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Human Metabolome Database Version 2.5

 

Showing metabocard for Aldosterone (HMDB00037)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:39
Accession Number HMDB00037
Secondary Accession Numbers Not Available
Common Name Aldosterone
Description Aldosterone is a steroid hormone produced by the adrenal cortex in the adrenal gland to regulate sodium and potassium balance in the blood. Specifically it regulates electrolyte and water balance by increasing the renal retention of sodium and the excretion of potassium. It is synthesized from cholesterol by aldosterone synthase, which is absent in other sections of the adrenal gland. It is the sole endogenous member of the class of mineralocorticoids. Aldosterone increases the permeability of the apical (luminal) membrane of the kidney's collecting ducts to potassium and sodium and activates their basolateral Na+/K+ pumps, stimulating ATP hydrolysis, reabsorbing sodium (Na+) ions and water into the blood, and excreting potassium (K+) ions into the urine.
Synonyms
  1. (+)-Aldosterone
  2. (11b)-11,21-dihydroxy-3,20-dioxo-pregn-4-en-18-al
  3. (11beta)-11,21-dihydroxy-3,20-dioxo-Pregn-4-en-18-al
  4. 11,21-Dihydroxy-3,20-dioxopregn-4-en-18-al
  5. 11-hydroxy-17-(2-hydroxyacetyl)-10-methyl-3-oxo-1,2,6,7,8,9,10,11,12,13,14,15,16,17-tetradecahydrocyclopenta[a]phenanthrene-13-carbaldehyde
  6. 11b,21-dihydroxy-3,20-dioxo-pregn-4-en-18-al
  7. 11beta,21-Dihydroxy-3,20-diketo-4-pregnen-18-al
  8. 11beta,21-Dihydroxy-3,20-diketopregn-4-ene-18-al
  9. 11beta,21-Dihydroxy-3,20-dioxo-pregn-4-en-18-al
  10. 11beta,21-Dihydroxypregn-4-ene-3,18,20-trione
  11. 18-Formyl-11beta,21-dihydroxy-4-pregnene-3,20-dione
  12. 18-Oxocorticosterone
  13. Aldocorten
  14. Aldocortene
  15. Aldocortin
  16. Aldosteronum
  17. Electrocortin
  18. Elektrocortin
  19. Reichstein X
  20. aldosterone
  21. d-Aldosterone
  22. delta-Aldosterone
Chemical IUPAC Name 11-hydroxy-17-(2-hydroxyacetyl)-10-methyl-3-oxo-1,2,6,7,8,9,11,12,14,15,16,17-dodecahydrocyclopenta[a]phenanthrene-13-carbaldehyde
Chemical Formula C21H28O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • ketone
  • primary alcohol
  • secondary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
Source
  • Endogenous
Average Molecular Weight 360.444
Monoisotopic Molecular Weight 360.193665
Isomeric SMILES C[C@]12CCC(=O)C=C1CCC1C3CC[C@H](C(=O)CO)[C@]3(C[C@H](O)C21)C=O
Canonical SMILES CC12CCC(=O)C=C1CCC1C3CCC(C(=O)CO)C3(CC(O)C21)C=O
KEGG Compound ID C01780 Link Image
BioCyc ID ALDOSTERONE Link Image
BiGG ID 38397 Link Image
Wikipedia Link Aldosterone Link Image
NuGOwiki Link HMDB00037 Link Image
Metagene Link HMDB00037 Link Image
METLIN ID 418 Link Image
PubChem Compound 5839 Link Image
PubChem Substance 841789 Link Image
ChEBI ID 27584 Link Image
CAS Registry Number 52-39-1
InChI Identifier InChI=1/C21H28O5/c1-20-7-6-13(24)8-12(20)2-3-14-15-4-5-16(18(26)10-22)21(15,11-23)9-17(25)19(14)20/h8,11,14-17,19,22,25H,2-7,9-10H2,1H3/t14?,15?,16-,17+,19?,20+,21-/m1/s1
Synthesis Reference Bear, Brian R.; Parnes, Jason S.; Shea, Kenneth J. Progress toward the Total Synthesis of (+)-Aldosterone: Synthesis of the A-D Rings. Organic Letters (2003), 5(10), 1613-1616.
Melting Point (Experimental) 166.5 oC
Experimental Water Solubility 0.0512 mg/mL at 37 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 0.148 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity 1.08 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 1.54 [Predicted by ALOGPS]; 0.2 [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 (Bruker)
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 Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Adrenal Cortex
Adrenal Gland
Adrenal Medulla
Cardiovascular System
Fibroblasts
Intestine
Kidney
Lung
Muscle
Nerve Cells
Pancreas
Placenta
Platelet
Skeletal Muscle
Testes
Thyroid Gland
Concentrations (Normal)
Biofluid Blood
Value 0.000026 (0.000008 - 0.000044) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wu AHB. Tietz clinical guide to laboratory tests. 4th ed. St. Louis: Saunders/Elsevier, 2006.
Biofluid Blood
Value 0.00011 (0.000055 - 0.002) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Touger L, Joseph M, Hasan KS: Hypertension in a patient with aldosterone deficiency. Endocr Pract. 2005 Mar-Apr;11(2):104-7. [PubMed Link Image]
Biofluid Blood
Value 0.00042 +/- 0.00004 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments In plasma after 8 days of low-salt intake
References
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
Biofluid Blood
Value 0.000282 +/- 0.000037 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments In plasma from subjects older than 55 years after low-salt intake
References
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
Biofluid Blood
Value 0.000263 +/- 0.000014 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments In plasma from subjects less than 30 yo after normal salt-intake
References
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
Biofluid Saliva
Value <1.00 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Few JD, Chaudry S, James VH: The direct determination of aldosterone in human saliva. J Steroid Biochem. 1984 Jul;21(1):87-92. [PubMed Link Image]
Biofluid Urine
Value 0.01 (0.006-0.014) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wu AHB. Tietz clinical guide to laboratory tests. 4th ed. St. Louis: Saunders/Elsevier, 2006.
Concentrations (Abnormal)
Biofluid Blood
Value 0.00041 +/- 0.00005 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments In plasma after 8 days of low-salt intake
References
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
Biofluid Blood
Value 0.000233 +/- 0.000040 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments In plasma after 8 days of normal-salt intake
References
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
Associated Disorders
Condition References
Heart failure
  • Ferreira A, Bettencourt P, Pestana M, Correia F, Serrao P, Martins L, Cerqueira-Gomes M, Soares-Da-Silva P: Heart failure, aging, and renal synthesis of dopamine. Am J Kidney Dis. 2001 Sep;38(3):502-9. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroidogenesis SMP00130 Link Image map00140 Link Image
General References
  1. Funder JW: The nongenomic actions of aldosterone. Endocr Rev. 2005 May;26(3):313-21. Epub 2005 Apr 6. [PubMed Link Image]
  2. Shima H, Kawanaka H, Yabumoto Y, Okamoto E, Ikoma F: A case of 17 alpha-hydroxylase deficiency with chromosomal karyotype 46,XY and high plasma aldosterone concentration. Int Urol Nephrol. 1991;23(6):611-8. [PubMed Link Image]
  3. Rosendahl W, Konig M, Haack D, Vecsei P, Lewicka S: [Variability of corticosterone methyl oxidase (type II) deficiency. Presentation of three case reports] Klin Padiatr. 1993 May-Jun;205(3):180-4. [PubMed Link Image]
  4. Christ M, Zange J, Janson CP, Muller K, Kuklinski P, Schmidt BM, Tillmann HC, Gerzer R, Wehling M: Hypoxia modulates rapid effects of aldosterone on oxidative metabolism in human calf muscle. J Endocrinol Invest. 2001 Sep;24(8):587-97. [PubMed Link Image]
  5. Lijnen P, Petrov V: Induction of cardiac fibrosis by aldosterone. J Mol Cell Cardiol. 2000 Jun;32(6):865-79. [PubMed Link Image]
  6. du Cheyron D, Lesage A, Daubin C, Ramakers M, Charbonneau P: Hyperreninemic hypoaldosteronism: a possible etiological factor of septic shock-induced acute renal failure. Intensive Care Med. 2003 Oct;29(10):1703-9. Epub 2003 Aug 28. [PubMed Link Image]
  7. Laskowska M, Leszczynska-Gorzelak B, Laskowska K, Oleszczuk J: Evaluation of the renin-angiotensin-aldosterone system in pregnancy complicated by preeclampsia with and without intrauterine growth retardation. Ann Univ Mariae Curie Sklodowska [Med]. 2004;59(2):451-6. [PubMed Link Image]
  8. Few JD, Chaudry S, James VH: The direct determination of aldosterone in human saliva. J Steroid Biochem. 1984 Jul;21(1):87-92. [PubMed Link Image]
  9. Cicoira M, Zanolla L, Franceschini L, Rossi A, Golia G, Zeni P, Caruso B, Zardini P: Relation of aldosterone &quot;escape&quot; despite angiotensin-converting enzyme inhibitor administration to impaired exercise capacity in chronic congestive heart failure secondary to ischemic or idiopathic dilated cardiomyopathy. Am J Cardiol. 2002 Feb 15;89(4):403-7. [PubMed Link Image]
  10. Goodfriend TL, Kelley DE, Goodpaster BH, Winters SJ: Visceral obesity and insulin resistance are associated with plasma aldosterone levels in women. Obes Res. 1999 Jul;7(4):355-62. [PubMed Link Image]
  11. Lewicka S, Vecsei P, Bige K, Fisher T, Winter J, Abdelhamid S, Heinrich U, Bokkenheuser VD: Urinary excretion of aldosterone metabolite Kelly-M1 in patients with adrenal dysfunction. J Steroid Biochem. 1988 Mar;29(3):333-9. [PubMed Link Image]
  12. Heindl S, Holzschneider J, Hinz A, Sayk F, Fehm HL, Dodt C: Acute effects of aldosterone on the autonomic nervous system and the baroreflex function in healthy humans. J Neuroendocrinol. 2006 Feb;18(2):115-21. [PubMed Link Image]
  13. Engeli S, Bohnke J, Gorzelniak K, Janke J, Schling P, Bader M, Luft FC, Sharma AM: Weight loss and the renin-angiotensin-aldosterone system. Hypertension. 2005 Mar;45(3):356-62. Epub 2005 Jan 3. [PubMed Link Image]
  14. Velazquez H, Perazella MA, Wright FS, Ellison DH: Renal mechanism of trimethoprim-induced hyperkalemia. Ann Intern Med. 1993 Aug 15;119(4):296-301. [PubMed Link Image]
  15. Touger L, Joseph M, Hasan KS: Hypertension in a patient with aldosterone deficiency. Endocr Pract. 2005 Mar-Apr;11(2):104-7. [PubMed Link Image]
  16. Summa V, Camargo SM, Bauch C, Zecevic M, Verrey F: Isoform specificity of human Na(+), K(+)-ATPase localization and aldosterone regulation in mouse kidney cells. J Physiol. 2004 Mar 1;555(Pt 2):355-64. Epub 2003 Dec 23. [PubMed Link Image]
  17. Fox CS, Larson MG, Hwang SJ, Leip EP, Rifai N, Levy D, Benjamin EJ, Murabito JM, Meigs JB, Vasan RS: Cross-sectional relations of serum aldosterone and urine sodium excretion to urinary albumin excretion in a community-based sample. Kidney Int. 2006 Jun;69(11):2064-9. [PubMed Link Image]
  18. Badalian SS, Mikhailov AV: [Characteristics of the renin-aldosterone system of the fetoplacental complex in fetal erythroblastosis] Akush Ginekol (Mosk). 1990 May;(5):55-8. [PubMed Link Image]
  19. Tanemoto M, Abe T, Obara N, Abe M, Satoh F, Ito S: Successful treatment of severe hypertension with the combination of angiotensin converting enzyme inhibitor and angiotensin II receptor blocker. Hypertens Res. 2003 Oct;26(10):863-8. [PubMed Link Image]
  20. Pitt B, Stier CT Jr, Rajagopalan S: Mineralocorticoid receptor blockade: new insights into the mechanism of action in patients with cardiovascular disease. J Renin Angiotensin Aldosterone Syst. 2003 Sep;4(3):164-8. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Cytochrome P450 11B1, mitochondrial precursor
  2. Cytochrome P450 11B2, mitochondrial precursor
  3. 3-oxo-5-beta-steroid 4-dehydrogenase
  4. Serine/threonine-protein kinase Sgk1
  5. Epidermal growth factor receptor precursor
  6. Serine/threonine-protein kinase D1
  7. Glucocorticoid receptor
  8. Fibronectin precursor
  9. Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32
  10. Connective tissue growth factor precursor
  11. Type-1 angiotensin II receptor
  12. Mineralocorticoid receptor
  13. ADM precursor [Contains: Adrenomedullin
  14. Prostaglandin E2 receptor, EP4 subtype
  15. Melanophilin
  16. Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
Enzyme 1 [top]
Enzyme 1 ID 5683
Enzyme 1 Name Cytochrome P450 11B1, mitochondrial precursor
Enzyme 1 Synonyms
  1. CYPXIB1
  2. P450C11
  3. P-450c11
  4. Steroid 11-beta-hydroxylase
Enzyme 1 Gene Name CYP11B1
Enzyme 1 Protein Sequence >Cytochrome P450 11B1, mitochondrial precursor
MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPQRPGNRWLRLLQIWREQG
YEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELS
PDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRP
ERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQED
IKMVYSFILRPSMCPLLTFRAIN
Enzyme 1 Number of Residues 503
Enzyme 1 Molecular Weight 57530
Enzyme 1 Theoretical pI 9.42
Enzyme 1 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 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Has steroid 11-beta-hydroxylase activity. In addition to this activity, the 18 or 19-hydroxylation of steroids and the aromatization of androstendione to estrone have also been ascribed to cytochrome P450 XIB
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a steroid + reduced adrenal ferredoxin + O2 = an 11beta-hydroxysteroid + oxidized adrenal ferredoxin + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-23
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181333 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P15538 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name C11B1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCATGGCAGTGCCCTGGCTGTCCCTGCAAAGG
GCACAGGCACTGGGCACGAGAGCCGCCCGGGTCCCCAGGACAGTGCTGCCCTTTGAAGCC
ATGCCCCGGCGTCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATCTGGAGGGAGCAGGGT
TATGAGGACCTGCACCTGGAAGTACACCAGACCTTCCAGGAACTGGGGCCCATTTTCAGG
TACGATTTGGGAGGAGCAGGCATGGTGTGTGTGATGCTGCCGGAGGACGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCCACAGGATGAGCCTGGAGCCCTGGGTGGCCTACAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGCTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAATCCAGAAGTGCTGTCGCCCAACGCTGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTCTCCCAGGCCCTGAAGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTGGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGACCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGCGACAACTGTATCCAGAAAATCTATCAGGAACTGGCCTTC
AGCCGCCCTCAACAGTACACCAGCATCGTGGCGGAGCTCCTGTTGAATGCGGAACTGTCG
CCAGATGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACGGTG
TTTCCCTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCAACGTGCAGCAGGCCCTG
CGCCAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTGCCCTTGCTGCGTGCGGCCCTCAAGGAGACCTTGCGGCTCTACCCTGTGGGTCTG
TTTCTGGAGCGAGTGGCGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTGCGCGTGTTCCTCTACTCTCTGGGTCGCAACCCCGCCTTGTTCCCGAGGCCT
GAGCGCTATAACCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTCTACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTTGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCATGTGCTGAAACACCTCCAGGTGGAGACACTAACCCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCCAGCATGTGCCCCCTCCTCACCTTCAGA
GCCATCAACTAA
Enzyme 1 GenBank Gene ID M32879 Link Image
Enzyme 1 GeneCard ID CYP11B1 Link Image
Enzyme 1 GenAtlas ID CYP11B1 Link Image
Enzyme 1 HGNC ID HGNC:2591 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed Link Image]
  2. Kawamoto T, Mitsuuchi Y, Toda K, Miyahara K, Yokoyama Y, Nakao K, Hosoda K, Yamamoto Y, Imura H, Shizuta Y: Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta. FEBS Lett. 1990 Sep 3;269(2):345-9. [PubMed Link Image]
  3. Naiki Y, Kawamoto T, Mitsuuchi Y, Miyahara K, Toda K, Orii T, Imura H, Shizuta Y: A nonsense mutation (TGG [Trp116]--&gt;TAG [Stop]) in CYP11B1 causes steroid 11 beta-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Dec;77(6):1677-82. [PubMed Link Image]
  4. Chua SC, Szabo P, Vitek A, Grzeschik KH, John M, White PC: Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11). Proc Natl Acad Sci U S A. 1987 Oct;84(20):7193-7. [PubMed Link Image]
  5. Kawamoto T, Mitsuuchi Y, Toda K, Yokoyama Y, Miyahara K, Miura S, Ohnishi T, Ichikawa Y, Nakao K, Imura H, et al.: Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1458-62. [PubMed Link Image]
  6. White PC, Dupont J, New MI, Leiberman E, Hochberg Z, Rosler A: A mutation in CYP11B1 (Arg-448----His) associated with steroid 11 beta-hydroxylase deficiency in Jews of Moroccan origin. J Clin Invest. 1991 May;87(5):1664-7. [PubMed Link Image]
  7. Joehrer K, Geley S, Strasser-Wozak EM, Azziz R, Wollmann HA, Schmitt K, Kofler R, White PC: CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11 beta-hydroxylase deficiency. Hum Mol Genet. 1997 Oct;6(11):1829-34. [PubMed Link Image]
  8. Loidi L, Quinteiro C, Barros F, Dominguez F, Barreiro J, Pombo M: The C494F variant in the CYP11B1 gene is a sequence polymorphism in the Spanish population. J Clin Endocrinol Metab. 1999 Dec;84(12):4749. [PubMed Link Image]
  9. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  10. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5808
Enzyme 2 Name Cytochrome P450 11B2, mitochondrial precursor
Enzyme 2 Synonyms
  1. CYPXIB2
  2. P-450Aldo
  3. Aldosterone synthase
  4. ALDOS
  5. Aldosterone-synthesizing enzyme
  6. Steroid 18-hydroxylase
  7. P-450C18
Enzyme 2 Gene Name CYP11B2
Enzyme 2 Protein Sequence >Cytochrome P450 11B2, mitochondrial precursor
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
Enzyme 2 Number of Residues 503
Enzyme 2 Molecular Weight 57561
Enzyme 2 Theoretical pI 9.78
Enzyme 2 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 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone
Enzyme 2 Pathways
Enzyme 2 Reactions
  • corticosterone + reduced adrenal ferredoxin + O2 = 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 181340 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P19099 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name C11B2_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1512 bp
ATGGCACTCAGGGCAAAGGCAGAGGTGTGCGTGGCAGCGCCCTGGCTGTGCCTGCAAAGG
GCACGGGCACTGGGCACTAGAGCCGCTCGGGCCCCTAGGACGGTGCTGCCGTTTGAAGCC
ATGCCCCAGCATCCAGGCAACAGGTGGCTGAGGCTGCTGCAGATGTGGAGGGAGCAGGGT
TATGAGCACCTGCACCTGGAGATGCACCAGACCTTCCAGGAGCTGGGGCCCATTTTCAGG
TACAACTTGGGAGGACCACGCATGGTGTGTGTGATGCTGCCGGAGGATGTGGAGAAGCTG
CAACAGGTGGACAGCCTGCATCCCTGCAGGATGATCCTGGAGCCCTGGGTGGCCATCAGA
CAACATCGTGGGCACAAATGTGGCGTGTTCTTGTTGAATGGGCCTGAATGGCGCTTCAAC
CGATTGCGGCTGAACCCAGATGTGCTGTCGCCCAAGGCCGTGCAGAGGTTCCTCCCGATG
GTGGATGCAGTGGCCAGGGACTTTTCCCAGGCCCTGAGGAAGAAGGTGCTGCAGAACGCC
CGGGGGAGCCTGACCCTGGACGTCCAGCCCAGCATCTTCCACTACACCATAGAAGCCAGC
AACTTAGCTCTTTTTGGAGAGCGGCTGGGCCTGGTTGGCCACAGCCCCAGTTCTGCCAGC
CTGAACTTCCTCCATGCCCTGGAGGTCATGTTCAAATCCACCGTCCAGCTCATGTTCATG
CCCAGGAGCCTGTCTCGCTGGATCAGCCCCAAGGTGTGGAAGGAGCACTTTGAGGCCTGG
GACTGCATCTTCCAGTACGGTGACAACTGTATCCAGAAAATCTACCAGGAACTGGCCTTC
AACCGCCCTCAACACTACACAGGCATCGTGGCAGAGCTCCTGTTGAAGGCGGAACTGTCA
CTAGAAGCCATCAAGGCCAACTCTATGGAACTCACTGCAGGGAGCGTGGACACGACAGCG
TTTCCGTTGCTGATGACGCTCTTTGAGCTGGCTCGGAACCCCGACGTGCAGCAGATCCTG
CGCAAGGAGAGCCTGGCCGCCGCAGCCAGCATCAGTGAACATCCCCAGAAGGCAACCACC
GAGCTGCCCTTGCTGCGGGCGGCCCTCAAGGAGACCTTGAGGCTCTACCCTGTGGGTCTG
TTTTTGGAGCGAGTGGTGAGCTCAGACTTGGTGCTTCAGAACTACCACATCCCAGCTGGG
ACATTGGTACAGGTTTTCCTCTACTCGCTGGGTCGCAATGCCGCCTTGTTCCCGAGGCCT
GAGCGGTATAATCCCCAGCGCTGGCTAGACATCAGGGGCTCCGGCAGGAACTTGCACCAC
GTGCCCTTTGGCTTTGGCATGCGCCAGTGCCTCGGGCGGCGCCTGGCAGAGGCAGAGATG
CTGCTGCTGCTGCACCACGTGCTGAAGCGCTTCCTGGTGGAGACACTAACTCAAGAGGAC
ATAAAGATGGTCTACAGCTTCATATTGAGGCCTGGCACGTCCCCCCTCCTCACTTTCAGA
GCGATTAACTAG
Enzyme 2 GenBank Gene ID M32881 Link Image
Enzyme 2 GeneCard ID CYP11B2 Link Image
Enzyme 2 GenAtlas ID CYP11B2 Link Image
Enzyme 2 HGNC ID HGNC:2592 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q21-q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Mornet E, Dupont J, Vitek A, White PC: Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). J Biol Chem. 1989 Dec 15;264(35):20961-7. [PubMed Link Image]
  2. Kawainoto T, Mitsuuchi Y, Ohnishi T, Ichikawa Y, Yokoyama Y, Sumimoto H, Toda K, Miyahara K, Kuribayashi I, Nakao K, et al.: Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism. Biochem Biophys Res Commun. 1990 Nov 30;173(1):309-16. [PubMed Link Image]
  3. Pascoe L, Curnow KM, Slutsker L, Rosler A, White PC: Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4996-5000. [PubMed Link Image]
  4. Mitsuuchi Y, Kawamoto T, Naiki Y, Miyahara K, Toda K, Kuribayashi I, Orii T, Yasuda K, Miura K, Nakao K, et al.: Congenitally defective aldosterone biosynthesis in humans: the involvement of point mutations of the P-450C18 gene (CYP11B2) in CMO II deficient patients. Biochem Biophys Res Commun. 1992 Jan 31;182(2):974-9. [PubMed Link Image]
  5. Mitsuuchi Y, Kawamoto T, Miyahara K, Ulick S, Morton DH, Naiki Y, Kuribayashi I, Toda K, Hara T, Orii T, et al.: Congenitally defective aldosterone biosynthesis in humans: inactivation of the P-450C18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients. Biochem Biophys Res Commun. 1993 Feb 15;190(3):864-9. [PubMed Link Image]
  6. Nomoto S, Massa G, Mitani F, Ishimura Y, Miyahara K, Toda K, Nagano I, Yamashiro T, Ogoshi S, Fukata J, Onishi S, Hashimoto K, Doi Y, Imura H, Shizuta Y: CMO I deficiency caused by a point mutation in exon 8 of the human CYP11B2 gene encoding steroid 18-hydroxylase (P450C18). Biochem Biophys Res Commun. 1997 May 19;234(2):382-5. [PubMed Link Image]
  7. Peter M, Bunger K, Solyom J, Sippell WG: Mutation THR-185 ILE is associated with corticosterone methyl oxidase deficiency type II. Eur J Pediatr. 1998 May;157(5):378-81. [PubMed Link Image]
  8. Portrat-Doyen S, Tourniaire J, Richard O, Mulatero P, Aupetit-Faisant B, Curnow KM, Pascoe L, Morel Y: Isolated aldosterone synthase deficiency caused by simultaneous E198D and V386A mutations in the CYP11B2 gene. J Clin Endocrinol Metab. 1998 Nov;83(11):4156-61. [PubMed Link Image]
  9. Tamaki S, Iwai N, Tsujita Y, Kinoshita M: Genetic polymorphism of CYP11B2 gene and hypertension in Japanese. Hypertension. 1999 Jan;33(1 Pt 2):266-70. [PubMed Link Image]
  10. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  11. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  12. Kayes-Wandover KM, Schindler RE, Taylor HC, White PC: Type 1 aldosterone synthase deficiency presenting in a middle-aged man. J Clin Endocrinol Metab. 2001 Mar;86(3):1008-12. [PubMed Link Image]
  13. Dunlop FM, Crock PA, Montalto J, Funder JW, Curnow KM: A compound heterozygote case of type II aldosterone synthase deficiency. J Clin Endocrinol Metab. 2003 Jun;88(6):2518-26. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Freel EM, Ingram M, Wallace AM, White A, Fraser R, Davies E, Connell JM: Effect of variation in CYP11B1 and CYP11B2 on corticosteroid phenotype and hypothalamic-pituitary-adrenal axis activity in hypertensive and normotensive subjects. Clin Endocrinol (Oxf). 2008 May;68(5):700-6. Epub 2007 Nov 2. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 5822
Enzyme 3 Name 3-oxo-5-beta-steroid 4-dehydrogenase
Enzyme 3 Synonyms
  1. Delta(4-3- ketosteroid 5-beta-reductase
  2. Aldo-keto reductase family 1 member D1
Enzyme 3 Gene Name AKR1D1
Enzyme 3 Protein Sequence >3-oxo-5-beta-steroid 4-dehydrogenase
MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQN
EHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIE
VPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELIL
NKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLK
DALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE
ALNKNVRFVELLMWRDHPEYPFHDEY
Enzyme 3 Number of Residues 326
Enzyme 3 Molecular Weight 37377
Enzyme 3 Theoretical pI 7.58
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7- alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- cholesten-3-one can also act as substrates
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 4,5beta-dihydrocortisone + NADP+ = cortisone + NADPH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 431857 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P51857 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name AK1D1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >981 bp
ATGGATCTCAGTGCTGCAAGTCACCGCATACCTCTAAGTGATGGAAACAGCATTCCCATC
ATCGGACTTGGTACCTACTCAGAACCTAAATCGACCCCTAAGGGAGCCTGTGCAACATCG
GTGAAGGTTGCTATTGACACAGGGTACCGACATATTGATGGGGCCTACATCTACCAAAAT
GAACACGAAGTTGGGGAGGCCATCAGGGAGAAGATAGCAGAAGGAAAGGTGCGGAGGGAA
GATATCTTCTACTGTGGAAAGCTATGGGCTACAAATCATGTCCCAGAGATGGTCCGCCCA
ACCCTGGAGAGGACACTCAGGGTCCTCCAGCTAGATTATGTGGATCTTTACATCATTGAA
GTACCCATGGCCTTTAAGCCAGGAGATGAAATATACCCTAGAGATGAGAATGGCAAATGG
TTATATCACAAGTCAAATCTGTGTGCCACTTGGGAGGCGATGGAAGCTTGCAAAGACGCT
GGCTTGGTGAAATCCCTGGGAGTGTCCAATTTTAACCGCAGGCAGCTGGAGCTCATCCTG
AACAAGCCAGGACTCAAACACAAGCCAGTCAGCAACCAGGTTGAGTGCCATCCGTATTTC
ACCCAGCCAAAACTCTTGAAATTTTGCCAACAACATGACATTGTCATTACTGCATATAGC
CCTTTGGGGACCAGTAGGAATCCAATCTGGGTGAATGTTTCTTCTCCACCTTTGTTAAAG
GATGCACTTCTAAACTCATTGGGGAAAAGGTACAATAAGACAGCAGCTCAAATTGTTTTG
CGTTTCAACATCCAGCGAGGGGTGGTTGTCATTCCTAAAAGCTTTAATCTTGAAAGGATC
AAAGAAAATTTTCAGATCTTTGACTTTTCTCTCACTGAAGAAGAAATGAAGGACATTGAA
GCCTTGAATAAAAATGTCCGCTTTGTAGAATTGCTCATGTGGCGCGATCATCCTGAATAC
CCATTTCATGATGAATACTGA
Enzyme 3 GenBank Gene ID Z28339 Link Image
Enzyme 3 GeneCard ID AKR1D1 Link Image
Enzyme 3 GenAtlas ID AKR1D1 Link Image
Enzyme 3 HGNC ID HGNC:388 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q32-q33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Setoguchi T, Okuda KI, Bjorkhem I: Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme. Eur J Biochem. 1994 Jan 15;219(1-2):357-63. [PubMed Link Image]
  2. Charbonneau A, The VL: Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim Biophys Acta. 2001 Jan 26;1517(2):228-35. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6554
Enzyme 4 Name Serine/threonine-protein kinase Sgk1
Enzyme 4 Synonyms
  1. Serum/glucocorticoid-regulated kinase 1
Enzyme 4 Gene Name SGK
Enzyme 4 Protein Sequence >Serine/threonine-protein kinase Sgk1
MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKI
SQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAE
EVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYIN
GGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTD
FGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSR
NTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINW
DDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLG
FSYAPPTDSFL
Enzyme 4 Number of Residues 431
Enzyme 4 Molecular Weight 48943
Enzyme 4 Theoretical pI 8.81
Enzyme 4 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 4 General Function Not Available
Enzyme 4 Specific Function Protein kinase that plays an important role in cellular stress response. Activates certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Mediates cell survival signals, phosphorylates and negatively regulates pro-apoptotic FOXO3A. Phosphorylates NEDD4L, which leads to its inactivation and to the subsequent activation of various channels and transporters such as ENaC, Kv1.3, or EAAT1
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1834511 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O00141 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SGK1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1296 bp
ATGACGGTGAAAACTGAGGCTGCTAAGGGCACCCTCACTTACTCCAGGATGAGGGGCATG
GTGGCAATTCTCATCGCTTTCATGAAGCAGAGGAGGATGGGTCTGAACGACTTTATTCAG
AAGATTGCCAATAACTCCTATGCATGCAAACACCCTGAAGTTCAGTCCATCTTGAAGATC
TCCCAACCTCAGGAGCCTGAGCTTATGAATGCCAACCCTTCTCCTCCACCAAGTCCTTCT
CAGCAAATCAACCTTGGCCCGTCGTCCAATCCTCATGCTAAACCATCTGACTTTCACTTC
TTGAAAGTGATCGGAAAGGGCAGTTTTGGAAAGGTTCTTCTAGCAAGACACAAGGCAGAA
GAAGTGTTCTATGCAGTCAAAGTTTTACAGAAGAAAGCAATCCTGAAAAAGAAAGAGGAG
AAGCATATTATGTCGGAGCGGAATGTTCTGTTGAAGAATGTGAAGCACCCTTTCCTGGTG
GGCCTTCACTTCTCTTTCCAGACTGCTGACAAATTGTACTTTGTCCTAGACTACATTAAT
GGTGGAGAGTTGTTCTACCATCTCCAGAGGGAACGCTGCTTCCTGGAACCACGGGCTCGT
TTCTATGCTGCTGAAATAGCCAGTGCCTTGGGCTACCTGCATTCACTGAACATCGTTTAT
AGAGACTTAAAACCAGAGAATATTTTGCTAGATTCACAGGGACACATTGTCCTTACTGAT
TTCGGACTCTGCAAGGAGAACATTGAACACAACAGCACAACATCCACCTTCTGTGGCACG
CCGGAGTATCTCGCACCTGAGGTGCTTCATAAGCAGCCTTATGACAGGACTGTGGACTGG
TGGTGCCTGGGAGCTGTCTTGTATGAGATGCTGTATGGCCTGCCGCCTTTTTATAGCCGA
AACACAGCTGAAATGTACGACAACATTCTGAACAAGCCTCTCCAGCTGAAACCAAATATT
ACAAATTCCGCAAGACACCTCCTGGAGGGCCTCCTGCAGAAGGACAGGACAAAGCGGCTC
GGGGCCAAGGATGACTTCATGGAGATTAAGAGTCATGTCTTCTTCTCCTTAATTAACTGG
GATGATCTCATTAATAAGAAGATTACTCCCCCTTTTAACCCAAATGTGAGTGGGCCCAAC
GAGCTACGGCACTTTGACCCCGAGTTTACCGAAGAGCCTGTCCCCAACTCCATTGGCAAG
TCCCCTGACAGCGTCCTCGTCACAGCCAGCGTCAAGGAAGCTGCCGAGGCTTTCCTAGGC
TTTTCCTATGCGCCTCCCACGGACTCTTTCCTCTGA
Enzyme 4 GenBank Gene ID Y10032 Link Image
Enzyme 4 GeneCard ID SGK Link Image
Enzyme 4 GenAtlas ID SGK Link Image
Enzyme 4 HGNC ID HGNC:10810 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6q23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Waldegger S, Barth P, Raber G, Lang F: Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4440-5. [PubMed Link Image]
  2. Waldegger S, Erdel M, Nagl UO, Barth P, Raber G, Steuer S, Utermann G, Paulmichl M, Lang F: Genomic organization and chromosomal localization of the human SGK protein kinase gene. Genomics. 1998 Jul 15;51(2):299-302. [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. Kobayashi T, Deak M, Morrice N, Cohen P: Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem J. 1999 Nov 15;344 Pt 1:189-97. [PubMed Link Image]
  5. Kobayashi T, Cohen P: Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem J. 1999 Apr 15;339 ( Pt 2):319-28. [PubMed Link Image]
  6. Lang F, Klingel K, Wagner CA, Stegen C, Warntges S, Friedrich B, Lanzendorfer M, Melzig J, Moschen I, Steuer S, Waldegger S, Sauter M, Paulmichl M, Gerke V, Risler T, Gamba G, Capasso G, Kandolf R, Hebert SC, Massry SG, Broer S: Deranged transcriptional regulation of cell-volume-sensitive kinase hSGK in diabetic nephropathy. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):8157-62. [PubMed Link Image]
  7. Brunet A, Park J, Tran H, Hu LS, Hemmings BA, Greenberg ME: Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol Cell Biol. 2001 Feb;21(3):952-65. [PubMed Link Image]
  8. Gamper N, Fillon S, Feng Y, Friedrich B, Lang PA, Henke G, Huber SM, Kobayashi T, Cohen P, Lang F: K+ channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK. Pflugers Arch. 2002 Oct;445(1):60-6. Epub 2002 Aug 28. [PubMed Link Image]
  9. Maiyar AC, Leong ML, Firestone GL: Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain. Mol Biol Cell. 2003 Mar;14(3):1221-39. [PubMed Link Image]
Enzyme 4 Metabolite References
  1. Cordas E, Naray-Fejes-Toth A, Fejes-Toth G: Subcellular location of serum- and glucocorticoid-induced kinase-1 in renal and mammary epithelial cells. Am J Physiol Cell Physiol. 2007 May;292(5):C1971-81. Epub 2007 Jan 3. [PubMed Link Image]
Enzyme 5 [top]
Enzyme 5 ID 6752
Enzyme 5 Name Epidermal growth factor receptor precursor
Enzyme 5 Synonyms
  1. Receptor tyrosine-protein kinase ErbB-1
Enzyme 5 Gene Name EGFR
Enzyme 5 Protein Sequence >Epidermal growth factor receptor precursor
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI
CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA
RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ
QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED
SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN
TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
APQSSEFIGA
Enzyme 5 Number of Residues 1210
Enzyme 5 Molecular Weight 134279
Enzyme 5 Theoretical pI 6.67
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • epidermal growth factor receptor activity
  • kinase activity
  • nucleotide binding
  • protein kinase activity
  • protein-tyrosine kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transmembrane receptor protein tyrosine kinase activity
Process
  • biopolymer metabolism
  • biopolymer modification
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • enzyme linked receptor protein signaling pathway
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
  • signal transduction
  • transmembrane receptor protein tyrosine kinase signaling pathway
Component
  • cell
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Isoform 2/truncated isoform may act as an antagonist
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-24
Enzyme 5 Transmembrane Regions
  • 646-668
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 757924 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P00533 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name EGFR_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >3633 bp
ATGCGACCCTCCGGGACGGCCGGGGCAGCGCTCCTGGCGCTGCTGGCTGCGCTCTGCCCG
GCGAGTCGGGCTCTGGAGGAAAAGAAAGTTTGCCAAGGCACGAGTAACAAGCTCACGCAG
TTGGGCACTTTTGAAGATCATTTTCTCAGCCTCCAGAGGATGTTCAATAACTGTGAGGTG
GTCCTTGGGAATTTGGAAATTACCTATGTGCAGAGGAATTATGATCTTTCCTTCTTAAAG
ACCATCCAGGAGGTGGCTGGTTATGTCCTCATTGCCCTCAACACAGTGGAGCGAATTCCT
TTGGAAAACCTGCAGATCATCAGAGGAAATATGTACTACGAAAATTCCTATGCCTTAGCA
GTCTTATCTAACTATGATGCAAATAAAACCGGACTGAAGGAGCTGCCCATGAGAAATTTA
CAGGAAATCCTGCATGGCGCCGTGCGGTTCAGCAACAACCCTGCCCTGTGCAACGTGGAG
AGCATCCAGTGGCGGGACATAGTCAGCAGTGACTTTCTCAGCAACATGTCGATGGACTTC
CAGAACCACCTGGGCAGCTGCCAAAAGTGTGATCCAAGCTGTCCCAATGGGAGCTGCTGG
GGTGCAGGAGAGGAGAACTGCCAGAAACTGACCAAAATCATCTGTGCCCAGCAGTGCTCC
GGGCGCTGCCGTGGCAAGTCCCCCAGTGACTGCTGCCACAACCAGTGTGCTGCAGGCTGC
ACAGGCCCCCGGGAGAGCGACTGCCTGGTCTGCCGCAAATTCCGAGACGAAGCCACGTGC
AAGGACACCTGCCCCCCACTCATGCTCTACAACCCCACCACGTACCAGATGGATGTGAAC
CCCGAGGGCAAATACAGCTTTGGTGCCACCTGCGTGAAGAAGTGTCCCCGTAATTATGTG
GTGACAGATCACGGCTCGTGCGTCCGAGCCTGTGGGGCCGACAGCTATGAGATGGAGGAA
GACGGCGTCCGCAAGTGTAAGAAGTGCGAAGGGCCTTGCCGCAAAGTGTGTAACGGAATA
GGTATTGGTGAATTTAAAGACTCACTCTCCATAAATGCTACGAATATTAAACACTTCAAA
AACTGCACCTCCATCAGTGGCGATCTCCACATCCTGCCGGTGGCATTTAGGGGTGACTCC
TTCACACATACTCCTCCTCTGGATCCACAGGAACTGGATATTCTGAAAACCGTAAAGGAA
ATCACAGGGTTTTTGCTGATTCAGGCTTGGCCTGAAAACAGGACGGACCTCCATGCCTTT
GAGAACCTAGAAATCATACGCGGCAGGACCAAGCAACATGGTCAGTTTTCTCTTGCAGTC
GTCAGCCTGAACATAACATCCTTGGGATTACGCTCCCTCAAGGAGATAAGTGATGGAGAT
GTGATAATTTCAGGAAACAAAAATTTGTGCTATGCAAATACAATAAACTGGAAAAAACTG
TTTGGGACCTCCGGTCAGAAAACCAAAATTATAAGCAACAGAGGTGAAAACAGCTGCAAG
GCCACAGGCCAGGTCTGCCATGCCTTGTGCTCCCCCGAGGGCTGCTGGGGCCCGGAGCCC
AGGGACTGCGTCTCTTGCCGGAATGTCAGCCGAGGCAGGGAATGCGTGGACAAGTGCAAG
CTTCTGGAGGGTGAGCCAAGGGAGTTTGTGGAGAACTCTGAGTGCATACAGTGCCACCCA
GAGTGCCTGCCTCAGGCCATGAACATCACCTGCACAGGACGGGGACCAGACAACTGTATC
CAGTGTGCCCACTACATTGACGGCCCCCACTGCGTCAAGACCTGCCCGGCAGGAGTCATG
GGAGAAAACAACACCCTGGTCTGGAAGTACGCAGACGCCGGCCATGTGTGCCACCTGTGC
CATCCAAACTGCACCTACGGATGCACTGGGCCAGGTCTTGAAGGCTGTCCAACGAATGGG
CCTAAGATCCCGTCCATCGCCACTGGGATGGTGGGGGCCCTCCTCTTGCTGCTGGTGGTG
GCCCTGGGGATCGGCCTCTTCATGCGAAGGCGCCACATCGTTCGGAAGCGCACGCTGCGG
AGGCTGCTGCAGGAGAGGGAGCTTGTGGAGCCTCTTACACCCAGTGGAGAAGCTCCCAAC
CAAGCTCTCTTGAGGATCTTGAAGGAAACTGAATTCAAAAAGATCAAAGTGCTGGGCTCC
GGTGCGTTCGGCACGGTGTATAAGGGACTCTGGATCCCAGAAGGTGAGAAAGTTAAAATT
CCCGTCGCTATCAAGGAATTAAGAGAAGCAACATCTCCGAAAGCCAACAAGGAAATCCTC
GATGAAGCCTACGTGATGGCCAGCGTGGACAACCCCCACGTGTGCCGCCTGCTGGGCATC
TGCCTCACCTCCACCGTGCAACTCATCACGCAGCTCATGCCCTTCGGCTGCCTCCTGGAC
TATGTCCGGGAACACAAAGACAATATTGGCTCCCAGTACCTGCTCAACTGGTGTGTGCAG
ATCGCAAAGGGCATGAACTACTTGGAGGACCGTCGCTTGGTGCACCGCGACCTGGCAGCC
AGGAACGTACTGGTGAAAACACCGCAGCATGTCAAGATCACAGATTTTGGGCTGGCCAAA
CTGCTGGGTGCGGAAGAGAAAGAATACCATGCAGAAGGAGGCAAAGTGCCTATCAAGTGG
ATGGCATTGGAATCAATTTTACACAGAATCTATACCCACCAGAGTGATGTCTGGAGCTAC
GGGGTGACCGTTTGGGAGTTGATGACCTTTGGATCCAAGCCATATGACGGAATCCCTGCC
AGCGAGATCTCCTCCATCCTGGAGAAAGGAGAACGCCTCCCTCAGCCACCCATATGTACC
ATCGATGTCTACATGATCATGGTCAAGTGCTGGATGATAGACGCAGATAGTCGCCCAAAG
TTCCGTGAGTTGATCATCGAATTCTCCAAAATGGCCCGAGACCCCCAGCGCTACCTTGTC
ATTCAGGGGGATGAAAGAATGCATTTGCCAAGTCCTACAGACTCCAACTTCTACCGTGCC
CTGATGGATGAAGAAGACATGGACGACGTGGTGGATGCCGACGAGTACCTCATCCCACAG
CAGGGCTTCTTCAGCAGCCCCTCCACGTCACGGACTCCCCTCCTGAGCTCTCTGAGTGCA
ACCAGCAACAATTCCACCGTGGCTTGCATTGATAGAAATGGGCTGCAAAGCTGTCCCATC
AAGGAAGACAGCTTCTTGCAGCGATACAGCTCAGACCCCACAGGCGCCTTGACTGAGGAC
AGCATAGACGACACCTTCCTCCCAGTGCCTGAATACATAAACCAGTCCGTTCCCAAAAGG
CCCGCTGGCTCTGTGCAGAATCCTGTCTATCACAATCAGCCTCTGAACCCCGCGCCCAGC
AGAGACCCACACTACCAGGACCCCCACAGCACTGCAGTGGGCAACCCCGAGTATCTCAAC
ACTGTCCAGCCCACCTGTGTCAACAGCACATTCGACAGCCCTGCCCACTGGGCCCAGAAA
GGCAGCCACCAAATTAGCCTGGACAACCCTGACTACCAGCAGGACTTCTTTCCCAAGGAA
GCCAAGCCAAATGGCATCTTTAAGGGCTCCACAGCTGAAAATGCAGAATACCTAAGGGTC
GCGCCACAAAGCAGTGAATTTATTGGAGCATGA
Enzyme 5 GenBank Gene ID X00588 Link Image
Enzyme 5 GeneCard ID EGFR Link Image
Enzyme 5 GenAtlas ID EGFR Link Image
Enzyme 5 HGNC ID HGNC:3236 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7p12
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, Tam AW, Lee J, Yarden Y, Libermann TA, Schlessinger J, et al.: Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature. 1984 May 31-Jun 6;309(5967):418-25. [PubMed Link Image]
  2. Ilekis JV, Stark BC, Scoccia B: Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta. Mol Reprod Dev. 1995 Jun;41(2):149-56. [PubMed Link Image]
  3. Reiter JL, Maihle NJ: A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor. Nucleic Acids Res. 1996 Oct 15;24(20):4050-6. [PubMed Link Image]
  4. Ilekis JV, Gariti J, Niederberger C, Scoccia B: Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol. 1997 Apr;65(1):36-41. [PubMed Link Image]
  5. Reiter JL, Threadgill DW, Eley GD, Strunk KE, Danielsen AJ, Sinclair CS, Pearsall RS, Green PJ, Yee D, Lampland AL, Balasubramaniam S, Crossley TD, Magnuson TR, James CD, Maihle NJ: Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms. Genomics. 2001 Jan 1;71(1):1-20. [PubMed Link Image]
  6. Lin CR, Chen WS, Kruiger W, Stolarsky LS, Weber W, Evans RM, Verma IM, Gill GN, Rosenfeld MG: Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells. Science. 1984 May 25;224(4651):843-8. [PubMed Link Image]
  7. Xu YH, Ishii S, Clark AJ, Sullivan M, Wilson RK, Ma DP, Roe BA, Merlino GT, Pastan I: Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells. Nature. 1984 Jun 28-Jul 4;309(5971):806-10. [PubMed Link Image]
  8. Simmen FA, Gope ML, Schulz TZ, Wright DA, Carpenter G, O'Malley BW: Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells. Biochem Biophys Res Commun. 1984 Oct 15;124(1):125-32. [PubMed Link Image]
  9. Haley J, Whittle N, Bennet P, Kinchington D, Ullrich A, Waterfield M: The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription. Oncogene Res. 1987 Sep-Oct;1(4):375-96. [PubMed Link Image]
  10. Haley JD, Waterfield MD: Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis. J Biol Chem. 1991 Jan 25;266(3):1746-53. [PubMed Link Image]
  11. Ishii S, Xu YH, Stratton RH, Roe BA, Merlino GT, Pastan I: Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4920-4. [PubMed Link Image]
  12. Weber W, Gill GN, Spiess J: Production of an epidermal growth factor receptor-related protein. Science. 1984 Apr 20;224(4646):294-7. [PubMed Link Image]
  13. Heisermann GJ, Gill GN: Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo. J Biol Chem. 1988 Sep 15;263(26):13152-8. [PubMed Link Image]
  14. Russo MW, Lukas TJ, Cohen S, Staros JV: Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase. J Biol Chem. 1985 May 10;260(9):5205-8. [PubMed Link Image]
  15. Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D: Disulfide bond structure of human epidermal growth factor receptor. J Biol Chem. 1998 May 1;273(18):11150-7. [PubMed Link Image]
  16. Mroczkowski B, Mosig G, Cohen S: ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature. 1984 May 17-23;309(5965):270-3. [PubMed Link Image]
  17. Carpenter G: Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem. 1987;56:881-914. [PubMed Link Image]
  18. Chen WS, Lazar CS, Lund KA, Welsh JB, Chang CP, Walton GM, Der CJ, Wiley HS, Gill GN, Rosenfeld MG: Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell. 1989 Oct 6;59(1):33-43. [PubMed Link Image]
  19. Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J: All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor. J Biol Chem. 1989 Jun 25;264(18):10667-71. [PubMed Link Image]
  20. Smith KD, Davies MJ, Bailey D, Renouf DV, Hounsell EF: Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Growth Factors. 1996;13(1-2):121-32. [PubMed Link Image]
  21. Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D: Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J Biochem (Tokyo). 2000 Jan;127(1):65-72. [PubMed Link Image]
  22. Habib AA, Chatterjee S, Park SK, Ratan RR, Lefebvre S, Vartanian T: The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome. J Biol Chem. 2001 Mar 23;276(12):8865-74. Epub 2000 Dec 14. [PubMed Link Image]
Enzyme 5 Metabolite References
  1. McEneaney V, Harvey BJ, Thomas W: Aldosterone rapidly activates protein kinase D via a mineralocorticoid receptor/EGFR trans-activation pathway in the M1 kidney CCD cell line. J Steroid Biochem Mol Biol. 2007 Nov-Dec;107(3-5):180-90. Epub 2007 Jun 22. [PubMed Link Image]
Enzyme 6 [top]
Enzyme 6 ID 6767
Enzyme 6 Name Serine/threonine-protein kinase D1
Enzyme 6 Synonyms
  1. nPKC-D1
  2. Protein kinase D
  3. Protein kinase C mu type
  4. nPKC-mu
Enzyme 6 Gene Name PRKD1
Enzyme 6 Protein Sequence >Serine/threonine-protein kinase D1
MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSRE
PVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAA
SDIQEGDLIEVVLSRSATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGC
GLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESF
IGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQ
CKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDM
EEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKS
STVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTS
ALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHAL
MPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGG
KHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME
KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPF
PQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT
FPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ
DYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQRLQYPTHLINPSASHSDTPETEET
EMKALGERVSIL
Enzyme 6 Number of Residues 912
Enzyme 6 Molecular Weight 101890
Enzyme 6 Theoretical pI 6.71
Enzyme 6 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
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid phosphorylation
  • protein modification
  • signal transduction
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-25
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 438373 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q15139 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name KPCD1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2739 bp
ATGAGCGCCCCTCCGGTCCTGCGGCCGCCCAGTCCGCTGCTGCCCGTGGCGGCGGCAGCT
GCCGCAGCGGCCGCCGCACTGGTCCCAGGGTCCGGGCCCGGGCCCGCGCCGTTCTTGGCT
CCTGTCGCGGCCCCGGTCGGGGGCATCTCGTTCCATCTGCAGATCGGCCTGAGCCGTGAG
CCGGTGCTGCTGCTGCAGGACTCGTCCGGGGACTACAGCCTGGCGCACGTCCGCGAGATG
GCTTGCTCCATTGTCGACCAGAAGTTCCCTGAATGTGGTTTCTACGGAATGTATGATAAG
ATCCTGCTTTTTCGCCATGACCCTACCTCTGAAAACATCCTTCAGCTGGTGAAAGCGGCC
AGTGATATCCAGGAAGGCGATCTTATTGAAGTGGTCTTGTCACGTTCCGCCACCTTTGAA
GACTTTCAGATTCGTCCCCACGCTCTCTTTGTTCATTCATACAGAGCTCCAGCTTTCTGT
GATCACTGTGGAGAAATGCTGTGGGGGCTGGTACGTCAAGGTCTTAAATGTGAAGGGTGT
GGTCTGAATTACCATAAGAGATGTGCATTTAAAATACCCAACAATTGCAGCGGTGTGAGG
CGGAGAAGGCTCTCAAACGTTTCCCTCACTGGGGTCAGCACCATCCGCACATCATCTGCT
GAACTCTCTACAAGTGCCCCTGATGAGCCCCTTCTGCAAAAATCACCATCAGAGTCGTTT
ATTGGTCGAGAGAAGAGGTCAAATTCTCAATCATACATTGGACGACCAATTCACCTTGAC
AAGATTTTGATGTCTAAAGTTAAAGTGCCGCACACATTTGTCATCCACTCCTACACCCGG
CCCACAGTGTGCCAGTACTGCAAGAAGCTTCTGAAGGGGCTTTTCAGGCAGGGCTTGCAG
TGCAAAGATTGCAGATTCAACTGCCATAAACGTTGTGCACCGAAAGTACCAAACAACTGC
CTTGGCGAAGTGACCATTAATGGAGATTTGCTTAGCCCTGGGGCAGAGTCTGATGTGGTC
ATGGAAGAAGGGAGTGATGACAATGATAGTGAAAGGAACAGTGGGCTCATGGATGATATG
GAAGAAGCAATGGTCCAAGATGCAGAGATGGCAATGGCAGAGTGCCAGAACGACAGTGGC
GAGATGCAAGATCCAGACCCAGACCACGAGGACGCCAACAGAACCATCAGTCCATCAACA
AGCAACAATATCCCACTCATGAGGGTAGTGCAGTCTGTCAAACACACGAAGAGGAAAAGC
AGCACAGTCATGAAAGAAGGATGGATGGTCCACTACACCAGCAAGGACACGCTGCGGAAA
CGGCACTATTGGAGATTGGATAGCAAATGTATTACCCTCTTTCAGAATGACACAGGAAGC
AGGTACTACAAGGAAATTCCTTTATCTGAAATTTTGTCTCTGGAACCAGTAAAAACTTCA
GCTTTAATTCCTAATGGGGCCAATCCTCATTGTTTCGAAATCACTACGGCAAATGTAGTG
TATTATGTGGGAGAAAATGTGGTCAATCCTTCCAGCCCATCACCAAATAACAGTGTTCTC
ACCAGTGGCGTTGGTGCAGATGTGGCCAGGATGTGGGAGATAGCCATCCAGCATGCCCTT
ATGCCCGTCATTCCCAAGGGCTCCTCCGTGGGTACAGGAACCAACTTGCACAGAGATATC
TCTGTGAGTATTTCAGTATCAAATTGCCAGATTCAAGAAAATGTGGACATCAGCACAGTA
TATCAGATTTTTCCTGATGAAGTACTGGGTTCTGGACAGTTTGGAATTGTTTATGGAGGA
AAACATCGTAAAACAGGAAGAGATGTAGCTATTAAAATCATTGACAAATTACGATTTCCA
ACAAAACAAGAAAGCCAGCTTCGTAATGAGGTTGCAATTCTACAGAACCTTCATCACCCT
GGTGTTGTAAATTTGGAGTGTATGTTTGAGACGCCTGAAAGAGTGTTTGTTGTTATGGAA
AAACTCCATGGAGACATGCTGGAAATGATCTTGTCAAGTGAAAAGGGCAGGTTGCCAGAG
CACATAACGAAGTTTTTAATTACTCAGATACTCGTGGCTTTGCGGCACCTTCATTTTAAA
AATATCGTTCACTGTGACCTCAAACCAGAAAATGTGTTGCTAGCCTCAGCTGATCCTTTT
CCTCAGGTGAAACTTTGTGATTTTGGTTTTGCCCGGATCATTGGAGAGAAGTCTTTCCGG
AGGTCAGTGGTGGGTACCCCCGCTTACCTGGCTCCTGAGGTCCTAAGGAACAAGGGCTAC
AATCGCTCTCTAGACATGTGGTCTGTTGGGGTCATCATCTATGTAAGCCTAAGCGGCACA
TTCCCATTTAATGAAGATGAAGACATACACGACCAAATTCAGAATGCAGCTTTCATGTAT
CCACCAAATCCCTGGAAGGAAATATCTCATGAAGCCATTGATCTTATCAACAATTTGCTG
CAAGTAAAAATGAGAAAGCGCTACAGTGTGGATAAGACCTTGAGCCACCCTTGGCTACAG
GACTATCAGACCTGGTTAGATTTGCGAGAGCTGGAATGCAAAATCGGGGAGCGCTACATC
ACCCATGAAAGTGATGACCTGAGGTGGGAGAAGTATGCAGGCGAGCAGCGGCTGCAGTAC
CCCACACACCTGATCAATCCAAGTGCTAGCCACAGTGACACTCCTGAGACTGAAGAAACA
GAAATGAAAGCCCTCGGTGAGCGTGTCAGCATCCTCTGA
Enzyme 6 GenBank Gene ID X75756 Link Image
Enzyme 6 GeneCard ID PRKD1 Link Image
Enzyme 6 GenAtlas ID PRKD1 Link Image
Enzyme 6 HGNC ID HGNC:9407 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q11
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K: PKCu is a novel, atypical member of the protein kinase C family. J Biol Chem. 1994 Feb 25;269(8):6140-8. [PubMed Link Image]
  2. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
Enzyme 6 Metabolite References
  1. McEneaney V, Harvey BJ, Thomas W: Aldosterone regulates rapid trafficking of epithelial sodium channel subunits in renal cortical collecting duct cells via protein kinase D activation. Mol Endocrinol. 2008 Apr;22(4):881-92. Epub 2008 Jan 17. [PubMed Link Image]
Enzyme 7 [top]
Enzyme 7 ID 7297
Enzyme 7 Name Glucocorticoid receptor
Enzyme 7 Synonyms
  1. GR
Enzyme 7 Gene Name NR3C1
Enzyme 7 Protein Sequence >Glucocorticoid receptor
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRR
LLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLK
LLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGN
VKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGN
SNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTV
YCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVG
SENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKL
CLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRK
CLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIE
PEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSW
MFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSY
EEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTK
LLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
Enzyme 7 Number of Residues 777
Enzyme 7 Molecular Weight 85660
Enzyme 7 Theoretical pI 6.31
Enzyme 7 GO Classification
Function
  • DNA binding
  • binding
  • glucocorticoid receptor activity
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid binding
  • steroid hormone receptor activity
  • transcription factor activity
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 7 General Function Not Available
Enzyme 7 Specific Function Receptor for glucocorticoids (GC). Has a dual mode of action:as a transcription factor that binds to glucocorticoid response elements (GRE) and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 31680 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P04150 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GCR_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2334 bp
ATGGACTCCAAAGAATCATTAACTCCTGGTAGAGAAGAAAACCCCAGCAGTGTGCTTGCT
CAGGAGAGGGGAGATGTGATGGACTTCTATAAAACCCTAAGAGGAGGAGCTACTGTGAAG
GTTTCTGCGTCTTCACCCTCACTGGCTGTCGCTTCTCAATCAGACTCCAAGCAGCGAAGA
CTTTTGGTTGATTTTCCAAAAGGCTCAGTAAGCAATGCGCAGCAGCCAGATCTGTCCAAA
GCAGTTTCACTCTCAATGGGACTGTATATGGGAGAGACAGAAACAAAAGTGATGGGAAAT
GACCTGGGATTCCCACAGCAGGGCCAAATCAGCCTTTCCTCGGGGGAAACAGACTTAAAG
CTTTTGGAAGAAAGCATTGCAAACCTCAATAGGTCGACCAGTGTTCCAGAGAACCCCAAG
AGTTCAGCATCCACTGCTGTGTCTGCTGCCCCCACAGAGAAGGAGTTTCCAAAAACTCAC
TCTGATGTATCTTCAGAACAGCAACATTTGAAGGGCCAGACTGGCACCAACGGTGGCAAT
GTGAAATTGTATACCACAGACCAAAGCACCTTTGACATTTTGCAGGATTTGGAGTTTTCT
TCTGGGTCCCCAGGTAAAGAGACGAATGAGAGTCCTTGGAGATCAGACCTGTTGATAGAT
GAAAACTGTTTGCTTTCTCCTCTGGCGGGAGAAGACGATTCATTCCTTTTGGAAGGAAAC
TCGAATGAGGACTGCAAGCCTCTCATTTTACCGGACACTAAACCCAAAATTAAGGATAAT
GGAGATCTGGTTTTGTCAAGCCCCAGTAATGTAACACTGCCCCAAGTGAAAACAGAAAAA
GAAGATTTCATCGAACTCTGCACCCCTGGGGTAATTAAGCAAGAGAAACTGGGCACAGTT
TACTGTCAGGCAAGCTTTCCTGGAGCAAATATAATTGGTAATAAAATGTCTGCCATTTCT
GTTCATGGTGTGAGTACCTCTGGAGGACAGATGTACCACTATGACATGAATACAGCATCC
CTTTCTCAACAGCAGGATCAGAAGCCTATTTTTAATGTCATTCCACCAATTCCCGTTGGT
TCCGAAAATTGGAATAGGTGCCAAGGATCTGGAGATGACAACTTGACTTCTCTGGGGACT
CTGAACTTCCCTGGTCGAACAGTTTTTTCTAATGGCTATTCAAGCCCCAGCATGAGACCA
GATGTAAGCTCTCCTCCATCCAGCTCCTCAACAGCAACAACAGGACCACCTCCCAAACTC
TGCCTGGTGTGCTCTGATGAAGCTTCAGGATGTCATTATGGAGTCTTAACTTGTGGAAGC
TGTAAAGTTTTCTTCAAAAGAGCAGTGGAAGGACAGCACAATTACCTATGTGCTGGAAGG
AATGATTGCATCATCGATAAAATTCGAAGAAAAAACTGCCCAGCATGCCGCTATCGAAAA
TGTCTTCAGGCTGGAATGAACCTGGAAGCTCGAAAAACAAAGAAAAAAATAAAAGGAATT
CAGCAGGCCACTACAGGAGTCTCACAAGAAACCTCTGAAAATCCTGGTAACAAAACAATA
GTTCCTGCAACGTTACCACAACTCACCCCTACCCTGGTGTCACTGTTGGAGGTTATTGAA
CCTGAAGTGTTATATGCAGGATATGATAGCTCTGTTCCAGACTCAACTTGGAGGATCATG
ACTACGCTCAACATGTTAGGAGGGCGGCAAGTGATTGCAGCAGTGAAATGGGCAAAGGCA
ATACCAGGTTTCAGGAACTTACACCTGGATGACCAAATGACCCTACTGCAGTACTCCTGG
ATGTTTCTTATGGCATTTGCTCTGGGGTGGAGATCATATAGACAATCAAGTGCAAACCTG
CTGTGTTTTGCTCCTGATCTGATTATTAATGAGCAGAGAATGACTCTACCCTGCATGTAC
GACCAATGTAAACACATGCTGTATGTTTCCTCTGAGTTACACAGGCTTCAGGTATCTTAT
GAAGAGTATCTCTGTATGAAAACCTTACTGCTTCTCTCTTCAGTTCCTAAGGACGGTCTG
AAGAGCCAAGAGCTATTTGATGAAATTAGAATGACCTACATCAAAGAGCTAGGAAAAGCC
ATTGTCAAGAGGGAAGGAAACTCCAGCCAGAACTGGCAGCGGTTTTATCAACTGACAAAA
CTCTTGGATTCTATGCATGAAGTGGTTGAAAATCTCCTTAACTATTGCTTCCAAACATTT
TTGGATAAGACCATGAGTATTGAATTCCCCGAGATGTTAGCTGAAATCATCACCAATCAG
ATACCAAAATATTCAAATGGAAATATCAAAAAACTTCTGTTTCATCAAAAGTGA
Enzyme 7 GenBank Gene ID X03225 Link Image
Enzyme 7 GeneCard ID NR3C1 Link Image
Enzyme 7 GenAtlas ID NR3C1 Link Image
Enzyme 7 HGNC ID HGNC:7978 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5q31.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hollenberg SM, Weinberger C, Ong ES, Cerelli G, Oro A, Lebo R, Thompson EB, Rosenfeld MG, Evans RM: Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature. 1985 Dec 19-1986 Jan 1;318(6047):635-41. [PubMed Link Image]
  2. Encio IJ, Detera-Wadleigh SD: The genomic structure of the human glucocorticoid receptor. J Biol Chem. 1991 Apr 15;266(11):7182-8. [PubMed Link Image]
  3. Leclerc S, Xie BX, Roy R, Govindan MV: Purification of a human glucocorticoid receptor gene promoter-binding protein. Production of polyclonal antibodies against the purified factor. J Biol Chem. 1991 May 15;266(14):8711-9. [PubMed Link Image]
  4. Govindan MV, Pothier F, Leclerc S, Palaniswami R, Xie B: Human glucocorticoid receptor gene promotor-homologous down regulation. J Steroid Biochem Mol Biol. 1991;40(1-3):317-23. [PubMed Link Image]
  5. Yudt MR, Cidlowski JA: Molecular identification and characterization of a and b forms of the glucocorticoid receptor. Mol Endocrinol. 2001 Jul;15(7):1093-103. [PubMed Link Image]
  6. Weinberger C, Hollenberg SM, Rosenfeld MG, Evans RM: Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product. Nature. 1985 Dec 19-1986 Jan 1;318(6047):670-2. [PubMed Link Image]
  7. Henriksson A, Almlof T, Ford J, McEwan IJ, Gustafsson JA, Wright AP: Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor. Mol Cell Biol. 1997 Jun;17(6):3065-73. [PubMed Link Image]
  8. 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]
  9. Schneikert J, Hubner S, Martin E, Cato AC: A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J Cell Biol. 1999 Sep 6;146(5):929-40. [PubMed Link Image]
  10. Rivers C, Levy A, Hancock J, Lightman S, Norman M: Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing. J Clin Endocrinol Metab. 1999 Nov;84(11):4283-6. [PubMed Link Image]
  11. Moalli PA, Pillay S, Krett NL, Rosen ST: Alternatively spliced glucocorticoid receptor messenger RNAs in glucocorticoid-resistant human multiple myeloma cells. Cancer Res. 1993 Sep 1;53(17):3877-9. [PubMed Link Image]
  12. Kayes-Wandover KM, White PC: Steroidogenic enzyme gene expression in the human heart. J Clin Endocrinol Metab. 2000 Jul;85(7):2519-25. [PubMed Link Image]
  13. 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]
  14. Diamond MI, Robinson MR, Yamamoto KR: Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):657-61. [PubMed Link Image]
  15. Wallace AD, Cidlowski JA: Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem. 2001 Nov 16;276(46):42714-21. Epub 2001 Sep 12. [PubMed Link Image]
  16. Strickland I, Kisich K, Hauk PJ, Vottero A, Chrousos GP, Klemm DJ, Leung DY: High constitutive glucocorticoid receptor beta in human neutrophils enables them to reduce their spontaneous rate of cell death in response to corticosteroids. J Exp Med. 2001 Mar 5;193(5):585-93. [PubMed Link Image]
  17. Tian S, Poukka H, Palvimo JJ, Janne OA: Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Biochem J. 2002 Nov 1;367(Pt 3):907-11. [PubMed Link Image]
  18. Wang Z, Frederick J, Garabedian MJ: Deciphering the phosphorylation &quot;code&quot; of the glucocorticoid receptor in vivo. J Biol Chem. 2002 Jul 19;277(29):26573-80. Epub 2002 May 8. [PubMed Link Image]
  19. Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed Link Image]
  20. Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE: Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell. 2002 Jul 12;110(1):93-105. [PubMed Link Image]
  21. Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M: The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9. [PubMed Link Image]
  22. Hurley DM, Accili D, Stratakis CA, Karl M, Vamvakopoulos N, Rorer E, Constantine K, Taylor SI, Chrousos GP: Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance. J Clin Invest. 1991 Feb;87(2):680-6. [PubMed Link Image]
  23. Powers JH, Hillmann AG, Tang DC, Harmon JM: Cloning and expression of mutant glucocorticoid receptors from glucocorticoid-sensitive and -resistant human leukemic cells. Cancer Res. 1993 Sep 1;53(17):4059-65. [PubMed Link Image]
  24. Karl M, Lamberts SW, Detera-Wadleigh SD, Encio IJ, Stratakis CA, Hurley DM, Accili D, Chrousos GP: Familial glucocorticoid resistance caused by a splice site deletion in the human glucocorticoid receptor gene. J Clin Endocrinol Metab. 1993 Mar;76(3):683-9. [PubMed Link Image]
  25. Malchoff DM, Brufsky A, Reardon G, McDermott P, Javier EC, Bergh CH, Rowe D, Malchoff CD: A mutation of the glucocorticoid receptor in primary cortisol resistance. J Clin Invest. 1993 May;91(5):1918-25. [PubMed Link Image]
  26. Ashraf J, Thompson EB: Identification of the activation-labile gene: a single point mutation in the human glucocorticoid receptor presents as two distinct receptor phenotypes. Mol Endocrinol. 1993 May;7(5):631-42. [PubMed Link Image]
  27. Koper JW, Stolk RP, de Lange P, Huizenga NA, Molijn GJ, Pols HA, Grobbee DE, Karl M, de Jong FH, Brinkmann AO, Lamberts SW: Lack of association between five polymorphisms in the human glucocorticoid receptor gene and glucocorticoid resistance. Hum Genet. 1997 May;99(5):663-8. [PubMed Link Image]
  28. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  29. Feng J, Zheng J, Bennett WP, Heston LL, Jones IR, Craddock N, Sommer SS: Five missense variants in the amino-terminal domain of the glucocorticoid receptor: no association with puerperal psychosis or schizophrenia. Am J Med Genet. 2000 Jun 12;96(3):412-7. [PubMed Link Image]
  30. Ruiz M, Lind U, Gafvels M, Eggertsen G, Carlstedt-Duke J, Nilsson L, Holtmann M, Stierna P, Wikstrom AC, Werner S: Characterization of two novel mutations in the glucocorticoid receptor gene in patients with primary cortisol resistance. Clin Endocrinol (Oxf). 2001 Sep;55(3):363-71. [PubMed Link Image]
  31. Dobson MG, Redfern CP, Unwin N, Weaver JU: The N363S polymorphism of the glucocorticoid receptor: potential contribution to central obesity in men and lack of association with other risk factors for coronary heart disease and diabetes mellitus. J Clin Endocrinol Metab. 2001 May;86(5):2270-4. [PubMed Link Image]
  32. Kino T, Stauber RH, Resau JH, Pavlakis GN, Chrousos GP: Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking. J Clin Endocrinol Metab. 2001 Nov;86(11):5600-8. [PubMed Link Image]
  33. Mendonca BB, Leite MV, de Castro M, Kino T, Elias LL, Bachega TA, Arnhold IJ, Chrousos GP, Latronico AC: Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene. J Clin Endocrinol Metab. 2002 Apr;87(4):1805-9. [PubMed Link Image]
  34. Vottero A, Kino T, Combe H, Lecomte P, Chrousos GP: A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators. J Clin Endocrinol Metab. 2002 Jun;87(6):2658-67. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. Gauer S, Segitz V, Goppelt-Struebe M: Aldosterone induces CTGF in mesangial cells by activation of the glucocorticoid receptor. Nephrol Dial Transplant. 2007 Nov;22(11):3154-9. Epub 2007 Jun 30. [PubMed Link Image]
Enzyme 8 [top]
Enzyme 8 ID 7555
Enzyme 8 Name Fibronectin precursor
Enzyme 8 Synonyms
  1. FN
  2. Cold-insoluble globulin
  3. CIG
Enzyme 8 Gene Name FN1
Enzyme 8 Protein Sequence >Fibronectin precursor
MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQ
INQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMI
WDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCK
PIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSY
RIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHP
QPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPC
VLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTQGGNSNGALC
HFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRI
GDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHM
LNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQ
PLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIP
GHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSP
LVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDL
LPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITG
YRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTG
TPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNT
FAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPP
RAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATG
VFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVV
SGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTT
PDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPIS
DTIIPAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSD
NAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIA
PRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLL
IGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSK
STATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISV
KWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGE
SQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAP
DGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSA
QWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLT
SRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRT
IKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLL
VSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQ
KSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTS
GQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYP
HGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLT
GLTRGATYNIIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDE
WERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLG
NGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEP
SPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE
Enzyme 8 Number of Residues 2386
Enzyme 8 Molecular Weight 262609
Enzyme 8 Theoretical pI 5.42
Enzyme 8 GO Classification
Function
Process
Component
  • extracellular region
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Interaction with TNR mediates inhibition of cell adhesion and neurite outgrowth
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-31
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 12053817 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P02751 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name FINC_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1929 bp
ATGCTTAGGGGTCCGGGGCCCGGGCTGCTGCTGCTGGCCGTCCAGTGCCTGGGGACAGCG
GTGCCCTCCACGGGAGCCTCGAAGAGCAAGAGGCAGGCTCAGCAAATGGTTCAGCCCCAG
TCCCCGGTGGCTGTCAGTCAAAGCAAGCCCGGTTGTTATGACAATGGAAAACACTATCAG
ATAAATCAACAGTGGGAGCGGACCTACCTAGGCAATGCGTTGGTTTGTACTTGTTATGGA
GGAAGCCGAGGTTTTAACTGCGAGAGTAAACCTGAAGCTGAAGAGACTTGCTTTGACAAG
TACACTGGGAACACTTACCGAGTGGGTGACACTTATGAGCGTCCTAAAGACTCCATGATC
TGGGACTGTACCTGCATCGGGGCTGGGCGAGGGAGAATAAGCTGTACCATCGCAAACCGC
TGCCATGAAGGGGGTCAGTCCTACAAGATTGGTGACACCTGGAGGAGACCACATGAGACT
GGTGGTTACATGTTAGAGTGTGTGTGTCTTGGTAATGGAAAAGGAGAATGGACCTGCAAG
CCCATAGCTGAGAAGTGTTTTGATCATGCTGCTGGGACTTCCTATGTGGTCGGAGAAACG
TGGGAGAAGCCCTACCAAGGCTGGATGATGGTAGATTGTACTTGCCTGGGAGAAGGCAGC
GGACGCATCACTTGCACTTCTAGAAATAGATGCAACGATCAGGACACAAGGACATCCTAT
AGAATTGGAGACACCTGGAGCAAGAAGGATAATCGAGGAAACCTGCTCCAGTGCATCTGC
ACAGGCAACGGCCGAGGAGAGTGGAAGTGTGAGAGGCACACCTCTGTGCAGACCACATCG
AGCGGATCTGGCCCCTTCACCGATGTTCGTGCAGCTGTTTACCAACCGCAGCCTCACCCC
CAGCCTCCTCCCTATGGCCACTGTGTCACAGACAGTGGTGTGGTCTACTCTGTGGGGATG
CAGTGGCTGAAGACACAAGGAAATAAGCAAATGCTTTGCACGTGCCTGGGCAACGGAGTC
AGCTGCCAAGAGACAGCTGTAACCCAGACTTACGGTGGCAACTCAAATGGAGAGCCATGT
GTCTTACCATTCACCTACAACGACAGGACGGACAGCACAACTTCGAATTATGAGCAGGAC
CAGAAATACTCTTTCTGCACAGACCACACTGTTTTGGTTCAGACTCGAGGAGGAAATTCC
AATGGTGCCTTGTGCCACTTCCCCTTCCTATACAACAACCACAATTACACTGATTGCACT
TCTGAGGGCAGAAGAGACAACATGAAGTGGTGTGGGACCACACAGAACTATGATGCCGAC
CAGAAGTTTGGGTTCTGCCCCATGGCTGCCCACGAGGAAATCTGCACAACCAATGAAGGG
GTCATGTACCGCATTGGAGATCAGTGGGATAAGCAGCATGACATGGGTCACATGATGAGG
TGCACGTGTGTTGGGAATGGTCGTGGGGAATGGACATGCATTGCCTACTCGCAGCTTCGA
GATCAGTGCATTGTTGATGACATCACTTACAATGTGAACGACACATTCCACAAGCGTCAT
GAAGAGGGGCACATGCTGAACTGTACATGCTTCGGTCAGGGTCGGGGCAGGTGGAAGTGT
GATCCCGTCGACCAATGCCAGGATTCAGAGACTGGGACGTTTTATCAAATTGGAGATTCA
TGGGAGAAGTATGTGCATGGTGTCAGATACCAGTGCTACTGCTATGGCCGTGGCATTGGG
GAGTGGCATTGCCAACCTTTACAGACCTATCCAAGCTCAAGTGGTCCTGTCGAAGTATTT
ATCACTGAGACTCCGAGTCAGCCCAACTCCCACCCCATCCAGTGGAATGCACCACAGCCA
TCTCACATTTCCAAGTACATTCTCAGGTGGAGACCTGTGAGTATCCCACCCAGAAACCTT
GGATACTGA
Enzyme 8 GenBank Gene ID AJ276395 Link Image
Enzyme 8 GeneCard ID FN1 Link Image
Enzyme 8 GenAtlas ID FN1 Link Image
Enzyme 8 HGNC ID HGNC:3778 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2q34
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Schor SL, Schor AM: Phenotypic and genetic alterations in mammary stroma: implications for tumour progression. Breast Cancer Res. 2001;3(6):373-9. Epub 2001 Sep 6. [PubMed Link Image]
  2. Gutman A, Yamada KM, Kornblihtt A: Human fibronectin is synthesized as a pre-propolypeptide. FEBS Lett. 1986 Oct 20;207(1):145-8. [PubMed Link Image]
  3. Dean DC, Bowlus CL, Bourgeois S: Cloning and analysis of the promotor region of the human fibronectin gene. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1876-80. [PubMed Link Image]
  4. Kornblihtt AR, Umezawa K, Vibe-Pedersen K, Baralle FE: Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. EMBO J. 1985 Jul;4(7):1755-9. [PubMed Link Image]
  5. Calaycay J, Pande H, Lee T, Borsi L, Siri A, Shively JE, Zardi L: Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin. J Biol Chem. 1985 Oct 5;260(22):12136-41. [PubMed Link Image]
  6. Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Human fibronectin: cell specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats. Nucleic Acids Res. 1984 Jul 25;12(14):5853-68. [PubMed Link Image]
  7. Paolella G, Henchcliffe C, Sebastio G, Baralle FE: Sequence analysis and in vivo expression show that alternative splicing of ED-B and ED-A regions of the human fibronectin gene are independent events. Nucleic Acids Res. 1988 Apr 25;16(8):3545-57. [PubMed Link Image]
  8. Zardi L, Carnemolla B, Siri A, Petersen TE, Paolella G, Sebastio G, Baralle FE: Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon. EMBO J. 1987 Aug;6(8):2337-42. [PubMed Link Image]
  9. Gutman A, Kornblihtt AR: Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA. Proc Natl Acad Sci U S A. 1987 Oct;84(20):7179-82. [PubMed Link Image]
  10. Pierschbacher MD, Ruoslahti E, Sundelin J, Lind P, Peterson PA: The cell attachment domain of fibronectin. Determination of the primary structure. J Biol Chem. 1982 Aug 25;257(16):9593-7. [PubMed Link Image]
  11. Oldberg A, Linney E, Ruoslahti E: Molecular cloning and nucleotide sequence of a cDNA clone coding for the cell attachment domain in human fibronectin. J Biol Chem. 1983 Sep 10;258(17):10193-6. [PubMed Link Image]
  12. Oldberg A, Ruoslahti E: Evolution of the fibronectin gene. Exon structure of cell attachment domain. J Biol Chem. 1986 Feb 15;261(5):2113-6. [PubMed Link Image]
  13. Garcia-Pardo A, Rostagno A, Frangione B: Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity. Biochem J. 1987 Feb 1;241(3):923-8. [PubMed Link Image]
  14. Bernard MP, Kolbe M, Weil D, Chu ML: Human cellular fibronectin: comparison of the carboxyl-terminal portion with rat identifies primary structural domains separated by hypervariable regions. Biochemistry. 1985 May 21;24(11):2698-704. [PubMed Link Image]
  15. Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain. EMBO J. 1984 Jan;3(1):221-6. [PubMed Link Image]
  16. Sekiguchi K, Klos AM, Kurachi K, Yoshitake S, Hakomori S: Human liver fibronectin complementary DNAs: identification of two different messenger RNAs possibly encoding the alpha and beta subunits of plasma fibronectin. Biochemistry. 1986 Aug 26;25(17):4936-41. [PubMed Link Image]
  17. Parker AE, Boutell J, Carr A, Maciewicz RA: Novel cartilage-specific splice variants of fibronectin. Osteoarthritis Cartilage. 2002 Jul;10(7):528-34. [PubMed Link Image]
  18. Umezawa K, Kornblihtt AR, Baralle FE: Isolation and characterization of cDNA clones for human liver fibronectin. FEBS Lett. 1985 Jul 1;186(1):31-4. [PubMed Link Image]
  19. Vibe-Pedersen K, Magnusson S, Baralle FE: Donor and acceptor splice signals within an exon of the human fibronectin gene: a new type of differential splicing. FEBS Lett. 1986 Oct 27;207(2):287-91. [PubMed Link Image]
  20. Garcia-Pardo A, Pearlstein E, Frangione B: Primary structure of human plasma fibronectin. Characterization of a 31,000-dalton fragment from the COOH-terminal region containing a free sulfhydryl group and a fibrin-binding site. J Biol Chem. 1985 Aug 25;260(18):10320-5. [PubMed Link Image]
  21. Kornblihtt AR, Vibe-Pedersen K, Baralle FE: Isolation and characterization of cDNA clones for human and bovine fibronectins. Proc Natl Acad Sci U S A. 1983 Jun;80(11):3218-22. [PubMed Link Image]
  22. Garcia-Pardo A, Pearlstein E, Frangione B: Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain. J Biol Chem. 1983 Oct 25;258(20):12670-4. [PubMed Link Image]
  23. Owens RJ, Baralle FE: Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli. EMBO J. 1986 Nov;5(11):2825-30. [PubMed Link Image]
  24. Liu MC, Yu S, Sy J, Redman CM, Lipmann F: Tyrosine sulfation of proteins from the human hepatoma cell line HepG2. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7160-4. [PubMed Link Image]
  25. Tressel T, McCarthy JB, Calaycay J, Lee TD, Legesse K, Shively JE, Pande H: Human plasma fibronectin. Demonstration of structural differences between the A- and B-chains in the III CS region. Biochem J. 1991 Mar 15;274 ( Pt 3):731-8. [PubMed Link Image]
  26. Balbona K, Tran H, Godyna S, Ingham KC, Strickland DK, Argraves WS: Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin. J Biol Chem. 1992 Oct 5;267(28):20120-5. [PubMed Link Image]
  27. Rostagno A, Williams MJ, Baron M, Campbell ID, Gold LI: Further characterization of the NH2-terminal fibrin-binding site on fibronectin. J Biol Chem. 1994 Dec 16;269(50):31938-45. [PubMed Link Image]
  28. Sasaki T, Brakebusch C, Engel J, Timpl R: Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. EMBO J. 1998 Mar 16;17(6):1606-13. [PubMed Link Image]
  29. Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID: 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 1992 Feb 25;31(7):2068-73. [PubMed Link Image]
  30. Main AL, Harvey TS, Baron M, Boyd J, Campbell ID: The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 1992 Nov 13;71(4):671-8. [PubMed Link Image]
  31. Williams MJ, Phan I, Harvey TS, Rostagno A, Gold LI, Campbell ID: Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity. J Mol Biol. 1994 Jan 28;235(4):1302-11. [PubMed Link Image]
  32. Potts JR, Phan I, Williams MJ, Campbell ID: High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin. Nat Struct Biol. 1995 Nov;2(11):946-50. [PubMed Link Image]
  33. Sticht H, Pickford AR, Potts JR, Campbell ID: Solution structure of the glycosylated second type 2 module of fibronectin. J Mol Biol. 1998 Feb 13;276(1):177-87. [PubMed Link Image]
  34. Fattorusso R, Pellecchia M, Viti F, Neri P, Neri D, Wuthrich K: NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis. Structure. 1999 Apr 15;7(4):381-90. [PubMed Link Image]
  35. Bocquier AA, Potts JR, Pickford AR, Campbell ID: Solution structure of a pair of modules from the gelatin-binding domain of fibronectin. Structure. 1999 Dec 15;7(12):1451-60. [PubMed Link Image]
  36. Pickford AR, Smith SP, Staunton D, Boyd J, Campbell ID: The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J. 2001 Apr 2;20(7):1519-29. [PubMed Link Image]
  37. Niimi T, Osawa M, Yamaji N, Yasunaga K, Sakashita H, Mase T, Tanaka A, Fujita S: NMR structure of human fibronectin EDA. J Biomol NMR. 2001 Nov;21(3):281-4. [PubMed Link Image]
  38. Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Hook M, Campbell ID, Potts JR: Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. Nature. 2003 May 8;423(6936):177-81. [PubMed Link Image]
  39. Dickinson CD, Veerapandian B, Dai XP, Hamlin RC, Xuong NH, Ruoslahti E, Ely KR: Crystal structure of the tenth type III cell adhesion module of human fibronectin. J Mol Biol. 1994 Mar 4;236(4):1079-92. [PubMed Link Image]
  40. Leahy DJ, Aukhil I, Erickson HP: 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell. 1996 Jan 12;84(1):155-64. [PubMed Link Image]
  41. Sharma A, Askari JA, Humphries MJ, Jones EY, Stuart DI: Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 1999 Mar 15;18(6):1468-79. [PubMed Link Image]
Enzyme 8 Metabolite References
  1. Lai L, Chen J, Hao CM, Lin S, Gu Y: Aldosterone promotes fibronectin production through a Smad2-dependent TGF-beta1 pathway in mesangial cells. Biochem Biophys Res Commun. 2006 Sep 15;348(1):70-5. Epub 2006 Jul 21. [PubMed Link Image]
Enzyme 9 [top]
Enzyme 9 ID 7620
Enzyme 9 Name Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32
Enzyme 9 Synonyms
  1. BNP-32]
Enzyme 9 Gene Name NPPB
Enzyme 9 Protein Sequence >Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32
MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVE
QTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRI
SSSSGLGCKVLRRH
Enzyme 9 Number of Residues 134
Enzyme 9 Molecular Weight 14726
Enzyme 9 Theoretical pI 11.01
Enzyme 9 GO Classification
Function
  • hormone activity
  • receptor binding
  • signal transducer activity
Process
Component
  • extracellular region
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-26
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 179515 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P16860 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ANFB_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >405 bp
ATGGATCCCCAGACAGCACCTTCCCGGGCGCTCCTGCTCCTGCTCTTCTTGCATCTGGCT
TTCCTGGGAGGTCGTTCCCACCCGCTGGGCAGCCCCGGTTCAGCCTCGGACTTGGAAACG
TCCGGGTTACAGGAGCAGCGCAACCATTTGCAGGGCAAACTGTCGGAGCTGCAGGTGGAG
CAGACATCCCTGGAGCCCCTCCAGGAGAGCCCCCGTCCCACAGGTGTCTGGAAGTCCCGG
GAGGTAGCCACCGAGGGCATCCGTGGGCACCGCAAAATGGTCCTCTACACCCTGCGGGCA
CCACGAAGCCCCAAGATGGTGCAAGGGTCTGGCTGCTTTGGGAGGAAGATGGACCGGATC
AGCTCCTCCAGTGGCCTGGGCTGCAAAGTGCTGAGGCGGCATTAA
Enzyme 9 GenBank Gene ID M31776 Link Image
Enzyme 9 GeneCard ID NPPB Link Image
Enzyme 9 GenAtlas ID NPPB Link Image
Enzyme 9 HGNC ID HGNC:7940 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p36.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Seilhamer JJ, Arfsten A, Miller JA, Lundquist P, Scarborough RM, Lewicki JA, Porter JG: Human and canine gene homologs of porcine brain natriuretic peptide. Biochem Biophys Res Commun. 1989 Dec 15;165(2):650-8. [PubMed Link Image]
  2. Sudoh T, Maekawa K, Kojima M, Minamino N, Kangawa K, Matsuo H: Cloning and sequence analysis of cDNA encoding a precursor for human brain natriuretic peptide. Biochem Biophys Res Commun. 1989 Mar 31;159(3):1427-34. [PubMed Link Image]
  3. Hino J, Tateyama H, Minamino N, Kangawa K, Matsuo H: Isolation and identification of human brain natriuretic peptides in cardiac atrium. Biochem Biophys Res Commun. 1990 Mar 16;167(2):693-700. [PubMed Link Image]
  4. Kambayashi Y, Nakao K, Mukoyama M, Saito Y, Ogawa Y, Shiono S, Inouye K, Yoshida N, Imura H: Isolation and sequence determination of human brain natriuretic peptide in human atrium. FEBS Lett. 1990 Jan 1;259(2):341-5. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 7645
Enzyme 10 Name Connective tissue growth factor precursor
Enzyme 10 Synonyms
  1. Hypertrophic chondrocyte- specific protein 24
Enzyme 10 Gene Name CTGF
Enzyme 10 Protein Sequence >Connective tissue growth factor precursor
MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVC
AKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSC
KYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALA
AYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVR
PCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTT
LPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA
Enzyme 10 Number of Residues 349
Enzyme 10 Molecular Weight 38092
Enzyme 10 Theoretical pI 8.03
Enzyme 10 GO Classification
Function
  • binding
  • growth factor binding
  • insulin-like growth factor binding
  • protein binding
Process
  • regulation of biological process
  • regulation of cell growth
  • regulation of growth
Component
  • extracellular region
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-26
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 180924 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P29279 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name CTGF_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1050 bp
ATGACCGCCGCCAGTATGGGCCCCGTCCGCGTCGCCTTCGTGGTCCTCCTCGCCCTCTGC
AGCCGGCCGGCCGTCGGCCAGAACTGCAGCGGGCCGTGCCGGTGCCCGGACGAGCCGGCG
CCGCGCTGCCCGGCGGGCGTGAGCCTCGTGCTGGACGGCTGCGGCTGCTGCCGCGTCTGC
GCCAAGCAGCTGGGCGAGCTGTGCACCGAGCGCGACCCCTGCGACCCGCACAAGGGCCTC
TTCTGTGACTTCGGCTCCCCGGCCAACCGCAAGATCGGCGTGTGCACCGCCAAAGATGGT
GCTCCCTGCATCTTCGGTGGTACGGTGTACCGCAGCGGAGAGTCCTTCCAGAGCAGCTGC
AAGTACCAGTGCACGTGCCTGGACGGGGCGGTGGGCTGCATGCCCCTGTGCAGCATGGAC
GTTCGTCTGCCCAGCCCTGACTGCCCCTTCCCGAGGAGGGTCAAGCTGCCCGGGAAATGC
TGCGAGGAGTGGGTGTGTGACGAGCCCAAGGACCAAACCGTGGTTGGGCCTGCCCTCGCG
GCTTACCGACTGGAAGACACGTTTGGCCCAGACCCAACTATGATTAGAGCCAACTGCCTG
GTCCAGACCACAGAGTGGAGCGCCTGTTCCAAGACCTGTGGGATGGGCATCTCCACCCGG
GTTACCAATGACAACGCCTCCTGCAGGCTAGAGAAGCAGAGCCGCCTGTGCATGGTCAGG
CCTTGCGAAGCTGACCTGGAAGAGAACATTAAGAAGGGCAAAAAGTGCATCCGTACTCCC
AAAATCTCCAAGCCTATCAAGTTTGAGCTTTCTGGCTGCACCAGCATGAAGACATACCGA
GCTAAATTCTGTGGAGTATGTACCGACGGCCGATGCTGCACCCCCCACAGAACCACCACC
CTGCCGGTGGAGTTCAAGTGCCCTGACGGCGAGGTCATGAAGAAGAACATGATGTTCATC
AAGACCTGTGCCTGCCATTACAACTGTCCCGGAGACAATGACATCTTTGAATCGCTGTAC
TACAGGAAGATGTACGGAGACATGGCATGA
Enzyme 10 GenBank Gene ID M92934 Link Image
Enzyme 10 GeneCard ID CTGF Link Image
Enzyme 10 GenAtlas ID CTGF Link Image
Enzyme 10 HGNC ID HGNC:2500 Link Image
Enzyme 10 Chromosome Location 6
Enzyme 10 Locus 6q23.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Bradham DM, Igarashi A, Potter RL, Grotendorst GR: Connective tissue growth factor: a cysteine-rich mitogen secreted by human vascular endothelial cells is related to the SRC-induced immediate early gene product CEF-10. J Cell Biol. 1991 Sep;114(6):1285-94. [PubMed Link Image]
  2. Igarashi A, Bradham DM, Okochi H, Grotendorst GR: Connective tissue growth factor. J Dermatol. 1992 Nov;19(11):642-3. [PubMed Link Image]
  3. Oemar BS, Werner A, Garnier JM, Do DD, Godoy N, Nauck M, Marz W, Rupp J, Pech M, Luscher TF: Human connective tissue growth factor is expressed in advanced atherosclerotic lesions. Circulation. 1997 Feb 18;95(4):831-9. [PubMed Link Image]
  4. 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]
  5. Nakanishi T, Nishida T, Shimo T, Kobayashi K, Kubo T, Tamatani T, Tezuka K, Takigawa M: Effects of CTGF/Hcs24, a product of a hypertrophic chondrocyte-specific gene, on the proliferation and differentiation of chondrocytes in culture. Endocrinology. 2000 Jan;141(1):264-73. [PubMed Link Image]
  6. Ball DK, Rachfal AW, Kemper SA, Brigstock DR: The heparin-binding 10 kDa fragment of connective tissue growth factor (CTGF) containing module 4 alone stimulates cell adhesion. J Endocrinol. 2003 Feb;176(2):R1-7. [PubMed Link Image]
Enzyme 10 Metabolite References
  1. Gauer S, Segitz V, Goppelt-Struebe M: Aldosterone induces CTGF in mesangial cells by activation of the glucocorticoid receptor. Nephrol Dial Transplant. 2007 Nov;22(11):3154-9. Epub 2007 Jun 30. [PubMed Link Image]
Enzyme 11 [top]
Enzyme 11 ID 7648
Enzyme 11 Name Type-1 angiotensin II receptor
Enzyme 11 Synonyms
  1. AT1
  2. AT1AR
  3. AT1BR
Enzyme 11 Gene Name AGTR1
Enzyme 11 Protein Sequence >Type-1 angiotensin II receptor
MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLK
TVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLT
CLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVC
AFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFK
IIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPL
FYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE
Enzyme 11 Number of Residues 359
Enzyme 11 Molecular Weight 41062
Enzyme 11 Theoretical pI 9.71
Enzyme 11 GO Classification
Function
  • C-X-C chemokine receptor activity
  • G-protein chemoattractant receptor activity
  • G-protein coupled receptor activity
  • angiotensin receptor activity
  • angiotensin type II receptor activity
  • bradykinin receptor activity
  • chemokine receptor activity
  • peptide receptor activity, G-protein coupled
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 28-52 65-87 103-124 143-162 193-214 241-262 276-296
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 179122 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P30556 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name AGTR1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1080 bp
ATGATTCTCAACTCTTCTACTGAAGATGGTATTAAAAGAATCCAAGATGATTGTCCCAAA
GCTGGAAGGCATAATTACATATTTGTCATGATTCCTACTTTATACAGTATCATCTTTGTG
GTGGGAATATTTGGAAACAGCTTGGTGGTGATAGTCATTTACTTTTATATGAAGCTGAAG
ACTGTGGCCAGTGTTTTTCTTTTGAATTTAGCACTGGCTGACTTATGCTTTTTACTGACT
TTGCCACTATGGGCTGTCTACACAGCTATGGAATACCGCTGGCCCTTTGGCAATTACCTA
TGTAAGATTGCTTCAGCCAGCGTCAGTTTCAACCTGTACGCTAGTGTGTTTCTACTCACG
TGTCTCAGCATTGATCGATACCTGGCTATTGTTCACCCAATGAAGTCCCGCCTTCGACGC
ACAATGCTTGTAGCCAAAGTCACCTGCATCATCATTTGGCTGCTGGCAGGCTTGGCCAGT
TTGCCAGCTATAATCCATCGAAATGTATTTTTCATTGAGAACACCAATATTACAGTTTGT
GCTTTCCATTATGAGTCCCAAAATTCAACCCTCCCGATAGGGCTGGGCCTGACCAAAAAT
ATACTGGGTTTCCTGTTTCCTTTTCTGATCATTCTTACAAGTTATACTCTTATTTGGAAG
GCCCTAAAGAAGGCTTATGAAATTCAGAAGAACAAACCAAGAAATGATGATATTTTTAAG
ATAATTATGGCAATTGTGCTTTTCTTTTTCTTTTCCTGGATTCCCCACCAAATATTCACT
TTTCTGGATGTATTGATTCAACTAGGCATCATACGTGACTGTAGAATTGCAGATATTGTG
GACACGGCCATGCCTATCACCATTTGTATAGCTTATTTTAACAATTGCCTGAATCCTCTT
TTTTATGGCTTTCTGGGGAAAAAATTTAAAAGATATTTTCTCCAGCTTCTAAAATATATT
CCCCCAAAAGCCAAATCCCACTCAAACCTTTCAACAAAAATGAGCACGCTTTCCTACCGC
CCCTCAGATAATGTAAGCTCATCCACCAAGAAGCCTGCACCATGTTTTGAGGTTGAGTGA
Enzyme 11 GenBank Gene ID M91464 Link Image
Enzyme 11 GeneCard ID AGTR1 Link Image
Enzyme 11 GenAtlas ID AGTR1 Link Image
Enzyme 11 HGNC ID HGNC:336 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3q21-q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Mauzy CA, Hwang O, Egloff AM, Wu LH, Chung FZ: Cloning, expression, and characterization of a gene encoding the human angiotensin II type 1A receptor. Biochem Biophys Res Commun. 1992 Jul 15;186(1):277-84. [PubMed Link Image]
  2. Furuta H, Guo DF, Inagami T: Molecular cloning and sequencing of the gene encoding human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Feb 28;183(1):8-13. [PubMed Link Image]
  3. Bergsma DJ, Ellis C, Kumar C, Nuthulaganti P, Kersten H, Elshourbagy N, Griffin E, Stadel JM, Aiyar N: Cloning and characterization of a human angiotensin II type 1 receptor. Biochem Biophys Res Commun. 1992 Mar 31;183(3):989-95. [PubMed Link Image]
  4. Takayanagi R, Ohnaka K, Sakai Y, Nakao R, Yanase T, Haji M, Inagami T, Furuta H, Gou DF, Nakamuta M, et al.: Molecular cloning, sequence analysis and expression of a cDNA encoding human type-1 angiotensin II receptor. Biochem Biophys Res Commun. 1992 Mar 16;183(2):910-6. [PubMed Link Image]
  5. Curnow KM, Pascoe L, White PC: Genetic analysis of the human type-1 angiotensin II receptor. Mol Endocrinol. 1992 Jul;6(7):1113-8. [PubMed Link Image]
  6. Konishi H, Kuroda S, Inada Y, Fujisawa Y: Novel subtype of human angiotensin II type 1 receptor: cDNA cloning and expression. Biochem Biophys Res Commun. 1994 Mar 15;199(2):467-74. [PubMed Link Image]
  7. Nawata H, Takayanagi R, Ohnaka K, Sakai Y, Imasaki K, Yanase T, Ikuyama S, Tanaka S, Ohe K: Type 1 angiotensin II receptors of adrenal tumors. Steroids. 1995 Jan;60(1):28-34. [PubMed Link Image]
Enzyme 11 Metabolite References
  1. Yamada M, Kushibiki M, Osanai T, Tomita H, Okumura K: Vasoconstrictor effect of aldosterone via angiotensin II type 1 (AT1) receptor: possible role of AT1 receptor dimerization. Cardiovasc Res. 2008 Jul 1;79(1):169-78. Epub 2008 Mar 7. [PubMed Link Image]
Enzyme 12 [top]
Enzyme 12 ID 8137
Enzyme 12 Name Mineralocorticoid receptor
Enzyme 12 Synonyms
  1. MR
Enzyme 12 Gene Name NR3C2
Enzyme 12 Protein Sequence >Mineralocorticoid receptor
METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNST
QGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYE
QQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAI
VKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPN
AENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSP
ANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVP
SPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSD
SSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGF
DGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSAR
DQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPS
KICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRL
QKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVN
TALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQV
VKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKM
HQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYI
KELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAML
VEIISDQLPKVESGNAKPLYFHRK
Enzyme 12 Number of Residues 984
Enzyme 12 Molecular Weight 107068
Enzyme 12 Theoretical pI 7.42
Enzyme 12 GO Classification
Function
  • DNA binding
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transcription factor activity
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 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 307166 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P08235 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name MCR_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >2955 bp
ATGGAGACCAAAGGCTACCACAGTCTCCCTGAAGGTCTAGATATGGAAAGACGGTGGGGT
CAAGTTTCTCAGGCTGTGGAGCGTTCTTCCCTGGGACCTACAGAGAGGACCGATGAGAAT
AACTACATGGAGATTGTCAACGTAAGCTGTGTTTCCGGTGCTATTCCAAACAACAGTACT
CAAGGAAGCAGCAAAGAAAAACAAGAACTACTCCCTTGCCTTCAGCAAGACAATAATCGG
CCTGGGATTTTAACATCTGATATTAAAACTGAGCTGGAATCTAAGGAACTTTCAGCAACT
GTAGCTGAGTCCATGGGTTTATATATGGATTCTGTAAGAGATGCTGACTATTCCTATGAG
CAGCAGAACCAACAAGGAAGCATGAGTCCAGCTAAGATTTATCAGAATGTTGAACAGCTG
GTGAAATTTTACAAAGGAAATGGCCATCGTCCTTCCACTCTAAGTTGTGTGAACACGCCC
TTGAGATCATTTATGTCTGACTCTGGGAGCTCCGTGAATGGTGGCGTCATGCGCGCCATT
GTTAAAAGCCCTATCATGTGTCATGAGAAAAGCCCGTCTGTTTGCAGCCCTCTGAACATG
ACATCTTCGGTTTGCAGCCCTGCTGGAATCAACTCTGTGTCCTCCACCACAGCCAGCTTT
GGCAGTTTTCCAGTGCACAGCCCAATCACCCAGGGAACTCCTCTGACATGCTCCCCTAAT
GCTGAAAATCGAGGCTCCAGGTCGCACAGCCCTGCACATGCTAGCAATGTGGGCTCTCCT
CTCTCAAGTCCGTTAAGTAGCATGAAATCCTCAATTTCCAGCCCTCCAAGTCACTGCAGT
GTAAAATCTCCAGTCTCCAGTCCCAATAATGTCACTCTGAGATCCTCTGTGTCTAGCCCT
GCAAATATTAACAACTCAAGGTGCTCTGTTTCCAGCCCTTCGAACACTAATAACAGATCC
ACGCTTTCCAGTCCGGCAGCCAGTACTGTGGGATCTATCTGTAGCCCTGTAAACAATGCC
TTCAGCTACACTGCTTCTGGCACCTCTGCTGGATCCAGTACATTGCGGGATGTGGTTCCC
AGTCCAGACACGCAGGAGAAAGGTGCTCAAGAGGTCCCTTTTCCTAAGACTGAGGAAGTA
GAGAGTGCCATCTCAAATGGTGTGACTGGCCAGCTTAATATTGTCCAGTACATAAAACCA
GAACCAGATGGAGCTTTTAGCAGCTCATGTCTAGGAGGAAATAGCAAAATAAATTCGGAT
TCTTCATTCTCAGTACCAATAAAGCAAGAATCAACCAAGCATTCATGTTCAGGCACCTCT
TTTAAAGGGAATCCAACAGTAAACCCGTTTCCATTTATGGATGGCTCGTATTTTTCCTTT
ATGGATGATAAAGACTATTATTCCCTATCAGGAATTTTAGGACCACCTGTGCCCGGCTTT
GATGGTAACTGTGAAGGCAGCGGATTCCCAGTGGGTATTAAACAAGAACCAGATGACGGG
AGCTATTACCCAGAGGCCAGCATCCCTTCCTCTGCTATTGTTGGGGTGAATTCAGGTGGA
CAGTCCTTCCACTACAGGATTGGTGCTCAAGGTACAATATCTTTATCACGATCGGCTAGA
GACCAATCTTTCCAACACCTGAGTTCCTTTCCTCCTGTCAATACTTTAGTGGAGTCATGG
AAATCACACGGCGACCTGTCGTCTAGAAGAAGTGATGGGTATCCGGTCTTAGAATACATT
CCAGAAAATGTATCAAGCTCTACTTTACGAAGTGTTTCTACTGGATCTTCAAGACCTTCA
AAAATATGTTTGGTGTGTGGGGATGAGGCTTCAGGATGCCATTATGGGGTAGTCACCTGT
GGCAGCTGCAAAGTTTTCTTCAAAAGAGCAGTGGAAGGGCAACACAACTATTTATGTGCT
GGAAGAAATGATTGCATCATTGATAAGATTCGACGAAAGAATTGTCCTGCTTGCAGACTT
CAGAAATGTCTTCAAGCTGGAATGAATTTAGGAGCACGAAAGTCAAAGAAGTTGGGAAAG
TTAAAAGGGATTCACGAGGAGCAGCCACAGCAGCAGCAGCCCCCACCCCCACCCCCACCC
CCGCAAAGCCCAGAGGAAGGGACAACGTACATCGCTCCTGCAAAAGAACCCTCGGTCAAC
ACAGCACTGGTTCCTCAGCTCTCCACAATCTCACGAGCGCTCACACCTTCCCCCGTTATG
GTCCTTGAAAACATTGAACCTGAAATTGTATATGCAGGCTATGACAGCTCAAAACCAGAT
ACAGCCGAAAATCTGCTCTCCACGCTCAACCGCTTAGCAGGCAAACAGATGATCCAAGTC
GTGAAGTGGGCAAAGGTACTTCCAGGATTTAAAAACTTGCCTCTTGAGGACCAAATTACC
CTAATCCAGTATTCTTGGATGTGTCTATCATCATTTGCCTTGAGCTGGAGATCGTACAAA
CATACGAACAGCCAATTTCTCTATTTTGCACCAGACCTAGTCTTTAATGAAGAGAAGATG
CATCAGTCTGCCATGTATGAACTATGCCAGGGGATGCACCAAATCAGCCTTCAGTTCGTT
CGACTGCAGCTCACCTTTGAAGAATACACCATCATGAAAGTTTTGCTGCTACTAAGCACA
ATTCCAAAGGATGGCCTCAAAAGCCAGGCTGCATTTGAAGAAATGAGGACAAATTACATC
AAAGAACTGAGGAAGATGGTAACTAAGTGTCCCAACAATTCTGGGCAGAGCTGGCAGAGG
TTCTACCAACTGACCAAGCTGCTGGACTCCATGCATGACCTGGTGAGCGACCTGCTGGAA
TTCTGCTTCTACACCTTCCGAGAGTCCCATGCGCTGAAGGTAGAGTTCCCCGCAATGCTG
GTGGAGATCATCAGCGACCAGCTGCCCAAGGTGGAGTCGGGGAACGCCAAGCCGCTCTAC
TTCCACCGGAAGTGA
Enzyme 12 GenBank Gene ID M16801 Link Image
Enzyme 12 GeneCard ID NR3C2 Link Image
Enzyme 12 GenAtlas ID NR3C2 Link Image
Enzyme 12 HGNC ID HGNC:7979 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4q31.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Arriza JL, Weinberger C, Cerelli G, Glaser TM, Handelin BL, Housman DE, Evans RM: Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 1987 Jul 17;237(4812):268-75. [PubMed Link Image]
  2. Zennaro MC, Souque A, Viengchareun S, Poisson E, Lombes M: A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action. Mol Endocrinol. 2001 Sep;15(9):1586-98. [PubMed Link Image]
  3. Geller DS, Rodriguez-Soriano J, Vallo Boado A, Schifter S, Bayer M, Chang SS, Lifton RP: Mutations in the mineralocorticoid receptor gene cause autosomal dominant pseudohypoaldosteronism type I. Nat Genet. 1998 Jul;19(3):279-81. [PubMed Link Image]
  4. Alnemri ES, Maksymowych AB, Robertson NM, Litwack G: Overexpression and characterization of the human mineralocorticoid receptor. J Biol Chem. 1991 Sep 25;266(27):18072-81. [PubMed Link Image]
  5. Bloem LJ, Guo C, Pratt JH: Identification of a splice variant of the rat and human mineralocorticoid receptor genes. J Steroid Biochem Mol Biol. 1995 Nov;55(2):159-62. [PubMed Link Image]
  6. Zennaro MC, Farman N, Bonvalet JP, Lombes M: Tissue-specific expression of alpha and beta messenger ribonucleic acid isoforms of the human mineralocorticoid receptor in normal and pathological states. J Clin Endocrinol Metab. 1997 May;82(5):1345-52. [PubMed Link Image]
  7. Bruner KL, Derfoul A, Robertson NM, Guerriero G, Fernandes-Alnemri T, Alnemri ES, Litwack G: The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52. Recept Signal Transduct. 1997;7(2):85-98. [PubMed Link Image]
  8. Lupo B, Mesnier D, Auzou G: Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for steroid binding. Biochemistry. 1998 Sep 1;37(35):12153-9. [PubMed Link Image]
  9. Hellal-Levy C, Fagart J, Souque A, Rafestin-Oblin ME: Mechanistic aspects of mineralocorticoid receptor activation. Kidney Int. 2000 Apr;57(4):1250-5. [PubMed Link Image]
  10. Hellal-Levy C, Fagart J, Souque A, Wurtz JM, Moras D, Rafestin-Oblin ME: Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor. Mol Endocrinol. 2000 Aug;14(8):1210-21. [PubMed Link Image]
  11. Odermatt A, Arnold P, Frey FJ: The intracellular localization of the mineralocorticoid receptor is regulated by 11beta-hydroxysteroid dehydrogenase type 2. J Biol Chem. 2001 Jul 27;276(30):28484-92. Epub 2001 May 11. [PubMed Link Image]
  12. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  13. Tajima T, Kitagawa H, Yokoya S, Tachibana K, Adachi M, Nakae J, Suwa S, Katoh S, Fujieda K: A novel missense mutation of mineralocorticoid receptor gene in one Japanese family with a renal form of pseudohypoaldosteronism type 1. J Clin Endocrinol Metab. 2000 Dec;85(12):4690-4. [PubMed Link Image]
  14. Geller DS, Farhi A, Pinkerton N, Fradley M, Moritz M, Spitzer A, Meinke G, Tsai FT, Sigler PB, Lifton RP: Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy. Science. 2000 Jul 7;289(5476):119-23. [PubMed Link Image]
  15. Arai K, Nakagomi Y, Iketani M, Shimura Y, Amemiya S, Ohyama K, Shibasaki T: Functional polymorphisms in the mineralocorticoid receptor and amirolide-sensitive sodium channel genes in a patient with sporadic pseudohypoaldosteronism. Hum Genet. 2003 Jan;112(1):91-7. Epub 2002 Oct 25. [PubMed Link Image]
Enzyme 12 Metabolite References
  1. White WB: Drospirenone with 17beta-estradiol in the postmenopausal woman with hypertension. Climacteric. 2007 Feb;10 Suppl 1:25-31. [PubMed Link Image]
Enzyme 13 [top]
Enzyme 13 ID 8258
Enzyme 13 Name ADM precursor [Contains: Adrenomedullin
Enzyme 13 Synonyms
  1. AM
  2. Proadrenomedullin N-20 terminal peptide
  3. ProAM-N20
  4. ProAM N-terminal 20 peptide
  5. PAMP]
Enzyme 13 Gene Name ADM
Enzyme 13 Protein Sequence >ADM precursor [Contains: Adrenomedullin
MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVK
AGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKL
AHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGS
APHFL
Enzyme 13 Number of Residues 185
Enzyme 13 Molecular Weight 20421
Enzyme 13 Theoretical pI 11.45
Enzyme 13 GO Classification
Function
  • hormone activity
  • receptor binding
  • signal transducer activity
Process
Component
  • extracellular region
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-21
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 500612 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P35318 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ADML_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >558 bp
ATGAAGCTGGTTTCCGTCGCCCTGATGTACCTGGGTTCGCTCGCCTTCCTAGGCGCTGAC
ACCGCTCGGTTGGATGTCGCGTCGGAGTTTCGAAAGAAGTGGAATAAGTGGGCTCTGAGT
CGTGGGAAGAGGGAACTGCGGATGTCCAGCAGCTACCCCACCGGGCTCGCTGACGTGAAG
GCCGGGCCTGCCCAGACCCTTATTCGGCCCCAGGACATGAAGGGTGCCTCTCGAAGCCCC
GAAGACAGCAGTCCGGATGCCGCCCGCATCCGAGTCAAGCGCTACCGCCAGAGCATGAAC
AACTTCCAGGGCCTCCGGAGCTTTGGCTGCCGCTTCGGGACGTGCACGGTGCAGAAGCTG
GCACACCAGATCTACCAGTTCACAGATAAGGACAAGGACAACGTCGCCCCCAGGAGCAAG
ATCAGCCCCCAGGGCTACGGCCGCCGGCGCCGGCGCTCCCTGCCCGAGGCCGGCCCGGGT
CGGACTCTGGTGTCTTCTAAGCCACAAGCACACGGGGCTCCAGCCCCCCCGAGTGGAAGT
GCTCCCCACTTTCTTTAG
Enzyme 13 GenBank Gene ID D14874 Link Image
Enzyme 13 GeneCard ID ADM Link Image
Enzyme 13 GenAtlas ID ADM Link Image
Enzyme 13 HGNC ID HGNC:259 Link Image
Enzyme 13 Chromosome Location 11
Enzyme 13 Locus 11p15.4
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Kitamura K, Sakata J, Kangawa K, Kojima M, Matsuo H, Eto T: Cloning and characterization of cDNA encoding a precursor for human adrenomedullin. Biochem Biophys Res Commun. 1993 Jul 30;194(2):720-5. [PubMed Link Image]
  2. Ishimitsu T, Kojima M, Kangawa K, Hino J, Matsuoka H, Kitamura K, Eto T, Matsuo H: Genomic structure of human adrenomedullin gene. Biochem Biophys Res Commun. 1994 Aug 30;203(1):631-9. [PubMed Link Image]
  3. Kitamura K, Kangawa K, Kawamoto M, Ichiki Y, Nakamura S, Matsuo H, Eto T: Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma. Biochem Biophys Res Commun. 1993 Apr 30;192(2):553-60. [PubMed Link Image]
  4. Samson WK: Proadrenomedullin-derived peptides. Front Neuroendocrinol. 1998 Apr;19(2):100-27. [PubMed Link Image]
  5. Champion HC, Nussdorfer GG, Kadowitz PJ: Structure-activity relationships of adrenomedullin in the circulation and adrenal gland. Regul Pept. 1999 Nov 30;85(1):1-8. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8295
Enzyme 14 Name Prostaglandin E2 receptor, EP4 subtype
Enzyme 14 Synonyms
  1. Prostanoid EP4 receptor
  2. PGE receptor, EP4 subtype
Enzyme 14 Gene Name PTGER4
Enzyme 14 Protein Sequence >Prostaglandin E2 receptor, EP4 subtype
MSTPGVNSSASLSPDRLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCG
LAVTDLLGTLLVSPVTIATYMKGQWPGGQPLCEYSTFILLFFSLSGLSIICAMSVERYLA
INHAYFYSHYVDKRLAGLTLFAVYASNVLFCALPNMGLGSSRLQYPDTWCFIDWTTNVTA
HAAYSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAASVASRG
HPAASPALPRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFVNQLYQP
SLEREVSKNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSRRERSG
QHCSDSQRTSSAMSGHSRSFISRELKEISSTSQTLLPDLSLPDLSENGLGGRNLLPGVPG
MGLAQEDTTSLRTLRISETSDSSQGQDSESVLLVDEAGGSGRAGPAPKGSSLQVTFPSET
LNLSEKCI
Enzyme 14 Number of Residues 488
Enzyme 14 Molecular Weight 53120
Enzyme 14 Theoretical pI 8.91
Enzyme 14 GO Classification
Function
  • G-protein coupled receptor activity
  • icosanoid receptor activity
  • prostaglandin E receptor activity
  • prostaglandin receptor activity
  • prostanoid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-38
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 452496 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P35408 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PE2R4_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1467 bp
ATGTCCACTCCCGGGGTCAATTCGTCCGCCTCCTTGAGCCCCGACCGGCTGAACAGCCCA
GTGACCATCCCGGCGGTGATGTTCATCTTCGGGGTGGTGGGCAACCTGGTGGCCATCGTG
GTGCTGTGCAAGTCGCGCAAGGAGCAGAAGGAGACGACCTTCTACACGCTGGTATGTGGG
CTGGCTGTCACCGACCTGTTGGGCACTTTGTTGGTGAGCCCGGTGACCATCGCCACGTAC
ATGAAGGGCCAATGGCCCGGGGGCCAGCCGCTGTGCGAGTACAGCACCTTCATTCTGCTC
TTCTTCAGCCTGTCCGGCCTCAGCATCATCTGCGCCATGAGTGTCGAGCGCTACCTGGCC
ATCAACCATGCCTATTTCTACAGCCACTACGTGGACAAGCGATTGGCGGGCCTCACGCTC
TTTGCAGTCTATGCGTCCAACGTGCTCTTTTGCGCGCTGCCCAACATGGGTCTCGGTAGC
TCGCGGCTGCAGTACCCAGACACCTGGTGCTTCATCGACTGGACCACCAACGTGACGGCG
CACGCCGCCTACTCCTACATGTACGCGGGCTTCAGCTCCTTCCTCATTCTCGCCACCGTC
CTCTGCAACGTGCTTGTGTGCGGCGCGCTGCTCCGCATGCACCGCCAGTTCATGCGCCGC
ACCTCGCTGGGCACCGAGCAGCACCACGCGGCCGCGGCCGCCTCGGTTGCCTCCCGGGGC
CACCCCGCTGCCTCCCCAGCCTTGCCGCGCCTCAGCGACTTTCGGCGCCGCCGGAGCTTC
CGCCGCATCGCGGGCGCCGAGATCCAGATGGTCATCTTACTCATTGCCACCTCCCTGGTG
GTGCTCATCTGCTCCATCCCGCTCGTGGTGCGAGTATTCGTCAACCAGTTATATCAGCCA
AGTTTGGAGCGAGAAGTCAGTAAAAATCCAGATTTGCAGGCCATCCGAATTGCTTCTGTG
AACCCCATCCTAGACCCCTGGATATATATCCTCCTGAGAAAGACAGTGCTCAGTAAAGCA
ATAGAGAAGATCAAATGCCTCTTCTGCCGCATTGGCGGGTCCCGCAGGGAGCGCTCCGGA
CAGCACTGCTCAGACAGTCAAAGGACATCTTCTGCCATGTCAGGCCACTCTCGCTCCTTC
ATCTCCCGGGAGCTGAAGGAGATCAGCAGTACATCTCAGACCCTCCTGCCAGACCTCTCA
CTGCCAGACCTCAGTGAAAATGGCCTTGGAGGCAGGAATTTGCTTCCAGGTGTGCCTGGC
ATGGGCCTGGCCCAGGAAGACACCACCTCACTGAGGACTTTGCGAATATCAGAGACCTCA
GACTCTTCACAGGGTCAGGACTCAGAGAGTGTCTTACTGGTGGATGAGGCTGGTGGGAGC
GGCAGGGCTGGGCCTGCCCCTAAGGGGAGCTCCCTGCAAGTCACATTTCCCAGTGAAACA
CTGAACTTATCAGAAAAATGTATATAA
Enzyme 14 GenBank Gene ID L28175 Link Image
Enzyme 14 GeneCard ID PTGER4 Link Image
Enzyme 14 GenAtlas ID PTGER4 Link Image
Enzyme 14 HGNC ID HGNC:9596 Link Image
Enzyme 14 Chromosome Location 5
Enzyme 14 Locus 5p13.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Bastien L, Sawyer N, Grygorczyk R, Metters KM, Adam M: Cloning, functional expression, and characterization of the human prostaglandin E2 receptor EP2 subtype. J Biol Chem. 1994 Apr 22;269(16):11873-7. [PubMed Link Image]
  2. An S, Yang J, Xia M, Goetzl EJ: Cloning and expression of the EP2 subtype of human receptors for prostaglandin E2. Biochem Biophys Res Commun. 1993 Nov 30;197(1):263-70. [PubMed Link Image]
  3. Foord SM, Marks B, Stolz M, Bufflier E, Fraser NJ, Lee MG: The structure of the prostaglandin EP4 receptor gene and related pseudogenes. Genomics. 1996 Jul 1;35(1):182-8. [PubMed Link Image]
  4. Mori K, Tanaka I, Kotani M, Miyaoka F, Sando T, Muro S, Sasaki Y, Nakagawa O, Ogawa Y, Usui T, Ozaki S, Ichikawa A, Narumiya S, Nakao K: Gene expression of the human prostaglandin E receptor EP4 subtype: differential regulation in monocytoid and lymphoid lineage cells by phorbol ester. J Mol Med. 1996 Jun;74(6):333-6. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 14192
Enzyme 15 Name Melanophilin
Enzyme 15 Synonyms
  1. Exophilin-3
  2. Synaptotagmin-like protein 2a
  3. Slp homolog lacking C2 domains a
  4. SlaC2-a
Enzyme 15 Gene Name MLPH
Enzyme 15 Protein Sequence >Melanophilin
MGKKLDLSKLTDEEAQHVLEVVQRDFDLRRKEEERLEALKGKIKKESSKRELLSDTAHLN
ETHCARCLQPYQLLVNSKRQCLECGLFTCKSCGRVHPEEQGWICDPCHLARVVKIGSLEW
YYEHVKARFKRFGSAKVIRSLHGRLQGGAGPELISEERSGDSDQTDEDGEPGSEAQAQAQ
PFGSKKKRLLSVHDFDFEGDSDDSTQPQGHSLHLSSVPEARDSPQSLTDESCSEKAAPHK
AEGLEEADTGASGCHSHPEEQPTSISPSRHGALAELCPPGGSHRMALGTAAALGSNVIRN
EQLPLQYLADVDTSDEESIRAHVMASHHSKRRGRASSESQIFELNKHISAVECLLTYLEN
TVVPPLAKGLGAGVRTEADVEEEALRRKLEELTSNVSDQETSSEEEEAKDEKAEPNRDKS
VGPLPQADPEVGTAAHQTNRQEKSPQDPGDPVQYNRTTDEELSELEDRVAVTASEVQQAE
SEVSDIESRIAALRAAGLTVKPSGKPRRKSNLPIFLPRVAGKLGKRPEDPNADPSSEAKA
MAVPYLLRRKFSNSLKSQGKDDDSFDRKSVYRGSLTQRNPNARKGMASHTFAKPVVAHQS
Enzyme 15 Number of Residues 600
Enzyme 15 Molecular Weight 65950
Enzyme 15 Theoretical pI 5.98
Enzyme 15 GO Classification
Function
  • GTPase binding
  • Rab GTPase binding
  • binding
  • enzyme binding
  • protein binding
  • small GTPase binding
Process
  • cellular physiological process
  • intracellular protein transport
  • physiological process
  • protein transport
  • transport
Component
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 10433552 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9BV36 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name MELPH_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1719 bp
ATGGGGAAGAAACTGGATCTTTCCAAGCTCACTGATGAAGAGGCCCAGCATGTCTTGGAA
GTTGTTCAACGAGATTTTGACCTCCGAAGGAAAGAAGAGGAACGGCTAGAGGCGTTGAAG
GGCAAGATTAAGAAGGAAAGCTCCAAGAGGGAGCTGCTTTCCGACACTGCCCATCTGAAC
GAGACCCACTGCGCCCGCTGCCTGCAGCCCTACCAGCTGCTTGTGAATAGCAAAAGGCAG
TGCCTGGAATGTGGCCTCTTCACCTGCAAAAGCTGTGGCCGCGTCCACCCGGAGGAGCAG
GGCTGGATCTGTGACCCCTGCCATCCGGCCAGAGTCGTGAAGATCGGCTCACTGGAGTGG
TACTATGAGCATGTGAAAGCCCGCTTCAAGAGGTTCGGAAGTGCCAAGGTCATCCGGTCC
CTCCACGGGCGGCTGCAGGGTGGAGCTGGGCCTGAACTGATATCTGAAGAGAGAAGTGGA
GACAGCGACCAGACAGATGAGGATGGAGAACCTGGCTCAGAGGCCCAGGCCCAGGCCCAG
CCCTTTGGCAGCAAAAAAAAGCGCCTCCTCTCCGTCCACGACTTCGACTTCGAGGGAGAC
TCAGATGACTCCACTCAGCCTCAAGGTCACTCCCTGCACCTGTCCTCAGTCCCTGAGGCC
AGGGACAGCCCACAGTCCCTTACAGATGAGTCCTGCTCAGAGAAGGCAGCCCCTCACAAG
GCTGAGGGCCTGGAGGAGGCTGATACTGGGGCCTCTGGGTGCCACTCCCATCCGGAAGAG
CAGCCGACCAGCATCTCACCTTCCAGACACGGCGCCCTGGCTGAGCTCTGCCCGCCTGGA
GGCTCCCACAGGATGGCCCTGGGGACTGCTGCTGCACTCGGGTCGAATGTCATCAGGAAT
GAGCAGCTGCCCCTGCAGTACTTGGCCGATGTGGACACCTCTGATGAGGAAAGCATCCGG
GCTCACGTGATGGCCTCCCACCATTCCAAGCGGAGAGGCCGGGCGTCTTCTGAGAGTCAG
GGTCTAGGTGCTGGAGCGCGCACGGAGGCCGACGTAGAGGAGGAGGCCCTGAGGAGGAAG
CTGGAGGAGCTGACCAGCAACGTCAGTGACCAGGAGACCTCGTCCGAGGAGGAGGAGGCC
AAGGACGAAAAGGCAGAGCCCAACAGGGACAAATCAGTTGGGCCTCTCCCCCAGGCGGAC
CCGGAGGTGGGCACGGCTGCCCATCAAACCAACAGACAGGAAAAAAGCCCCCAGGACCCT
GGGGACCCCGTCCAGTACAACAGGACCACAGATGAGGAGCTGTCAGAGCTGGAGGACAGA
GTGGCAGTGACGGCCTCAGAAGTCCAGCAGGCAGAGAGCGAGGTTTCAGACATTGAATCC
AGGATTGCAGCCCTGAGGGCCGCAGGGCTCACGGTGAAGCCCTCGGGAAAGCCCCGGAGG
AAGTCAAACCTCCCGATATTTCTCCCTCGAGTGGCTGGGAAACTTGGCAAGAGACCAGAG
GACCCAAATGCAGACCCTTCAAGTGAGGCCAAGGCAATGGCTGTGCCCTATCTTCTGAGA
AGAAAGTTCAGTAATTCCCTGAAAAGTCAAGGTAAAGATGATGATTCTTTTGATCGGAAA
TCAGTGTACCGAGGCTCGCTGACACGGAGAAACCCCAACGCGAGGAAAGGAATGGCCAGC
CACACCTTCGCGAAACCTGTGGTGGCCCACCAGTCCTAA
Enzyme 15 GenBank Gene ID AK022207 Link Image
Enzyme 15 GeneCard ID Q9BV36 Link Image
Enzyme 15 GenAtlas ID MLPH Link Image
Enzyme 15 HGNC ID HGNC:29643 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. Nagashima K, Torii S, Yi Z, Igarashi M, Okamoto K, Takeuchi T, Izumi T: Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 2002 Apr 24;517(1-3):233-8. [PubMed Link Image]
Enzyme 15 Metabolite References
  1. Martel JA, Michael D, Fejes-Toth G, Naray-Fejes-Toth A: Melanophilin, a novel aldosterone-induced gene in mouse cortical collecting duct cells. Am J Physiol Renal Physiol. 2007 Sep;293(3):F904-13. Epub 2007 Jul 3. [PubMed Link Image]
Enzyme 16 [top]
Enzyme 16 ID 16423
Enzyme 16 Name Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name CYP11B2
Enzyme 16 Protein Sequence >Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQG
YEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYR
QHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNA
RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM
PRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELS
LEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATT
ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRP
ERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQED
IKMVYSFILRPGTSPLLTFRAIN
Enzyme 16 Number of Residues 503
Enzyme 16 Molecular Weight 57561
Enzyme 16 Theoretical pI 9.78
Enzyme 16 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 16 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B0ZBE4 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B0ZBE4_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID EU326306 Link Image
Enzyme 16 GeneCard ID B0ZBE4 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available