-catalytic subunit
  42. Ribosomal protein S6 kinase alpha-5
  43. Serine/threonine-protein kinase PRKX
  44. Serine/threonine-protein kinase 11
  45. ATP-binding cassette sub-family A member 1
  46. Ezrin-radixin-moesin-binding phosphoprotein 50
  47. Aryl hydrocarbon receptor precursor
  48. cAMP response element-binding protein 5
  49. Class B basic helix-loop-helix protein 2
  50. Splicing factor, proline- and glutamine-rich
  51. Ras-related protein Rap-1A precursor
  52. Calcitonin gene-related peptide 1 precursor
  53. cAMP response element-binding protein
  54. Thyrotropin receptor precursor
  55. Glial cell line-derived neurotrophic factor precursor
  56. Potassium voltage-gated channel subfamily H member 2
  57. Potassium voltage-gated channel subfamily H member 6
  58. Methyl-CpG-binding domain protein 2
  59. Relaxin receptor 1
  60. cAMP-responsive element modulator
  61. Adiponectin precursor
  62. cAMP-dependent protein kinase type I-alpha regulatory subunit
  63. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
  64. Cortistatin precursor [Contains: Cortistatin-29; Cortistatin-17]
  65. Perilipin
  66. Prostaglandin D2 receptor
  67. Rap guanine nucleotide exchange factor 3
  68. Platelet basic protein precursor
  69. Vasodilator-stimulated phosphoprotein
  70. Inositol 1,4,5-trisphosphate receptor type 1
  71. Rap guanine nucleotide exchange factor 4
  72. Steroidogenic factor 1
  73. Sodium bicarbonate cotransporter 3
  74. Testicular soluble adenylyl cyclase
  75. Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
  76. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  77. P2Y purinoceptor 5
  78. Adenylate cyclase 1
  79. A-kinase anchor protein 7 isoforms alpha and beta
  80. A-kinase anchor protein 13
  81. CNGA4 protein
  82. CREB-regulated transcription coactivator 1
  83. CREB-regulated transcription coactivator 2
  84. Uncharacterized protein GNAT3
  85. Protein phosphatase 1 regulatory subunit 1A
  86. Transient receptor potential cation channel subfamily V member 2
  87. ATP-binding cassette transporter sub-family C member 11
  88. ADM2 precursor
  89. A-kinase anchor protein 7 isoform gamma
  90. A-kinase anchor protein 2
  91. A-kinase anchor protein 5
  92. A-kinase anchor protein 8
  93. Agouti-signaling protein precursor
  94. Cyclic AMP-dependent transcription factor ATF-1
  95. Cyclic AMP-dependent transcription factor ATF-2
  96. Cyclic AMP-dependent transcription factor ATF-3
  97. Cyclic AMP-dependent transcription factor ATF-4
  98. Cyclic AMP-dependent transcription factor ATF-5
  99. Cyclic AMP-dependent transcription factor ATF-7
  100. Basic leucine zipper transcriptional factor ATF-like
  101. Cyclic nucleotide-gated olfactory channel
  102. cAMP responsive element-binding protein 3-like protein 1
  103. cAMP responsive element-binding protein 3-like protein 2
  104. cAMP responsive element-binding protein 3-like protein 3
  105. Cyclic AMP-responsive element-binding protein 3
  106. Cisplatin resistance-associated overexpressed protein
  107. CREB-regulated transcription coactivator 3
  108. Dematin
  109. Erythrocyte membrane protein band 4.2
  110. FERM, RhoGEF and pleckstrin domain-containing protein 1
  111. G-protein coupled bile acid receptor 1
  112. Glycoprotein hormone alpha-2 precursor
  113. Glycoprotein hormone beta-5 precursor
  114. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
  115. Histamine H4 receptor
  116. cAMP-dependent protein kinase inhibitor alpha
  117. cAMP-dependent protein kinase inhibitor beta
  118. cAMP-dependent protein kinase inhibitor gamma
  119. Jun dimerization protein 2
  120. cAMP-dependent protein kinase type I-beta regulatory subunit
  121. cAMP-dependent protein kinase type II-alpha regulatory subunit
  122. cAMP-dependent protein kinase type II-beta regulatory subunit
  123. Potassium voltage-gated channel subfamily A member 10
  124. Potassium voltage-gated channel subfamily E member 3
  125. Potassium voltage-gated channel subfamily H member 1
  126. Potassium voltage-gated channel subfamily H member 3
  127. Potassium voltage-gated channel subfamily H member 4
  128. Potassium voltage-gated channel subfamily H member 5
  129. Potassium voltage-gated channel subfamily H member 7
  130. Potassium voltage-gated channel subfamily H member 8
  131. Leucine zipper putative tumor suppressor 1
  132. Homeobox protein Meis1
  133. Mas-related G-protein coupled receptor member D
  134. Mas-related G-protein coupled receptor member X2
  135. Myomegalin
  136. Na(+)/H(+) exchange regulatory cofactor NHE-RF2
  137. Non-POU domain-containing octamer-binding protein
  138. Pre-B-cell leukemia transcription factor 1
  139. Prostaglandin E2 receptor EP2 subtype
  140. Phosducin
  141. Paired mesoderm homeobox protein 2B
  142. Phospholemman precursor
  143. Protein prune homolog
  144. Tyrosine-protein phosphatase non-receptor type 7
  145. Ras-related protein Rap-1b precursor
  146. Ras-related protein Rap-2a precursor
  147. FMRFamide-related peptides precursor
  148. Rhophilin-2
  149. Synembryn-B
  150. Relaxin-3 receptor 1
  151. Relaxin-3 receptor 2
  152. Uncharacterized protein ENSP00000345280
  153. Rap guanine nucleotide exchange factor 6
  154. 40S ribosomal protein S27
  155. Relaxin receptor 2
  156. Solute carrier organic anion transporter family member 4C1
  157. SKIP protein
  158. Ras GTPase-activating protein SynGAP
  159. Transmembrane protein 132A precursor
  160. Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
  161. 3',5'-cyclic nucleotide phosphodiesterase 10A2
  162. Adenylate cyclase 9 (Adenylate cyclase 9, isoform CRA_a)
  163. Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
  164. cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
  165. cDNA FLJ16206 fis, clone CTONG2019590, highly similar to Adenylate cyclase type 4 (EC 4.6.1.1)
  166. Cyclic nucleotide-gated cation channel beta-1
Enzyme 1 [top]
Enzyme 1 ID 5240
Enzyme 1 Name Histone acetyltransferase p300
Enzyme 1 Synonyms
  1. E1A-associated protein p300
Enzyme 1 Gene Name EP300
Enzyme 1 Protein Sequence >Histone acetyltransferase p300
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGD
INQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINS
MVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGTNAGMNPGMLAA
GNGQGIMPNQVMNGSIGAGRGRQDMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQ
PLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGE
VRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNA
GDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQM
PTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQ
NPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPN
AAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSM
AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNI
PLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTP
TPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPNAPLLPPQPATPLSQPAVSIEGQVSNPPSTSST
EVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELK
TEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVD
PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK
YCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVL
HHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGE
VTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQE
YGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPP
SEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNK
SSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIP
CDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETR
WHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQ
SLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTG
QQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPG
PPPTAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHL
EPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISP
LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGG
MSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYP
PQPQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSP
QQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHV
SPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH
Enzyme 1 Number of Residues 2414
Enzyme 1 Molecular Weight 264147
Enzyme 1 Theoretical pI 8.56
Enzyme 1 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • protein binding
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transition metal ion binding
  • zinc ion binding
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 495301 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q09472 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name EP300_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7245 bp
ATGGCCGAGAATGTGGTGGAACCGGGGCCGCCTTCAGCCAAGCGGCCTAAACTCTCATCT
CCGGCCCTCTCGGCGTCCGCCAGCGATGGCACAGATTTTGGCTCTCTATTTGACTTGGAG
CACGACTTACCAGATGAATTAATCAACTCTACAGAATTGGGACTAACCAATGGTGGTGAT
ATTAATCAGCTTCAGACAAGTCTTGGCATGGTACAAGATGCAGCTTCTAAACATAAACAG
CTGTCAGAATTGCTGCGATCTGGTAGTTCCCCTAACCTCAATATGGGAGTTGGTGGCCCA
GGTCAAGTCATGGCCAGCCAGGCCCAACAGAGCAGTCCTGGATTAGGTTTGATAAATAGC
ATGGTCAAAAGCCCAATGACACAGGCAGGCTTGACTTCTCCCAACATGGGGATGGGCACT
AGTGGACCAAATCAGGGTCCTACGCAGTCAACAGGTATGATGAACAGTCCAGTAAATCAG
CCTGCCATGGGAATGAACACAGGGACGAATGCGGGCATGAATCCTGGAATGTTGGCTGCA
GGCAATGGACAAGGGATAATGCCTAATCAAGTCATGAACGGTTCAATTGGAGCAGGCCGA
GGGCGACAGGATATGCAGTACCCAAACCCAGGCATGGGAAGTGCTGGCAACTTACTGACT
GAGCCTCTTCAGCAGGGCTCTCCCCAGATGGGAGGACAAACAGGATTGAGAGGCCCCCAG
CCTCTTAAGATGGGAATGATGAACAACCCCAATCCTTATGGTTCACCATATACTCAGAAT
CCTGGACAGCAGATTGGAGCCAGTGGCCTTGGTCTCCAGATTCAGACAAAAACTGTACTA
TCAAATAACTTATCTCCATTTGCTATGGACAAAAAGGCAGTTCCTGGTGGAGGAATGCCC
AACATGGGTCAACAGCCAGCCCCGCAGGTCCAGCAGCCAGGTCTGGTGACTCCAGTTGCC
CAAGGGATGGGTTCTGGAGCACATACAGCTGATCCAGAGAAGCGCAAGCTCATCCAGCAG
CAGCTTGTTCTCCTTTTGCATGCTCACAAGTGCCAGCGCCGGGAACAGGCCAATGGGGAA
GTGAGGCAGTGCAACCTTCCCCACTGTCGCACAATGAAGAATGTCCTAAACCACATGACA
CACTGCCAGTCAGGCAAGTCTTGCCAAGTGGCACACTGTGCATCTTCTCGACAAATCATT
TCACACTGGAAGAATTGTACAAGACATGATTGTCCTGTGTGTCTCCCCCTCAAAAATGCT
GGTGATAAGAGAAATCAACAGCCAATTTTGACTGGAGCACCCGTTGGACTTGGAAATCCT
AGCTCTCTAGGGGTGGGTCAACAGTCTGCCCCCAACCTAAGCACTGTTAGTCAGATTGAT
CCCAGCTCCATAGAAAGAGCCTATGCAGCTCTTGGACTACCCTATCAAGTAAATCAGATG
CCGACACAACCCCAGGTGCAAGCAAAGAACCAGCAGAATCAGCAGCCTGGGCAGTCTCCC
CAAGGCATGCGGCCCATGAGCAACATGAGTGCTAGTCCTATGGGAGTAAATGGAGGTGTA
GGAGTTCAAACGCCGAGTCTTCTTTCTGACTCAATGTTGCATTCAGCCATAAATTCTCAA
AACCCAATGATGAGTGAAAATGCCAGTGTGCCCTCCCTGGGTCCTATGCCAACAGCAGCT
CAACCATCCACTACTGGAATTCGGAAACAGTGGCACGAAGATATTACTCAGGATCTTCGA
AATCATCTTGTTCACAAACTCGTCCAAGCCATATTTCCTACGCCGGATCCTGCTGCTTTA
AAAGACAGACGGATGGAAAACCTAGTTGCATATGCTCGGAAAGTTGAAGGGGACATGTAT
GAATCTGCAAACAATCGAGCGGAATACTACCACCTTCTAGCTGAGAAAATCTATAAGATC
CAGAAAGAACTAGAAGAAAAACGAAGGACCAGACTACAGAAGCAGAACATGCTACCAAAT
GCTGCAGGCATGGTTCCAGTTTCCATGAATCCAGGGCCTAACATGGGACAGCCGCAACCA
GGAATGACTTCTAATGGCCCTCTACCTGACCCAAGTATGATCCGTGGCAGTGTGCCAAAC
CAGATGATGCCTCGAATAACTCCACAATCTGGTTTGAATCAATTTGGCCAGATGAGCATG
GCCCAGCCCCCTATTGTACCCCGGCAAACCCCTCCTCTTCAGCACCATGGACAGTTGGCT
CAACCTGGAGCTCTCAACCCGCCTATGGGCTATGGGCCTCGTATGCAACAGCCTTCCAAC
CAGGGCCAGTTCCTTCCTCAGACTCAGTTCCCATCACAGGGAATGAATGTAACAAATATC
CCTTTGGCTCCGTCCAGCGGTCAAGCTCCAGTGTCTCAAGCACAAATGTCTAGTTCTTCC
TGCCCGGTGAACTCTCCTATAATGCCTCCAGGGTCTCAGGGGAGCCACATTCACTGTCCC
CAGCTTCCTCAACCAGCTCTTCATCAGAATTCACCCTCGCCTGTACCTAGTCGTACCCCC
ACCCCTCACCATACTCCCCCAAGCATAGGGGCTCAGCAGCCACCAGCAACAACAATTCCA
GCCCCTGTTCCTACACCACCAGCCATGCCACCTGGGCCACAGTCCCAGGCTCTACATCCC
CCTCCAAGGCAGACACCTACACCACCAACAACACAACTTCCCCAACAAGTGCAGCCTTCA
CTTCCTGCTGCACCTTCTGCTGACCAGCCCCAGCAGCAGCCTCGCTCACAGCAGAGCACA
GCAGCGTCTGTTCCTACCCCAAACGCACCGCTGCTTCCTCCGCAGCCTGCAACTCCACTT
TCCCAGCCAGCTGTAAGCATTGAAGGACAGGTATCAAATCCTCCATCTACTAGTAGCACA
GAAGTGAATTCTCAGGCCATTGCTGAGAAGCAGCCTTCCCAGGAAGTGAAGATGGAGGCC
AAAATGGAAGTGGATCAACCAGAACCAGCAGATACGCAGCCGGAGGATATTTCAGAGTCT
AAAGTGGAAGACTGTAAAATGGAATCTACCGAAACAGAAGAGAGAAGCACTGAGTTAAAA
ACTGAAATAAAAGAGGAGGAAGACCAGCCAAGTACTTCAGCTACCCAGTCATCTCCGGCT
CCAGGACAGTCAAAGAAAAAGATTTTCAAACCAGAAGAACTACGACAGGCACTGATGCCA
ACATTGGAGGCACTTTACCGTCAGGATCCAGAATCCCTTCCCTTTCGTCAACCTGTGGAC
CCTCAGCTTTTAGGAATCCCTGATTACTTTGATATTGTGAAGAGCCCCATGGATCTTTCT
ACCATTAAGAGGAAGTTAGACACTGGACAGTATCAGGAGCCCTGGCAGTATGTCGATGAT
ATTTGGCTTATGTTCAATAATGCCTGGTTATATAACCGGAAAACATCACGGGTATACAAA
TACTGCTCCAAGCTCTCTGAGGTCTTTGAACAAGAAATTGACCCAGTGATGCAAAGCCTT
GGATACTGTTGTGGCAGAAAGTTGGAGTTCTCTCCACAGACACTGTGTTGCTACGGCAAA
CAGTTGTGCACAATACCTCGTGATGCCACTTATTACAGTTACCAGAACAGGTATCATTTC
TGTGAGAAGTGTTTCAATGAGATCCAAGGGGAGAGCGTTTCTTTGGGGGATGACCCTTCC
CAGCCTCAAACTACAATAAATAAAGAACAATTTTCCAAGAGAAAAAATGACACACTGGAT
CCTGAACTGTTTGTTGAATGTACAGAGTGCGGAAGAAAGATGCATCAGATCTGTGTCCTT
CACCATGAGATCATCTGGCCTGCTGGATTCGTCTGTGATGGCTGTTTAAAGAAAAGTGCA
CGAACTAGGAAAGAAAATAAGTTTTCTGCTAAAAGGTTGCCATCTACCAGACTTGGCACC
TTTCTAGAGAATCGTGTGAATGACTTTCTGAGGCGACAGAATCACCCTGAGTCAGGAGAG
GTCACTGTTAGAGTAGTTCATGCTTCTGACAAAACCGTGGAAGTAAAACCAGGCATGAAA
GCAAGGTTTGTGGACAGTGGAGAGATGGCAGAATCCTTTCCATACCGAACCAAAGCCCTC
TTTGCCTTTGAAGAAATTGATGGTGTTGACCTGTGCTTCTTTGGCATGCATGTTCAAGAG
TATGGCTCTGACTGCCCTCCACCCAACCAGAGGAGAGTATACATATCTTACCTCGATAGT
GTTCATTTCTTCCGTCCTAAATGCTTGAGGACTGCAGTCTATCATGAAATCCTAATTGGA
TATTTAGAATATGTCAAGAAATTAGGTTACACAACAGGGCATATTTGGGCATGTCCACCA
AGTGAGGGAGATGATTATATCTTCCATTGCCATCCTCCTGACCAGAAGATACCCAAGCCC
AAGCGACTGCAGGAATGGTACAAAAAAATGCTTGACAAGGCTGTATCAGAGCGTATTGTC
CATGACTACAAGGATATTTTTAAACAAGCTACTGAAGATAGATTAACAAGTGCAAAGGAA
TTGCCTTATTTCGAGGGTGATTTCTGGCCCAATGTTCTGGAAGAAAGCATTAAGGAACTG
GAACAGGAGGAAGAAGAGAGAAAACGAGAGGAAAACACCAGCAATGAAAGCACAGATGTG
ACCAAGGGAGACAGCAAAAATGCTAAAAAGAAGAATAATAAGAAAACCAGCAAAAATAAG
AGCAGCCTGAGTAGGGGCAACAAGAAGAAACCCGGGATGCCCAATGTATCTAACGACCTC
TCACAGAAACTATATGCCACCATGGAGAAGCATAAAGAGGTCTTCTTTGTGATCCGCCTC
ATTGCTGGCCCTGCTGCCAACTCCCTGCCTCCCATTGTTGATCCTGATCCTCTCATCCCC
TGCGATCTGATGGATGGTCGGGATGCGTTTCTCACGCTGGCAAGGGACAAGCACCTGGAG
TTCTCTTCACTCCGAAGAGCCCAGTGGTCCACCATGTGCATGCTGGTGGAGCTGCACACG
CAGAGCCAGGACCGCTTTGTCTACACCTGCAATGAATGCAAGCACCATGTGGAGACACGC
TGGCACTGTACTGTCTGTGAGGATTATGACTTGTGTATCACCTGCTATAACACTAAAAAC
CATGACCACAAAATGGAGAAACTAGGCCTTGGCTTAGATGATGAGAGCAACAACCAGCAG
GCTGCAGCCACCCAGAGCCCAGGCGATTCTCGCCGCCTGAGTATCCAGCGCTGCATCCAG
TCTCTGGTCCATGCTTGCCAGTGTCGGAATGCCAATTGCTCACTGCCATCCTGCCAGAAG
ATGAAGCGGGTTGTGCAGCATACCAAGGGTTGCAAACGGAAAACCAATGGCGGGTGCCCC
ATCTGCAAGCAGCTCATTGCCCTCTGCTGCTACCATGCCAAGCACTGCCAGGAGAACAAA
TGCCCGGTGCCGTTCTGCCTAAACATCAAGCAGAAGCTCCGGCAGCAACAGCTGCAGCAC
CGACTACAGCAGGCCCAAATGCTTCGCAGGAGGATGGCCAGCATGCAGCGGACTGGTGTG
GTTGGGCAGCAACAGGGCCTCCCTTCCCCCACTCCTGCCACTCCAACGACACCAACTGGC
CAACAGCCAACCACCCCGCAGACGCCCCAGCCCACTTCTCAGCCTCAGCCTACCCCTCCC
AATAGCATGCCACCCTACTTGCCCAGGACTCAAGCTGCTGGCCCTGTGTCCCAGGGTAAG
GCAGCAGGCCAGGTGACCCCTCCAACCCCTCCTCAGACTGCTCAGCCACCCCTTCCAGGG
CCCCCACCTACAGCAGTGGAAATGGCAATGCAGATTCAGAGAGCAGCGGAGACGCAGCGC
CAGATGGCCCACGTGCAAATTTTTCAAAGGCCAATCCAACACCAGATGCCCCCGATGACT
CCCATGGCCCCCATGGGTATGAACCCACCTCCCATGACCAGAGGTCCCAGTGGGCATTTG
GAGCCAGGGATGGGACCGACAGGGATGCAGCAACAGCCACCCTGGAGCCAAGGAGGATTG
CCTCAGCCCCAGCAACTACAGTCTGGGATGCCAAGGCCAGCCATGATGTCAGTGGCCCAG
CATGGTCAACCTTTGAACATGGCTCCACAACCAGGATTGGGCCAGGTAGGTATCAGCCCA
CTCAAACCAGGCACTGTGTCTCAACAAGCCTTACAAAACCTTTTGCGGACTCTCAGGTCT
CCCAGCTCTCCCCTGCAGCAGCAACAGGTGCTTAGTATCCTTCACGCCAACCCCCAGCTG
TTGGCTGCATTCATCAAGCAGCGGGCTGCCAAGTATGCCAACTCTAATCCACAACCCATC
CCTGGGCAGCCTGGCATGCCCCAGGGGCAGCCAGGGCTACAGCCACCTACCATGCCAGGT
CAGCAGGGGGTCCACTCCAATCCAGCCATGCAGAACATGAATCCAATGCAGGCGGGCGTT
CAGAGGGCTGGCCTGCCCCAGCAGCAACCACAGCAGCAACTCCAGCCACCCATGGGAGGG
ATGAGCCCCCAGGCTCAGCAGATGAACATGAACCACAACACCATGCCTTCACAATTCCGA
GACATCTTGAGACGACAGCAAATGATGCAACAGCAGCAGCAACAGGGAGCAGGGCCAGGA
ATAGGCCCTGGAATGGCCAACCATAACCAGTTCCAGCAACCCCAAGGAGTTGGCTACCCA
CCACAGCCGCAGCAGCGGATGCAGCATCACATGCAACAGATGCAACAAGGAAATATGGGA
CAGATAGGCCAGCTTCCCCAGGCCTTGGGAGCAGAGGCAGGTGCCAGTCTACAGGCCTAT
CAGCAGCGACTCCTTCAGCAACAGATGGGGTCCCCTGTTCAGCCCAACCCCATGAGCCCC
CAGCAGCATATGCTCCCAAATCAGGCCCAGTCCCCACACCTACAAGGCCAGCAGATCCCT
AATTCTCTCTCCAATCAAGTGCGCTCTCCCCAGCCTGTCCCTTCTCCACGGCCACAGTCC
CAGCCCCCCCACTCCAGTCCTTCCCCAAGGATGCAGCCTCAGCCTTCTCCACACCACGTT
TCCCCACAGACAAGTTCCCCACATCCTGGACTGGTAGCTGCCCAGGCCAACCCCATGGAA
CAAGGGCATTTTGCCAGCCCGGACCAGAATTCAATGCTTTCTCAGCTTGCTAGCAATCCA
GGCATGGCAAACCTCCATGGTGCAAGCGCCACGGACCTGGGACTCAGCACCGATAACTCA
GACTTGAATTCAAACCTCTCACAGAGTACACTAGACATACACTAG
Enzyme 1 GenBank Gene ID U01877 Link Image
Enzyme 1 GeneCard ID EP300 Link Image
Enzyme 1 GenAtlas ID EP300 Link Image
Enzyme 1 HGNC ID HGNC:3373 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM: Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 1994 Apr 15;8(8):869-84. [PubMed Link Image]
  2. Xu W, Chen H, Du K, Asahara H, Tini M, Emerson BM, Montminy M, Evans RM: A transcriptional switch mediated by cofactor methylation. Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8. [PubMed Link Image]
  3. Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed Link Image]
  4. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed Link Image]
  5. Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed Link Image]
  6. Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [PubMed Link Image]
  7. Ko L, Cardona GR, Chin WW: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6212-7. [PubMed Link Image]
  8. Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed Link Image]
  9. Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed Link Image]
  10. Yamamoto N, Yamamoto S, Inagaki F, Kawaichi M, Fukamizu A, Kishi N, Matsuno K, Nakamura K, Weinmaster G, Okano H, Nakafuku M: Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor. J Biol Chem. 2001 Nov 30;276(48):45031-40. Epub 2001 Sep 19. [PubMed Link Image]
  11. Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed Link Image]
  12. Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC: p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity. Cancer Res. 2003 May 15;63(10):2373-8. [PubMed Link Image]
  13. Hecht A, Stemmler MP: Identification of a promoter-specific transcriptional activation domain at the C terminus of the Wnt effector protein T-cell factor 4. J Biol Chem. 2003 Feb 7;278(6):3776-85. Epub 2002 Nov 22. [PubMed Link Image]
  14. Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. [PubMed Link Image]
  15. Gayther SA, Batley SJ, Linger L, Bannister A, Thorpe K, Chin SF, Daigo Y, Russell P, Wilson A, Sowter HM, Delhanty JD, Ponder BA, Kouzarides T, Caldas C: Mutations truncating the EP300 acetylase in human cancers. Nat Genet. 2000 Mar;24(3):300-3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5243
Enzyme 2 Name CREB-binding protein
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name CREBBP
Enzyme 2 Protein Sequence >CREB-binding protein
MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLV
PDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGK
SPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNAN
FNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLA
ETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASK
QSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVL
LLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWK
NCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSS
MQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQ
QPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDL
RSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYK
IQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQG
MNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHT
NNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQA
SQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPT
PTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTP
LSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSE
MMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQP
RKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKR
KLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCC
GRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQT
TISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRK
ENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFV
DSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFF
RPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQ
EWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEE
EERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQK
LYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSS
LRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAH
KMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKR
VVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQ
QAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAG
FPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNS
MPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVI
SMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAF
IKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQA
MGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAG
MAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLG
ADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLS
NQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHL
GNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL
Enzyme 2 Number of Residues 2442
Enzyme 2 Molecular Weight 265354
Enzyme 2 Theoretical pI 8.63
Enzyme 2 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • protein binding
  • transcription coactivator activity
  • transcription cofactor activity
  • transcription factor binding
  • transition metal ion binding
  • zinc ion binding
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non- histone proteins, like NCOA3 coactivator. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. CREBBP, as coactivator, augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • acetyl-CoA + histone = CoA + acetylhistone
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4321116 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q92793 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CBP_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >7329 bp
ATGGCTGAGAACTTGCTGGACGGACCGCCCAACCCCAAAAGAGCCAAACTCAGCTCGCCC
GGTTTCTCGGCGAATGACAGCACAGATTTTGGATCATTGTTTGACTTGGAAAATGATCTT
CCTGATGAGCTGATACCCAATGGAGGAGAATTAGGCCTTTTAAACAGTGGGAACCTTGTT
CCAGATGCTGCTTCCAAACATAAACAACTGTCGGAGCTTCTACGAGGAGGCAGCGGCTCT
AGTATCAACCCAGGAATAGGAAATGTGAGCGCCAGCAGCCCCGTGCAGCAGGGCCTGGGT
GGCCAGGCTCAAGGGCAGCCGAACAGTGCTAACATGGCCAGCCTCAGTGCCATGGGCAAG
AGCCCTCTGAGCCAGGGAGATTCTTCAGCCCCCAGCCTGCCTAAACAGGCAGCCAGCACC
TCTGGGCCCACCCCCGCTGCCTCCCAAGCACTGAATCCGCAAGCACAAAAGCAAGTGGGG
CTGGCGACTAGCAGCCCTGCCACGTCACAGACTGGACCTGGTATCTGCATGAATGCTAAC
TTTAACCAGACCCACCCAGGCCTCCTCAATAGTAACTCTGGCCATAGCTTAATTAATCAG
GCTTCACAAGGGCAGGCGCAAGTCATGAATGGATCTCTTGGGGCTGCTGGCAGAGGAAGG
GGAGCTGGAATGCCGTACCCTACTCCAGCCATGCAGGGCGCCTCGAGCAGCGTGCTGGCT
GAGACCCTAACGCAGGTTTCCCCGCAAATGACTGGTCACGCGGGACTGAACACCGCACAG
GCAGGAGGCATGGCCAAGATGGGAATAACTGGGAACACAAGTCCATTTGGACAGCCCTTT
AGTCAAGCTGGAGGGCAGCCAATGGGAGCCACTGGAGTGAACCCCCAGTTAGCCAGCAAA
CAGAGCATGGTCAACAGTTTGCCCACCTTCCCTACAGATATCAAGAATACTTCAGTCACC
AACGTGCCAAATATGTCTCAGATGCAAACATCAGTGGGAATTGTACCCACACAAGCAATT
GCAACAGGCCCCACTGCAGATCCTGAAAAACGCAAACTGATACAGCAGCAGCTGGTTCTA
CTGCTTCATGCTCATAAGTGTCAGAGACGAGAGCAAGCAAACGGAGAGGTTCGGGCCTGC
TCGCTCCCGCATTGTCGAACCATGAAAAACGTTTTGAATCACATGACGCATTGTCAGGCT
GGGAAAGCCTGCCAAGTTGCCCATTGTGCATCTTCACGACAAATCATCTCTCATTGGAAG
AACTGCACACGACATGACTGTCCTGTTTGCCTCCCTTTGAAAAATGCCAGTGACAAGCGA
AACCAACAAACCATCCTGGGGTCTCCAGCTAGTGGAATTCAAAACACAATTGGTTCTGTT
GGCACAGGGCAACAGAATGCCACTTCTTTAAGTAACCCAAATCCCATAGACCCCAGCTCC
ATGCAGCGAGCCTATGCTGCTCTCGGACTCCCCTACATGAACCAGCCCCAGACGCAGCTG
CAGCCTCAGGTTCCTGGCCAGCAACCAGCACAGCCTCAAACCCACCAGCAGATGAGGACT
CTCAACCCCCTGGGAAATAATCCAATGAACATTCCAGCAGGAGGAATAACAACAGATCAG
CAGCCCCCAAACTTGATTTCAGAATCAGCTCTTCCGACTTCCCTGGGGGCCACAAACCCA
CTGATGAACGATGGCTCCAACTCTGGTAACATTGGAACCCTCAGCACTATACCAACAGCA
GCTCCTCCTTCTAGCACCGGTGTAAGGAAAGGCTGGCACGAACATGTCACTCAGGACCTG
CGGAGCCATCTAGTGCATAAACTCGTCCAAGCCATCTTCCCAACACCTGATCCCGCAGCT
CTAAAGGATCGCCGCATGGAAAACCTGGTAGCCTATGCTAAGAAAGTGGAAGGGGACATG
TACGAGTCTGCCAACAGCAGGGATGAATATTATCACTTATTAGCAGAGAAAATCTACAAG
ATACAAAAAGAACTAGAAGAAAAACGGAGGTCGCGTTTACATAAACAAGGCATCTTGGGG
AACCAGCCAGCCTTACCAGCCCCGGGGGCTCAGCCCCCTGTGATTCCACAGGCACAACCT
GTGAGACCTCCAAATGGACCCCTGTCCCTGCCAGTGAATCGCATGCAAGTTTCTCAAGGG
ATGAATTCATTTAACCCCATGTCCTTGGGGAACGTCCAGTTGCCACAAGCACCCATGGGA
CCTCGTGCAGCCTCCCCAATGAACCACTCTGTCCAGATGAACAGCATGGGCTCAGTGCCA
GGGATGGCCATTTCTCCTTCCCGAATGCCTCAGCCTCCGAACATGATGGGTGCACACACC
AACAACATGATGGCCCAGGCGCCCGCTCAGAGCCAGTTTCTGCCACAGAACCAGTTCCCG
TCATCCAGCGGGGCGATGAGTGTGGGCATGGGGCAGCCGCCAGCCCAAACAGGCGTGTCA
CAGGGACAGGTGCCTGGTGCTGCTCTTCCTAACCCTCTCAACATGCTGGGGCCTCAGGCC
AGCCAGCTACCTTGCCCTCCAGTGACACAGTCACCACTGCACCCAACACCGCCTCCTGCT
TCCACGGCTGCTGGCATGCCATCTCTCCAGCACACGACACCACCTGGGATGACTCCTCCC
CAGCCAGCAGCTCCCACTCAGCCATCAACTCCTGTGTCGTCTTCCGGGCAGACTCCCACC
CCGACTCCTGGCTCAGTGCCCAGTGCTACCCAAACCCAGAGCACCCCTACAGTCCAGGCA
GCAGCCCAGGCCCAGGTGACCCCGCAGCCTCAAACCCCAGTTCAGCCCCCGTCTGTGGCT
ACCCCTCAGTCATCGCAGCAACAGCCGACGCCTGTGCACGCCCAGCCTCCTGGCACACCG
CTTTCCCAGGCAGCAGCCAGCATTGATAACAGAGTCCCTACCCCCTCCTCGGTGGCCAGC
GCAGAAACCAATTCCCAGCAGCCAGGACCTGACGTACCTGTGCTGGAAATGAAGACGGAG
ACCCAAGCAGAGGACACTGAGCCCGATCCTGGTGAATCCAAAGGGGAGCCCAGGTCTGAG
ATGATGGAGGAGGATTTGCAAGGAGCTTCCCAAGTTAAAGAAGAAACAGACATAGCAGAG
CAGAAATCAGAACCAATGGAAGTGGATGAAAAGAAACCTGAAGTGAAAGTAGAAGTTAAA
GAGGAAGAAGAGAGTAGCAGTAACGGCACAGCCTCTCAGTCAACATCTCCTTCGCAGCCG
CGCAAAAAAATCTTTAAACCAGAGGAGTTACGCCAGGCCCTCATGCCAACCCTAGAAGCA
CTGTATCGACAGGACCCAGAGTCATTACCTTTCCGGCAGCCTGTAGATCCCCAGCTCCTC
GGAATTCCAGACTATTTTGACATCGTAAAGAATCCCATGGACCTCTCCACCATCAAGCGG
AAGCTGGACACAGGGCAATACCAAGAGCCCTGGCAGTACGTGGACGACGTCTGGCTCATG
TTCAACAATGCCTGGCTCTATAATCGCAAGACATCCCGAGTCTATAAGTTTTGCAGTAAG
CTTGCAGAGGTCTTTGAGCAGGAAATTGACCCTGTCATGCAGTCCCTTGGATATTGCTGT
GGACGCAAGTATGAGTTTTCCCCACAGACTTTGTGCTGCTATGGGAAGCAGCTGTGTACC
ATTCCTCGCGATGCTGCCTACTACAGCTATCAGAATAGGTATCATTTCTGTGAGAAGTGT
TTCACAGAGATCCAGGGCGAGAATGTGACCCTGGGTGACGACCCTTCACAGCCCCAGACG
ACAATTTCAAAGGATCAGTTTGAAAAGAAGAAAAATGATACCTTAGACCCCGAACCTTTC
GTTGATTGCAAGGAGTGTGGCCGGAAGATGCATCAGATTTGCGTTCTGCACTATGACATC
ATTTGGCCTTCAGGTTTTGTGTGCGACAACTGCTTGAAGAAAACTGGCAGACCTCGAAAA
GAAAACAAATTCAGTGCTAAGAGGCTGCAGACCACAAGACTGGGAAACCACTTGGAAGAC
CGAGTGAACAAATTTTTGCGGCGCCAGAATCACCCTGAAGCCGGGGAGGTTTTTGTCCGA
GTGGTGGCCAGCTCAGACAAGACGGTGGAGGTCAAGCCCGGGATGAAGTCACGGTTTGTG
GATTCTGGGGAAATGTCTGAATCTTTCCCATATCGAACCAAAGCTCTGTTTGCTTTTGAG
GAAATTGACGGCGTGGATGTCTGCTTTTTTGGAATGCACGTCCAAGAATACGGCTCTGAT
TGCCCCCCTCCAAACACGAGGCGTGTGTACATTTCTTATCTGGATAGTATTCATTTCTTC
CGGCCACGTTGCCTCCGCACAGCCGTTTACCATGAGATCCTTATTGGATATTTAGAGTAT
GTGAAGAAATTAGGGTATGTGACAGGGCACATCTGGGCCTGTCCTCCAAGTGAAGGAGAT
GATTACATCTTCCATTGCCACCCACCTGATCAAAAAATACCCAAGCCAAAACGACTGCAG
GAGTGGTACAAAAAGATGCTGGACAAGGCGTTTGCAGAGCGGATCATCCATGACTACAAG
GATATTTTCAAACAAGCAACTGAAGACAGGCTCACCAGTGCCAAGGAACTGCCCTATTTT
GAAGGTGATTTCTGGCCCAATGTGTTAGAAGAGAGCATTAAGGAACTAGAACAAGAAGAA
GAGGAGAGGAAAAAGGAAGAGAGCACTGCAGCCAGTGAAACCACTGAGGGCAGTCAGGGC
GACAGCAAGAATGCCAAGAAGAAGAACAACAAGAAAACCAACAAGAACAAAAGCAGCATC
AGCCGCGCCAACAAGAAGAAGCCCAGCATGCCCAACGTGTCCAATGACCTGTCCCAGAAG
CTGTATGCCACCATGGAGAAGCACAAGGAGGTCTTCTTCGTGATCCACCTGCACGCTGGG
CCTGTCATCAACACCCTGCCCCCCATCGTCGACCCCGACCCCCTGCTCAGCTGTGACCTC
ATGGATGGGCGCGACGCCTTCCTCACCCTCGCCAGAGACAAGCACTGGGAGTTCTCCTCC
TTGCGCCGCTCCAAGTGGTCCACGCTCTGCATGCTGGTGGAGCTGCACACCCAGGGCCAG
GACCGCTTTGTCTACACCTGCAACGAGTGCAAGCACCACGTGGAGACGCGCTGGCACTGC
ACTGTGTGCGAGGACTACGACCTCTGCATCAACTGCTATAACACGAAGAGCCATGCCCAT
AAGATGGTGAAGTGGGGGCTGGGCCTGGATGACGAGGGCAGCAGCCAGGGCGAGCCACAG
TCAAAGAGCCCCCAGGAGTCACGCCGGCTGAGCATCCAGCGCTGCATCCAGTCGCTGGTG
CACGCGTGCCAGTGCCGCAACGCCAACTGCTCGCTGCCATCCTGCCAGAAGATGAAGCGG
GTGGTGCAGCACACCAAGGGCTGCAAACGCAAGACCAACGGGGGCTGCCCGGTGTGCAAG
CAGCTCATCGCCCTCTGCTGCTACCACGCCAAGCACTGCCAAGAAAACAAATGCCCCGTG
CCCTTCTGCCTCAACATCAAACACAAGCTCCGCCAGCAGCAGATCCAGCACCGCCTGCAG
CAGGCCCAGCTCATGCGCCGGCGGATGGCCACCATGAACACCCGCAACGTGCCTCAGCAG
AGTCTGCCTTCTCCTACCTCAGCACCGCCCGGGACCCCCACACAGCAGCCCAGCACACCC
CAGACGCCGCAGCCCCCTGCCCAGCCCCAACCCTCACCCGTGAGCATGTCACCAGCTGGC
TTCCCCAGCGTGGCCCGGACTCAGCCCCCCACCACGGTGTCCACAGGGAAGCCTACCAGC
CAGGTGCCGGCCCCCCCACCCCCGGCCCAGCCCCCTCCTGCAGCGGTGGAAGCGGCTCGG
CAGATCGAGCGTGAGGCCCAGCAGCAGCAGCACCTGTACCGGGTGAACATCAACAACAGC
ATGCCCCCAGGACGCACGGGCATGGGGACCCCGGGGAGCCAGATGGCCCCCGTGAGCCTG
AATGTGCCCCGACCCAACCAGGTGAGCGGGCCCGTCATGCCCAGCATGCCTCCCGGGCAG
TGGCAGCAGGCGCCCCTTCCCCAGCAGCAGCCCATGCCAGGCTTGCCCAGGCCTGTGATA
TCCATGCAGGCCCAGGCGGCCGTGGCTGGGCCCCGGATGCCCAGCGTGCAGCCACCCAGG
AGCATCTCACCCAGCGCTCTGCAAGACCTGCTGCGGACCCTGAAGTCGCCCAGCTCCCCT
CAGCAGCAACAGCAGGTGCTGAACATTCTCAAATCAAACCCGCAGCTAATGGCAGCTTTC
ATCAAACAGCGCACAGCCAAGTACGTGGCCAATCAGCCCGGCATGCAGCCCCAGCCTGGC
CTCCAGTCCCAGCCCGGCATGCAACCCCAGCCTGGCATGCACCAGCAGCCCAGCCTGCAG
AACCTGAATGCCATGCAGGCTGGCGTGCCGCGGCCCGGTGTGCCTCCACAGCAGCAGGCG
ATGGGAGGCCTGAACCCCCAGGGCCAGGCCTTGAACATCATGAACCCAGGACACAACCCC
AACATGGCGAGTATGAATCCACAGTACCGAGAAATGTTACGGAGGCAGCTGCTGCAGCAG
CAGCAGCAACAGCAGCAGCAACAACAGCAGCAACAGCAGCAGCAGCAAGGGAGTGCCGGC
ATGGCTGGGGGCATGGCGGGGCACGGCCAGTTCCAGCAGCCTCAAGGACCCGGAGGCTAC
CCACCGGCCATGCAGCAGCAGCAGCGCATGCAGCAGCATCTCCCCCTCCAGGGCAGCTCC
ATGGGCCAGATGGCGGCTCAGATGGGACAGCTTGGCCAGATGGGGCAGCCGGGGCTGGGG
GCAGACAGCACCCCCAACATCCAGCAAGCCCTGCAGCAGCGGATTCTGCAGCAACAGCAG
ATGAAGCAGCAGATTGGGTCCCCAGGCCAGCCGAACCCCATGAGCCCCCAGCAACACATG
CTCTCAGGACAGCCACAGGCCTCGCATCTCCCTGGCCAGCAGATCGCCACGTCCCTTAGT
AACCAGGTGCGGTCTCCAGCCCCTGTCCAGTCTCCACGGCCCCAGTCCCAGCCTCCACAT
TCCAGCCCGTCACCACGGATACAGCCCCAGCCTTCGCCACACCACGTCTCACCCCAGACT
GGTTCCCCCCACCCCGGACTCGCAGTCACCATGGCCAGCTCCATAGATCAGGGACACTTG
GGGAACCCCGAACAGAGTGCAATGCTCCCCCAGCTGAACACCCCCAGCAGGAGTGCGCTG
TCCAGCGAACTGTCCCTGGTCGGGGACACCACGGGGGACACGCTAGAGAAGTTTGTGGAG
GGCTTGTAG
Enzyme 2 GenBank Gene ID U85962 Link Image
Enzyme 2 GeneCard ID CREBBP Link Image
Enzyme 2 GenAtlas ID CREBBP Link Image
Enzyme 2 HGNC ID HGNC:2348 Link Image
Enzyme 2 Chromosome Location 16
Enzyme 2 Locus 16p13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sobulo OM, Borrow J, Tomek R, Reshmi S, Harden A, Schlegelberger B, Housman D, Doggett NA, Rowley JD, Zeleznik-Le NJ: MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8732-7. [PubMed Link Image]
  2. Giles RH, Petrij F, Dauwerse HG, den Hollander AI, Lushnikova T, van Ommen GJ, Goodman RH, Deaven LL, Doggett NA, Peters DJ, Breuning MH: Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3. Genomics. 1997 May 15;42(1):96-114. [PubMed Link Image]
  3. Borrow J, Stanton VP Jr, Andresen JM, Becher R, Behm FG, Chaganti RS, Civin CI, Disteche C, Dube I, Frischauf AM, Horsman D, Mitelman F, Volinia S, Watmore AE, Housman DE: The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet. 1996 Sep;14(1):33-41. [PubMed Link Image]
  4. Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. [PubMed Link Image]
  5. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed Link Image]
  6. Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed Link Image]
  7. Doucas V, Tini M, Egan DA, Evans RM: Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2627-32. [PubMed Link Image]
  8. Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell. 1999 Sep 3;98(5):675-86. [PubMed Link Image]
  9. Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed Link Image]
  10. Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed Link Image]
  11. Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed Link Image]
  12. Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed Link Image]
  13. Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Mol Cell Biol. 2002 May;22(10):3549-61. [PubMed Link Image]
  14. Watanabe N, Wachi S, Fujita T: Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination. J Biol Chem. 2003 Jul 11;278(28):26102-10. Epub 2003 May 2. [PubMed Link Image]
  15. Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5271-6. [PubMed Link Image]
  16. Murata T, Kurokawa R, Krones A, Tatsumi K, Ishii M, Taki T, Masuno M, Ohashi H, Yanagisawa M, Rosenfeld MG, Glass CK, Hayashi Y: Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. Hum Mol Genet. 2001 May 1;10(10):1071-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5351
Enzyme 3 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 3 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 3 Gene Name ENPP1
Enzyme 3 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 3 Number of Residues 925
Enzyme 3 Molecular Weight 104925
Enzyme 3 Theoretical pI 7.14
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 77-97
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 189650 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2622 bp
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 3 GenBank Gene ID M57736 Link Image
Enzyme 3 GeneCard ID ENPP1 Link Image
Enzyme 3 GenAtlas ID ENPP1 Link Image
Enzyme 3 HGNC ID HGNC:3356 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6q22-q23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5781
Enzyme 4 Name Hormone-sensitive lipase
Enzyme 4 Synonyms
  1. HSL
Enzyme 4 Gene Name LIPE
Enzyme 4 Protein Sequence >Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
Enzyme 4 Number of Residues 1076
Enzyme 4 Molecular Weight 116599
Enzyme 4 Theoretical pI 6.68
Enzyme 4 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • cholesterol metabolism
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • sterol metabolism
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate
  • (2) triacylglycerol + H2O = diacylglycerol + a carboxylate
  • (3) monoacylglycerol + H2O = glycerol + a carboxylate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 896476 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q05469 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name LIPS_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2328 bp
ATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCCTTC
TTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGTGTA
CGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCACCTC
TTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCCCGC
TGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGCATC
TTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACCCAG
CTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTACTC
TTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTGCAT
AAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCATTC
CTGCAGACCATCTCCATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAGACA
GGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCCGAG
CTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAAGCC
TTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCCACC
GTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACTGCC
GACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCCGTC
CTCGTCAGGCTCATCTCCTATGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGCAGC
CTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCACCC
CGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCCAGA
TCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCCATC
GACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTCGCC
TACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGCCTT
GCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCCTAC
GGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCTGCC
GCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTCTCC
AAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAGAAA
GCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTCCGC
CTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAGAAG
ATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCCCAG
CCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGCCTG
AGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACACTT
AGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAAGAG
GCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCCTTC
CCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTACTCC
TCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTCAAG
AGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCGGTC
ATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAGGAC
CTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCAGAG
CTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGCGGG
GAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
Enzyme 4 GenBank Gene ID L11706 Link Image
Enzyme 4 GeneCard ID LIPE Link Image
Enzyme 4 GenAtlas ID LIPE Link Image
Enzyme 4 HGNC ID HGNC:6621 Link Image
Enzyme 4 Chromosome Location 19
Enzyme 4 Locus 19q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed Link Image]
  2. Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5833
Enzyme 5 Name Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 5 Synonyms
  1. GMP-PDE gamma
Enzyme 5 Gene Name PDE6H
Enzyme 5 Protein Sequence >Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII
Enzyme 5 Number of Residues 83
Enzyme 5 Molecular Weight 9074
Enzyme 5 Theoretical pI 9.98
Enzyme 5 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • cGMP-specific phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 5 Pathways
Enzyme 5 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1311544 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q13956 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CNCG_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >252 bp
ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA
Enzyme 5 GenBank Gene ID D45399 Link Image
Enzyme 5 GeneCard ID PDE6H Link Image
Enzyme 5 GenAtlas ID PDE6H Link Image
Enzyme 5 HGNC ID HGNC:8790 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12p13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Shimizu-Matsumoto A, Itoh K, Inazawa J, Nishida K, Matsumoto Y, Kinoshita S, Matsubara K, Okubo K: Isolation and chromosomal localization of the human cone cGMP phosphodiesterase gamma cDNA (PDE6H). Genomics. 1996 Feb 15;32(1):121-4. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5843
Enzyme 6 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Enzyme 6 Synonyms
  1. Cam-PDE 1A
  2. 61 kDa Cam-PDE
  3. hCam-1
Enzyme 6 Gene Name PDE1A
Enzyme 6 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ
Enzyme 6 Number of Residues 535
Enzyme 6 Molecular Weight 61253
Enzyme 6 Theoretical pI 6.02
Enzyme 6 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Has a higher affinity for cGMP than for cAMP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1151109 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P54750 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PDE1A_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1608 bp
ATGGGGTCTAGTGCCACAGAGATTGAAGAATTGGAAAACACCACTTTTAAGTATCTTACA
GGAGAACAGACTGAAAAAATGTGGCAGCGCCTGAAAGGAATACTAAGATGCTTGGTGAAG
CAGCTGGAAAGAGGTGATGTTAACGTCGTCGACTTAAAGAAGAATATTGAATATGCGGCA
TCTGTGCTGGAAGCAGTTTATATCGATGAAACAAGAAGACTTCTGGATACTGAAGATGAG
CTCAGTGACATTCAGACTGACTCAGTCCCATCTGAAGTCCGGGACTGGTTGGCTTCTACC
TTTACACGGAAAATGGGGATGACAAAAAAGAAACCTGAGGAAAAACCAAAATTTCGGAGC
ATTGTGCATGCTGTTCAAGCTGGAATTTTTGTGGAAAGAATGTACCGAAAAACATATCAT
ATGGTTGGTTTGGCATATCCAGCAGCTGTCATCGTAACATTAAAGGATGTTGATAAATGG
TCTTTCGATGTATTTGCCCTAAATGAAGCAAGTGGAGAGCATAGTCTGAAGTTTATGATT
TATGAACTGTTTACCAGATATGATCTTATCAACCGTTTCAAGATTCCTGTTTCTTGCCTA
ATCACCTTTGCAGAAGCTTTAGAAGTTGGTTACAGCAAGTACAAAAATCCATATCACAAT
TTGATTCATGCAGCTGATGTCACTCAAACTGTGCATTACATAATGCTTCATACAGGTATC
ATGCACTGGCTCACTGAACTGGAAATTTTAGCAATGGTCTTTGCTGCTGCCATTCATGAT
TATGAGCATACAGGGACAACAAACAACTTTCACATTCAGACAAGGTCAGATGTTGCCATT
TTGTATAATGATCGCTCTGTCCTTGAGAATCACCACGTGAGTGCAGCTTATCGACTTATG
CAAGAAGAAGAAATGAATATCTTGATAAATTTATCCAAAGATGACTGGAGGGATCTTCGG
AACCTAGTGATTGAAATGGTTTTATCTACAGACATGTCAGGTCACTTCCAGCAAATTAAA
AATATAAGAAACAGTTTGCAGCAGCCTGAAGGGATTGACAGAGCCAAAACCATGTCCCTG
ATTCTCCACGCAGCAGACATCAGCCACCCAGCCAAATCCTGGAAGCTGCATTATCGGTGG
ACCATGGCCCTAATGGAGGAGTTTTTCCTGCAGGGAGATAAAGAAGCTGAATTAGGGCTT
CCATTTTCCCCACTTTGTGATCGGAAGTCAACCATGGTGGCCCAGTCACAAATAGGTTTC
ATCGATTTCATAGTAGAGCCAACATTTTCTCTTCTGACAGACTCAACAGAGAAAATTGTT
ATTCCTCTTATAGAGGAAGCCTCAAAAGCCGAAACTTCTTCCTATGTGGCAAGCAGCTCA
ACCACCATTGTGGGGTTACACATTGCTGATGCACTAAGACGATCAAATACAAAAGGCTCC
ATGAGTGATGGGTCCTATTCCCCAGACTACTCCCTTGCAGCAGTGGACCTGAAGAGTTTC
AAGAACAACCTGGTGGACATCATTCAGCAGAACAAAGAGAGGTGGAAAGAGTTAGCTGCA
CAAGAAGCAAGAACCAGTTCACAGAAGTGTGAGTTTATTCATCAGTAA
Enzyme 6 GenBank Gene ID U40370 Link Image
Enzyme 6 GeneCard ID PDE1A Link Image
Enzyme 6 GenAtlas ID PDE1A Link Image
Enzyme 6 HGNC ID HGNC:8774 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q32.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed Link Image]
  2. Michibata H, Yanaka N, Kanoh Y, Okumura K, Omori K: Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim Biophys Acta. 2001 Jan 26;1517(2):278-87. [PubMed Link Image]
  3. Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5847
Enzyme 7 Name High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name PDE8A
Enzyme 7 Protein Sequence >High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSG
KKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACF
LDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGF
TRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYA
NPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI
QQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSL
DVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLE
ILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPIS
LDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRS
WLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDH
PGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQG
IIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRM
LIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQIS
FIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE
Enzyme 7 Number of Residues 829
Enzyme 7 Molecular Weight 93305
Enzyme 7 Theoretical pI 6.03
Enzyme 7 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • DNA binding
  • binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • kinase activity
  • nucleic acid binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein histidine kinase activity
  • protein kinase activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • two-component response regulator activity
  • two-component sensor molecule activity
Process
  • cell communication
  • cellular process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • two-component signal transduction system (phosphorelay)
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 7 General Function Signal transduction mechanisms
Enzyme 7 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase, which has a high affinity for cAMP, may be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development
Enzyme 7 Pathways
Enzyme 7 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 16417190 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O60658 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PDE8A_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2490 bp
ATGGGCTGTGCCCCGAGCATCCACATTTCCGAGCGCCTGGTGGCCGAGGACGCGCCTAGC
CCCGCGGCACCGCCGCTGTCGTCCGGCGGGCCGCGCCTCCCGCAGGGCCAGAAGACGGCC
GCCTTGCCCCGGACCCGCGGCGCCGGCCTCTTGGAGTCGGAGCTTCGCGACGGCAGCGGC
AAGAAGGTAGCAGTAGCTGATGTGCAGTTTGGCCCCATGAGATTTCATCAAGATCAACTT
CAGGTACTTTTAGTGTTTACCAAAGAAGATAACCAATGTAATGGATTCTGCAGGGCATGT
GAAAAAGCAGGGTTTAAGTGTACAGTTACCAAGGAGGCTCAGGCTGTCCTTGCCTGTTTC
CTGGACAAACATCATGACATTATCATCATAGACCACAGAAATCCTCGACAGCTGGATGCA
GAGGCACTGTGCAGGTCTATCAGATCATCAAAACTCTCAGAAAACACAGTTATTGTTGGT
GTAGTACGCAGGGTGGATAGAGAAGAGTTGTCCGTAATGCCTTTCATTTCTGCTGGATTT
ACAAGGAGGTATGTAGAAAACCCCAACATCATGGCCTGCTACAATGAACTGCTCCAGCTG
GAGTTTGGAGAGGTGCGATCACAACTGAAACTCAGGGCTTGTAACTCAGTATTCACTGCA
TTAGAAAACAGTGAAGATGCAATTGAAATTACAAGCGAAGACCGTTTTATACAGTATGCA
AATCCTGCATTTGAAACAACAATGGGCTATCAGTCAGGTGAATTAATAGGGAAGGAGTTA
GGAGAAGTGCCTATAAATGAAAAAAAGGCTGACTTGCTCGATACTATAAATTCATGCATC
AGGATAGGCAAGGAGTGGCAAGGAATTTACTATGCAAAAAAGAAAAACGGAGATAATATA
CAACAAAATGTGAAGATAATACCTGTCATTGGACAGGGAGGAAAAATTAGACACTATGTG
TCCATTATCAGAGTGTGCAATGGCAACAATAAGGCTGAGAAAATATCCGAATGTGTTCAG
TCTGACACTCATACAGATAATCAGACAGGCAAACATAAAGACAGGAGAAAAGGCTCACTA
GACGTCAAAGCTGTTGCCTCCCGTGCAACTGAAGTTTCCAGCCAGAGACGACACTCTTCC
ATGGCCCGGATACATTCCATGACAATTGAGGCGCCCATCACCAAGGTAATCAATATTATC
AATGCTGCCCAGGAAAGTAGTCCCATGCCTGTGACAGAAGCCCTAGACCGTGTGCTGGAA
ATTCTAAGAACCACTGAGTTATATTCACCACAGTTTGGTGCTAAAGATGATGATCCCCAT
GCCAATGACCTTGTTGGGGGCTTAATGTCTGATGGTTTGCGAAGACTATCAGGGAATGAA
TATGTTCTTTCAACAAAAAACACTCAAATGGTTTCAAGCAATATAATCACTCCCATCTCC
CTTGATGATGTCCCACCACGGATAGCTCGGGCCATGGAAAATGAGGAATACTGGGACTTT
GATATTTTTGAACTGGAGGCTGCCACCCACAATAGGCCTTTGATTTATCTTGGTCTCAAA
ATGTTTGCTCGCTTTGGAATCTGTGAATTCTTACACTGCTCCGAGTCAACGCTAAGATCA
TGGTTACAAATTATCGAAGCCAATTATCATTCCTCCAATCCCTACCACAATTCTACACAT
TCTGCTGATGTGCTTCATGCCACTGCCTATTTTCTCTCCAAGGAGAGGATAAAGGAAACT
TTAGATCCAATTGATGAGGTCGCTGCACTCATCGCAGCCACCATTCATGATGTGGATCAC
CCTGGGAGAACCAACTCCTTCCTGTGTAATGCTGGAAGTGAGCTGGCCATTTTGTACAAT
GACACTGCTGTGCTGGAGAGCCACCATGCGGCCTTGGCCTTCCAGCTGACCACTGGAGAT
GATAAATGCAATATATTTAAAAACATGGAGAGGAATGATTATCGGACACTGCGCCAGGGG
ATTATCGACATGGTCTTAGCCACAGAAATGACAAAGCACTTTGAGCATGTCAACAAATTT
GTCAACAGCATCAACAAACCCTTGGCAACACTAGAAGAAAATGGGGAAACTGATAAAAAC
CAGGAAGTGATAAACACTATGCTTAGGACTCCAGAGAACCGGACCCTAATCAAACGAATG
CTGATTAAATGTGCTGATGTGTCCAATCCCTGCCGACCCCTGCAGTACTGCATCGAGTGG
GCTGCACGCATTTCGGAAGAATATTTTTCTCAGACTGATGAAGAGAAGCAGCAGGGCTTA
CCTGTGGTGATGCCAGTGTTTGACAGAAATACCTGCAGCATCCCCAAATCCCAAATCTCT
TTCATTGATTACTTCATCACAGACATGTTTGATGCTTGGGATGCCTTTGTAGACCTGCCT
GATTTAATGCAGCATCTTGACAACAACTTTAAATACTGGAAAGGACTGGACGAAATGAAG
CTGCGGAACCTCCGACCACCTCCTGAATAG
Enzyme 7 GenBank Gene ID AF388183 Link Image
Enzyme 7 GeneCard ID PDE8A Link Image
Enzyme 7 GenAtlas ID PDE8A Link Image
Enzyme 7 HGNC ID HGNC:8793 Link Image
Enzyme 7 Chromosome Location 15
Enzyme 7 Locus 15q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Wang P, Wu P, Egan RW, Billah MM: Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution. Gene. 2001 Dec 12;280(1-2):183-94. [PubMed Link Image]
  2. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 1998 May 29;246(3):570-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5848
Enzyme 8 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
Enzyme 8 Synonyms
  1. Cam-PDE 1B
  2. 63 kDa Cam-PDE
Enzyme 8 Gene Name PDE1B
Enzyme 8 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
Enzyme 8 Number of Residues 536
Enzyme 8 Molecular Weight 61380
Enzyme 8 Theoretical pI 5.22
Enzyme 8 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Has a preference for cGMP as a substrate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1621592 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q01064 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PDE1B_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1611 bp
ATGGAGCTGTCCCCCCGCAGTCCTCCGGAGATGCTGGAGGAGTCGGATTGCCCGTCACCC
CTGGAGCTGAAGTCAGCCCCCAGCAAGAAGATGTGGATTAAGCTTCGGTCTCTGCTGCGC
TACATGGTGAAGCAGTTGGAGAATGGGGAGATAAACATTGAGGAGCTGAAGAAAAATCTG
GAGTACACAGCTTCTCTGCTGGAAGCCGTCTACATAGATGAGACACGGCAAATCTTGGAC
ACGGAGGACGAGCTGCAGGAGCTGCGGTCAGATGCCGTGCCTTCGGAGGTGCGGGACTGG
CTGGCCTCCACCTTCACCCAGCAGGCCCGGGCCAAAGGCCGCCGAGCAGAGGAGAAGCCC
AAGTTCCGAAGCATTGTGCACGCTGTGCAGGCTGGGATCTTCGTGGAACGGATGTTCCGG
AGAACATACACCTCTGTGGGCCCCACTTACTCTACTGCGGTTCTCAACTGTCTCAAGAAC
CTGGATCTCTGGTGCTTTGATGTCTTTTCCTTGAACCAGGCAGCAGATGACCATGCCCTG
AGGACCATTGTTTTTGAGTTGCTGACTCGGCATAACCTCATCAGCCGCTTCAAGATTCCC
ACTGTGTTTTTGATGAGTTTCCTGGATGCCTTGGAGACAGGCTATGGGAAGTACAAGAAT
CCTTACCACAACCAGATCCACGCAGCCGATGTTACCCAGACAGTCCATTGCTTCTTGCTC
CGCACAGGGATGGTGCACTGCCTGTCGGAGATTGAGCTCCTGGCCATCATCTTTGCTGCA
GCTATCCATGATTATGAGCACACGGGCACTACCAACAGCTTCCACATCCAGACCAAGTCA
GAATGTGCCATCGTGTACAATGATCGTTCAGTGCTGGAGAATCACCACATCAGCTCTGTT
TTCCGATTGATGCAGGATGATGAGATGAACATTTTCATCAACCTCACCAAGGATGAGTTT
GTAGAACTCCGAGCCCTGGTCATTGAGATGGTGTTGGCCACAGACATGTCCTGCCATTTC
CAGCAAGTGAAGACCATGAAGACAGCCTTGCAACAGCTGGAGAGGATTGACAAGCCCAAG
GCCCTGTCTCTACTGCTCCATGCTGCTGACATCAGCCACCCAACCAAGCAGTGGTTGGTC
CACAGCCGTTGGACCAAGGCCCTCATGGAGGAATTCTTCCGTCAGGGTGACAAGGAGGCA
GAGTTGGGCCTGCCCTTTTCTCCACTCTGTGACCGCACTTCCACTCTAGTGGCACAGTCT
CAGATAGGGTTCATCGACTTCATTGTGGAGCCCACATTCTCTGTGCTGACTGACGTGGCA
GAGAAGAGTGTTCAGCCCCTGGCGGATGAGGACTCCAAGTCTAAAAACCAGCCCAGCTTT
CAGTGGCGCCAGCCCTCTCTGGATGTGGAAGTGGGAGACCCCAACCCTGATGTGGTCAGC
TTTCGTTCCACCTGGGTCAAGCGCATTCAGGAGAACAAGCAGAAATGGAAGGAACGGGCA
GCAAGTGGCATCACCAACCAGATGTCCATTGACGAGCTGTCCCCCTGTGAAGAAGAGGCC
CCCCCATCCCCTGCCGAAGATGAACACAACCAGAATGGGAATCTGGATTAG
Enzyme 8 GenBank Gene ID U56976 Link Image
Enzyme 8 GeneCard ID PDE1B Link Image
Enzyme 8 GenAtlas ID PDE1B Link Image
Enzyme 8 HGNC ID HGNC:8775 Link Image
Enzyme 8 Chromosome Location 12
Enzyme 8 Locus 12q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Jiang X, Li J, Paskind M, Epstein PM: Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11236-41. [PubMed Link Image]
  2. Yu J, Wolda SL, Frazier AL, Florio VA, Martins TJ, Snyder PB, Harris EA, McCaw KN, Farrell CA, Steiner B, Bentley JK, Beavo JA, Ferguson K, Gelinas R: Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 1997 Nov;9(7):519-29. [PubMed Link Image]
  3. Repaske DR, Swinnen JV, Jin SL, Van Wyk JJ, Conti M: A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase. J Biol Chem. 1992 Sep 15;267(26):18683-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5850
Enzyme 9 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase B
Enzyme 9 Synonyms
  1. Cyclic GMP-inhibited phosphodiesterase B
  2. CGI-PDE B
  3. CGIPDE1
  4. CGIP1
Enzyme 9 Gene Name PDE3B
Enzyme 9 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase B
MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELR
PPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLS
PLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGD
AGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSL
PSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSL
GETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEAR
NMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKG
DRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGP
FNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDT
ADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSG
KSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLD
LILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQF
MNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRIN
HGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQ
AVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFD
FLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFY
EQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDN
DTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEE
KCKADGNKLQVENSSLPQADEIQVIEEADEEE
Enzyme 9 Number of Residues 1112
Enzyme 9 Molecular Weight 124335
Enzyme 9 Theoretical pI 5.75
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function May play a role in fat metabolism
Enzyme 9 Pathways
Enzyme 9 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 88-108 117-137 152-172 192-212 220-240 247-267
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1145302 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13370 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PDE3B_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >3339 bp
ATGAGGAGGGACGAGCGAGACGCCAAAGCCATGCGGTCCCTGCAGCCGCCGGATGGGGCC
GGCTCGCCCCCCGAGAGTCTGAGGAACGGCTACGTGAAGAGCTGCGTGAGCCCCTTGCGG
CAGGACCCTCCGCGCGGCTTCTTCTTCCACCTCTGCCGCTTCTGCAACGTGGAGCTGCGG
CCGCCGCCGGCCTCTCCCCAGCAGCCGCGGCGCTGCTCCCCCTTCTGCCGGGCGCGCCTC
TCGCTGGGCGACCTGGCTGCCTTTGTCCTCGCCCTGCTGCTGGGAGCGGAACCCGAGAGC
TGGGCTGCCGGGGCCGCCTGGCTGCGGACGCTGCTGAGCGTGTGTTCGCACAGCTTGAGC
CCCCTCTTCAGCATCGCCTGTGCCTTCTTCTTCCTCACCTGCTTCCTCACCCGGACCAAG
CGGGGACCCGGCCCGGGCCGGAGCTGCGGCTCCTGGTGGCTGCTGGCGCTGCCCGCCTGC
TGTTACCTGGGGGACTTCTTGGTGTGGCAGTGGTGGTCTTGGCCTTGGGGGGATGGCGAC
GCAGGGTCCGCGGCCCCGCACACGCCCCCGGAGGCGGCAGCGGGCAGGTTGCTGCTGGTG
CTGAGCTGCGTAGGGCTGCTGCTGACGCTCGCGCACCCGCTGCGGCTCCGGCACTGCGTT
CTGGTGCTGCTCCTGGCCAGCTTCGTCTGGTGGGTCTCCTTCACCAGCCTCGGGTCGCTG
CCCTCCGCCCTCAGGCCGCTGCTCTCCGGCCTGGTGGGGGGCGCTGGCTGCCTGCTGGCC
CTGGGGTTGGATCACTTCTTTCAAATCAGGGAAGCGCCTCTTCATCCTCGACTGTCCAGT
GCCGCCGAAGAAAAAGTGCCTGTGATCCGACCCCGGAGGAGGTCCAGCTGCGTGTCGTTA
GGAGAAACTGCAGCCAGTTACTATGGCAGTTGCAAAATATTCAGGAGACCGTCGTTGCCT
TGTATTTCCAGAGAACAGATGATTCTTTGGGATTGGGACTTAAAACAATGGTATAAGCCT
CATTATCAAAATTCTGGAGGTGGAAATGGAGTTGATCTTTCAGTGCTAAATGAGGCTCGC
AATATGGTGTCAGATCTTCTGACTGATCCAAGCCTTCCACCACAAGTCATTTCCTCTCTA
CGGAGTATTAGTAGCTTAATGGGTGCTTTCTCAGGTTCCTGTAGGCCAAAGATTAATCCT
CTCACACCATTTCCTGGATTTTACCCCTGTTCTGAAATAGAGGACCCAGCTGAGAAAGGG
GATAGAAAACTTAACAAGGGACTAAATAGGAATAGTTTGCCAACTCCACAGCTGAGGAGA
AGCTCAGGAACTTCAGGATTGCTACCTGTTGAACAGTCTTCAAGGTGGGATCGTAATAAT
GGCAAAAGGCCTCACCAAGAATTTGGCATTTCAAGTCAAGGATGCTATCTAAATGGGCCT
TTTAATTCAAATCTACTGACTATCCCGAAGCAAAGGTCATCTTCTGTATCACTGACTCAC
CATGTAGGTCTCAGAAGAGCTGGTGTTTTGTCCAGTCTGAGTCCTGTGAATTCTTCCAAC
CATGGACCAGTGTCTACTGGCTCTCTAACTAATCGATCACCCATAGAATTTCCTGATACT
GCTGATTTTCTTAATAAGCCAAGCGTTATCTTGCAGAGATCTCTGGGCAATGCACCTAAT
ACTCCAGATTTTTATCAGCAACTTAGAAATTCTGATAGCAATCTGTGTAACAGCTGTGGA
CATCAAATGCTGAAATATGTTTCAACATCTGAATCAGATGGTACAGATTGCTGCAGTGGA
AAATCAGGTGAAGAAGAAAACATTTTCTCGAAAGAATCATTCAAACTTATGGAAACTCAA
CAAGAAGAGGAAACAGAGAAGAAAGACAGCAGAAAATTATTTCAGGAAGGTGATAAGTGG
CTAACAGAAGAGGCACAGAGTGAACAGCAAACAAATATTGAACAGGAAGTATCACTGGAC
CTGATTTTAGTAGAAGAGTATGACTCATTAATAGAAAAGATGAGCAACTGGAATTTTCCA
ATTTTTGAACTTGTAGAAAAGATGGGAGAGAAATCAGGAAGGATTCTCAGTCAGGTTATG
TATACCTTATTTCAAGACACTGGTTTATTGGAAATATTTAAAATTCCCACTCAACAATTT
ATGAACTATTTTCGTGCATTAGAAAATGGCTATCGAGACATTCCTTATCACAATCGTATA
CATGCCACAGATGTGCTACATGCAGTTTGGTATCTGACAACACGGCCAGTTCCTGGCTTA
CAGCAGATCCACAATGGTTGTGGAACAGGAAATGAAACAGATTCTGATGGTAGAATTAAC
CATGGGCGAATTGCTTATATTTCTTCGAAGAGCTGCTCTAATCCTGATGAGAGTTATGGC
TGCCTGTCTTCAAACATTCCTGCATTAGAATTGATGGCTCTATACGTGGCAGCTGCCATG
CATGATTATGATCACCCAGGGAGGACAAATGCATTTCTAGTGGCTACAAATGCCCCTCAG
GCAGTTTTATACAATGACAGATCTGTTCTGGAAAATCATCATGCTGCGTCAGCTTGGAAT
CTATATCTTTCTCGCCCAGAATACAACTTCCTTCTTCATCTTGATCATGTGGAATTCAAG
CGCTTTCGTTTTTTAGTCATTGAAGCAATCCTTGCTACGGATCTTAAAAAGCATTTTGAT
TTTCTCGCAGAATTCAATGCCAAGGCAAATGATGTAAATAGTAATGGCATAGAATGGAGT
AATGAAAATGATCGCCTCTTGGTATGCCAGGTGTGCATCAAACTGGCAGATATAAATGGC
CCAGCAAAAGTTCGAGACTTGCATTTGAAATGGACAGAAGGCATTGTCAATGAATTTTAT
GAGCAGGGAGATGAAGAAGCAAATCTTGGTCTGCCCATCAGTCCATTCATGGATCGTTCT
TCTCCTCAACTAGCAAAACTCCAAGAATCTTTTATCACCCACATAGTGGGTCCCCTGTGT
AACTCCTATGATGCTGCTGGTTTGCTACCAGGTCAGTGGTTAGAAGCAGAAGAGGATAAT
GATACTGAAAGTGGTGATGATGAAGACGGTGAAGAATTAGATACAGAAGATGAAGAAATG
GAAAACAATCTAAATCCAAAACCACCAAGAAGGAAAAGCAGACGGCGAATATTTTGTCAG
CTAATGCACCACCTCACTGAAAACCACAAGATATGGAAGGAAATCGTAGAGGAAGAAGAA
AAATGTAAAGCTGATGGGAATAAACTGCAGGTGGAGAATTCCTCCTTACCTCAAGCAGAT
GAGATTCAGGTAATTGAAGAGGCAGATGAAGAGGAATAG
Enzyme 9 GenBank Gene ID U38178 Link Image
Enzyme 9 GeneCard ID PDE3B Link Image
Enzyme 9 GenAtlas ID PDE3B Link Image
Enzyme 9 HGNC ID HGNC:8779 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11p15.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Miki T, Taira M, Hockman S, Shimada F, Lieman J, Napolitano M, Ward D, Taira M, Makino H, Manganiello VC: Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Genomics. 1996 Sep 15;36(3):476-85. [PubMed Link Image]
  2. Lobbert RW, Winterpacht A, Seipel B, Zabel BU: Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A)--a gene involved in fat metabolism located at 11p 15.1. Genomics. 1996 Oct 15;37(2):211-8. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5862
Enzyme 10 Name High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
Enzyme 10 Synonyms
  1. HCP1
  2. TM22
Enzyme 10 Gene Name PDE7A
Enzyme 10 Protein Sequence >High-affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQRRGAISYDSSDQTA
LYIRMLGDVRVRSRAGFESERRGSHPYIDFRIFHSQSEIEVSVSARNIRRLLSFQRYLRS
SRFFRGTAVSNSLNILDDDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSL
HGLIEYFHLDMMKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLANSVTPW
DILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAVGLLRESGLFS
HLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDLCLEDTRHRHLVLQMALKC
ADICNPCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRHTESIANIQIGFMTYL
VEPLFTEWARFSNTRLSQTMLGHVGLNKASWKGLQREQSSSEDTDAAFELNSQLLPQENR
LS
Enzyme 10 Number of Residues 482
Enzyme 10 Molecular Weight 55506
Enzyme 10 Theoretical pI 7.53
Enzyme 10 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase is highly specific for cAMP and may have a role in muscle signal transduction
Enzyme 10 Pathways
Enzyme 10 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 5566609 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q13946 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PDE7A_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1449 bp
ATGGAAGTGTGTTACCAGCTGCCGGTACTGCCCCTGGACAGGCCGGTCCCCCAGCACGTC
CTCAGCCGCCGAGGAGCCATCAGCTTCAGCTCCAGCTCCGCTCTCTTCGGCTGCCCCAAT
CCCCGGCAGCTCTCTCAGAGGCGTGGAGCTATTTCCTATGACAGTTCTGATCAGACTGCA
TTATACATTCGTATGCTAGGAGATGTACGTGTAAGGAGCCGAGCAGGATTTGAATCAGAA
AGAAGAGGTTCTCACCCATATATTGATTTTCGTATTTTCCACTCTCAATCTGAAATTGAA
GTGTCTGTCTCTGCAAGGAATATCAGAAGGCTACTAAGTTTCCAGCGATATCTTAGATCT
TCACGCTTTTTTCGTGGTACTGCGGTTTCAAATTCCCTAAACATTTTAGATGATGATTAT
AATGGACAAGCCAAGTGTATGCTGGAAAAAGTTGGAAATTGGAATTTTGATATCTTTCTA
TTTGATAGACTAACAAATGGAAATAGTCTAGTAAGCTTAACCTTTCATTTATTTAGTCTT
CATGGATTAATTGAGTACTTCCATTTAGATATGATGAAACTTCGTAGATTTTTAGTTATG
ATTCAAGAAGATTACCACAGTCAAAATCCTTACCATAACGCAGTCCACGCTGCGGATGTT
ACTCAGGCCATGCACTGTTACTTAAAGGAACCTAAGCTTGCCAATTCTGTAACTCCTTGG
GATATCTTGCTGAGCTTAATTGCAGCTGCCACTCATGATCTGGATCATCCAGGTGTTAAT
CAACCTTTCCTTATTAAAACTAACCATTACTTGGCAACTTTATACAAGAATACCTCAGTA
CTGGAAAATCACCACTGGAGATCTGCAGTGGGCTTATTGAGAGAATCAGGCTTATTCTCA
CATCTGCCATTAGAAAGCAGGCAACAAATGGAGACACAGATAGGTGCTCTGATACTAGCC
ACAGACATCAGTCGCCAGAATGAGTATCTGTCTTTGTTTAGGTCCCATTTGGATAGAGGT
GATTTATGCCTAGAAGACACCAGACACAGACATTTGGTTTTACAGATGGCTTTGAAATGT
GCTGATATTTGTAACCCATGTCGGACGTGGGAATTAAGCAAGCAGTGGAGTGAAAAAGTA
ACGGAGGAATTCTTCCATCAAGGAGATATAGAAAAAAAATATCATTTGGGTGTGAGTCCA
CTTTGCGATCGTCACACTGAATCTATTGCCAACATCCAGATTGGTTTTATGACTTACCTA
GTGGAGCCTTTATTTACAGAATGGGCCAGGTTTTCCAATACAAGGCTATCCCAGACAATG
CTTGGACACGTGGGGCTGAATAAAGCCAGCTGGAAGGGACTGCAGAGAGAACAGTCGAGC
AGTGAGGACACTGATGCTGCATTTGAGTTGAACTCACAGTTATTACCTCAGGAAAATCGG
TTATCATAA
Enzyme 10 GenBank Gene ID L12052 Link Image
Enzyme 10 GeneCard ID PDE7A Link Image
Enzyme 10 GenAtlas ID PDE7A Link Image
Enzyme 10 HGNC ID HGNC:8791 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Michaeli T, Bloom TJ, Martins T, Loughney K, Ferguson K, Riggs M, Rodgers L, Beavo JA, Wigler M: Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J Biol Chem. 1993 Jun 15;268(17):12925-32. [PubMed Link Image]
  2. Han P, Zhu X, Michaeli T: Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart. J Biol Chem. 1997 Jun 27;272(26):16152-7. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5872
Enzyme 11 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase A
Enzyme 11 Synonyms
  1. Cyclic GMP-inhibited phosphodiesterase A
  2. CGI-PDE A
Enzyme 11 Gene Name PDE3A
Enzyme 11 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase A
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q
Enzyme 11 Number of Residues 1141
Enzyme 11 Molecular Weight 124980
Enzyme 11 Theoretical pI 5.87
Enzyme 11 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP)
Enzyme 11 Pathways
Enzyme 11 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 61-83
  • 129-151
  • 158-180
  • 184-206
  • 238-255
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 38201493 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q14432 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PDE3A_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >3426 bp
ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA
Enzyme 11 GenBank Gene ID M91667 Link Image
Enzyme 11 GeneCard ID PDE3A Link Image
Enzyme 11 GenAtlas ID PDE3A Link Image
Enzyme 11 HGNC ID HGNC:8778 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed Link Image]
  2. Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5876
Enzyme 12 Name cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name PDE10A
Enzyme 12 Protein Sequence >cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAP
KEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGEC
NNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLE
SGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVC
RGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELY
SDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYT
GYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHR
IRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIF
VYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTD
LERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNI
FSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMM
TACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFY
NAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Enzyme 12 Number of Residues 779
Enzyme 12 Molecular Weight 88413
Enzyme 12 Theoretical pI 6.57
Enzyme 12 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This enzyme can hydrolyze both cAMP and cGMP, having a higher affinity for cAMP
Enzyme 12 Pathways
Enzyme 12 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 4958858 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y233 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PDE10_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >2340 bp
ATGAGGATAGAAGAGAGGAAATCCCAACATTTAACAGGTTTGACAGATGAAAAAGTGAAG
GCATATCTTTCTCTTCACCCCCAGGTATTAGATGAATTTGTATCTGAAAGTGTTAGTGCA
GAGACAGTAGAGAAATGGCTGAAGAGGAAGAACAACAAATCAGAAGATGAATCAGCTCCT
AAGGAAGTCAGCAGGTACCAAGATACGAATATGCAGGGAGTTGTATATGAACTAAACAGC
TATATAGAACAACGGTTGGACACAGGAGGAGACAACCAGCTACTCCTCTATGAACTGAGC
AGCATCATTAAAATAGCCACAAAAGCCGATGGATTTGCACTGTATTTCCTTGGAGAGTGC
AATAATAGCCTGTGTATATTCACGCCACCTGGGATAAAGGAAGGAAAACCCCGCCTCATC
CCTGCTGGGCCCATCACTCAGGGCACCACCGTCTCTGCTTATGTGGCCAAGTCCAGGAAA
ACACTGCTAGTAGAAGACATCCTTGGAGATGAACGATTTCCAAGAGGTACTGGACTGGAA
TCAGGGACTCGTATCCAGTCTGTTCTTTGCTTACCAATTGTCACTGCAATTGGTGACTTG
ATTGGTATTCTCGAGCTGTATCGGCACTGGGGCAAAGAAGCCTTCTGTCTTAGTCACCAG
GAGGTTGCAACAGCAAATCTTGCCTGGGCTTCAGTAGCAATACATCAGGTGCAGGTATGC
AGAGGCCTTGCCAAACAGACAGAATTGAATGACTTCCTACTCGACGTATCAAAAACATAT
TTTGATAACATAGTTGCAATAGATTCTCTACTTGAACACATAATGATATATGCAAAAAAC
CTGGTGAATGCCGATCGTTGTGCGCTTTTCCAGGTGGACCATAAGAACAAGGAGTTATAT
TCAGACCTTTTTGATATTGGAGAGGAAAAGGAAGGAAAACCTGTCTTCAAGAAGACCAAA
GAGATAAGATTTTCAATTGAGAAAGGAATTGCTGGCCAAGTAGCAAGAACAGGGGAAGTC
CTGAACATTCCAGATGCCTATGCAGACCCACGCTTTAACAGAGAAGTAGACTTGTACACA
GGCTACACCACGCGGAACATCCTGTGCATGCCCATCGTCAGCCGAGGCAGCGTGATAGGT
GTGGTGCAGATGGTCAACAAAATCAGTGGCAGTGCCTTCTCTAAAACAGATGAAAACAAC
TTCAAAATGTTTGCCGTCTTTTGTGCTTTAGCCTTACACTGTGCTAATATGTATCATAGA
ATTCGCCACTCAGAGTGCATTTACCGGGTAACGATGGAAAAGCTGTCCTACCATAGCATT
TGTACTTCAGAAGAGTGGCAAGGTCTCATGCAATTCACCCTTCCCGTGCGTCTCTGCAAA
GAAATTGAATTATTCCACTTTGACATTGGTCCTTTTGAAAACATGTGGCCTGGAATTTTT
GTCTACATGGTTCATCGGTCCTGTGGGACATCCTGCTTTGAGCTTGAAAAGTTGTGTCGT
TTTATTATGTCTGTGAAGAAGAACTATCGGCGGGTTCCTTATCACAACTGGAAGCATGCG
GTCACTGTAGCACACTGCATGTATGCCATACTTCAGAACAATCACACGCTTTTCACAGAC
CTTGAGCGCAAAGGACTGCTGATTGCGTGTCTGTGTCATGACCTGGACCACAGGGGCTTC
AGTAACAGCTACCTGCAGAAGTTCGACCACCCTCTGGCCGCTCTCTACTCCACTTCCACC
ATGGAGCAGCACCACTTCTCCCAGACTGTGTCCATCCTTCAGTTGGAAGGGCACAATATC
TTCTCCACTCTGAGCTCCAGTGAATATGAGCAGGTGCTTGAGATCATCCGCAAAGCCATC
ATTGCCACAGACCTTGCTTTATACTTTGGAAACAGGAAGCAGTTGGAAGAGATGTACCAG
ACCGGATCACTAAACCTTAATAATCAATCACATAGAGACCGTGTAATTGGTTTGATGATG
ACTGCCTGTGACCTTTGTTCTGTGACAAAACTGTGGCCCGTTACAAAATTGACGGCAAAT
GATATATATGCAGAATTCTGGGCTGAGGGTGATGAAATGAAGAAATTGGGAATACAGCCT
ATTCCTATGATGGACAGAGACAAGAAGGATGAAGTCCCCCAAGGCCAGCTTGGGTTCTAC
AATGCCGTGGCCATTCCCTGCTATACAACCCTTACCCAGATCCTCCCTCCCACGGAGCCT
CTTCTGAAAGCATGCAGGGATAATCTCAGTCAGTGGGAGAAGGTGATTCGAGGGGAGGAG
ACTGCAACCTGGATTTCATCCCCATCCGTGGCTCAGAAGGCAGCTGCATCTGAAGATTGA
Enzyme 12 GenBank Gene ID AB020593 Link Image
Enzyme 12 GeneCard ID PDE10A Link Image
Enzyme 12 GenAtlas ID PDE10A Link Image
Enzyme 12 HGNC ID HGNC:8772 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Fujishige K, Kotera J, Michibata H, Yuasa K, Takebayashi S, Okumura K, Omori K: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [PubMed Link Image]
  2. Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA: Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5877
Enzyme 13 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
Enzyme 13 Synonyms
  1. Cam-PDE 1C
  2. hCam-3
Enzyme 13 Gene Name PDE1C
Enzyme 13 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK
Enzyme 13 Number of Residues 709
Enzyme 13 Molecular Weight 80761
Enzyme 13 Theoretical pI 9.31
Enzyme 13 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Has a high affinity for both cAMP and cGMP
Enzyme 13 Pathways
Enzyme 13 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 1151111 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q14123 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PDE1C_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1905 bp
ATGGAGTCGCCAACCAAGGAGATTGAAGAATTTGAGAGCAACTCTCTGAAATACCTGCAA
CCGGAACAGATCGAGAAAATCTGGCTTCGGCTCCGCGGGCTGAGGAAATATAAGAAAACG
TCCCAGAGATTACGGTCTTTGGTCAAACAATTAGAGAGAGGGGAAGCTTCAGTGGTAGAT
CTTAAGAAGAATTTGGAATATGCAGCCACAGTGCTTGAATCTGTGTATATTGATGAAACA
AGGAGACTCCTGGATACAGAGGATGAGCTCAGTGACATTCAGTCAGATGCTGTGCCTTCT
GAGGTCCGAGACTGGCTGGCCTCCACCTTCACGCGGCAGATGGGGATGATGCTCAGGAGG
AGCGACGAGAAGCCCCGGTTCAAGAGCATCGTTCACGCAGTGCAGGCTGGGATATTTGTG
GAGAGAATGTATAGACGGACATCAAACATGGTTGGACTGAGCTATCCACCAGCTGTTATT
GAGGCATTAAAGGATGTGGACAAGTGGTCCTTTGACGTCTTTTCCCTCAATGAGGCCAGT
GGGGATCATGCACTGAAATTTATTTTCTATGAACTACTCACACGTTATGATCTGATCAGC
CGTTTCAAGATCCCCATTTCTGCACTTGTCTCATTTGTGGAGGCCCTGGAAGTGGGATAC
AGCAAGCACAAAAATCCTTACCATAACTTAATGCACGCTGCCGATGTTACACAGACAGTG
CATTACCTCCTCTATAAGACAGGAGTGGCGAACTGGCTGACGGAGCTGGAGATCTTTGCT
ATAATCTTCTCAGCTGCCATCCATGACTACGAGCATACCGGAACCACCAACAATTTCCAC
ATTCAGACTCGGTCTGATCCAGCTATTCTGTATAATGACAGATCTGTACTGGAGAATCAC
CATTTAAGTGCAGCTTATCGCCTTCTGCAAGATGACGAGGAAATGAATATTTTGATTAAC
CTCTCAAAGGATGACTGGAGGGAGTTTCGAACCTTGGTAATTGAAATGGTGATGGCCACA
GATATGTCTTGTCACTTCCAACAAATCAAAGCAATGAAGACTGCTCTGCAGCAGCCAGAA
GCCATTGAAAAGCCAAAAGCCTTATCCCTTATGCTGCATACAGCAGATATTAGCCATCCA
GCAAAAGCATGGGACCTCCATCATCGCTGGACAATGTCACTCCTGGAGGAGTTCTTCAGA
CAGGGTGACAGAGAAGCAGAGCTGGGGCTGCCTTTTTCTCCTCTGTGTGACCGAAAGTCC
ACTATGGTTGCTCAGTCACAAGTAGGTTTCATTGATTTCATCGTGGAACCCACCTTCACT
GTGCTTACGGACATGACCGAGAAGATTGTGAGTCCATTAATCGATGAAACCTCTCAAACT
GGTGGGACAGGACAGAGGCGTTCGAGTTTGAATAGCATCAGCTCGTCAGATGCCAAGCGA
TCAGGTGTCAAGACCTCTGGTTCAGAGGGAAGTGCCCCGATCAACAATTCTGTCATCTCC
GTTGACTATAAGAGCTTTAAAGCTACTTGGACGGAAGTGGTGCACATCAATCGGGAGAGA
TGGAGGGCCAAGGTACCCAAAGAGGAGAAGGCCAAGAAGGAAGCAGAGGAAAAGGCTCGC
CTGGCCGCAGAGGAGCAGCAAAAGGAAATGGAAGCCAAAAGCCAGGCTGAAGAAGGCGCA
TCTGGCAAAGCTGAGAAAAAGACGTCTGGAGAAACTAAGAATCAAGTCAATGGAACACGG
GCAAACAAAAGTGACAACCCTCGTGGGAAAAATTCCAAAGCCGAGAAGTCATCAGGAGAA
CAGCAACAGAATGGTGACTTCAAAGATGGTAAAAATAAGACAGACAAGAAGGATCACTCT
AACATCGGAAATGATTCAAAGAAAACAGATGATTCACAAGAGTAA
Enzyme 13 GenBank Gene ID U40371 Link Image
Enzyme 13 GeneCard ID PDE1C Link Image
Enzyme 13 GenAtlas ID PDE1C Link Image
Enzyme 13 HGNC ID HGNC:8776 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5881
Enzyme 14 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4B
Enzyme 14 Synonyms
  1. DPDE4
  2. PDE32
Enzyme 14 Gene Name PDE4B
Enzyme 14 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4B
MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT
Enzyme 14 Number of Residues 736
Enzyme 14 Molecular Weight 83344
Enzyme 14 Theoretical pI 4.89
Enzyme 14 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents
Enzyme 14 Pathways
Enzyme 14 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 347122 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q07343 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PDE4B_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2211 bp
ATGAAGAAAAGCAGGAGTGTGATGACGGTGATGGCTGATGATAATGTTAAAGATTATTTT
GAATGTAGCTTGAGTAAATCCTACAGTTCTTCCAGTAACACACTTGGGATCGACCTCTGG
AGAGGGAGAAGGTGTTGCTCAGGAAACTTACAGTTACCACCACTGTCTCAAAGACAGAGT
GAAAGGGCAAGGACTCCTGAGGGAGATGGTATTTCCAGGCCGACCACACTGCCTTTGACA
ACGCTTCCAAGCATTGCTATTACAACTGTAAGCCAGGAGTGCTTTGATGTGGAAAATGGC
CCTTCCCCAGGTCGGAGTCCACTGGATCCCCAGGCCAGCTCTTCCGCTGGGCTGGTACTT
CACGCCACCTTTCCTGGGCACAGCCAGCGCAGAGAGTCATTTCTCTACAGATCAGACAGC
GACTATGACTTGTCACCAAAGGCGATGTCGAGAAACTCTTCTCTTCCAAGCGAGCAACAC
GGCGATGACTTGATTGTAACTCCTTTTGCCCAGGTCCTTGCCAGCTTGCGAAGTGTGAGA
AACAACTTCACTATACTGACAAACCTTCATGGTACATCTAACAAGAGGTCCCCAGCTGCT
AGTCAGCCTCCTGTCTCCAGAGTCAACCCACAAGAAGAATCTTATCAAAAATTAGCAATG
GAAACGCTGGAGGAATTAGACTGGTGTTTAGACCAGCTAGAGACCATACAGACCTACCGG
TCTGTCAGTGAGATGGCTTCTAACAAGTTCAAAAGAATGCTGAACCGGGAGCTGACACAC
CTCTCAGAGATGAGCCGATCAGGGAACCAGGTGTCTGAATACATTTCAAATACTTTCTTA
GACAAGCAGAATGATGTGGAGATCCCATCTCCTACCCAGAAAGACAGGGAGAAAAAGAAA
AAGCAGCAGCTCATGACCCAGATAAGTGGAGTGAAGAAATTAATGCATAGTTCAAGCCTA
AACAATACAAGCATCTCACGCTTTGGAGTCAACACTGAAAATGAAGATCACCTGGCCAAG
GAGCTGGAAGACCTGAACAAATGGGGTCTTAACATCTTTAATGTGGCTGGATATTCTCAC
AATAGACCCCTAACATGCATCATGTATGCTATATTCCAGGAAAGAGACCTCCTAAAGACA
TTCAGAATCTCATCTGACACATTTATAACCTACATGATGACTTTAGAAGACCATTACCAT
TCTGACGTGGCATATCACAACAGCCTGCACGCTGCTGATGTAGCCCAGTCGACCCATGTT
CTCCTTTCTACACCAGCATTAGACGCTGTCTTCACAGATTTGGAGATCCTGGCTGCCATT
TTTGCAGCTGCCATCCATGACGTTGATCATCCTGGAGTCTCCAATCAGTTTCTCATCAAC
ACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTGGAAAATCATCACCTT
GCTGTGGGTTTCAAACTGCTGCAAGAAGAACACTGTGACATCTTCATGAATCTCACCAAG
AAGCAGCGTCAGACACTCAGGAAGATGGTTATTGACATGGTGTTAGCAACTGATATGTCT
AAACATATGAGCCTGCTGGCAGACCTGAAGACAATGGTAGAAACGAAGAAAGTTACAAGT
TCAGGCGTTCTTCTCCTAGACAACTATACCGATCGCATTCAGGTCCTTCGCAACATGGTA
CACTGTGCAGACCTGAGCAACCCCACCAAGTCCTTGGAATTGTATCGGCAATGGACAGAC
CGCATCATGGAGGAATTTTTCCAGCAGGGAGACAAAGAGCGGGAGAGGGGAATGGAAATT
AGCCCAATGTGTGATAAACACACAGCTTCTGTGGAAAAATCCCAGGTTGGTTTCATCGAC
TACATTGTCCATCCATTGTGGGAGACATGGGCAGATTTGGTACAGCCTGATGCTCAGGAC
ATTCTCGATACCTTAGAAGATAACAGGAACTGGTATCAGAGCATGATACCTCAAAGTCCC
TCACCACCACTGGACGAGCAGAACAGGGACTGCCAGGGTCTGATGGAGAAGTTTCAGTTT
GAACTGACTCTCGATGAGGAAGATTCTGAAGGACCTGAGAAGGAGGGAGAGGGACACAGC
TATTTCAGCAGCACAAAGACGCTTTGTGTGATTGATCCAGAAAACAGAGATTCCCTGGGA
GAGACTGACATAGACATTGCAACAGAAGACAAGTCCCCCGTGGATACATAA
Enzyme 14 GenBank Gene ID L20966 Link Image
Enzyme 14 GeneCard ID PDE4B Link Image
Enzyme 14 GenAtlas ID PDE4B Link Image
Enzyme 14 HGNC ID HGNC:8781 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Huston E, Lumb S, Russell A, Catterall C, Ross AH, Steele MR, Bolger GB, Perry MJ, Owens RJ, Houslay MD: Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem J. 1997 Dec 1;328 ( Pt 2):549-58. [PubMed Link Image]
  3. McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem. 1993 Mar 25;268(9):6470-6. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5884
Enzyme 15 Name cAMP-specific 3',5'-cyclic phosphodiesterase 7B
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name PDE7B
Enzyme 15 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 7B
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP
Enzyme 15 Number of Residues 450
Enzyme 15 Molecular Weight 51836
Enzyme 15 Theoretical pI 7.03
Enzyme 15 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain
Enzyme 15 Pathways
Enzyme 15 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 8439497 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9NP56 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PDE7B_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1353 bp
ATGTCTTGTTTAATGGTTGAGAGGTGTGGCGAAATCTTGTTTGAGAACCCCGATCAGAAT
GCCAAATGTGTTTGCATGCTGGGAGATATACGACTAAGGGGTCAGACGGGGGTTCGTGCT
GAACGCCGTGGCTCCTACCCATTCATTGACTTCCGCCTACTTAACAGTACAACATACTCA
GGGGAGATTGGCACCAAGAAAAAGGTGAAAAGACTATTAAGCTTTCAAAGATACTTCCAT
GCATCAAGGCTGCTTCGTGGAATTATACCACAAGCCCCTCTGCACCTGCTGGATGAAGAC
TACCTTGGACAAGCAAGGCATATGCTCTCCAAAGTGGGAATGTGGGATTTTGACATTTTC
TTGTTTGATCGCTTGACAAATGGAAACAGCCTGGTAACACTGTTGTGCCACCTCTTCAAT
ACCCATGGACTCATTCACCATTTCAAGTTAGATATGGTGACCTTACACCGATTTTTAGTC
ATGGTTCAAGAAGATTACCACAGCCAAAACCCGTATCACAATGCTGTTCACGCAGCCGAC
GTCACCCAGGCCATGCACTGCTACCTGAAAGAGCCAAAGCTTGCCAGCTTCCTCACGCCT
CTGGACATCATGCTTGGACTGCTGGCTGCAGCAGCACACGATGTGGACCACCCAGGGGTG
AACCAGCCATTTTTGATAAAAACTAACCACCATCTTGCAAACCTATATCAGAATATGTCT
GTGCTGGAGAATCATCACTGGCGATCTACAATTGGCATGCTTCGAGAATCAAGGCTTCTT
GCTCATTTGCCAAAGGAAATGACACAGGATATTGAACAGCAGCTGGGCTCCTTGATCTTG
GCAACAGACATCAACAGGCAGAATGAATTTTTGACCAGATTGAAAGCTCACCTCCACAAT
AAAGACTTAAGACTGGAGGATGCACAGGACAGGCACTTTATGCTTCAGATCGCCTTGAAG
TGTGCTGACATTTGCAATCCTTGTAGAATCTGGGAGATGAGCAAGCAGTGGAGTGAAAGG
GTCTGTGAAGAATTCTACAGGCAAGGTGAACTTGAACAGAAATTTGAACTGGAAATCAGT
CCTCTTTGTAATCAACAGAAAGATTCCATCCCTAGTATACAAATTGGTTTCATGAGCTAC
ATCGTGGAGCCGCTCTTCCGGGAATGGGCCCATTTCACGGGTAACAGCACCCTGTCGGAG
AACATGCTGGGCCACCTCGCACACAACAAGGCCCAGTGGAAGAGCCTGTTGCCCAGGCAG
CACAGAAGCAGGGGCAGCAGTGGCAGCGGGCCTGACCACGACCACGCAGGCCAAGGGACT
GAGAGCGAGGAGCAGGAAGGCGACAGCCCCTAG
Enzyme 15 GenBank Gene ID AB038040 Link Image
Enzyme 15 GeneCard ID PDE7B Link Image
Enzyme 15 GenAtlas ID PDE7B Link Image
Enzyme 15 HGNC ID HGNC:8792 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Sasaki T, Kotera J, Yuasa K, Omori K: Identification of human PDE7B, a cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 2000 May 19;271(3):575-83. [PubMed Link Image]
  2. Gardner C, Robas N, Cawkill D, Fidock M: Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 2000 May 27;272(1):186-92. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5888
Enzyme 16 Name High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name PDE9A
Enzyme 16 Protein Sequence >High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
Enzyme 16 Number of Residues 593
Enzyme 16 Molecular Weight 68493
Enzyme 16 Theoretical pI 6.10
Enzyme 16 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase has a high affinity for cGMP
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 3242777 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O76083 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PDE9A_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1782 bp
ATGGGATCCGGCTCCTCCAGCTACCGGCCCAAGGCCATCTACCTGGACATCGATGGACGC
ATTCAGAAGGTAATCTTCAGCAAGTACTGCAACTCCAGCGACATCATGGACCTGTTCTGC
ATCGCCACCGGCCTGCCTCGGAACACGACCATCTCCCTGCTGACCACCGACGACGCCATG
GTCTCCATCGACCCCACCATGCCCGCGAATTCAGAACGCACTCCGTACAAAGTGAGACCT
GTGGCCATCAAGCAACTCTCCGCTGGTGTCGAGGACAAGAGAACCACAAGCCGTGGCCAG
TCTGCTGAGAGACCACTGAGGGACAGACGGGTTGTGGGCCTGGAGCAGCCCCGGAGGGAA
GGAGCATTTGAAAGTGGACAGGTAGAGCCCAGGCCCAGAGAGCCCCAGGGCTGCTACCAG
GAAGGCCAGCGCATCCCTCCAGAGAGAGAAGAATTAATCCAGAGCGTGCTGGCGCAGGTT
GCAGAGCAGTTCTCAAGAGCATTCAAAATCAATGAACTGAAAGCTGAAGTTGCAAATCAC
TTGGCTGTCCTAGAGAAACGCGTGGAATTGGAAGGACTAAAAGTGGTGGAGATTGAGAAA
TGCAAGAGTGACATTAAGAAGATGAGGGAGGAGCTGGCGGCCAGAAGCAGCAGGACCAAC
TGCCCCTGTAAGTACAGTTTTTTGGATAACCACAAGAAGTTGACTCCTCGACGCGATGTT
CCCACTTACCCCAAGTACCTGCTCTCTCCAGAGACCATCGAGGCCCTGCGGAAGCCGACC
TTTGACGTCTGGCTTTGGGAGCCCAATGAGATGCTGAGCTGCCTGGAGCACATGTACCAC
GACCTCGGGCTGGTCAGGGACTTCAGCATCAACCCTGTCACCCTCAGGAGGTGGCTGTTC
TGTGTCCACGACAACTACAGAAACAACCCCTTCCACAACTTCCGGCACTGCTTCTGCGTG
GCCCAGATGATGTACAGCATGGTCTGGCTCTGCAGTCTCCAGGAGAAGTTCTCACAAACG
GATATCCTGATCCTAATGACAGCGGCCATCTGCCACGATCTGGACCATCCCGGCTACAAC
AACACGTACCAGATCAATGCCCGCACAGAGCTGGCGGTCCGCTACAATGACATCTCACCG
CTGGAGAACCACCACTGCGCCGTGGCCTTCCAGATCCTCGCCGAGCCTGAGTGCAACATC
TTCTCCAACATCCCACCTGATGGGTTCAAGCAGATCCGACAGGGAATGATCACATTAATC
TTGGCCACTGACATGGCAAGACATGCAGAAATTATGGATTCTTTCAAAGAGAAAATGGAG
AATTTTGACTACAGCAACGAGGAGCACATGACCCTGCTGAAGATGATTTTGATAAAATGC
TGTGATATCTCTAACGAGGTCCGTCCAATGGAAGTCGCAGAGCCTTGGGTGGACTGTTTA
TTAGAGGAATATTTTATGCAGAGCGACCGTGAGAAGTCAGAAGGCCTTCCTGTGGCACCG
TTCATGGACCGAGACAAAGTGACCAAGGCCACAGCCCAGATTGGGTTCATCAAGTTTGTC
CTGATCCCAATGTTTGAAACAGTGACCAAGCTCTTCCCCATGGTTGAGGAGATCATGCTG
CAGCCACTTTGGGAATCCCGAGATCGCTACGAGGAGCTGAAGCGGATAGATGACGCCATG
AAAGAGTTACAGAAGAAGACTGACAGCTTGACGTCTGGGGCCACCGAGAAGTCCAGAGAG
AGAAGCAGAGATGTGAAAAACAGTGAAGGAGACTGTGCCTGA
Enzyme 16 GenBank Gene ID AF048837 Link Image
Enzyme 16 GeneCard ID PDE9A Link Image
Enzyme 16 GenAtlas ID PDE9A Link Image
Enzyme 16 HGNC ID HGNC:8795 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 1998 Jun 19;273(25):15559-64. [PubMed Link Image]
  2. Guipponi M, Scott HS, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Chen H, Lalioti MD, Rossier C, Minoshima S, Shimizu N, Antonarakis SE: Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence. Hum Genet. 1998 Oct;103(4):386-92. [PubMed Link Image]
  3. Rentero C, Monfort A, Puigdomenech P: Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem Biophys Res Commun. 2003 Feb 14;301(3):686-92. [PubMed Link Image]
  4. Wang P, Wu P, Egan RW, Billah MM: Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants. Gene. 2003 Sep 18;314:15-27. [PubMed Link Image]
  5. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5889
Enzyme 17 Name cGMP-dependent 3',5'-cyclic phosphodiesterase
Enzyme 17 Synonyms
  1. Cyclic GMP-stimulated phosphodiesterase
  2. CGS-PDE
  3. cGSPDE
Enzyme 17 Gene Name PDE2A
Enzyme 17 Protein Sequence >cGMP-dependent 3',5'-cyclic phosphodiesterase
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
Enzyme 17 Number of Residues 941
Enzyme 17 Molecular Weight 105718
Enzyme 17 Theoretical pI 5.08
Enzyme 17 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP)
Enzyme 17 Pathways
Enzyme 17 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2108052 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O00408 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PDE2A_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2826 bp
ATGGGGCAGGCATGCGGCCACTCCATCCTCTGCAGGAGCCAGCAGTACCCGGCAGCGCGA
CCGGCTGAGCCGCGGGGCCAGCAGGTCTTCCTCAAGCCGGACGAGCCGCCGCCGCCGCCG
CAGCCATGCGCCGACAGCCTGCAGGACGCCTTGCTGAGTCTGGGCTCTGTCATCGACATT
TCAGGCCTGCAACGTGCTGTCAAGGAGGCCCTGTCAGCTGTGCTCCCCCGAGTGGAAACT
GTCTACACCTACCTACTGGATGGTGAGTCCCAGCTGGTGTGTGAGGACCCCCCACATGAG
CTGCCCCAGGAGGGGAAAGTCCGGGAGGCTATCATCTCCCAGAAGCGGCTGGGCTGCAAT
GGGCTGGGCTTCTCAGACCTGCCAGGGAAGCCCTTGGCCAGGCTGGTGGCTCCACTGGCT
CCTGATACCCAAGTGCTGGTCATGCCGCTAGCGGACAAGGAGGCTGGGGCCGTGGCAGCT
GTCATCTTGGTGCACTGTGGCCAGCTGAGTGATAATGAGGAATGGAGCCTGCAGGCGGTG
GAGAAGCATACCCTGGTCGCCCTGCGGAGGGTGCAGGTCCTGCAGCAGCGCGGGCCCAGG
GAGGCTCCCCGAGCCGTCCAGAACCCCCCGGAGGGGACGGCGGAAGACCAGAAGGGCGGG
GCGGCGTACACCGACCGCGACCGCAAGATCCTCCAACTGTGCGGGGAACTCTACGACCTG
GATGCCTCTTCCCTGCAGCTCAAAGTGCTCCAATACCTGCAGCAGGAGACCCGGGCATCC
CGCTGCTGCCTCCTGCTGGTGTCGGAGGACAATCTCCAGCTTTCTTGCAAGGTCATCGGA
GACAAAGTGCTCGGGGAAGAGGTCAGCTTTCCCTTGACAGGATGCCTGGGCCAGGTGGTG
GAAGACAAGAAGTCCATCCAGCTGAAGGACCTCACCTCCGAGGATGTACAACAGCTGCAG
AGCATGTTGGGCTGTGAGCTGCAGGCCATGCTCTGTGTCCCTGTCATCAGCCGGGCCACT
GACCAGGTGGTGGCCTTGGCCTGCGCCTTCAACAAGCTAGAAGGAGACTTGTTCACCGAC
GAGGACGAGCATGTGATCCAGCACTGCTTCCACTACACCAGCACCGTGCTCACCAGCACC
CTGGCCTTCCAGAAGGAACAGAAACTCAAGTGTGAGTGCCAGGCTCTTCTCCAAGTGGCA
AAGAACCTCTTCACCCACCTGGATGACGTCTCTGTCCTGCTCCAGGAGATCATCACGGAG
GCCAGAAACCTCAGCAACGCAGAGATCTGCTCTGTGTTCCTGCTGGATCAGAATGAGCTG
GTGGCCAAGGTGTTCGACGGGGGCGTGGTGGATGATGAGAGCTATGAGATCCGCATCCCG
GCCGATCAGGGCATCGCGGGACACGTGGCGACCACGGGCCAGATCCTGAACATCCCTGAC
GCATATGCCCATCCGCTTTTCTACCGCGGCGTGGACGACAGCACCGGCTTCCGCACGCGC
AACATCCTCTGCTTCCCCATCAAGAACGAGAACCAGGAGGTCATCGGTGTGGCCGAGCTG
GTGAACAAGATCAATGGGCCATGGTTCAGCAAGTTCGACGAGGACCTGGCGACGGCCTTC
TCCATCTACTGCGGCATCAGCATCGCCCATTCTCTCCTATACAAAAAAGTGAATGAGGCT
CAGTATCGCAGCCACCTGGCCAATGAGATGATGATGTACCACATGAAGGTCTCCGACGAT
GAGTATACCAAACTTCTCCATGATGGGATCCAGCCTGTGGCTGCCATTGACTCCAATTTT
GCAAGTTTCACCTATACCCCTCGTTCCCTGCCCGAGGATGACACGTCCATGGCCATCCTG
AGCATGCTGCAGGACATGAATTTCATCAACAACTACAAAATTGACTGCCCGACCCTGGCC
CGGTTCTGTTTGATGGTGAAGAAGGGCTACCGGGATCCCCCCTACCACAACTGGATGCAC
GCCTTTTCTGTCTCCCACTTCTGCTACCTGCTCTACAAGAACCTGGAGCTCACCAACTAC
CTCGAGGACATCGAGATCTTTGCCTTGTTTATTTCCTGCATGTGTCATGACCTGGACCAC
AGAGGCACAAACAACTCTTTCCAGGTGGCCTCGAAATCTGTGCTGGCTGCGCTCTACAGC
TCTGAGGGCTCCGTCATGGAGAGGCACCACTTTGCTCAGGCCATCGCCATCCTCAACACC
CACGGCTGCAACATCTTTGATCATTTCTCCCGGAAGGACTATCAGCGCATGCTGGATCTG
ATGCGGGACATCATCTTGGCCACAGACCTGGCCCACCATCTCCGCATCTTCAAGGACCTC
CAGAAGATGGCTGAGGTGGGCTACGACCGAAACAACAAGCAGCACCACAGACTTCTCCTC
TGCCTCCTCATGACCTCCTGTGACCTCTCTGACCAGACCAAGGGCTGGAAGACTACGAGA
AAGATCGCGGAGCTGATCTACAAAGAATTCTTCTCCCAGGGAGACCTGGAGAAGGCCATG
GGCAACAGGCCGATGGAGATGATGGACCGGGAGAAGGCCTATATCCCTGAGCTGCAAATC
AGCTTCATGGAGCACATTGCAATGCCCATCTACAAGCTGTTGCAGGACCTGTTCCCCAAA
GCGGCAGAGCTGTACGAGCGCGTGGCCTCCAACCGTGAGCACTGGACCAAGGTGTCCCAC
AAGTTCACCATCCGCGGCCTCCCAAGTAACAACTCGCTGGACTTCCTGGATGAGGAGTAC
GAGGTGCCTGATCTGGATGGCACTAGGGCCCCCATCAATGGCTGCTGCAGCCTTGATGCT
GAGTGA
Enzyme 17 GenBank Gene ID U67733 Link Image
Enzyme 17 GeneCard ID PDE2A Link Image
Enzyme 17 GenAtlas ID PDE2A Link Image
Enzyme 17 HGNC ID HGNC:8777 Link Image
Enzyme 17 Chromosome Location 11
Enzyme 17 Locus 11q13.4
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Rosman GJ, Martins TJ, Sonnenburg WK, Beavo JA, Ferguson K, Loughney K: Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1997 May 20;191(1):89-95. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5902
Enzyme 18 Name High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
Enzyme 18 Synonyms
  1. HSPDE8B
Enzyme 18 Gene Name PDE8B
Enzyme 18 Protein Sequence >High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASG
PPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEV
RIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEII
VIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFME
NSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFER
MMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVK
ITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDV
KSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLE
ILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITI
NDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAW
FQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHP
GRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAI
IDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCA
DVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYF
ITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
Enzyme 18 Number of Residues 885
Enzyme 18 Molecular Weight 98980
Enzyme 18 Theoretical pI 6.81
Enzyme 18 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • DNA binding
  • binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleic acid binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • signal transducer activity
  • two-component response regulator activity
Process
  • cell communication
  • cellular process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 18 General Function Signal transduction mechanisms
Enzyme 18 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase has high affinity for cAMP and may be involved in specific signaling in the thyroid gland
Enzyme 18 Pathways
Enzyme 18 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 32261241 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O95263 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PDE8B_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2517 bp
ATGGGCTGCGCCCCCAGCATCCATGTCTCGCAGAGCGGCGTGATCTACTGCCGGGACTCG
GACGAGTCCAGCTCGCCCCGCCAGACCACCAGCGTGTCGCAGGGCCCGGCGGCACCCCTG
CCCGGCCTCTTCGTCCAGACCGACGCCGCCGACGCCATCCCCCCGAGCCGCGCGTCGGGA
CCCCCCAGCGTAGCCCGCGTCCGCAGGGCCCGCACCGAGCTGGGCAGCGGTAGCAGCGCG
GGTTCCGCAGCCCCCGCCGCGACCACCAGCAGGGGCCGGAGGCGCCACTGCTGCAGCAGC
GCCGAGGCCGAGACTCAGACCTGCTACACCAGCGTGAAGCAGGTGTCTTCTGCGGAGGTG
CGCATCGGGCCCATGAGACTGACGCAGGACCCTATTCAGGTTTTGCTGATCTTTGCAAAG
GAAGATAGTCAGAGCGATGGCTTCTGGTGGGCCTGCGACAGAGCTGGTTATAGATGCAAT
ATTGCTCGGACTCCAGAGTCAGCCCTTGAATGCTTTCTTGATAAGCATCATGAAATTATT
GTAATTGATCATAGACAAACTCAGAACTTCGATGCAGAAGCAGTGTGCAGGTCGATCCGG
GCCACAAATCCCTCCGAGCACACGGTGATCCTCGCAGTGGTTTCGCGAGTATCGGATGAC
CATGAAGAGGCGTCAGTCCTTCCTCTTCTCCACGCAGGCTTCAACAGGAGATTTATGGAG
AATAGCAGCATAATTGCTTGCTATAATGAACTGATTCAAATAGAACATGGGGAAGTTCGC
TCCCAGTTCAAATTACGGGCCTGTAATTCAGTGTTTACAGCATTAGATCACTGTCATGAA
GCCATAGAAATAACAAGCGATGACCACGTGATTCAGGAGTGGCAGGGGGTTTACTATGCC
AGACGGAAATCCGGGGACAGCATCCAACAGCACGTGAAGATCACCCCAGTGATTGGCCAA
GGAGGGAAAATTAGGCATTTTGTCTCGCTCAAGAAACTGTGTTGTACCACTGACAATAAT
AAGCAGATTCACAAGATTCATCGTGATTCAGGAGATAATTCTCAGACAGAGCCTCATTCA
TTCAGATATAAGAACAGGAGGAAAGAGTCCATTGACGTGAAATCGATATCATCTCGAGGC
AGTGATGCACCAAGCCTGCAGAATCGTCGCTATCCGTCCATGGCGAGGATCCACTCCATG
ACCATCGAGGCTCCCATCACAAAGGTTATAAATATAATCAATGCAGCCCAAGAAAACAGC
CCAGTCACAGTAGCGGAAGCCTTGGACAGAGTTCTAGAGATTTTACGGACCACAGAACTG
TACTCCCCTCAGCTGGGTACCAAAGATGAAGATCCCCACACCAGTGATCTTGTTGGAGGC
CTGATGACTGACGGCTTGAGAAGACTGTCAGGAAACGAGTATGTGTTTACTAAGAATGTG
CACCAGAGTCACAGTCACCTTGCAATGCCAATAACCATCAATGATGTTCCCCCTTGTATC
TCTCAATTACTTGATAATGAGGAGAGTTGGGACTTCAACATCTTTGAATTGGAAGCCATT
ACGCATAAAAGGCCATTGGTTTATCTGGGCTTAAAGGTCTTCTCTCGGTTTGGAGTATGT
GAGTTTTTAAACTGTTCTGAAACCACTCTTCGGGCCTGGTTCCAAGTGATCGAAGCCAAC
TACCACTCTTCCAATGCCTACCACAACTCCACCCATGCTGCCGACGTCCTGCACGCCACC
GCTTTCTTTCTTGGAAAGGAAAGAGTAAAGGGAAGCCTCGATCAGTTGGATGAGGTGGCA
GCCCTCATTGCTGCCACAGTCCATGACGTGGATCACCCGGGAAGGACCAACTCTTTCCTC
TGCAATGCAGGCAGTGAGCTTGCTGTGCTCTACAATGACACTGCTGTTCTGGAGAGTCAC
CACACCGCCCTGGCCTTCCAGCTCACGGTCAAGGACACCAAATGCAACATTTTCAAGAAT
ATTGACAGGAACCATTATCGAACGCTGCGCCAGGCTATTATTGACATGGTTTTGGCAACA
GAGATGACAAAACACTTTGAACATGTGAATAAGTTTGTGAACAGCATCAACAAGCCAATG
GCAGCTGAGATTGAAGGCAGCGACTGTGAATGCAACCCTGCTGGGAAGAACTTCCCTGAA
AACCAAATCCTGATCAAACGCATGATGATTAAGTGTGCTGACGTGGCCAACCCATGCCGC
CCCTTGGACCTGTGCATTGAATGGGCTGGGAGGATCTCTGAGGAGTATTTTGCACAGACT
GATGAAGAGAAGAGACAGGGACTACCTGTGGTGATGCCAGTGTTTGACCGGAATACCTGT
AGCATCCCCAAGTCTCAGATCTCTTTCATTGACTACTTCATAACAGACATGTTTGATGCT
TGGGATGCCTTTGCACATCTACCAGCCCTGATGCAACATTTGGCTGACAACTACAAACAC
TGGAAGACACTAGATGACCTAAAGTGCAAAAGTTTGAGGCTTCCATCTGACAGCTAA
Enzyme 18 GenBank Gene ID AY129948 Link Image
Enzyme 18 GeneCard ID PDE8B Link Image
Enzyme 18 GenAtlas ID PDE8B Link Image
Enzyme 18 HGNC ID HGNC:8794 Link Image
Enzyme 18 Chromosome Location 5
Enzyme 18 Locus 5q14.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hayashi M, Shimada Y, Nishimura Y, Hama T, Tanaka T: Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem Biophys Res Commun. 2002 Oct 11;297(5):1253-8. [PubMed Link Image]
  2. Gamanuma M, Yuasa K, Sasaki T, Sakurai N, Kotera J, Omori K: Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell Signal. 2003 Jun;15(6):565-74. [PubMed Link Image]
  3. Hayashi M, Matsushima K, Ohashi H, Tsunoda H, Murase S, Kawarada Y, Tanaka T: Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1998 Sep 29;250(3):751-6. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5903
Enzyme 19 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4C
Enzyme 19 Synonyms
  1. DPDE1
  2. PDE21
Enzyme 19 Gene Name PDE4C
Enzyme 19 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4C
MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT
Enzyme 19 Number of Residues 712
Enzyme 19 Molecular Weight 79902
Enzyme 19 Theoretical pI 4.84
Enzyme 19 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 727223 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q08493 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PDE4C_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2139 bp
ATGGAGAACCTGGGGGTCGGCGAAGGGGCAGAGGCTTGCAGCAGGTTGAGTCGCTCTCGC
GGCCGCCACAGCATGACCAGAGCCCCGAAGCACCTGTGGCGGCAACCCCGGCGCCCCATC
CGCATCCAACAGCGCTTCTATTCGGATCCGGACAAGTCCGCGGGCTGCCGCGAGAGGGAC
CTGAGCCCGCGGCCGGAGCTCAGGAAGTCGCGGCTCTCCTGGCCCGTTTCCTCCTGCAGG
CGCTTTGACCTGGAAAATGGGCTCTCGTGTGGGAGGAGGGCCCTGGACCCTCAGTCCAGC
CCTGGCCTGGGCCGGATTATGCAGGCTCCAGTCCCGCACAGCCAGCGGCGCGAGTCCTTC
CTGTACCGCTCAGATAGCGACTATGAACTCTCGCCCAAGGCCATGTCTCGGAACTCCTCT
GTGGCCAGCGACCTACATGGAGAGGACATGATTGTGACGCCCTTTGCCCAGGTCCTGGCC
AGTCTGCGGACCGTTCGGAGCAACGTGGCGGCCCTTGCCCGCCAGCAATGCCTAGGAGCA
GCCAAGCAGGGACCCGTCGGAAACCCTTCATCCAGCAATCAGCTCCCTCCTGCAGAGGAC
ACGGGGCAGAAGCTGGCATTGGAGACGCTAGACGAGCTGGACTGGTGCCTGGATCAGTTG
GAGACGCTGCAGACCCGGCACTCGGTGGGGGAGATGGCCTCCAACAAGTTCAAGCGGATC
CTGAACCGGGAGTTGACCCACCTGTCCGAAACCAGCCGCTCCGGGAACCAGGTGTCCGAG
TACATCTCCCGGACCTTCCTGGACCAGCAGACCGAGGTGGAGCTGCCCAAGGTGACCGCT
GAGGAGGCCCCACAGCCCATGTCCCGGATCAGTGGCCTACATGGGCTCTGCCACAGTGCC
AGCCTCTCCTCAGCCACTGTCCCACGCTTTGGGGTCCAGACTGACCAGGAGGAGCAACTG
GCCAAGGAGCTAGAAGACACCAACAAGTGGGGACTTGATGTGTTCAAGGTGGCGGACGTA
AGTGGGAACCGGCCCCTCACAGCTATCATATTCAGCATTTTTCAGGAGCGGGACCTGCTG
AAGACATTCCAGATCCCAGCAGACACACTGGCCACCTACCTGCTGATGCTGGAGGGTCAC
TACCACGCCAATGTGGCCTACCACAACAGCCTACATGCCGCCGACGTGGCCCAGTCCACG
CATGTGCTGCTGGCTACGCCCGCCCTCGAGGCTGTGTTCACAGACTTGGAAATCCTGGCT
GCCCTCTTTGCAAGCGCCATCCACGACGTGGACCATCCTGGGGTCTCCAACCAGTTTCTG
ATTAACACCAACTCAGACGTGGCGCTTATGTACAACGACGCCTCGGTGCTGGAGAACCAT
CACCTGGCTGTGGGCTTCAAGCTGCTGCAGGCAGAGAACTGCGATATCTTCCAGAACCTC
AGCGCCAAGCAGCGACTGAGTCTGCGCAGGATGGTCATTGACATGGTGCTGGCCACAGAC
ATGTCCAAACACATGAACCTCCTGGCCGACCTCAAGACCATGGTGGAGACCAAGAAGGTG
ACAAGCCTCGGTGTCCTCCTCCTGGACAACTATTCCGACCGAATCCAGGTCTTGCAGAAC
CTGGTGCACTGTGCTGATCTGAGCAACCCCACCAAGCCGCTGCCCCTGTACCGCCAGTGG
ACGGACCGCATCATGGCCGAGTTCTTCCAGCAGGGAGACCGCGAGCGTGAGTCGGGCCTG
GACATCAGTCCCATGTGTGACAAGCATACGGCCTCAGTGGAGAAGTCCCAGGTGGGTTTC
ATTGACTACATTGCTCACCCACTGTGGGAGACTTGGGCTGACCTGGTCCACCCAGATGCA
CAGGACCTGCTGGACACGCTGGAGGACAATCGAGAGTGGTACCAGAGCAAGATCCCCCGA
AGTCCCTCAGACCTCACCAACCCCGAGCGGGACGGGCCTGACAGATTCCAGTTTGAACTG
ACTCTGGAGGAGGCAGAGGAAGAGGATGAGGAGGAAGAAGAGGAGGGGGAAGAGACAGCT
TTAGCCAAAGAGGCCTTGGAGTTGCCTGACACTGAACTCCTGTCCCCTGAAGCCGGCCCA
GACCCTGGGGACTTACCCCTCGACAACCAGAGGACTTAG
Enzyme 19 GenBank Gene ID Z46632 Link Image
Enzyme 19 GeneCard ID PDE4C Link Image
Enzyme 19 GenAtlas ID PDE4C Link Image
Enzyme 19 HGNC ID HGNC:8782 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Engels P, Sullivan M, Muller T, Lubbert H: Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C). FEBS Lett. 1995 Jan 30;358(3):305-10. [PubMed Link Image]
  2. Sullivan M, Olsen AS, Houslay MD: Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell Signal. 1999 Oct;11(10):735-42. [PubMed Link Image]
  3. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5908
Enzyme 20 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Enzyme 20 Synonyms
  1. DPDE3
  2. PDE43
Enzyme 20 Gene Name PDE4D
Enzyme 20 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4D
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
Enzyme 20 Number of Residues 809
Enzyme 20 Molecular Weight 91116
Enzyme 20 Theoretical pI 5.25
Enzyme 20 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 20 General Function Cell wall/membrane/envelope biogenesis
Enzyme 20 Specific Function Regulates the levels of cAMP in the cell
Enzyme 20 Pathways
Enzyme 20 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 347130 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q08499 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PDE4D_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2024 bp
ACATGATGCACGTGAATAATTTTCCCTTTAGAAGGCATTCCTGGATATGTTTTGATGTGG
ACAATGGCACATCTGCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGC
TAATTCTCCAAGCAAATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCG
ACAGCGATTATGACCTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATA
TACACGGAGATGACTTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTG
TACGAAACAACTTTGCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCAC
CCATGTGCAACCAACCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAAC
TGGCCAGCGAGACCCTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGA
CCAGGCACTCCGTCAGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGC
TCACCCATCTCTCTGAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACA
CATTCTTAGATAAGCAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGA
AAAAGAAAAGACCAATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTC
TGACTAATTCAAGTATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCA
AGGAACTAGAAGATGTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTG
GTAACCGGCCCTTGACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAA
CATTTAAAATTCCAGTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACC
ATGCTGATGTGGCCTATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATG
TGCTATTATCTACACCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAA
TTTTTGCCAGTGCAATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCA
ATACAAACTCTGAACTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATT
TGGCTGTGGGCTTTAAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCA
AAAAACAAAGACAATCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGT
CAAAACACATGAATCTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAA
GCTCTGGAGTTCTTCTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGG
TGCACTGTGCAGATCTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGG
ACCGGATAATGGAGGAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGA
TAAGCCCCATGTGTGACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAG
ACTATATTGTTCATCCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGG
ATATTTTGGACACTTTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCC
CCTCTCCTGCACCTGATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGT
TTGAACTAACTTTAGAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAG
TGGAAGAAGACACTAGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTA
CTGAAATTCCCCTTGATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCC
AGCCTGAAGCCTGTGTCATAGATGATCGTTCTCCTGACACGTAA
Enzyme 20 GenBank Gene ID L20970 Link Image
Enzyme 20 GeneCard ID PDE4D Link Image
Enzyme 20 GenAtlas ID PDE4D Link Image
Enzyme 20 HGNC ID HGNC:8783 Link Image
Enzyme 20 Chromosome Location 5
Enzyme 20 Locus 5q12
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed Link Image]
  3. Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed Link Image]
  4. Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed Link Image]
  5. Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed Link Image]
  6. Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed Link Image]
  7. Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5909
Enzyme 21 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 21 Synonyms
  1. GMP-PDE gamma
Enzyme 21 Gene Name PDE6G
Enzyme 21 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII
Enzyme 21 Number of Residues 87
Enzyme 21 Molecular Weight 9643
Enzyme 21 Theoretical pI 10.16
Enzyme 21 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • cGMP-specific phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 21 Pathways
Enzyme 21 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 189703 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P18545 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name CNRG_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >264 bp
ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG
Enzyme 21 GenBank Gene ID M36476 Link Image
Enzyme 21 GeneCard ID PDE6G Link Image
Enzyme 21 GenAtlas ID PDE6G Link Image
Enzyme 21 HGNC ID HGNC:8789 Link Image
Enzyme 21 Chromosome Location 17
Enzyme 21 Locus 17q25
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Tuteja N, Danciger M, Klisak I, Tuteja R, Inana G, Mohandas T, Sparkes RS, Farber DB: Isolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina. Gene. 1990 Apr 16;88(2):227-32. [PubMed Link Image]
  2. Piriev NI, Purishko VA, Khramtsov NV, Lipkin VM: [The organization of the gamma-subunit gene of human photoreceptor cyclic GMP phosphodiesterase] Dokl Akad Nauk SSSR. 1990;315(1):229-31. [PubMed Link Image]
  3. Hahn LB, Berson EL, Dryja TP: Evaluation of the gene encoding the gamma subunit of rod phosphodiesterase in retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1994 Mar;35(3):1077-82. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5913
Enzyme 22 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
Enzyme 22 Synonyms
  1. GMP-PDE delta
  2. p17 protein
Enzyme 22 Gene Name PDE6D
Enzyme 22 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV
Enzyme 22 Number of Residues 150
Enzyme 22 Molecular Weight 17420
Enzyme 22 Theoretical pI 5.35
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate
Enzyme 22 Pathways
Enzyme 22 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 2896020 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID O43924 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PDE6D_HUMAN Link Image
Enzyme 22 PDB ID 1KSG Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >453 bp
ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA
Enzyme 22 GenBank Gene ID AF045999 Link Image
Enzyme 22 GeneCard ID PDE6D Link Image
Enzyme 22 GenAtlas ID PDE6D Link Image
Enzyme 22 HGNC ID HGNC:8788 Link Image
Enzyme 22 Chromosome Location 2
Enzyme 22 Locus 2q35-q36
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Li N, Florio SK, Pettenati MJ, Rao PN, Beavo JA, Baehr W: Characterization of human and mouse rod cGMP phosphodiesterase delta subunit (PDE6D) and chromosomal localization of the human gene. Genomics. 1998 Apr 1;49(1):76-82. [PubMed Link Image]
  2. Ershova G, Derre J, Chetelin S, Nancy V, Berger R, Kaplan J, Munnich A, de Gunzburg J: cDNA sequence, genomic organization and mapping of PDE6D, the human gene encoding the delta subunit of the cGMP phosphodiesterase of retinal rod cells to chromosome 2q36. Cytogenet Cell Genet. 1997;79(1-2):139-41. [PubMed Link Image]
  3. Lorenz B, Migliaccio C, Lichtner P, Meyer C, Strom TM, D'Urso M, Becker J, Ciccodicola A, Meitinger T: Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit gene (PDED) in man and mouse. Eur J Hum Genet. 1998 May-Jun;6(3):283-90. [PubMed Link Image]
  4. Linari M, Hanzal-Bayer M, Becker J: The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [PubMed Link Image]
  5. Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC: The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 2002 May 1;21(9):2095-106. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5922
Enzyme 23 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4A
Enzyme 23 Synonyms
  1. DPDE2
  2. PDE46
Enzyme 23 Gene Name PDE4A
Enzyme 23 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4A
MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQ
PHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGR
SPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTP
FAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEI
PSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTD
QEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYML
TLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDM
VLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLE
LYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADL
VHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLT
QQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLP
STAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT
Enzyme 23 Number of Residues 886
Enzyme 23 Molecular Weight 98144
Enzyme 23 Theoretical pI 4.87
Enzyme 23 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate
Enzyme 23 Pathways
Enzyme 23 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 347120 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P27815 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PDE4A_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2661 bp
ATGGAACCCCCGACCGTCCCCTCGGAAAGGAGCCTGTCTCTGTCACTGCCCGGGCCCCGG
GAGGGCCAGGCCACCCTGAAGCCTCCCCCGCAGCACCTGTGGCGGCAGCCTCGGACCCCC
ATCCGTATCCAGCAGCGCGGCTACTCCGACAGCGCGGAGCGCGCCGAGCGGGAGCGGCAG
CCGCACCGGCCCATAGAGCGCGCCGATGCCATGGACACCAGCGACCGGCCCGGCCTGCGC
ACGACCCGCATGTCCTGGCCCTCGTCCTTCCATGGCACTGGCACCGGCAGCGGCGGCGCG
GGCGGAGGCAGCAGCAGGCGCTTCGAGGCAGAGAATGGGCCGACACCATCTCCTGGCCGC
AGCCCCCTGGACTCGCAGGCGAGCCCAGGACTCGTGCTGCACGCCGGGGCGGCCACCAGC
CAGCGCCGGGAGTCCTTCCTGTACCGCTCAGACAGCGACTATGACATGTCACCCAAGACC
ATGTCCCGGAACTCATCGGTCACCAGCGAGGCGCACGCTGAAGACCTCATCGTAACACCA
TTTGCTCAGGTGCTGGCCAGCCTCCGGAGCGTCCGTAGCAACTTCTCACTCCTGACCAAT
GTGCCCGTTCCCAGTAACAAGCGGTCCCCGCTGGGCGGCCCCACCCCTGTCTGCAAGGCC
ACGCTGTCAGAAGAAACGTGTCAGCAGTTGGCCCGGGAGACTCTGGAGGAGCTGGACTGG
TGTCTGGAGCAGCTGGAGACCATGCAGACCTATCGCTCTGTCAGCGAGATGGCCTCGCAC
AAGTTCAAAAGGATGTTGAACCGTGAGCTCACACACCTGTCAGAAATGAGCAGGTCCGGA
AACCAGGTCTCAGAGTACATTTCCACAACATTCCTGGACAAACAGAATGAAGTGGAGATC
CCATCACCCACGATGAAGGAACGAGAAAAACAGCAAGCGCCGCGACCAAGACCCTCCCAG
CCGCCCCCGCCCCCTGTACCACACTTACAGCCCATGTCCCAAATCACAGGGTTGAAAAAG
TTGATGCATAGTAACAGCCTGAACAACTCTAACATTCCCCGATTTGGGGTGAAGACCGAT
CAAGAAGAGCTCCTGGCCCAAGAACTGGAGAACCTGAACAAGTGGGGCCTGAACATCTTT
TGCGTGTCGGATTACGCTGGAGGCCGCTCACTCACCTGCATCATGTACATGATATTCCAG
GAGCGGGACCTGCTGAAGAAATTCCGCATCCCGGTGGACACGATGGTGACATACATGCTG
ACGCTGGAGGATCACTACCACGCTGACGTGGCCTACCATAACAGCCTGCACGCAGCTGAC
GTGCTGCAGTCCACCCACGTACTGCTGGCCACGCCTGCACTAGATGCAGTGTTCACGGAC
CTGGAGATTCTCGCCGCCCTCTTCGCGGCTGCCATCCACGATGTGGATCACCCTGGGGTC
TCCAACCAGTTCCTCATCAACACCAATTCGGAGCTGGCGCTCATGTACAACGATGAGTCG
GTGCTCGAGAATCACCACCTGGCCGTGGGCTTCAAGCTGCTGCAGGAGGACAACTGCGAC
ATCTTCCAGAACCTCAGCAAGCGCCAGCGGCAGAGCCTACGCAAGATGGTCATCGACATG
GTGCTGGCCACGGACATGTCCAAGCACATGACCCTCCTGGCTGACCTGAAGACCATGGTG
GAGACCAAGAAAGTGACCAGCTCAGGGGTCCTCCTGCTAGATAACTACTCCGACCGCATC
CAGGTCCTCCGGAACATGGTGCACTGTGCCGACCTCAGCAACCCCACCAAGCCGCTGGAG
CTGTACCGCCAGTGGACAGACCGCATCATGGCCGAGTTCTTCCAGCAGGGTGACCGAGAG
CGCGAGCGTGGCATGGAAATCAGCCCCATGTGTGACAAGCACACTGCCTCCGTGGAGAAG
TCTCAGGTGGGTTTTATTGACTACATTGTGCACCCATTGTGGGAGACCTGGGCGGACCTT
GTCCACCCAGATGCCCAGGAGATCTTGGACACTTTGGAGGACAACCGGGACTGGTACTAC
AGCGCCATCCGGCAGAGCCCATCTCCGCCACCCGAGGAGGAGTCAAGGGGGCCAGGCCAC
CCACCCCTGCCTGACAAGTTCCAGTTTGAGCTGACGCTGGAGGAGGAAGAGGAGGAAGAA
ATATCAATGGCCCAGATACCGTGCACAGCCCAAGAGGCATTGACTGCGCAGGGATTGTCA
GGAGTCGAGGAAGCTCTGGATGCAACCATAGCCTGGGAGGCATCCCCGGCCCAGGAGTCG
TTGGAAGTTATGGCACAGGAAGCATCCCTGGAGGCCGAGCTGGAGGCAGTGTATTTGACA
CAGCAGGCACAGTCCACAGGCAGTGCACCTGTGGCTCCGGATGAGTTCTCGTCCCGGGAG
GAATTCGTGGTTGCTGTAAGCCACAGCAGCCCCTCTGCCCTGGCTCTTCAAAGCCCCCTT
CTCCCTGCTTGGAGGACCCTGTCTGTTTCAGAGCATGCCCCGGGCCTCCCGGGCCTCCCC
TCCACGGCGGCCGAGGTGGAGGCCCAACGAGAGCACCAGGCTGCCAAGAGGGCTTGCAGT
GCCTGCGCAGGGACATTTGGGGAGGACACATCCGCACTCCCAGCTCCTGGTGGCGGGGGG
TCAGGTGGAGACCCTACCTGA
Enzyme 23 GenBank Gene ID L20965 Link Image
Enzyme 23 GeneCard ID PDE4A Link Image
Enzyme 23 GenAtlas ID PDE4A Link Image
Enzyme 23 HGNC ID HGNC:8780 Link Image
Enzyme 23 Chromosome Location 19
Enzyme 23 Locus 19p13.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Sullivan M, Rena G, Begg F, Gordon L, Olsen AS, Houslay MD: Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem J. 1998 Aug 1;333 ( Pt 3):693-703. [PubMed Link Image]
  3. Livi GP, Kmetz P, McHale MM, Cieslinski LB, Sathe GM, Taylor DP, Davis RL, Torphy TJ, Balcarek JM: Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase. Mol Cell Biol. 1990 Jun;10(6):2678-86. [PubMed Link Image]
  4. Horton YM, Sullivan M, Houslay MD: Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19 [corrected] Biochem J. 1995 Jun 1;308 ( Pt 2):683-91. [PubMed Link Image]
  5. Sullivan M, Egerton M, Shakur Y, Marquardsen A, Houslay MD: Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1). Cell Signal. 1994 Sep;6(7):793-812. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5927
Enzyme 24 Name cGMP-specific 3',5'-cyclic phosphodiesterase
Enzyme 24 Synonyms
  1. CGB-PDE
  2. cGMP-binding cGMP-specific phosphodiesterase
Enzyme 24 Gene Name PDE5A
Enzyme 24 Protein Sequence >cGMP-specific 3',5'-cyclic phosphodiesterase
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
Enzyme 24 Number of Residues 875
Enzyme 24 Molecular Weight 100014
Enzyme 24 Theoretical pI 6.00
Enzyme 24 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 3420185 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O76074 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PDE5A_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2628 bp
ATGGAGCGGGCCGGCCCCAGCTTCGGGCAGCAGCGACAGCAGCAGCAGCCCCAGCAGCAG
AAGCAGCAGCAGAGGGATCAGGACTCGGTCGAAGCATGGCTGGACGATCACTGGGACTTT
ACCTTCTCATACTTTGTTAGAAAAGCCACCAGAGAAATGGTCAATGCATGGTTTGCTGAG
AGAGTTCACACCATCCCTGTGTGCAAGGAAGGTATCAGAGGCCACACCGAATCTTGCTCT
TGTCCCTTGCAGCAGAGTCCTCGTGCAGATAACAGTGTCCCTGGAACACCAACCAGGAAA
ATCTCTGCCTCTGAATTTGACCGGCCTCTTAGACCCATTGTTGTCAAGGATTCTGAGGGA
ACTGTGAGCTTCCTCTCTGACTCAGAAAAGAAGGAACAGATGCCTCTAACCCCTCCAAGG
TTTGATCATGATGAAGGGGACCAGTGCTCAAGACTCTTGGAATTAGTGAAGGATATTTCT
AGTCATTTGGATGTCACAGCCTTATGTCACAAAATTTTCTTGCATATCCATGGACTGATA
TCTGCTGACCGCTATTCCCTGTTCCTTGTCTGTGAAGACAGCTCCAATGACAAGTTTCTT
ATCAGCCGCCTCTTTGATGTTGCTGAAGGTTCAACACTGGAAGAAGTTTCAAATAACTGT
ATCCGCTTAGAATGGAACAAAGGCATTGTGGGACATGTGGCAGCGCTTGGTGAGCCCTTG
AACATCAAAGATGCATATGAGGATCCTCGGTTCAATGCAGAAGTTGACCAAATTACAGGC
TACAAGACACAAAGCATTCTTTGTATGCCAATTAAGAATCATAGGGAAGAGGTTGTTGGT
GTAGCCCAGGCCATCAACAAGAAATCAGGAAACGGTGGGACATTTACTGAAAAAGATGAA
AAGGACTTTGCTGCTTATTTGGCATTTTGTGGTATTGTTCTTCATAATGCTCAGCTCTAT
GAGACTTCACTGCTGGAGAACAAGAGAAATCAGGTGCTGCTTGACCTTGCTAGTTTAATT
TTTGAAGAACAACAATCATTAGAAGTAATTTTGAAGAAAATAGCTGCCACTATTATCTCT
TTCATGCAAGTGCAGAAATGCACCATTTTCATAGTGGATGAAGATTGCTCCGATTCTTTT
TCTAGTGTGTTTCACATGGAGTGTGAGGAATTAGAAAAATCATCTGATACATTAACAAGG
GAACATGATGCAAACAAAATCAATTACATGTATGCTCAGTATGTCAAAAATACTATGGAA
CCACTTAATATCCCAGATGTCAGTAAGGATAAAAGATTTCCCTGGACAACTGAAAATACA
GGAAATGTAAACCAGCAGTGCATTAGAAGTTTGCTTTGTACACCTATAAAAAATGGAAAG
AAGAATAAAGTTATAGGGGTTTGCCAACTTGTTAATAAGATGGAGGAGAATACTGGCAAG
GTTAAGCCTTTCAACCGAAATGACGAACAGTTTCTGGAAGCTTTTGTCATCTTTTGTGGC
TTGGGGATCCAGAACACGCAGATGTATGAAGCAGTGGAGAGAGCCATGGCCAAGCAAATG
GTCACATTGGAGGTTCTGTCGTATCATGCTTCAGCAGCAGAGGAAGAAACAAGAGAGCTA
CAGTCGTTAGCGGCTGCTGTGGTGCCATCTGCCCAGACCCTTAAAATTACTGACTTTAGC
TTCAGTGACTTTGAGCTGTCTGATCTGGAAACAGCACTGTGTACAATTCGGATGTTTACT
GACCTCAACCTTGTGCAGAACTTCCAGATGAAACATGAGGTTCTTTGCAGATGGATTTTA
AGTGTTAAGAAGAATTATCGGAAGAATGTTGCCTATCATAATTGGAGACATGCCTTTAAT
ACAGCTCAGTGCATGTTTGCTGCTCTAAAAGCAGGCAAAATTCAGAACAAGCTGACTGAC
CTGGAGATACTTGCATTGCTGATTGCTGCACTAAGCCACGATTTGGATCACCGTGGTGTG
AATAACTCTTACATACAGCGAAGTGAACATCCACTTGCCCAGCTTTACTGCCATTCAATC
ATGGAACACCATCATTTTGACCAGTGCCTGATGATTCTTAATAGTCCAGGCAATCAGATT
CTCAGTGGCCTCTCCATTGAAGAATATAAGACCACGTTGAAAATAATCAAGCAAGCTATT
TTAGCTACAGACCTAGCACTGTACATTAAGAGGCGAGGAGAATTTTTTGAACTTATAAGA
AAAAATCAATTCAATTTGGAAGATCCTCATCAAAAGGAGTTGTTTTTGGCAATGCTGATG
ACAGCTTGTGATCTTTCTGCAATTACAAAACCCTGGCCTATTCAACAACGGATAGCAGAA
CTTGTAGCAACTGAATTTTTTGATCAAGGAGACAGAGAGAGAAAAGAACTCAACATAGAA
CCCACTGATCTAATGAACAGGGAGAAGAAAAACAAAATCCCAAGTATGCAAGTTGGGTTC
ATAGATGCCATCTGCTTGCAACTGTATGAGGCCCTGACCCACGTGTCAGAGGACTGTTTC
CCTTTGCTAGATGGCTGCAGAAAGAACAGGCAGAAATGGCAGGCCCTTGCAGAACAGCAG
GAGAAGATGCTGATTAATGGGGAAAGCGGCCAGGCCAAGCGGAACTGA
Enzyme 24 GenBank Gene ID AF043731 Link Image
Enzyme 24 GeneCard ID PDE5A Link Image
Enzyme 24 GenAtlas ID PDE5A Link Image
Enzyme 24 HGNC ID HGNC:8784 Link Image
Enzyme 24 Chromosome Location 4
Enzyme 24 Locus 4q25-q27
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, Beavo JA, Ferguson K: Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1998 Aug 17;216(1):139-47. [PubMed Link Image]
  2. Yanaka N, Kotera J, Ohtsuka A, Akatsuka H, Imai Y, Michibata H, Fujishige K, Kawai E, Takebayashi S, Okumura K, Omori K: Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur J Biochem. 1998 Jul 15;255(2):391-9. [PubMed Link Image]
  3. Stacey P, Rulten S, Dapling A, Phillips SC: Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem Biophys Res Commun. 1998 Jun 18;247(2):249-54. [PubMed Link Image]
  4. Zhou L, Thompson WJ, Potter DE: Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1745-52. [PubMed Link Image]
  5. Sung BJ, Hwang KY, Jeon YH, Lee JI, Heo YS, Kim JH, Moon J, Yoon JM, Hyun YL, Kim E, Eum SJ, Park SY, Lee JO, Lee TG, Ro S, Cho JM: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 2003 Sep 4;425(6953):98-102. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5977
Enzyme 25 Name Adenylate cyclase type 7
Enzyme 25 Synonyms
  1. Adenylate cyclase type VII
  2. ATP pyrophosphate-lyase 7
  3. Adenylyl cyclase 7
Enzyme 25 Gene Name ADCY7
Enzyme 25 Protein Sequence >Adenylate cyclase type 7
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
Enzyme 25 Number of Residues 1080
Enzyme 25 Molecular Weight 120310
Enzyme 25 Theoretical pI 8.16
Enzyme 25 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 25 General Function Signal transduction mechanisms
Enzyme 25 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 34-54 63-83 95-117 122-142 147-167 176-196 595-615 620-640 669-688 718-737 746-773 794-814
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 40788941 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P51828 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name ADCY7_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >3267 bp
CGACACGCGTGCCAAGGGTGGAGGATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGC
GAGGAGGGCCCTGACCAAGATGCGCTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGG
CCGCTGCTGCTCACGCTCCTGCTGGTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATT
GCCTTCAGCCAGGGGGACCCCTCCAGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTG
CTGGCGGTGTTTGCGGCCCTCTCTGTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGG
CTCAGGGCCTTGGCGCTGCTCACCTGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTG
TTCGACGCATGGACAAAGGCGGCCTGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATT
GTCTTCGTGGTGTACACACTACTGCCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCC
GTCTCCACTGCCTCCCACCTCCTGGTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCC
AGTGTCCGGGTGGGGCTGCAGCTGCTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTG
ACAGGCGCCTTCCACAAGCACCAAATGCAGGATGCGTCCCGGGACCTCTTCACCTACACT
GTGAAGTGCATCCAGATCCGCCGGAAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTG
CTGCTGTCAGTGCTTCCGGCCCACATCTCCATGGGCATGAAGCTGGCCATCATCGAACGG
CTCAAGGAGCATGGTGACCGTCGCTGCATGCCTGACAACAACTTCCACAGCCTCTACGTC
AAGAGGCACCAGAATGTCAGCATCCTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCC
AGCGACTGTTCTCCCAAGGAGCTGGTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGAC
CAGATCGCCAAGGCCAACGAGTGCATGCGAATCAAGATCCTCGGCGACTGCTACTACTGT
GTATCGGGCCTGCCCGTGTCGCTGCCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTG
GACATGTGCCAGGCCATCAAGCAGGTGCGGGAGGCCACGGGCGTGGACATCAACATGCGT
GTGGGCATACACTCGGGGAATGTGCTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTAT
GACGTGTGGTCCCACGACGTGTCCCTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGC
CGGGTGCACATCACGGAGGCCACGCTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGAT
GGGCACGGGCAGCAGCGGGACCCCTACCTCAAGGAGATGAACATCCGCACCTACCTGGTC
ATCGACCCCCGGAGCCAGCAGCCACCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGG
GACGCGGCCCTGAAGATGCGGGCGTCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGG
GCGGCACGGCCCTTTGCACATCTCAACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCAC
GTCCCCAACGGGCGGAGGCCTAAGAGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGA
AGCATGTCCCCCAAGGGGCGGTCGGAGGATGACTCGTACGATGACGAGATGCTGTCAGCC
ATTGAGGGGCTCAGCTCCACGAGGCCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTT
GGGTCCATCTTCCTGGAGAAGGGCTTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGG
GCCCGCCACGACTTTGCCTGCGCCAGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTC
CTGCTCATGCCCAGGACGGCGGCACTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTG
GGGCTGGTGCTGGGCCTGTGCTTTGCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGG
ACGCTCTGCACTATCTCTGAGAGGGTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCC
GTCCTGACCATCGGCAGCCTGCTCACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTC
CAAGTTCCAGAGCTGCCTGTTGGCAATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACA
AGAGCCCTGTGTGAGCCCCTCCCGTACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCC
TGCTCGGTCTTCCTGAGGATGAGCCTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTG
GTGGCCTACCTGGTGCTCTTCAACCTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAA
GGCCTGGGCAACCTCACCAAGCCCAACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGG
AAGGACCTGAAGACCATGACCAATTTCTACCTGGTCCTGTTCTACATCACCCTGCTTACA
CTCTCCAGACAGATTGACTATTACTGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAG
AAGGAGCACGAGGAGTTTGAGACCATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTC
CTGCCAGCCCACGTGGCTGCCCACTTTATCGGTGACAAGTTAAACGAGGACTGGTACCAT
CAGTCCTATGACTGCGTCTGTGTCATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTAC
ACAGAGTGCGATGTCAACAAAGAAGGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATT
GCCGACTTCGACGAGCTCCTACTGAAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACC
ATCGGCAGCACGTACATGGCAGCTGCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAG
GAGCTGGAGCGGCAGCATGCCCACATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATG
AGTAAGCTGGACGGCATCAACAGGCACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATA
AACCATGGGCCTGTGATTGCTGGAGTGATTGGGGCCCGAAAACCTCAGTATGACATCTGG
GGAAACACTGTCAATGTGGCCAGCCGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAG
GTTACCGAGGAGACCTGCACCATCCTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGC
CTGATCAACGTCAAAGGCAAAGGCGAGCTGAGGACTTACTTTGTCTGTACGGACACTGCC
AAGTTTCAGGGGCTGGGGCTGAACTGA
Enzyme 25 GenBank Gene ID D25538 Link Image
Enzyme 25 GeneCard ID ADCY7 Link Image
Enzyme 25 GenAtlas ID ADCY7 Link Image
Enzyme 25 HGNC ID HGNC:238 Link Image
Enzyme 25 Chromosome Location 16
Enzyme 25 Locus 16q12-q13
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5979
Enzyme 26 Name Adenylate cyclase type 6
Enzyme 26 Synonyms
  1. Adenylate cyclase type VI
  2. ATP pyrophosphate-lyase 6
  3. Adenylyl cyclase 6
  4. Ca(2+-inhibitable adenylyl cyclase
Enzyme 26 Gene Name ADCY6
Enzyme 26 Protein Sequence >Adenylate cyclase type 6
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
Enzyme 26 Number of Residues 1168
Enzyme 26 Molecular Weight 130617
Enzyme 26 Theoretical pI 8.27
Enzyme 26 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 26 General Function Signal transduction mechanisms
Enzyme 26 Specific Function Membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 152-168 181-197 214-230 239-255 259-275 289-305 674-691 702-718 743-759 820-836 839-855 897-913
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 9049783 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID O43306 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ADCY6_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3507 bp
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
Enzyme 26 GenBank Gene ID AF250226 Link Image
Enzyme 26 GeneCard ID ADCY6 Link Image
Enzyme 26 GenAtlas ID ADCY6 Link Image
Enzyme 26 HGNC ID HGNC:237 Link Image
Enzyme 26 Chromosome Location 12
Enzyme 26 Locus 12q12-q13
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5980
Enzyme 27 Name Adenylate cyclase type 5
Enzyme 27 Synonyms
  1. Adenylate cyclase type V
  2. ATP pyrophosphate-lyase 5
  3. Adenylyl cyclase 5
Enzyme 27 Gene Name ADCY5
Enzyme 27 Protein Sequence >Adenylate cyclase type 5
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
Enzyme 27 Number of Residues 1261
Enzyme 27 Molecular Weight 138909
Enzyme 27 Theoretical pI 7.25
Enzyme 27 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 27 General Function Signal transduction mechanisms
Enzyme 27 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 196-216 242-262 268-288 299-319 325-345 349-369 374-394 770-790 792-812 836-856 910-930 935-955 984-1004
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID O95622 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name ADCY5_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AC025571 Link Image
Enzyme 27 GeneCard ID ADCY5 Link Image
Enzyme 27 GenAtlas ID ADCY5 Link Image
Enzyme 27 HGNC ID HGNC:236 Link Image
Enzyme 27 Chromosome Location 3
Enzyme 27 Locus 3q13.2-q21
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  2. Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5981
Enzyme 28 Name Adenylate cyclase type 8
Enzyme 28 Synonyms
  1. Adenylate cyclase type VIII
  2. ATP pyrophosphate-lyase 8
  3. Adenylyl cyclase 8
  4. Ca(2+/calmodulin- activated adenylyl cyclase
Enzyme 28 Gene Name ADCY8
Enzyme 28 Protein Sequence >Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
Enzyme 28 Number of Residues 1251
Enzyme 28 Molecular Weight 140124
Enzyme 28 Theoretical pI 6.99
Enzyme 28 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 28 General Function Signal transduction mechanisms
Enzyme 28 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase. May be involved in learning, in memory and in drug dependence
Enzyme 28 Pathways
Enzyme 28 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 183-203 212-232 247-267 274-294 296-316 321-341 716-736 738-758 787-807 831-851 861-881 894-914
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 516263 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P40145 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name ADCY8_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >3756 bp
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
Enzyme 28 GenBank Gene ID Z35309 Link Image
Enzyme 28 GeneCard ID ADCY8 Link Image
Enzyme 28 GenAtlas ID ADCY8 Link Image
Enzyme 28 HGNC ID HGNC:239 Link Image
Enzyme 28 Chromosome Location 8
Enzyme 28 Locus 8q24
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed Link Image]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5982
Enzyme 29 Name Adenylate cyclase type 9
Enzyme 29 Synonyms
  1. Adenylate cyclase type IX
  2. ATP pyrophosphate-lyase 9
  3. Adenylyl cyclase 9
Enzyme 29 Gene Name ADCY9
Enzyme 29 Protein Sequence >Adenylate cyclase type 9
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDS
GGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYAL
FYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALT
LLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHL
PLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFV
MSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKR
HATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLN
DLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEK
KEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLD
DRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVS
SGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKN
STKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNI
REKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTF
ASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIR
MVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGS
AALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSER
NPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTK
IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKE
CYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFE
FAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTT
GVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISP
DIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEE
RGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
Enzyme 29 Number of Residues 1353
Enzyme 29 Molecular Weight 150702
Enzyme 29 Theoretical pI 7.35
Enzyme 29 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
Enzyme 29 General Function Signal transduction mechanisms
Enzyme 29 Specific Function May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin
Enzyme 29 Pathways
Enzyme 29 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 118-138 142-162 172-192 216-235 242-259 281-301 787-807 819-839 868-888 892-912 921-941 976-996
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 3138932 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID O60503 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name ADCY9_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >3885 bp
ATGGCTTCCCCGCCCCACCAGCAGCTGCTGCATCACCACAGCACCGAGGTGAGCTGCGAC
TCCAGCGGGGACAGCAACAGCGTGCGCGTCAAGATCAACCCCAAGCAGCTGTCCTCCAAC
AGCCACCCCAAGCACTGCAAATACAGCATCTCCTCTAGCTGCAGCAGCTCTGGGGACTCC
GGGGGCGTCCCCCGGCGAGTGGGCGGCGGAGGCCGGCTGCGCAGGCAGAAGAAGCTGCCC
CAGCTGTTCGAGAGGGCCTCCAGCCGCTGGTGGGACCCCAAGTTCGACTCGGTGAACCTG
GAGGAGGCCTGCCTGGAGCGCTGCTTCCCGCAGACCCAGCGCCGGTTCCGGTATGCGCTC
TTCTACATCGGCTTCGCCTGCCTTCTGTGGAGCATCTATTTTGCGGTCCACATGAGATCC
AGACTGATCGTCATGGTCGCCCCCGCGCTGTGCTTCCTCCTGGTGTGTGTGGGCTTCTTT
CTGTTTACCTTCACCAAGCTGTACGCCCGGCATTACGCGTGGACCTCGCTGGCTCTCACC
CTGCTGGTGTTCGCCCTGACCCTGGCTGCGCAGTTCCAGGTCTTGACGCCTGTCTCAGGA
CGCGGCGACAGCTCCAACCTTACGGCCACAGCCCGGCCCACAGATACTTGCTTATCTCAA
GTGGGGAGCTTCTCCATGTGCATCGAAGTGCTCTTTTTGCTCTATACCGTCATGCACTTA
CCTTTGTACCTGAGTTTGTGTCTGGGGGTGGCCTACTCTGTCCTTTTCGAGACCTTTGGC
TACCATTTCCGGGATGAAGCCTGCTTCCCCTCGCCCGGAGCCGGGGCCCTGCACTGGGAG
CTGCTGAGCAGGGGGCTGCTCCACGGCTGCATCCACGCCATCGGGGTCCACCTGTTCGTC
ATGTCCCAGGTGAGGTCCAGGAGCACCTTCCTCAAGGTGGGGCAATCCATTATGCACGGG
AAGGACCTGGAAGTGGAAAAAGCCCTCAAAGAGAGGATGATTCATTCCGTGATGCCAAGA
ATCATAGCCGATGACTTAATGAAGCAGGGAGATGAGGAGAGTGAGAATTCTGTCAAGAGG
CATGCCACCTCGAGCCCCAAGAACAGGAAGAAAAAGTCTTCCATCCAAAAAGCTCCTATA
GCCTTCCGCCCTTTTAAGATGCAGCAGATCGAAGAAGTCAGTATTTTATTTGCAGATATC
GTGGGCTTCACCAAGATGAGTGCCAACAAGTCTGCCCACGCCCTGGTGGGTCTCCTGAAC
GATCTGTTCGGTCGCTTCGACCGCCTGTGTGAGGAGACCAAGTGTGAGAAAATCAGCACC
CTGGGAGACTGTTACTACTGCGTGGCGGGCTGTCCCGAGCCCCGGGCCGACCATGCCTAC
TGCTGCATCGAGATGGGCCTGGGCATGATCAAGGCCATCGAGCAGTTCTGCCAGGAGAAG
AAGGAGATGGTGAACATGAGAGTCGGGGTGCACACGGGCACCGTCCTTTGCGGCATCCTG
GGCATGAGGAGGTTTAAATTTGACGTGTGGTCCAACGATGTGAACCTGGCCAATCTCATG
GAGCAGCTGGGAGTGGCCGGCAAAGTTCACATTTCTGAGGCCACCGCAAAATACTTAGAT
GACCGGTACGAAATGGAAGATGGGAAAGTTATTGAACGGCTGGGCCAGAGCGTGGTTGCT
GACCAGTTGAAAGGTTTGAAGACATACCTGATATCGGGTCAGAGAGCCAAGGAGTCTCGC
TGCAGCTGTGCAGAGGCCTTGCTTTCTGGCTTTGAGGTCATTGACGGCTCACAGGTGTCC
TCAGGCCCTAGGGGACAGGGGACAGCGTCATCAGGGAATGTCAGTGACTTGGCGCAGACT
GTCAAAACCTTTGATAACCTTAAGACCTGCCCTTCGTGCGGAATCACATTTGCTCCCAAA
TCTGAAGCCGGCGCCGAGGGAGGAGCACCTCAAAACGGCTGCCAAGACGAGCATAAAAAC
AGCACCAAGGCTTCTGGAGGACCTAATCCCAAAACTCAGAACGGGCTCCTCAGCCCTCCC
CAAGAGGAGAAGCTCACCAACAGTCAGACTTCTCTGTGTGAGATCTTGCAGGAGAAGGGA
AGGTGGGCAGGGGTGAGCCTGGACCAGTCGGCTCTCCTTCCGCTGAGGTTCAAGAACATC
CGGGAGAAAACGGACGCCCACTTTGTGGACGTTATCAAAGAAGACAGCCTGATGAAAGAT
TACTTTTTTAAGCCGCCCATTAATCAGTTCAGCCTGAACTTCCTGGATCAGGAGCTGGAG
CGATCCTACAGGACCAGCTATCAGGAAGAGGTCATAAAGAACTCCCCCGTGAAGACGTTT
GCTAGTCCCACCTTCAGCTCCCTCCTGGATGTGTTTCTGTCGACCACAGTGTTTCTGACG
CTGTCCACCACCTGCTTCCTGAAGTACGAGGCGGCCACCGTGCCTCCCCCGCCCGCCGCC
CTGGCGGTCTTCAGTGCAGCCCTGCTGCTGGAGGTGCTGTCCCTCGCGGTGTCCATCAGG
ATGGTGTTCTTCCTGGAGGACGTCATGGCCTGCACCAAGCGCCTGCTGGAGTGGATCGCC
GGCTGGCTACCACGTCACTGCATCGGGGCCATCCTGGTGTCGCTTCCCGCACTGGCCGTC
TACTCCCATGTCACCTCCGAATATGAGACCAACATACACTTCCCAGTGTTCACAGGCTCG
GCCGCACTGATTGCCGTCGTGCACTACTGTAACTTCTGCCAGCTCAGCTCCTGGATGAGG
TCCTCCCTCGCCACCGTCGTGGGGGCCGGGCCGCTGCTCCTGCTCTACGTCTCCCTGTGC
CCAGACAGTTCTGTATTAACTTCGCCCCTTGACGCAGTACAGAATTTCAGTTCCGAGAGG
AACCCGTGCAATAGTTCGGTGCCGCGTGACCTCCGGCGGCCCGCCAGCCTCATCGGCCAG
GAGGTGGTTCTCGTCTTCTTTCTCCTGCTCTTGTTGGTCTGGTTCCTGAATCGCGAATTT
GAAGTCAGCTACCGCCTCCACTACCACGGAGACGTGGAAGCGGATCTTCACCGCACCAAG
ATCCAGAGCATGCGGGACCAGGCAGACTGGCTGCTGAGGAACATCATCCCCTACCACGTG
GCTGAGCAGCTGAAGGTGTCCCAGACCTACTCCAAGAACCACGACAGCGGAGGGGTGATC
TTCGCCAGCATCGTCAACTTCAGCGAGTTCTACGAGGAGAACTACGAGGGCGGCAAGGAG
TGCTACCGGGTCCTCAACGAGCTCATCGGGGACTTTGACGAGCTCCTAAGCAAGCCGGAC
TACAGCAGCATCGAGAAGATCAAGACCATCGGAGCCACGTACATGGCGGCGTCAGGGCTG
AACACCGCGCAGGCCCAGGACGGCAGCCACCCGCAGGAGCACCTGCAGATCCTGTTCGAG
TTCGCCAAGGAGATGATGCGCGTGGTGGACGACTTCAACAACAACATGCTGTGGTTCAAC
TTCAAGCTCCGCGTCGGCTTCAACCATGGGCCCCTCACGGCCGGGGTCATCGGCACCACC
AAGCTGCTGTACGACATCTGGGGAGACACCGTCAACATCGCCAGCAGGATGGACACCACC
GGCGTGGAGTGCCGCATCCAGGTGAGCGAAGAGAGCTACCGCGTCTTGAGCAAGATGGGC
TATGACTTCGACTACAGAGGGACCGTGAATGTCAAGGGGAAAGGCCAGATGAAGACCTAC
CTGTACCCAAAGTGCACGGATCACAGGGTCATCCCAGCACCAGCTGTCCATCTCCCCAGA
CATCCGCGTCCAGGTGGATGGCAGCATCGGACGGTCTCCCACAGACGAGATTGCCAACCT
GGTGCCTTCTGTCCAGTATGTGGACAAGACATCTCTGGGTTCTGA
Enzyme 29 GenBank Gene ID AF036927 Link Image
Enzyme 29 GeneCard ID ADCY9 Link Image
Enzyme 29 GenAtlas ID ADCY9 Link Image
Enzyme 29 HGNC ID HGNC:240 Link Image
Enzyme 29 Chromosome Location 16
Enzyme 29 Locus 16p13.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Hacker BM, Tomlinson JE, Wayman GA, Sultana R, Chan G, Villacres E, Disteche C, Storm DR: Cloning, chromosomal mapping, and regulatory properties of the human type 9 adenylyl cyclase (ADCY9). Genomics. 1998 May 15;50(1):97-104. [PubMed Link Image]
  2. Small KM, Brown KM, Theiss CT, Seman CA, Weiss ST, Liggett SB: An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase type 9 confers reduced beta2-adrenergic receptor stimulation. Pharmacogenetics. 2003 Sep;13(9):535-41. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  4. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5983
Enzyme 30 Name Adenylate cyclase type 3
Enzyme 30 Synonyms
  1. Adenylate cyclase type III
  2. ATP pyrophosphate-lyase 3
  3. Adenylyl cyclase 3
  4. AC-III
  5. AC3
  6. Adenylate cyclase, olfactive type
Enzyme 30 Gene Name ADCY3
Enzyme 30 Protein Sequence >Adenylate cyclase type 3
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
Enzyme 30 Number of Residues 1144
Enzyme 30 Molecular Weight 128962
Enzyme 30 Theoretical pI 6.55
Enzyme 30 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
Enzyme 30 General Function Signal transduction mechanisms
Enzyme 30 Specific Function Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration
Enzyme 30 Pathways
Enzyme 30 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 80-100 105-125 139-159 173-193 226-246 381-401 633-653 664-684 708-728 754-774 775-795 833-853
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 4104226 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O60266 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ADCY3_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3435 bp
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTCCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCTGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAGACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
Enzyme 30 GenBank Gene ID AF033861 Link Image
Enzyme 30 GeneCard ID ADCY3 Link Image
Enzyme 30 GenAtlas ID ADCY3 Link Image
Enzyme 30 HGNC ID HGNC:234 Link Image
Enzyme 30 Chromosome Location 2
Enzyme 30 Locus 2p24-p22
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  3. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5984
Enzyme 31 Name Adenylate cyclase type 1
Enzyme 31 Synonyms
  1. Adenylate cyclase type I
  2. ATP pyrophosphate-lyase 1
  3. Adenylyl cyclase 1
  4. Ca(2+/calmodulin- activated adenylyl cyclase
Enzyme 31 Gene Name ADCY1
Enzyme 31 Protein Sequence >Adenylate cyclase type 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 31 Number of Residues 1119
Enzyme 31 Molecular Weight 123442
Enzyme 31 Theoretical pI 8.49
Enzyme 31 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
Enzyme 31 General Function Signal transduction mechanisms
Enzyme 31 Specific Function This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning
Enzyme 31 Pathways
Enzyme 31 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 64-84 88-108 125-145 158-178 183-203 214-234 611-631 635-655 674-694 725-745 753-773 775-794
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 41472630 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q08828 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ADCY1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >314 bp
ATGAAGGAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGG
CACGACAATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAG
TGCACAGCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTA
GCCACGGAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCG
GGCCTCACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATG
ATTGATACCATCAC
Enzyme 31 GenBank Gene ID AC069008 Link Image
Enzyme 31 GeneCard ID ADCY1 Link Image
Enzyme 31 GenAtlas ID ADCY1 Link Image
Enzyme 31 HGNC ID HGNC:232 Link Image
Enzyme 31 Chromosome Location 7
Enzyme 31 Locus 7p13-p12
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6209
Enzyme 32 Name Adenylate cyclase type 2
Enzyme 32 Synonyms
  1. Adenylate cyclase type II
  2. ATP pyrophosphate-lyase 2
  3. Adenylyl cyclase 2
Enzyme 32 Gene Name ADCY2
Enzyme 32 Protein Sequence >Adenylate cyclase type 2
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
Enzyme 32 Number of Residues 1091
Enzyme 32 Molecular Weight 123605
Enzyme 32 Theoretical pI 8.15
Enzyme 32 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 32 General Function Signal transduction mechanisms
Enzyme 32 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 32 Pathways
Enzyme 32 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 46-66 76-96 108-128 133-153 159-179 187-207 602-622 628-652 680-701 734-755 763-780 801-821
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 33150814 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q08462 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ADCY2_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >3276 bp
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTG
TGGGAACCTGGCNGGACTAACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCTGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
Enzyme 32 GenBank Gene ID AF410885 Link Image
Enzyme 32 GeneCard ID ADCY2 Link Image
Enzyme 32 GenAtlas ID ADCY2 Link Image
Enzyme 32 HGNC ID HGNC:233 Link Image
Enzyme 32 Chromosome Location 5
Enzyme 32 Locus 5p15.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  2. Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6332
Enzyme 33 Name Cytochrome P450 17A1
Enzyme 33 Synonyms
  1. CYPXVII
  2. P450-C17
  3. P450c17
  4. Steroid 17-alpha-monooxygenase
  5. Steroid 17-alpha-hydroxylase/17,20 lyase
Enzyme 33 Gene Name CYP17A1
Enzyme 33 Protein Sequence >Cytochrome P450 17A1
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
Enzyme 33 Number of Residues 508
Enzyme 33 Molecular Weight 57371
Enzyme 33 Theoretical pI 8.87
Enzyme 33 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 33 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 33 Specific Function Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty
Enzyme 33 Pathways
Enzyme 33 Reactions
  • a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-24
Enzyme 33 Transmembrane Regions Not Available
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 181342 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P05093 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name CP17A_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1527 bp
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
Enzyme 33 GenBank Gene ID M14564 Link Image
Enzyme 33 GeneCard ID CYP17A1 Link Image
Enzyme 33 GenAtlas ID CYP17A1 Link Image
Enzyme 33 HGNC ID HGNC:2593 Link Image
Enzyme 33 Chromosome Location 10
Enzyme 33 Locus 10q24.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed Link Image]
  2. Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed Link Image]
  3. Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed Link Image]
  4. Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed Link Image]
  5. Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed Link Image]
  6. Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed Link Image]
  7. Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed Link Image]
  8. Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed Link Image]
  9. Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed Link Image]
  10. Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed Link Image]
  11. Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed Link Image]
  12. Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed Link Image]
  13. Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed Link Image]
  14. Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed Link Image]
  15. Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed Link Image]
  16. Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed Link Image]
  17. Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed Link Image]
  18. Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed Link Image]
  19. Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6413
Enzyme 34 Name Cyclic nucleotide-gated cation channel alpha 3
Enzyme 34 Synonyms
  1. CNG channel alpha 3
  2. CNG-3
  3. CNG3
  4. Cyclic nucleotide-gated channel alpha 3
  5. Cone photoreceptor cGMP-gated channel subunit alpha
Enzyme 34 Gene Name CNGA3
Enzyme 34 Protein Sequence >Cyclic nucleotide-gated cation channel alpha 3
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
Enzyme 34 Number of Residues 694
Enzyme 34 Molecular Weight 78839
Enzyme 34 Theoretical pI 7.80
Enzyme 34 GO Classification
Function
  • ion channel activity
  • ion transporter activity
  • transporter activity
  • voltage-gated ion channel activity
  • voltage-gated potassium channel activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • physiological process
  • potassium ion transport
  • transport
Component
  • cell
  • membrane
Enzyme 34 General Function Signal transduction mechanisms
Enzyme 34 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 171-192 305-325 378-397
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 3153887 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q16281 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name CNGA3_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2085 bp
ATGGCCAAGATCAACACCCAATACTCCCACCCCTCCAGGACCCACCTCAAGGTAAAGACC
TCAGACCGAGATCTCAATCGCGCTGAAAATGGCCTCAGCAGAGCCCACTCGTCAAGTGAG
GAGACATCGTCAGTGCTGCAGCCGGGGATCGCCATGGAGACCAGAGGACTGGCTGACTCC
GGGCAGGGCTCCTTCACCGGCCAGGGGATCGCCAGGCTGTCGCGCCTCATCTTCTTGCTG
CGCAGGTGGGCTGCCAGGCATGTGCACCACCAGGACCAGGGACCGGACTCTTTTCCTGAT
CGTTTCCGTGGAGCCGAGCTTAAGGAGGTGTCCAGCCAAGAAAGCAATGCCCAGGCAAAT
GTGGGCAGCCAGGAGCCAGCAGACAGAGGGAGAAGCGCCTGGCCCCTGGCCAAATGCAAC
ACTAACACCAGCAACAACACGGAGGAGGAGAAGAAGACGAAAAAGAAGGATGCGATCGTG
GTGGACCCGTCCAGCAACCTGTACTACCGCTGGCTGACCGCCATCGCCCTGCCTGTCTTC
TATAACTGGTATCTGCTTATTTGCAGGGCCTGTTTCGATGAGCTGCAGTCCGAGTACCTG
ATGCTGTGGCTGGTCCTGGACTACTCGGCAGATGTCCTGTATGTCTTGGATGTGCTTGTA
CGAGCTCGGACAGGTTTTCTCGAGCAAGGCTTAATGGTCAGTGATACCAACAGGCTGTGG
CAGCATTACAAGACGACCACGCAGTTCAAGCTGGATGTGTTGTCCCTGGTCCCCACCGAC
CTGGCTTACTTAAAGGTGGGCACAAACTACCCAGAAGTGAGGTTCAACCGCCTACTGAAG
TTTTCCCGGCTCTTTGAATTCTTTGACCGCACAGAGACAAGGACCAACTACCCCAATATG
TTCAGGATTGGGAACTTGGTCTTGTACATTCTCATCATCATCCACTGGAATGCCTGCATC
TACTTTGCCATTTCCAAGTTCATTGGTTTTGGGACAGACTCCTGGGTCTACCCAAACATC
TCAATCCCAGAGCATGGGCGCCTCTCCAGGAAGTACATTTACAGTCTCTACTGGTCCACC
TTGACCCTTACCACCATTGGTGAGACCCCACCCCCCGTGAAAGATGAGGAGTATCTCTTT
GTGGTCGTAGACTTCTTGGTGGGTGTTCTGATTTTTGCCACCATTGTGGGCAATGTGGGC
TCCATGATCTCGAATATGAATGCCTCACGGGCAGAGTTCCAGGCCAAGATTGATTCCATC
AAGCAGTACATGCAGTTCCGCAAGGTCACCAAGGACTTGGAGACGCGGGTTATCCGGTGG
TTTGACTACCTGTGGGCCAACAAGAAGACGGTGGATGAGAAGGAGGTGCTCAAGAGCCTC
CCAGACAAGCTGAAGGCTGAGATCGCCATCAACGTGCACCTGGACACGCTGAAGAAGGTT
CGCATCTTCCAGGACTGTGAGGCAGGGCTGCTGGTGGAGCTGGTGCTGAAGCTGCGACCC
ACTGTGTTCAGCCCTGGGGATTATATCTGCAAGAAGGGAGATATTGGGAAGGAGATGTAC
ATCATCAACGAGGGCAAGCTGGCCGTGGTGGCTGATGATGGGGTCACCCAGTTCGTGGTC
CTCAGCGATGGCAGCTACTTCGGGGAGATCAGCATTCTGAACATCAAGGGGAGCAAGTCG
GGGAACCGCAGGACGGCCAACATCCGCAGCATTGGCTACTCAGACCTGTTCTGCCTCTCA
AAGGACGATCTCATGGAGGCCCTCACCGAGTACCCCGAAGCCAAGAAGGCCCTGGAGGAG
AAAGGACGGCAGATCCTGATGAAAGACAACCTGATCGATGAGGAGCTGGCCAGGGCGGGC
GCGGACCCCAAGGACCTTGAGGAGAAAGTGGAGCAGCTGGGGTCCTCCCTGGACACCCTG
CAGACCAGGTTTGCACGCCTCCTGGCTGAGTACAACGCCACCCAGATGAAGATGAAGCAG
CGTCTCAGCCAACTGGAAAGCCAGGTGAAGGGTGGTGGGGACAAGCCCCTGGCTGATGGG
GAAGTTCCCGGGGATGCTACAAAAACAGAGGACAAACAACAGTGA
Enzyme 34 GenBank Gene ID AF065314 Link Image
Enzyme 34 GeneCard ID CNGA3 Link Image
Enzyme 34 GenAtlas ID CNGA3 Link Image
Enzyme 34 HGNC ID HGNC:2150 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 2q11.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Wissinger B, Muller F, Weyand I, Schuffenhauer S, Thanos S, Kaupp UB, Zrenner E: Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors. Eur J Neurosci. 1997 Dec;9(12):2512-21. [PubMed Link Image]
  2. Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed Link Image]
  3. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  4. Kohl S, Marx T, Giddings I, Jagle H, Jacobson SG, Apfelstedt-Sylla E, Zrenner E, Sharpe LT, Wissinger B: Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet. 1998 Jul;19(3):257-9. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6416
Enzyme 35 Name Cyclic nucleotide-gated cation channel beta 3
Enzyme 35 Synonyms
  1. CNG channel beta 3
  2. Cyclic nucleotide-gated channel beta 3
  3. Cone photoreceptor cGMP- gated channel subunit beta
  4. Cyclic nucleotide-gated cation channel modulatory subunit
Enzyme 35 Gene Name CNGB3
Enzyme 35 Protein Sequence >Cyclic nucleotide-gated cation channel beta 3
MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPV
TSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPA
APVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKP
TEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCWFIPLRL
VFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKF
QLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYL
LFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEI
VFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVR
TWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRL
KSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGG
GNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRK
DLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQ
KENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTS
RQSLIISMAPSAEGGEEVLTIEVKEKAKQ
Enzyme 35 Number of Residues 809
Enzyme 35 Molecular Weight 92251
Enzyme 35 Theoretical pI 8.11
Enzyme 35 GO Classification
Function
  • ion channel activity
  • ion transporter activity
  • transporter activity
Process
  • cellular physiological process
  • ion transport
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 35 General Function Signal transduction mechanisms
Enzyme 35 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 217-237 251-271 303-323 360-380 418-438 505-525
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 9247066 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9NQW8 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CNGB3_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2430 bp
ATGTTTAAATCGCTGACAAAAGTCAACAAGGTGAAGCCTATAGGAGAGAACAATGAGAAT
GAACAAAGTTCTCGTCGGAATGAAGAAGGCTCTCACCCAAGTAATCAGTCTCAGCAAACC
ACAGCACAGGAAGAAAACAAAGGTGAAGAGAAATCTCTCAAAACCAAGTCAACTCCAGTC
ACGTCTGAAGAGCCACACACCAACATACAAGACAAACTCTCCAAGAAAAATTCCTCTGGA
GATCTGACCACAAACCCTGACCCTCAAAATGCAGCAGAACCAACTGGAACAGTGCCAGAG
CAGAAGGAAATGGACCCCGGGAAAGAAGGTCCAAACAGCCCACAAAACAAACCGCCTGCA
GCTCCTGTTATAAATGAGTATGCCGATGCCCAGCTACACAACCTGGTGAAAAGAATGCGT
CAAAGAACAGCCCTCTACAAGAAAAAGTTGGTAGAGGGAGATCTCTCCTCACCCGAAGCC
AGCCCACAAACTGCAAAGCCCACGGCTGTACCACCAGTAAAAGAAAGCGATGATAAGCCA
ACAGAACATTACTACAGGCTGTTGTGGTTCAAAGTCAAAAAGATGCCTTTAACAGAGTAC
TTAAAGCGAATTAAACTTCCAAACAGCATAGATTCATACACAGATCGACTCTATCTCCTG
TGGCTCTTGCTTGTCACTCTTGCCTATAACTGGAACTGCTGGTTTATACCACTGCGCCTC
GTCTTCCCATATCAAACCGCAGACAACATACACTACTGGCTTATTGCGGACATCATATGT
GATATCATCTACCTTTATGATATGCTATTTATCCAGCCCAGACTCCAGTTTGTAAGAGGA
GGAGACATAATAGTGGATTCAAATGAGCTAAGGAAACACTACAGGACTTCTACAAAATTT
CAGTTGGATGTCGCATCAATAATACCATTTGATATTTGCTACCTCTTCTTTGGGTTTAAT
CCAATGTTTAGAGCAAATAGGATGTTAAAGTACACTTCATTTTTTGAATTTAATCATCAC
CTAGAGTCTATAATGGACAAAGCATATATCTACAGAGTTATTCGAACAACTGGATACTTG
CTGTTTATTCTGCACATTAATGCCTGTGTTTATTACTGGGCTTCAAACTATGAAGGAATT
GGCACTACTAGATGGGTGTATGATGGGGAAGGAAACGAGTATCTGAGATGTTATTATTGG
GCAGTTCGAACTTTAATTACCATTGGTGGCCTTCCAGAACCACAAACTTTATTTGAAATT
GTTTTTCAACTCTTGAATTTTTTTTCTGGAGTTTTTGTGTTCTCCAGTTTAATTGGTCAG
ATGAGAGATGTGATTGGAGCAGCTACAGCCAATCAGAACTACTTCCGCGCCTGCATGGAT
GACACCATTGCCTACATGAACAATTACTCCATTCCTAAACTTGTGCAAAAGCGAGTTCGG
ACTTGGTATGAATATACATGGGACTCTCAAAGAATGCTAGATGAGTCTGATTTGCTTAAG
ACCCTACCAACTACGGTCCAGTTAGCCCTCGCCATTGATGTGAACTTCAGCATCATCAGC
AAAGTCGACTTGTTCAAGGGTTGTGATACACAGATGATTTATGACATGTTGCTAAGATTG
AAATCCGTTCTCTATTTGCCTGGTGACTTTGTCTGCAAAAAGGGAGAAATTGGCAAGGAA
ATGTATATCATCAAGCATGGAGAAGTCCAAGTTCTTGGAGGCCCTGATGGTACTAAAGTT
CTGGTTACTCTGAAAGCTGGGTCGGTGTTTGGAGAAATCAGCCTTCTAGCAGCAGGAGGA
GGAAACCGTCGAACTGCCAATGTGGTGGCCCACGGGTTTGCCAATCTTTTAACTCTAGAC
AAAAAGACCCTCCAAGAAATTCTAGTGCATTATCCAGATTCTGAAAGGATCCTCATGAAG
AAAGCCAGAGTGCTTTTAAAGCAGAAGGCTAAGACCGCAGAAGCAACCCCTCCAAGAAAA
GATCTTGCCCTCCTCTTCCCACCGAAAGAAGAGACACCCAAACTGTTTAAAACTCTCCTA
GGAGGCACAGGAAAAGCAAGTCTTGCAAGACTACTCAAATTGAAGCGAGAGCAAGCAGCT
CAGAAGAAAGAAAATTCTGAAGGAGGAGAGGAAGAAGGAAAAGAAAATGAAGATAAACAA
AAAGAAAATGAAGATAAACAAAAAGAAAATGAAGATAAAGGAAAAGAAAATGAAGATAAA
GATAAAGGAAGAGAGCCAGAAGAGAAGCCACTGGACAGACCTGAATGTACAGCAAGTCCT
ATTGCAGTGGAGGAAGAACCCCACTCAGTTAGAAGGACAGTTTTACCCAGAGGGACTTCT
CGTCAATCACTCATTATCAGCATGGCTCCTTCTGCTGAGGGCGGAGAAGAGGTTCTTACT
ATTGAAGTCAAAGAAAAGGCTAAGCAATAA
Enzyme 35 GenBank Gene ID AF272900 Link Image
Enzyme 35 GeneCard ID CNGB3 Link Image
Enzyme 35 GenAtlas ID CNGB3 Link Image
Enzyme 35 HGNC ID HGNC:2153 Link Image
Enzyme 35 Chromosome Location 8
Enzyme 35 Locus 8q21-q22
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Kohl S, Baumann B, Broghammer M, Jagle H, Sieving P, Kellner U, Spegal R, Anastasi M, Zrenner E, Sharpe LT, Wissinger B: Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21. Hum Mol Genet. 2000 Sep 1;9(14):2107-16. [PubMed Link Image]
  2. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6417
Enzyme 36 Name Rap guanine nucleotide exchange factor 2
Enzyme 36 Synonyms
  1. Neural RAP guanine nucleotide exchange protein
  2. nRap GEP
  3. PDZ domain-containing guanine nucleotide exchange factor 1
  4. PDZ-GEF1
  5. RA-GEF
Enzyme 36 Gene Name RAPGEF2
Enzyme 36 Protein Sequence >Rap guanine nucleotide exchange factor 2
MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLS
DIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTD
DDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGS
VEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLL
TYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENN
LEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGS
KATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKT
RISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFS
ATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPE
GVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETN
QLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDL
QDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMI
AKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSE
TSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINS
PQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNF
SDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNI
QTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQA
QSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAV
ASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
Enzyme 36 Number of Residues 1499
Enzyme 36 Molecular Weight 167419
Enzyme 36 Theoretical pI 6.64
Enzyme 36 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • protein binding
  • small GTPase regulator activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 40788210 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >4527 bp
ATTCAGTTCAGCATATGTTTCTTCATTATGAAACCACTAGCAATCCCAGCTAACCATGGA
GTTATGGGCCAGCAGGAGAAACACTCACTTCCTGCAGATTTCACAAAACTGCATCTTACT
GACAGTCTCCACCCACAGGTGACCCACGTTTCTTCTAGCCATTCAGGATGTAGTATCACT
AGTGATTCTGGGAGCAGCAGTCTTTCTGATATCTACCAGGCCACAGAAAGCGAGGCTGGT
GATATGGACCTGAGTGGGTTGCCAGAAACAGCAGTGGATTCCGAAGACGACGACGATGAA
GAAGACATTGAGAGAGCATCAGATCCTCTGATGAGCAGGGACATTGTGAGAGACTGCCTA
GAGAAGGACCCAATTGACCGGACAGATGATGACATTGAACAACTCTTGGAATTTATGCAC
CAGTTGCCTGCTTTTGCCAATATGACAATGTCAGTGAGGCGAGAACTCTGTGCTGTGATG
GTGTTCGCAGTGGTGGAAAGAGCAGGGACCATAGTGTTAAATGATGGTGAAGAGCTGGAC
TCCTGGTCAGTGATTCTCAATGGATCTGTGGAAGTGACTTATCCAGATGGAAAAGCAGAA
ATACTGTGCATGGGAAATAGTTTTGGTGTCTCTCCTACCATGGACAAAGAATACATGAAA
GGAGTGATGAGAACAAAGGTGGATGACTGCCAGTTTGTCTGCATAGCCCAGCAAGATTAC
TGCCGTATTCTCAATCAAGTAGAAAAGAACATGCAAAAAGTTGAAGAGGAAGGAGAGATT
GTTATGGTGAAAGAACACCGAGAACTTGATCGAACTGGAACAAGAAAGGGACACATTGTC
ATCAAGGGTACCTCAGAAAGGTTAACAATGCATTTGGTGGAAGAGCATTCAGTAGTAGAT
CCAACATTCATAGAAGACTTTCTGTTGACCTATAGGACTTTTCTTTCTAGCCCAATGGAA
GTGGGCAAAAAGTTATTGGAGTGGTTTAATGACCCGAGCCTCAGGGATAAGGTTACACGG
GTAGTATTATTGTGGGTAAATAATCACTTCAATGACTTTGAAGGAGATCCTGCAATGACT
CGATTTTTAGAAGAATTTGAAAACAATCTGGAAAGAGAGAAAATGGGTGGACACCTAAGG
CTGTTGAATATCGCGTGTGCTGCTAAAGCAAAAAGAAGATTGATGACGTTAACAAAACCA
TCCCGAGAAGCTCCTTTGCCTTTTATCTTACTTGGAGGCTCTGAGAAGGGATTTGGAATC
TTTGTTGACAGTGTAGATTCAGGTAGCAAAGCAACTGAAGCAGGCTTGAAACGGGGGGAT
CAGATATTAGAAGTAAATGGCCAAAACTTTGAAAACATTCAGCTGTCAAAAGCTATGGAA
ATTCTTAGAAATAACACACATTTATCTATCACTGTGAAAACCAATTTATTTGTATTTAAA
GAACTTCTAACAAGATTGTCAGAAGAGAAAAGAAATGGTGCCCCCCACCTTCCTAAAATT
GGTGACATTAAAAAGGCCAGTCGCTACTCCATTCCAGATCTTGCTGTAGATGTAGAACAG
GTGATAGGACTTGAAAAAGTGAACAAAAAAAGTAAAGCCAACACTGTGGGAGGAAGGAAC
AAGCTGAAAAAGATACTCGACAAGACTCGGATCAGTATCTTGCCACAGAAACCATACAAT
GATATTGGGATTGGTCAGTCTCAAGATGACAGCATAGTAGGATTAAGGCAGACAAAGCAC
ATCCCAACTGCATTGCCTGTCAGTGGAACCTTATCATCCAGTAATCCTGATTTATTGCAG
TCACATCATCGCATTTTAGACTTCAGTGCTACTCCTGACTTGCCAGATCAAGTGCTAAGG
GTTTTTAAGGCTGATCAGCAAAGCCGCTACATCATGATCAGTAAGGACACTACAGCAAAG
GAAGTGGTCATTCAGGCTATCAGGGAGTTTGCTGTTACTGCCACCCCGGATCAATATTCA
CTATGTGAGGTCTCTGTCACACCTGAGGGAGTAATCAAACAAAGAAGACTTCCAGATCAG
CTTTCCAAACTTGCAGACAGAATACAACTGAGTGGAAGGTATTATCTGAAAAACAACATG
GAAACAGAAACTCTTTGTTCAGATGAAGATGCTCAGGAGTTGTTGAGAGAGAGTCAAATT
TCCCTCCTTCAGCTCAGCACTGTGGAAGTTGCAACACAGCTCTCTATGCGAAATTTTGAA
CTCTTTCGCAACATTGAACCTACTGAATATATAGATGATTTATTTAAACTCAGATCAAAA
ACCAGCTGTGCCAACCTGAAGAGATTTGAAGAAGTCATTAACCAGGAAACATTTTGGGTA
GCATCTGAAATTCTCAGAGAAACAAACCAGCTGAAGAGGATGAAGATCATTAAGCATTTC
ATCAAGATAGCACTGCACTGTAGGGAATGCAAGAATTTTAACTCAATGTTTGCAATCATC
AGTGGCCTAAACCTGGCACCAGTGGCAAGACTGCGAACGACCTGGGAGAAACTTCCCAAT
AAATACGAAAAACTATTTCAAGATCTCCAAGACCTGTTTGATCCTTCCAGAAACATGGCA
AAATATCGTAATGTTCTCAATAGTCAAAATCTACAACCTCCCATAATCCCTCTATTCCCA
GTTATCAAAAAGGATCTCACCTTCCTTCACGAAGGAAATGACTCAAAAGTAGACGGGCTG
GTCAATTTTGAGAAGCTAAGGATGATTGCAAAAGAAATTCGTCACGTTGGCCGAATGGCT
TCAGTGAACATGGACCCTGCCCTCATGTTCAGGACTCGGAAGAAGAAATGGCGGAGTTTG
GGGTCTCTCAGCCAGGGTAGTACAAATGCAACAGTGCTAGATGTTGCTCAGACAGGTGGT
CATAAAAAGCGGGTACGTCGTAGTTCCTTTCTCAATGCCAAAAAGCTTTATGAAGATGCC
CAAATGGCTCGAAAAGTGAAGCAGTACCTTTCCAATTTGGAGCTAGAAATGGACGAGGAG
AGTCTTCAGACATTATCTCTGCAGTGTGAGCCAGCAACCAACACATTGCCTAAGAATCCT
GGTGACAAAAAGCCTGTCAAATCCGAGACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAA
CAGAAAGCTCAGTCCCTGCCACAGCCCCAGCAGCAGCCACCACCAGCACATAAAATCAAC
CAGGGACTACAGGTTCCCGCCGTGTCCCTTTATCCTTCACGGAAGAAAGTGCCCGTAAAG
GATCTCCCACCTTTTGGCATAAACTCTCCACAAGCTTTAAAAAAAATTCTTTCTTTGTCT
GAAGAAGGAAGTTTGGAACGTCACAAGAAACAGGCTGAAGATACAATATCAAATGCATCT
TCGCAGCTTTCTTCTCCTCCTACTTCTCCACAGAGTTCTCCAAGGAAAGGCTATACTTTG
GCTCCCAGTGGTACTGTGGATAATTTTTCAGATTCTGGTCACAGTGAAATTTCTTCACGA
TCCAGTATTGTTAGCAATTCGTCTTTTGACTCAGTGCCAGTCTCACTGCACGATGAGAGG
CGCCAGAGGCATTCTGTCAGCATCGTGGAAACAAACCTAGGGATGGGCAGGATGGAGAGG
CGGACCATGATTGAACCTGATCAGTATAGCTTGGGGTCCTATGCACCAATGTCCGAGGGC
CGAGGCTTATATGCTACAGCTACAGTAATTTCTTCTCCAAGCACAGAGGAACTTTCCCAG
GATCAGGGGGATCGCGCGTCACTTGATGCTGCTGACAGTGGCCGTGGGAGCTGGACGTCA
TGCTCAAGTGGCTCCCATGATAATATACAGACGATCCAGCACCAGAGAAGCTGGGAGACT
CTTCCATTCGGGCATACTCACTTTGATTATTCAGGGGATCCTGCAGGTTTATGGGCATCA
AGCAGCCATATGGACCAAATTATGTTTTCTGATCATAGCACAAAGTATAACAGGCAAAAT
CAAAGTAGAGAGAGCCTTGAACAAGCCCAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGT
TACTGGGGAGAAGACTCAGAAGGTGACACAGGCACAATAAAGCGGAGGGGTGGAAAGGAT
GTTTCCATTGAAGCCGAAAGCAGTAGCCTAACGTCTGTGACTACGGAAGAAACCAAGCCT
GTCCCCATGCCTGCCCACATAGCTGTGGCATCAAGTACTACAAAGGGGCTCATTGCACGA
AAGGAGGGCAGGTATCGAGAGCCCCCGCCCACCCCTCCCGGCTACATTGGAATTCCCATT
ACTGACTTTCCAGAAGGGCACTCCCATCCAGCCAGGAAACCGCCGGACTACAACGTGGCC
CTTCAGAGATCGCGGATGGTCGCACGATCCTCCGACACAGCTGGGCCTTCATCCGTACAG
CAGCCACATGGGCATCCCACCAGCAGCAGGCCTGTGAACAAACCTCAGTGGCATAAACCG
AACGAGTCTGACCCGCGCCTCGCCCCTTATCAGTCCCAAGGGTTTTCCACCGAGGAGGAT
GAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 36 GenBank Gene ID AB002311 Link Image
Enzyme 36 GeneCard ID RAPGEF2 Link Image
Enzyme 36 GenAtlas ID RAPGEF2 Link Image
Enzyme 36 HGNC ID HGNC:16854 Link Image
Enzyme 36 Chromosome Location 4
Enzyme 36 Locus 4q32.1
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed Link Image]
  3. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6420
Enzyme 37 Name Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
Enzyme 37 Synonyms
  1. Brain cyclic nucleotide-gated channel 1
  2. BCNG-1
Enzyme 37 Gene Name HCN1
Enzyme 37 Protein Sequence >Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFK
VDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAV
EKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNV
ASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVE
KGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFN
LIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIG
YGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSF
HKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANAD
PNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGE
ICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSI
LLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRM
RTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYA
SPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLT
REVRPFSAWQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVT
LFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL
Enzyme 37 Number of Residues 890
Enzyme 37 Molecular Weight 98930
Enzyme 37 Theoretical pI 8.54
Enzyme 37 GO Classification
Function
  • ion channel activity
  • ion transporter activity
  • transporter activity
  • voltage-gated ion channel activity
  • voltage-gated potassium channel activity
Process
  • cation transport
  • cellular physiological process
  • ion transport
  • monovalent inorganic cation transport
  • physiological process
  • potassium ion transport
  • transport
Component
  • cell
  • membrane
Enzyme 37 General Function Signal transduction mechanisms
Enzyme 37 Specific Function Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Activated by cAMP, and at 10-100 times higher concentrations, also by cGMP. May mediate responses to sour stimuli
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 147-167 174-194 220-240 249-269 301-321 345-366 372-392
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein Not Available
Enzyme 37 UniProtKB/Swiss-Prot ID O60741 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name HCN1_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence Not Available
Enzyme 37 GenBank Gene ID AC114975 Link Image
Enzyme 37 GeneCard ID HCN1 Link Image
Enzyme 37 GenAtlas ID HCN1 Link Image
Enzyme 37 HGNC ID HGNC:4845 Link Image
Enzyme 37 Chromosome Location 5
Enzyme 37 Locus 5p12
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Santoro B, Liu DT, Yao H, Bartsch D, Kandel ER, Siegelbaum SA, Tibbs GR: Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain. Cell. 1998 May 29;93(5):717-29. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6503
Enzyme 38 Name cAMP-dependent protein kinase, gamma-catalytic subunit
Enzyme 38 Synonyms
  1. PKA C-gamma
Enzyme 38 Gene Name PRKACG
Enzyme 38 Protein Sequence >cAMP-dependent protein kinase, gamma-catalytic subunit
MGNAPAKKDTEQEESVNEFLAKARGDFLYRWGNPAQNTASSDQFERLRTLGMGSFGRVML
VRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLV
MEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGY
LQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFY
ADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWFAT
TSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF
Enzyme 38 Number of Residues 351
Enzyme 38 Molecular Weight 40435
Enzyme 38 Theoretical pI 8.89
Enzyme 38 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 38 General Function Not Available
Enzyme 38 Specific Function Phosphorylates a large number of substrates in the cytoplasm and the nucleus
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 189987 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P22612 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name KAPCG_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1083 bp
ATGGCGGCCCCTGCCGCCGCCACCGCCATGGGCAACGCCCCCGCCAAGAAGGACACCGAG
CAGGAGGAGAGCGTGAACGAGTTCCTAGCCAAAGCCAGAGGAGATTTCCTCTACAGATGG
GGAAACCCCGCTCAAAACACCGCCAGCTCGGATCAGTTCGAACGGCTCAGGACGCTGGGC
ATGGGCTCCTTCGGGCGGGTGATGCTGGTGAGGCACCAGGAGACCGGCGGCCACTACGCC
ATGAAGATCCTCAACAAGCAGAAGGTGGTGAAGATGAAGCAGGTCGAGCACATACTGAAC
GAGAAGCGCATCCTGCAGGCGATCGACTTTCCGTTCCTCGTCAAGCTCCAGTTCTCCTTT
AAGGACAACTCCTACCTGTACCTGGTGATGGAGTACGTGCCGGGTGGGGAGATGTTCTCC
CGCCTACAGCGCGTCGGAAGGTTTAGCGAGCCCCATGCCTGTTTCTATGCCGCCCAGGTC
GTCCTGGCCGTCCAGTACCTACACTCGCTCGACCTCATCCACCGCGACCTGAAGCCCGAG
AATCTCCTCATCGACCAGCAGGGCTACCTGCAGGTGACGGACTTCGGTTTCGCCAAGCGC
GTGAAGGGCCGCACTTGGACCTTGTGCGGGACCCCAGAGTACCTGGCCCCCGAGATCATC
CTGAGCAAAGGCTACAACAAGGCCGTGGACTGGTGGGCCCTAGGGGTGCTCATCTATGAG
ATGGCCGTGGGCTTCCCACCCTTCTACGCCGACCAGCCCATCCAGATCTACGAGAAGATC
GTCTCTGGGAGGGTGCGGTTTCCCTCCAAACTCAGCTCTGACCTCAAGGATCTGCTGCGG
AGCCTGCTGCAGGTGGACCTCACCAAGCGCTTCGGAAACCTCAGGAACGGGGTTGGCGAC
ATCAAGAACCACAAGTGGTTCGCCACAACCAGCTGGATCGCCATCTATGAGAAGAAGGTG
GAAGCTCCCTTCATCCCGAAGTACACAGGCCCTGGGGATGCCAGTAACTTTGACGACTAC
GAGGAGGAAGAGCTCCGGATCTCCATCAATGAGAAGTGTGCCAAGGAGTTTTCTGAGTTT
TAG
Enzyme 38 GenBank Gene ID M34182 Link Image
Enzyme 38 GeneCard ID PRKACG Link Image
Enzyme 38 GenAtlas ID PRKACG Link Image
Enzyme 38 HGNC ID HGNC:9382 Link Image
Enzyme 38 Chromosome Location 9
Enzyme 38 Locus 9q13
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed Link Image]
  2. Reinton N, Haugen TB, Orstavik S, Skalhegg BS, Hansson V, Jahnsen T, Tasken K: The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon. Genomics. 1998 Apr 15;49(2):290-7. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6648
Enzyme 39 Name cAMP-dependent protein kinase, alpha-catalytic subunit
Enzyme 39 Synonyms
  1. PKA C-alpha
Enzyme 39 Gene Name PRKACA
Enzyme 39 Protein Sequence >cAMP-dependent protein kinase, alpha-catalytic subunit
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML
VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Enzyme 39 Number of Residues 351
Enzyme 39 Molecular Weight 40590
Enzyme 39 Theoretical pI 9.22
Enzyme 39 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Phosphorylates a large number of substrates in the cytoplasm and the nucleus
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 35479 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P17612 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name KAPCA_HUMAN Link Image
Enzyme 39 PDB ID 1CTP Link Image
Enzyme 39 PDB File Show
Enzyme 39 3D Structure
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1056 bp
ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA
GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC
TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG
GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG
GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC
TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC
ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT
GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG
CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC
ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC
GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG
GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC
GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC
CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG
CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA
ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA
GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC
AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG
Enzyme 39 GenBank Gene ID X07767 Link Image
Enzyme 39 GeneCard ID PRKACA Link Image
Enzyme 39 GenAtlas ID PRKACA Link Image
Enzyme 39 HGNC ID HGNC:9380 Link Image
Enzyme 39 Chromosome Location 19
Enzyme 39 Locus 19p13.1
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Maldonado F, Hanks SK: A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 1988 Aug 25;16(16):8189-90. [PubMed Link Image]
  2. Agustin JT, Wilkerson CG, Witman GB: The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells. Mol Biol Cell. 2000 Sep;11(9):3031-44. [PubMed Link Image]
  3. Desseyn JL, Burton KA, McKnight GS: Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6433-8. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6695
Enzyme 40 Name Serine/threonine-protein kinase PRKY
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name PRKY
Enzyme 40 Protein Sequence >Serine/threonine-protein kinase PRKY
MEAPGPAQAAAAESNSREVTEDAADWAPALCPSPEARSPEAPAYRLQDCDALVTMGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRRKQEQHVHNEKSVLKEVSHPFLIRLFWTWHEER
FLYMLMEYVPGGELFSYLRNRGHFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKLYFPRHLDFHVKTGRMM
Enzyme 40 Number of Residues 277
Enzyme 40 Molecular Weight 31709
Enzyme 40 Theoretical pI 6.96
Enzyme 40 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • protein-tyrosine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 2695984 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID O43930 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name PRKY_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >166 bp
ATGGAGGCGCCCGGGCCGGCCCAGGCGGCCGCGGCGGAGAGCAACTCCCGAGAGGTGACG
GAGGATGCCGCCGACTGGGCGCCCGCGCTCTGCCCCAGCCCCGAGGCGCGGTCGCCGGAG
GCGCCTGCCTACCGCCTGCAGGACTGCGACGCGCTGGTCACCATGG
Enzyme 40 GenBank Gene ID Y13927 Link Image
Enzyme 40 GeneCard ID PRKY Link Image
Enzyme 40 GenAtlas ID PRKY Link Image
Enzyme 40 HGNC ID HGNC:9444 Link Image
Enzyme 40 Chromosome Location Y
Enzyme 40 Locus Yp11.2
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed Link Image]
  2. Schiebel K, Mertz A, Winkelmann M, Glaser B, Schempp W, Rappold G: FISH localization of the human Y-homolog of protein kinase PRKX (PRKY) to Yp11.2 and two pseudogenes to 15q26 and Xq12-->q13. Cytogenet Cell Genet. 1997;76(1-2):49-52. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6711
Enzyme 41 Name cAMP-dependent protein kinase, beta-catalytic subunit
Enzyme 41 Synonyms
  1. PKA C-beta
Enzyme 41 Gene Name PRKACB
Enzyme 41 Protein Sequence >cAMP-dependent protein kinase, beta-catalytic subunit
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPTQNNAGLEDFERKKTLGTGSFGRVML
VKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFAT
TDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCAKEFGEF
Enzyme 41 Number of Residues 351
Enzyme 41 Molecular Weight 40623
Enzyme 41 Theoretical pI 9.19
Enzyme 41 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 189983 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P22694 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name KAPCB_HUMAN Link Image
Enzyme 41 PDB ID 1CTP Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1056 bp
ATGGGGAACGCGGCGACCGCCAAGAAAGGCAGCGAGGTGGAGAGCGTGAAAGAGTTTCTA
GCCAAAGCCAAAGAAGACTTTTTGAAAAAATGGGAGAATCCAACTCAGAATAATGCCGGA
CTTGAAGATTTTGAAAGGAAAAAAACCCTTGGAACAGGTTCATTTGGAAGAGTCATGTTG
GTAAAACACAAAGCCACTGAACAGTATTATGCCATGAAGATCTTAGATAAGCAGAAGGTT
GTTAAACTGAAGCAAATAGAGCATACTTTGAATGAGAAAAGAATATTACAGGCAGTGAAT
TTTCCTTTCCTTGTTCGACTGGAGTATGCTTTTAAGGATAATTCTAATTTATACATGGTT
ATGGAATATGTCCCTGGGGGTGAAATGTTTTCACATCTAAGAAGAATTGGAAGGTTCAGT
GAGCCCCATGCACGGTTCTATGCAGCTCAGATAGTGCTAACATTCGAGTACCTCCATTCA
CTAGACCTCATCTACAGAGATCTAAAACCTGAAAATCTCTTAATTGACCATCAAGGCTAT
ATCCAGGTCACAGACTTTGGGTTTGCCAAAAGAGTTAAAGGCAGAACTTGGACATTATGT
GGAACTCCAGAGTATTTGGCTCCAGAAATAATTCTCAGCAAGGGCTACAATAAGGCAGTG
GATTGGTGGGCATTAGGAGTGCTAATCTATGAAATGGCAGCTGGCTATCCCCCATTCTTT
GCAGACCAACCAATTCAGATTTATGAAAAGATTGTTTCTGGAAAGGTCCGATTCCCATCC
CACTTCAGTTCAGATCTCAAGGACCTTCTACGGAACCTGCTGCAGGTGGATTTGACCAAG
AGATTTGGAAATCTAAAGAATGGTGTCAGTGATATAAAAACTCACAAGTGGTTTGCCACG
ACAGATTGGATTGCTATTTACCAGAGGAAGGTTGAAGCTCCATTCATACCAAAGTTTAGA
GGCTCTGGAGATACCAGCAACTTTGATGACTATGAAGAAGAAGATATCCGTGTCTCTATA
ACAGAAAAATGTGCAAAAGAATTTGGTGAATTTTAA
Enzyme 41 GenBank Gene ID M34181 Link Image
Enzyme 41 GeneCard ID PRKACB Link Image
Enzyme 41 GenAtlas ID PRKACB Link Image
Enzyme 41 HGNC ID HGNC:9381 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 1p36.1
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T: Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase. Mol Endocrinol. 1990 Mar;4(3):465-75. [PubMed Link Image]
  2. Orstavik S, Reinton N, Frengen E, Langeland BT, Jahnsen T, Skalhegg BS: Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase. Eur J Biochem. 2001 Oct;268(19):5066-73. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6787
Enzyme 42 Name Ribosomal protein S6 kinase alpha-5
Enzyme 42 Synonyms
  1. Nuclear mitogen- and stress-activated protein kinase 1
  2. 90 kDa ribosomal protein S6 kinase 5
  3. RSK-like protein kinase
  4. RSKL
Enzyme 42 Gene Name RPS6KA5
Enzyme 42 Protein Sequence >Ribosomal protein S6 kinase alpha-5
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAY
GKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYA
FQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKL
ENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWS
LGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKK
RLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYS
PAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFY
QHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPN
IVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGV
VHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYD
ESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEA
KDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFH
AFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTL
QPSNPADSNNPETLFQFSDSVA
Enzyme 42 Number of Residues 802
Enzyme 42 Molecular Weight 89866
Enzyme 42 Theoretical pI 7.10
Enzyme 42 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 42 General Function Not Available
Enzyme 42 Specific Function Serine/threonine kinase required for the mitogen or stress-induced phosphorylation of the transcription factors CREB (cAMP response element-binding protein) and ATF1 (activating transcription factor-1). Essential role in the control of RELA transcriptional activity in response to TNF. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and epidemal growth-factor (EGF), which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 14 (HMG-14)
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 3411157 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID O75582 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name KS6A5_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2409 bp
ATGGAGGAGGAGGGTGGCAGCAGCGGCGGCGCCGCGGGGACCAGCGCGGACGGCGGCGAC
GGAGGAGAGCAGCTCCTCACTGTCAAGCACGAGCTGCGGACTGCTAATTTGACAGGACAT
GCTGAGAAGGTGGGAATAGAAAATTTTGAGCTCCTGAAGGTCCTAGGAACTGGAGCTTAT
GGAAAAGTATTTCTAGTTCGTAAAATAAGTGGCCATGATACTGGAAAGCTGTATGCCATG
AAAGTTTTGAAAAAGGCAACAATCGTTCAAAAGGCCAAAACCACAGAGCATACAAGGACA
GAACGACAAGTCCTGGAACACATTAGGCAGTCGCCATTTTTGGTAACATTACATTATGCT
TTCCAGACAGAAACCAAACTTCATCTCATTTTAGATTATATAAATGGTGGTGAACTTTTT
ACTCATCTTTCTCAAAGAGAGCGTTTCACAGAGCATGAGGTGCAGATTTATGTTGGAGAG
ATTGTGCTTGCCCTCGAACATCTCCACAAGTTGGGGATTATATATCGTGATATTAAGCTT
GAGAATATTCTACTTGATTCTAATGGCCATGTGGTGCTGACAGATTTTGGTCTGAGTAAG
GAGTTTGTGGCTGATGAAACTGAAAGAGCATATTCCTTTTGTGGAACTATTGAATACATG
GCACCAGATATTGTCAGAGGGGGAGATTCAGGACATGACAAGGCAGTTGACTGGTGGAGT
TTGGGTGTTCTAATGTATGAATTACTAACTGGAGCATCTCCTTTCACTGTTGATGGAGAA
AAAAATTCCCAAGCTGAGATATCTAGGAGAATATTAAAAAGTGAGCCTCCATATCCCCAA
GAAATGAGTGCTTTAGCGAAAGACCTAATTCAGCGTCTTTTGATGAAAGATCCCAAGAAG
AGATTGGGATGTGGTCCACGTGATGCAGATGAAATCAAAGAACATCTCTTCTTTCAGAAA
ATAAATTGGGATGATTTAGCCGCCAAAAAAGTGCCTGCACCATTTAAGCCAGTCATTCGA
GATGAATTAGATGTGAGTAACTTTGCAGAAGAGTTCACAGAAATGGATCCCACTTATTCT
CCCGCAGCCCTGCCCCAGAGTTCTGAGAAGCTGTTTCAGGGCTATTCCTTTGTTGCTCCT
TCCATCCTATTCAAGCGTAATGCAGCTGTCATAGACCCTCTTCAGTTTCACATGGGAGTT
GAACGTCCTGGAGTGACAAATGTTGCCAGGAGTGCAATGATGAAGGACTCTCCATTCTAT
CAACACTATGACCTAGATTTGAAGGACAAACCCCTGGGAGAAGGTAGTTTTTCAATTTGT
CGAAAGTGTGTGCATAAAAAAAGTAACCAAGCTTTTGCAGTCAAAATAATCAGCAAAAGG
ATGGAAGCCAATACTCAAAAGGAAATAACAGCTCTGAAACTCTGTGAAGGACACCCCAAT
ATTGTGAAGTTGCATGAAGTTTTTCATGATCAGCTTCACACGTTTCTAGTGATGGAACTT
CTGAATGGAGGAGAACTGTTTGAGCGCATTAAGAAAAAGAAGCACTTCAGTGAGACGGAA
GCCAGCTACATCATGAGGAAGCTTGTTTCAGCTGTAAGCCACATGCATGATGTTGGAGTG
GTGCACAGGGATCTGAAACCTGAGAATTTATTGTTCACCGATGAAAATGACAATTTGGAA
ATTAAAATAATTGATTTTGGATTTGCACGGCTAAAGCCACCGGATAATCAGCCCCTGAAG
ACTCCATGCTTCACCCTTCATTATGCCGCCCCAGAGCTCTTGAATCAGAACGGCTACGAT
GAGTCCTGTGACCTGTGGAGCTTGGGCGTCATTTTGTACACAATGTTGTCAGGACAGGTT
CCCTTCCAATCTCATGACCGAAGTTTGACGTGTACCAGCGCGGTGGAAATCATGAAGAAA
ATTAAAAAGGGAGATTTCTCCTTTGAAGGAGAAGCCTGGAAGAATGTATCCCAAGAGGCT
AAAGATTTGATCCAAGGACTTCTCACAGTAGATCCAAACAAAAGGCTTAAAATGTCTGGC
TTGAGGTACAATGAATGGCTACAAGATGGAAGTCAGCTGTCCTCCAATCCTCTGATGACT
CCGGATATTCTAGGATCTTCCGGAGCTGCCGTGCATACCTGTGTGAAAGCAACCTTCCAC
GCCTTTAACAAATACAAGAGAGAGGGGTTTTGCCTTCAGAATGTTGATAAGGCCCCTTTG
GCTAAGAGAAGAAAAATGAAAAAGACTAGCACCAGTACCGAGACGCGCAGCAGTTCCAGT
GAGAGTTCCCATTCTTCTTCCTCTCATTCTCACGGTAAAACTACACCCACCAAGACACTG
CAGCCCAGCAATCCTGCCGACAGCAATAACCCGGAGACCCTCTTCCAGTTCTCGGACTCA
GTAGCTTAG
Enzyme 42 GenBank Gene ID AF074393 Link Image
Enzyme 42 GeneCard ID RPS6KA5 Link Image
Enzyme 42 GenAtlas ID RPS6KA5 Link Image
Enzyme 42 HGNC ID HGNC:10434 Link Image
Enzyme 42 Chromosome Location 14
Enzyme 42 Locus 14q31-q32.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Deak M, Clifton AD, Lucocq LM, Alessi DR: Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 1998 Aug 3;17(15):4426-41. [PubMed Link Image]
  2. New L, Zhao M, Li Y, Bassett WW, Feng Y, Ludwig S, Padova FD, Gram H, Han J: Cloning and characterization of RLPK, a novel RSK-related protein kinase. J Biol Chem. 1999 Jan 8;274(2):1026-32. [PubMed Link Image]
  3. Jiang C, Yu L, Tu Q, Zhao Y, Zhang H, Zhao S: Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31-->q32.1 by radiation hybrid mapping. Cytogenet Cell Genet. 1999;87(3-4):261-2. [PubMed Link Image]
  4. Vermeulen L, De Wilde G, Van Damme P, Vanden Berghe W, Haegeman G: Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J. 2003 Mar 17;22(6):1313-24. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6794
Enzyme 43 Name Serine/threonine-protein kinase PRKX
Enzyme 43 Synonyms
  1. Protein kinase PKX1
Enzyme 43 Gene Name PRKX
Enzyme 43 Protein Sequence >Serine/threonine-protein kinase PRKX
MEAPGLAQAAAAESDSRKVAEETPDGAPALCPSPEALSPEPPVYSLQDFDTLATVGTGTF
GRVHLVKEKTAKHFFALKVMSIPDVIRLKQEQHVHNEKSVLKEVSHPFLIRLFWTWHDER
FLYMLMEYVPGGELFSYLRNRGRFSSTTGLFYSAEIICAIEYLHSKEIVYRDLKPENILL
DRDGHIKLTDFGFAKKLVDRTWTLCGTPEYLAPEVIQSKGHGRAVDWWALGILIFEMLSG
FPPFFDDNPFGIYQKILAGKIDFPRHLDFHVKDLIKKLLVVDRTRRLGNMKNGANDVKHH
RWFRSVDWEAVPQRKLKPPIVPKIAGDGDTSNFETYPENDWDTAAPVPQKDLEIFKNF
Enzyme 43 Number of Residues 358
Enzyme 43 Molecular Weight 40896
Enzyme 43 Theoretical pI 6.85
Enzyme 43 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • protein-tyrosine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function ATP + a protein = ADP + a phosphoprotein
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 1052737 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P51817 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PRKX_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1077 bp
ATGGAGGCGCCCGGGCTGGCCCAGGCGGCCGCGGCGGAGAGCGACTCCCGCAAGGTGGCG
GAGGAGACCCCCGACGGGGCGCCCGCGCTCTGCCCCAGCCCTGAGGCGCTGTCGCCGGAG
CCGCCTGTGTACAGCCTGCAGGACTTTGACACGCTGGCCACCGTGGGCACTGGGACGTTC
GGGCGGGTGCACCTGGTGAAGGAGAAGACAGCCAAGCATTTCTTCGCCCTCAAGGTGATG
AGCATTCCTGACGTCATCCGCCTAAAGCAGGAGCAACACGTACACAATGAGAAGTCTGTC
CTGAAGGAAGTCAGCCACCCGTTCCTCATCAGGCTGTTCTGGACGTGGCATGACGAGCGC
TTCCTCTACATGCTCATGGAGTACGTGCCGGGCGGCGAGCTCTTCAGCTACCTGCGCAAC
CGGGGGCGCTTCTCCAGCACCACGGGGCTCTTCTACTCTGCAGAGATCATCTGTGCCATC
GAGTACCTGCACTCCAAAGAGATCGTCTACAGGGACTTGAAGCCAGAGAACATCCTGCTG
GATAGGGATGGCCACATTAAGCTCACGGACTTTGGGTTCGCCAAGAAGCTGGTAGACAGG
ACTTGGACCCTCTGTGGAACACCCGAGTACCTAGCCCCCGAAGTCATTCAGAGCAAGGGC
CACGGAAGGGCCGTGGACTGGTGGGCCCTCGGCATCCTGATATTCGAGATGCTTTCGGGG
TTTCCTCCGTTTTTTGATGACAACCCGTTTGGCATTTATCAGAAAATTCTTGCAGGCAAA
ATAGATTTCCCCAGACATTTGGATTTCCATGTAAAAGACCTCATTAAGAAACTGCTCGTG
GTTGACAGAACAAGGCGATTAGGAAACATGAAGAACGGGGCGAATGATGTGAAGCATCAT
CGGTGGTTCCGCTCCGTGGACTGGGAAGCTGTTCCGCAGAGAAAACTGAAGCCTCCCATC
GTGCCCAAGATAGCTGGTGACGGCGACACTTCCAACTTCGAAACTTACCCTGAGAATGAC
TGGGACACAGCCGCGCCCGTGCCGCAGAAGGATTTAGAAATCTTCAAGAATTTCTGA
Enzyme 43 GenBank Gene ID X85545 Link Image
Enzyme 43 GeneCard ID PRKX Link Image
Enzyme 43 GenAtlas ID PRKX Link Image
Enzyme 43 HGNC ID HGNC:9441 Link Image
Enzyme 43 Chromosome Location X
Enzyme 43 Locus Xp22.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Klink A, Schiebel K, Winkelmann M, Rao E, Horsthemke B, Ludecke HJ, Claussen U, Scherer G, Rappold G: The human protein kinase gene PKX1 on Xp22.3 displays Xp/Yp homology and is a site of chromosomal instability. Hum Mol Genet. 1995 May;4(5):869-78. [PubMed Link Image]
  2. Schiebel K, Winkelmann M, Mertz A, Xu X, Page DC, Weil D, Petit C, Rappold GA: Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y-)XY females. Hum Mol Genet. 1997 Oct;6(11):1985-9. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6826
Enzyme 44 Name Serine/threonine-protein kinase 11
Enzyme 44 Synonyms
  1. Serine/threonine- protein kinase LKB1
  2. Renal carcinoma antigen NY-REN-19
Enzyme 44 Gene Name STK11
Enzyme 44 Protein Sequence >Serine/threonine-protein kinase 11
MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSY
GKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNE
EKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPG
NLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWS
AGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSI
RQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDI
IYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSA
SSKIRRLSACKQQ
Enzyme 44 Number of Residues 433
Enzyme 44 Molecular Weight 48636
Enzyme 44 Theoretical pI 7.47
Enzyme 44 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
Component
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Essential role in G1 cell cycle arrest. Phosphorylates and activates members of the AMPK-related subfamily of protein kinases. Tumor suppressor
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 2754827 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q15831 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name STK11_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1302 bp
ATGGAGGTGGTGGACCCGCAGCAGC