We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Adenosine (HMDB00050)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-03-23 10:06:10
Accession Number HMDB00050
Secondary Accession Numbers HMDB04401; HMDB04402; HMDB04421
Common Name Adenosine
Description A nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. For instance, adenosine plays an important role in energy transfer - as adenosine triphosphate (ATP) and adenosine diphosphate (ADP). It also plays a role in signal transduction as cyclic adenosine monophosphate, cAMP. Adenosine itself is both a neurotransmitter and potent vasodilator. When administered intravenously, adenosine causes transient heart block in the AV node. Because of the effects of adenosine on AV node-dependent supraventricular tachycardia, adenosine is considered a class V antiarrhythmic agent.
Synonyms
  1. 1-(6-amino-9H-purin-9-yl)-1-deoxy-beta-D-Ribofuranose
  2. 6-Amino-9beta-D-ribofuranosyl-9H-purine
  3. 9-beta-D-Arabinofuranosyladenine
  4. 9-beta-D-Ribofuranosidoadenine
  5. 9-beta-D-Ribofuranosyl-9H-purin-6-amine
  6. 9-beta-d-Ribofuranosyladenine
  7. 9beta-D-Ribofuranosyladenine
  8. 9beta-D-ribofuranosyl-9H-Purin-6-amine
  9. Adenine nucleoside
  10. Adenine riboside
  11. Adenocard
  12. Adenocor
  13. Adenoscan
  14. Adenosin
  15. Boniton
  16. Myocol
  17. Nucleocardyl
  18. Sandesin
  19. adenine-9beta-D-Ribofuranoside
  20. b-D-Adenosine
  21. beta-Adenosine
  22. 1-(6-amino-9H-purin-9-yl)-1-deoxy-beta-delta-Ribofuranose
  23. 6-Amino-9beta-delta-ribofuranosyl-9H-purine
  24. 9-beta-delta-Arabinofuranosyladenine
  25. 9-beta-delta-Ribofuranosidoadenine
  26. 9-beta-delta-Ribofuranosyl-9H-purin-6-amine
  27. 9-beta-delta-Ribofuranosyladenine
  28. 9beta-delta-Ribofuranosyladenine
  29. 9beta-delta-ribofuranosyl-9H-Purin-6-amine
  30. adenine-9beta-delta-Ribofuranoside
  31. beta-delta-Adenosine
  32. beta-D-Adenosine
Chemical IUPAC Name 2-(6-aminopurin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol
Chemical Formula C10H13N5O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Deoxy nucleosides
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Methionine metabolism
  • Component of Purine metabolism
  • Component of Selenoamino acid metabolism
Application
Source
  • Endogenous
Average Molecular Weight 267.241
Monoisotopic Molecular Weight 267.096741
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC(CO)C(O)C1O
KEGG Compound ID C00212 Link Image
BioCyc ID ADENOSINE Link Image
BiGG ID 34273 Link Image
Wikipedia Link Adenosine Link Image
NuGOwiki Link HMDB00050 Link Image
Metagene Link HMDB00050 Link Image
METLIN ID 86 Link Image
PubChem Compound 60961 Link Image
PubChem Substance 828107 Link Image
ChEBI ID 16335 Link Image
CAS Registry Number 58-61-7
InChI Identifier InChI=1/C10H13N5O4/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(18)6(17)4(1-16)19-10/h2-4,6-7,10,16-18H,1H2,(H2,11,12,13)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Liao, Ben-ren; Yuan, Zhen-wen. Synthesis of adenosine from inosine. Huaxue Shiji (2006), 28(10), 633-634.
Melting Point (Experimental) 235.5 oC
Experimental Water Solubility 7 mg/mL [Adenocard product monograph]; 37 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 8.23 mg/mL [MEYLAN,WM et al. (1996)]; 14.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.05 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.21 [Predicted by ALOGPS]; -1.6 [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 1BX4 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 0.2 (0.1-0.3) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
Biofluid Blood
Value 0.31 +/- 0.29 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 0.0425 +/- 0.0029 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kaufmann I, Hoelzl A, Schliephake F, Hummel T, Chouker A, Lysenko L, Peter K, Thiel M: Effects of adenosine on functions of polymorphonuclear leukocytes from patients with septic shock. Shock. 2007 Jan;27(1):25-31. [PubMed Link Image]
Biofluid Blood
Value 0.505 +/- 0.142 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal in plasma
Comments Not Available
References
  • Capogrossi MC, Holdiness MR, Israili ZH: Determination of adenosine in normal human plasma and serum by high-performance liquid chromatography. J Chromatogr. 1982 Jan 8;227(1):168-73. [PubMed Link Image]
Biofluid Blood
Value 5.66 +/- 1.71 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal in serum
Comments Not Available
References
  • Capogrossi MC, Holdiness MR, Israili ZH: Determination of adenosine in normal human plasma and serum by high-performance liquid chromatography. J Chromatogr. 1982 Jan 8;227(1):168-73. [PubMed Link Image]
Biofluid Blood
Value 0.285 +/- 0.060 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ontyd J, Schrader J: Measurement of adenosine, inosine, and hypoxanthine in human plasma. J Chromatogr. 1984 May 11;307(2):404-9. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 1.20 (0.90-1.50) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Biofluid CSF
Value 0 - 0.1 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
Biofluid CSF
Value 0.01 +/- 0.002 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Ballantyne PJ: Social context and outcomes for the ageing breast cancer patient: considerations for clinical practitioners. J Clin Nurs. 2004 Mar;13(3a):11-21. [PubMed Link Image]
Biofluid Urine
Value 4.7+/-7.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Vidotto C, Fousert D, Akkermann M, Griesmacher A, Muller MM: Purine and pyrimidine metabolites in children's urine. Clin Chim Acta. 2003 Sep;335(1-2):27-32. [PubMed Link Image]
Biofluid Urine
Value 17.5+/-14.6 umol/mmol creatinine
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Vidotto C, Fousert D, Akkermann M, Griesmacher A, Muller MM: Purine and pyrimidine metabolites in children's urine. Clin Chim Acta. 2003 Sep;335(1-2):27-32. [PubMed Link Image]
Biofluid Urine
Value 0.50 (0.09-0.92) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lee SH, Jung BH, Kim SY, Chung BC: A rapid and sensitive method for quantitation of nucleosides in human urine using liquid chromatography/mass spectrometry with direct urine injection. Rapid Commun Mass Spectrom. 2004;18(9):973-7. [PubMed Link Image]
Biofluid Urine
Value 0.17 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.126 +/- 0.018 uM
Age Adult:>18 yrs old
Sex Both
Condition Septic shock
Comments Not Available
References
  • Kaufmann I, Hoelzl A, Schliephake F, Hummel T, Chouker A, Lysenko L, Peter K, Thiel M: Effects of adenosine on functions of polymorphonuclear leukocytes from patients with septic shock. Shock. 2007 Jan;27(1):25-31. [PubMed Link Image]
Associated Disorders
Condition References
Septic shock
  • Kaufmann I, Hoelzl A, Schliephake F, Hummel T, Chouker A, Lysenko L, Peter K, Thiel M: Effects of adenosine on functions of polymorphonuclear leukocytes from patients with septic shock. Shock. 2007 Jan;27(1):25-31. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Skalhegg BS, Funderud A, Henanger HH, Hafte TT, Larsen AC, Kvissel AK, Eikvar S, Orstavik S: Protein kinase A (PKA)--a potential target for therapeutic intervention of dysfunctional immune cells. Curr Drug Targets. 2005 Sep;6(6):655-64. [PubMed Link Image]
  2. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  3. Lee SH, Jung BH, Kim SY, Chung BC: A rapid and sensitive method for quantitation of nucleosides in human urine using liquid chromatography/mass spectrometry with direct urine injection. Rapid Commun Mass Spectrom. 2004;18(9):973-7. [PubMed Link Image]
  4. Maytin M, Colucci WS: Cardioprotection: a new paradigm in the management of acute heart failure syndromes. Am J Cardiol. 2005 Sep 19;96(6A):26G-31G. [PubMed Link Image]
  5. Dodge-Kafka KL, Soughayer J, Pare GC, Carlisle Michel JJ, Langeberg LK, Kapiloff MS, Scott JD: The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways. Nature. 2005 Sep 22;437(7058):574-8. [PubMed Link Image]
  6. Gheorghiade M, Teerlink JR, Mebazaa A: Pharmacology of new agents for acute heart failure syndromes. Am J Cardiol. 2005 Sep 19;96(6A):68G-73G. [PubMed Link Image]
  7. Jansen RW, Kruijt JK, van Berkel TJ, Meijer DK: Coupling of the antiviral drug ara-AMP to lactosaminated albumin leads to specific uptake in rat and human hepatocytes. Hepatology. 1993 Jul;18(1):146-52. [PubMed Link Image]
  8. Ballantyne PJ: Social context and outcomes for the ageing breast cancer patient: considerations for clinical practitioners. J Clin Nurs. 2004 Mar;13(3a):11-21. [PubMed Link Image]
  9. Yamamoto T, Moriwaki Y, Takahashi S, Fujita T, Tsutsumi Z, Yamakita J, Shimizu K, Shiota M, Ohta S, Higashino K: Determination of adenosine and deoxyadenosine in urine by high-performance liquid chromatography with column switching. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):55-61. [PubMed Link Image]
  10. Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. [PubMed Link Image]
  11. Koeris M, Funke L, Shrestha J, Rich A, Maas S: Modulation of ADAR1 editing activity by Z-RNA in vitro. Nucleic Acids Res. 2005 Sep 21;33(16):5362-70. Print 2005. [PubMed Link Image]
  12. Vidotto C, Fousert D, Akkermann M, Griesmacher A, Muller MM: Purine and pyrimidine metabolites in children's urine. Clin Chim Acta. 2003 Sep;335(1-2):27-32. [PubMed Link Image]
  13. Dunne VG, Bhattachayya S, Besser M, Rae C, Griffin JL: Metabolites from cerebrospinal fluid in aneurysmal subarachnoid haemorrhage correlate with vasospasm and clinical outcome: a pattern-recognition 1H NMR study. NMR Biomed. 2005 Feb;18(1):24-33. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. Deoxycytidine kinase
  5. 5'(3')-deoxyribonucleotidase, mitochondrial precursor
  6. Cytosolic purine 5'-nucleotidase
  7. Purine nucleoside phosphorylase
  8. Adenosine kinase
  9. Putative adenosylhomocysteinase 3
  10. Putative adenosylhomocysteinase 2
  11. Adenosine deaminase
  12. Adenosine A1 receptor
  13. Adenosine A2a receptor
  14. Adenosine A3 receptor
  15. Adenosine A2b receptor
  16. Cytosolic 5'-nucleotidase III
  17. Adenosine 3'-phospho 5'-phosphosulfate transporter 1
  18. cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
  19. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  20. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  21. Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 1 [top]
Enzyme 1 ID 5232
Enzyme 1 Name Cytosolic 5'-nucleotidase 1B
Enzyme 1 Synonyms
  1. Cytosolic 5'-nucleotidase IB
  2. cN1B
  3. cN-IB
  4. Autoimmune infertility-related protein
Enzyme 1 Gene Name NT5C1B
Enzyme 1 Protein Sequence >Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
Enzyme 1 Number of Residues 610
Enzyme 1 Molecular Weight 68804
Enzyme 1 Theoretical pI 9.03
Enzyme 1 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 13774961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96P26 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 5NT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1699 bp
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
Enzyme 1 GenBank Gene ID AF356185 Link Image
Enzyme 1 GeneCard ID NT5C1B Link Image
Enzyme 1 GenAtlas ID NT5C1B Link Image
Enzyme 1 HGNC ID HGNC:17818 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5233
Enzyme 2 Name Cytosolic 5'-nucleotidase 1A
Enzyme 2 Synonyms
  1. Cytosolic 5'-nucleotidase IA
  2. cN1A
  3. cN-IA
  4. cN-I
Enzyme 2 Gene Name NT5C1A
Enzyme 2 Protein Sequence >Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
Enzyme 2 Number of Residues 368
Enzyme 2 Molecular Weight 41021
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12659324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BXI3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 5NT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
Enzyme 2 GenBank Gene ID AF331801 Link Image
Enzyme 2 GeneCard ID NT5C1A Link Image
Enzyme 2 GenAtlas ID NT5C1A Link Image
Enzyme 2 HGNC ID HGNC:17819 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p34.3-p33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5234
Enzyme 3 Name 5'(3')-deoxyribonucleotidase, cytosolic type
Enzyme 3 Synonyms
  1. Cytosolic 5',3'-pyrimidine nucleotidase
  2. Deoxy-5'-nucleotidase 1
  3. dNT-1
Enzyme 3 Gene Name NT5C
Enzyme 3 Protein Sequence >5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
Enzyme 3 Number of Residues 201
Enzyme 3 Molecular Weight 23383
Enzyme 3 Theoretical pI 6.63
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7524492 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TCD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NT5C_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
Enzyme 3 GenBank Gene ID AF154829 Link Image
Enzyme 3 GeneCard ID NT5C Link Image
Enzyme 3 GenAtlas ID NT5C Link Image
Enzyme 3 HGNC ID HGNC:17144 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed Link Image]
  2. Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5235
Enzyme 4 Name Deoxycytidine kinase
Enzyme 4 Synonyms
  1. dCK
Enzyme 4 Gene Name DCK
Enzyme 4 Protein Sequence >Deoxycytidine kinase
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL
Enzyme 4 Number of Residues 260
Enzyme 4 Molecular Weight 30519
Enzyme 4 Theoretical pI 4.88
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents
Enzyme 4 Pathways
Enzyme 4 Reactions
  • NTP + deoxycytidine = NDP + dCMP
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 181510 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P27707 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DCK_HUMAN Link Image
Enzyme 4 PDB ID 1P62 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >783 bp
ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA
Enzyme 4 GenBank Gene ID M60527 Link Image
Enzyme 4 GeneCard ID DCK Link Image
Enzyme 4 GenAtlas ID DCK Link Image
Enzyme 4 HGNC ID HGNC:2704 Link Image
Enzyme 4 Chromosome Location 4
Enzyme 4 Locus 4q13.3-q21.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed Link Image]
  2. Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed Link Image]
  3. Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5236
Enzyme 5 Name 5'(3')-deoxyribonucleotidase, mitochondrial precursor
Enzyme 5 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 5 Gene Name NT5M
Enzyme 5 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial precursor
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 5 Number of Residues 228
Enzyme 5 Molecular Weight 25862
Enzyme 5 Theoretical pI 8.12
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 9408106 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 5 PDB ID 1Q92 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 5 GenBank Gene ID AJ277557 Link Image
Enzyme 5 GeneCard ID NT5M Link Image
Enzyme 5 GenAtlas ID NT5M Link Image
Enzyme 5 HGNC ID HGNC:15769 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17p11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed Link Image]
  2. Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5237
Enzyme 6 Name Cytosolic purine 5'-nucleotidase
Enzyme 6 Synonyms
  1. 5'-nucleotidase cytosolic II
Enzyme 6 Gene Name NT5C2
Enzyme 6 Protein Sequence >Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
Enzyme 6 Number of Residues 561
Enzyme 6 Molecular Weight 64970
Enzyme 6 Theoretical pI 6.05
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and other purine nucleotides
Enzyme 6 Pathways
Enzyme 6 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 633071 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49902 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name 5NTC_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1686 bp
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 6 GenBank Gene ID D38524 Link Image
Enzyme 6 GeneCard ID NT5C2 Link Image
Enzyme 6 GenAtlas ID NT5C2 Link Image
Enzyme 6 HGNC ID HGNC:8022 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q24.32-q24.33
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5805
Enzyme 7 Name Purine nucleoside phosphorylase
Enzyme 7 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 7 Gene Name NP
Enzyme 7 Protein Sequence >Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 7 Number of Residues 289
Enzyme 7 Molecular Weight 32118
Enzyme 7 Theoretical pI 6.95
Enzyme 7 GO Classification
Function
  • catalytic activity
  • purine-nucleoside phosphorylase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 35565 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 7 PDB ID 1RT9 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 7 GenBank Gene ID X00737 Link Image
Enzyme 7 GeneCard ID NP Link Image
Enzyme 7 GenAtlas ID NP Link Image
Enzyme 7 HGNC ID HGNC:7892 Link Image
Enzyme 7 Chromosome Location 14
Enzyme 7 Locus 14q13.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  3. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  4. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  5. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  6. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5912
Enzyme 8 Name Adenosine kinase
Enzyme 8 Synonyms
  1. AK
  2. Adenosine 5'-phosphotransferase
Enzyme 8 Gene Name ADK
Enzyme 8 Protein Sequence >Adenosine kinase
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAED
KHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKA
AEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKAR
VCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGN
ETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFA
VLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPD
FH
Enzyme 8 Number of Residues 362
Enzyme 8 Molecular Weight 40546
Enzyme 8 Theoretical pI 6.67
Enzyme 8 GO Classification
Function
  • adenosine kinase activity
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • purine ribonucleoside salvage
  • purine salvage
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + adenosine = ADP + AMP
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1224125 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P55263 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ADK_HUMAN Link Image
Enzyme 8 PDB ID 1BX4 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1038 bp
ATGACGTCAGTCAGAGAAAATATTCTCTTTGGAATGGGAAATCCTCTGCTTGACATCTCT
GCTGTAGTGGACAAAGATTTCCTTGATAAGTATTCTCTGAAACCAAATGACCAAATCTTG
GCTGAAGACAAACACAAGGAACTGTTTGATGAACTTGTGAAAAAATTCAAAGTCGAATAT
CATGCTGGTGGCTCTACCCAGAATTCAATTAAAGTGGCTCAGTGGATGATTCAACAGCCA
CACAAAGCAGCAACATTTTTTGGATGCATTGGGATAGATAAATTTGGGGAGATCCTGAAG
AGAAAAGCTGCTGAAGCCCATGTGGATGCTCATTACTACGAGCAGAATGAGCAGCCAACA
GGAACTTGTGCTGCATGCATCACTGGTGACAACAGGTCCCTCATAGCTAATCTTGCTGCT
GCCAATTGTTATAAAAAGGAAAAACATCTTGATCTGGAGAAAAACTGGATGTTGGTAGAA
AAAGCAAGAGTTTGTTATATAGCAGGCTTTTTTCTTCACGTTTCCCCAGAGTCAGTATTA
AAGGTGGCTCACCATGCTTCTGAAAACAACAGGATTTTCACTTTGAATCTATCTGCACCG
TTTATTAGCCAGTTCTACAAGGAATCATTGATGAAAGTTATGCCTTATGTTGATATACTT
TTTGGAAATGAGACAGAAGCTGCCACTTTTGCTAGAGAGCAAGGCTTTGAGACTAAAGAC
ATTAAAGAGATAGCCAAAAAGACACAAGCCCTGCCAAAGATGAACTCAAAGAGGCAGCGA
ATCGTGATCTTCACCCAAGGGAGAGATGACACTATAATGGCTACAGAAAGTGAAGTCACT
GCTTTTGCTGTCTTGGATCAAGACCAGAAAGAAATTATTGATACCAATGGAGCTGGAGAT
GCATTTGTTGGAGGTTTTCTGTCTCAACTGGTCTCTGACAAGCCTCTGACTGAATGTATC
CGTGCTGGCCACTATGCAGCAAGCATCATAATTAGACGGACTGGCTGCACCTTTCCTGAG
AAGCCAGACTTCCACTGA
Enzyme 8 GenBank Gene ID U50196 Link Image
Enzyme 8 GeneCard ID ADK Link Image
Enzyme 8 GenAtlas ID ADK Link Image
Enzyme 8 HGNC ID HGNC:257 Link Image
Enzyme 8 Chromosome Location 10
Enzyme 8 Locus 10q22|10q11-q24
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1232-7. [PubMed Link Image]
  2. Singh B, Hao W, Wu Z, Eigl B, Gupta RS: Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. Eur J Biochem. 1996 Oct 15;241(2):564-71. [PubMed Link Image]
  3. McNally T, Helfrich RJ, Cowart M, Dorwin SA, Meuth JL, Idler KB, Klute KA, Simmer RL, Kowaluk EA, Halbert DN: Cloning and expression of the adenosine kinase gene from rat and human tissues. Biochem Biophys Res Commun. 1997 Feb 24;231(3):645-50. [PubMed Link Image]
  4. Mathews II, Erion MD, Ealick SE: Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. [PubMed Link Image]
  5. Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5933
Enzyme 9 Name Putative adenosylhomocysteinase 3
Enzyme 9 Synonyms
  1. S-adenosyl-L- homocysteine hydrolase 3
  2. AdoHcyase 3
Enzyme 9 Gene Name KIAA0828
Enzyme 9 Protein Sequence >Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
Enzyme 9 Number of Residues 611
Enzyme 9 Molecular Weight 66722
Enzyme 9 Theoretical pI 7.39
Enzyme 9 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
Enzyme 9 General Function Coenzyme transport and metabolism
Enzyme 9 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 9 Pathways
Enzyme 9 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 4240145 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q96HN2 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name SAHH3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1860 bp
GAGCCGGTGGTTGCAGCGGAGGCGGTGATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCC
GCCAAGGTGCCTGAGGTGGAGCTGAAGGACCTGAGCCCCTCCGAGGCGGAGTCGCAACTA
GGACTGAGCACGGCCGCCGTGGGCGCCATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAG
GCTCCAGCTCCCGCCGCGGAGCGGCCCCCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCC
GCTCTCAGCCCCGCCGCCGGGAAGGTGCCTCAGGCGTCGGCCATGAAGCGGAGCGACCCA
CATCACCAGCACCAGCGGCACCGCGACGGCGGCGAGGCCCTGGTCAGCCCCGACGGCACC
GTCACCGAGGCGCCGCGCACAGTCAAGAAGATCCAGTTTGCTGACCAGAAGCAAGAATTC
AACAAACGTCCCACCAAAATTGGACGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCT
ACTGACAGCTACAGCTCAGCGGCTTCATATACAGATAGCTCTGATGATGAGACATCGCCC
AGGGACAAGCAGCAAAAGAACTCTAAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAA
CAGGCAGAGTTTGGACGAAGAGAAATTGAAATTGCTGAACAAGAAATGCCTGCATTGATG
GCTTTGAGGAAGAGAGCTCAAGGAGAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGC
ACACACATCACTGCTCAGACTGCTGTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAG
TGCCGATGGGCTGCCTGCAACATCTATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCA
GAAAGTGGATTTCCTGTTTTTGCCTGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGT
ATCGATAGATGTGTGAATGTGGAGGGCTGGCAGCCAAACATGATCTTGGATGATGGAGGG
GATCTTACCCACTGGATTTATAAAAAGTATCCCAACATGTTTAAGAAAATCAAGGGCATA
GTAGAGGAGAGTGTTACTGGAGTTCACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTG
TGTGTTCCAGCCATGAATGTCAATGACTCAGTCACCAAACAGAAATTTGACAACCTCTAC
TGTTGCCGTGAATCAATTCTTGATGGACTTAAAAGGACAACAGACATGATGTTTGGTGGA
AAGCAAGTGGTAGTCTGTGGCTATGGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAA
GCCATGGGCTCCATTGTGTATGTAACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGT
ATGGATGGATTTCGACTGGTGAAATTAAATGAGGTCATCCGACAAGTGGACATTGTTATT
ACCTGTACAGGTAACAAGAATGTGGTAACCAGAGAGCACTTGGACCGTATGAAGAATAGC
TGCATCGTTTGTAACATGGGACATTCCAACACAGAGATTGACGTGGCGAGTCTGCGGACA
CCAGAACTGACCTGGGAGCGAGTGAGATCTCAAGTTGACCATGTGATATGGCCTGATGGC
AAGAGGATAGTACTGCTGGCAGAGGGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCT
ACATTTGTGCTCTCAATCACTGCTACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAAT
GCTCCTGAGGGTCGCTATAAGCAGGATGTCTACCTGTTGCCCAAGAAGATGGATGAGTAT
GTGGCCAGCCTACACCTGCCTACCTTTGATGCCCACTTGACAGAGCTGACAGATGAACAG
GCCAAGTATCTGGGACTCAACAAGAATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA
Enzyme 9 GenBank Gene ID AB020635 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location 7
Enzyme 9 Locus 7q32.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5935
Enzyme 10 Name Putative adenosylhomocysteinase 2
Enzyme 10 Synonyms
  1. S-adenosyl-L- homocysteine hydrolase 2
  2. AdoHcyase 2
  3. S-adenosylhomocysteine hydrolase-like 1
  4. DC-expressed AHCY-like molecule
Enzyme 10 Gene Name AHCYL1
Enzyme 10 Protein Sequence >Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
Enzyme 10 Number of Residues 530
Enzyme 10 Molecular Weight 58952
Enzyme 10 Theoretical pI 6.87
Enzyme 10 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • one-carbon compound metabolism
  • physiological process
Component
Enzyme 10 General Function Coenzyme transport and metabolism
Enzyme 10 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 10 Pathways
Enzyme 10 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 16588687 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O43865 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SAHH2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1593 bp
ATGTCGATGCCTGACGCGATGCCGCTGCCCGGGGTCGGGGAGGAGCTGAAGCAGGCCAAG
GAGATCGAGGACGCCGAGAAGTACTCCTTCATGGCCACCGTCACCAAGGCGCCCAAGAAG
CAAATCCAGTTTGCTGATGACATGCAGGAGTTCACCAAATTCCCCACCAAAACTGGCCGA
AGATCTTTGTCTCGCTCGATCTCACAGTCCTCCACTGACAGCTACAGTTCAGCTGCATCC
TACACAGATAGCTCTGATGATGAGGTTTCTCCCCGAGAGAAGCAGCAAACCAACTCCAAG
GGCAGCAGCAATTTCTGTGTGAAGAACATCAAGCAGGCAGAATTTGGACGCCGGGAGATT
GAGATTGCAGAGCAAGACATGTCTGCTCTGATTTCACTCAGGAAACGTGCTCAGGGGGAG
AAGCCCTTGGCTGGTGCTAAAATAGTGGGCTGTACACACATCACAGCCCAGACAGCGGTG
TTGATTGAGACACTCTGTGCCCTGGGGGCTCAGTGCCGCTGGTCTGCTTGTAACATCTAC
TCAACTCAGAATGAAGTAGCTGCAGCACTGGCTGAGGCTGGAGTTGCAGTGTTCGCTTGG
AAGGGCGAGTCAGAAGATGACTTCTGGTGGTGTATTGACCGCTGTGTGAACATGGATGGG
TGGCAGGCCAACATGATCCTGGATGATGGGGGAGACTTAACCCACTGGGTTTATAAGAAG
TATCCAAACGTGTTTAAGAAGATCCGAGGCATTGTGGAAGAGAGCGTGACTGGTGTTCAC
AGGCTGTATCAGCTCTCCAAAGCTGGGAAGCTCTGTGTTCCGGCCATGAACGTCAATGAT
TCTGTTACCAAACAGAAGTTTGATAACTTGTACTGCTGCCGAGAATCCATTTTGGATGGC
CTGAAGAGGACCACAGATGTGATGTTTGGTGGGAAACAAGTGGTGGTGTGTGGCTATGGT
GAGGTAGGCAAGGGCTGCTGTGCTGCTCTCAAAGCTCTTGGAGCAATTGTCTACATTACC
GAAATCGACCCCATCTGTGCTCTGCAGGCCTGCATGGATGGGTTCAGGGTGGTAAAGCTA
AATGAAGTCATCCGGCAAGTCGATGTCGTAATAACTTGCACAGGAAATAAGAATGTAGTG
ACACGGGAGCACTTGGATCGCATGAAAAACAGTTGTATCGTATGCAATATGGGCCACTCC
AACACAGAAATCGATGTGACCAGCCTCCGCACTCCGGAGCTGACGTGGGAGCGAGTACGT
TCTCAGGTGGACCATGTCATCTGGCCAGATGGCAAACGAGTTGTCCTCCTGGCAGAGGGT
CGTCTACTCAATTTGAGCTGCTCCACAGTTCCCACCTTTGTTCTGTCCATCACAGCCACA
ACACAGGCTTTGGCACTGATAGAACTCTATAATGCACCCGAGGGGCGATACAAGCAGGAT
GTGTACTTGCTTCCTAAGAAAATGGATGAATACGTTGCCAGCTTGCATCTGCCATCATTT
GATGCCCACCTTACAGAGCTGACAGATGACCAAGCAAAATATCTGGGACTCAACAAAAAT
GGGCCATTCAAACCTAATTATTACAGATACTAA
Enzyme 10 GenBank Gene ID AF315687 Link Image
Enzyme 10 GeneCard ID AHCYL1 Link Image
Enzyme 10 GenAtlas ID AHCYL1 Link Image
Enzyme 10 HGNC ID HGNC:344 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p13.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Dekker JW, Budhia S, Angel NZ, Cooper BJ, Clark GJ, Hart DN, Kato M: Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics. 2002 Mar;53(12):993-1001. Epub 2002 Feb 13. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5937
Enzyme 11 Name Adenosine deaminase
Enzyme 11 Synonyms
  1. Adenosine aminohydrolase
Enzyme 11 Gene Name ADA
Enzyme 11 Protein Sequence >Adenosine deaminase
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPD
FLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQA
EGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAI
DLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGY
HTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIF
KSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAG
QNL
Enzyme 11 Number of Residues 363
Enzyme 11 Molecular Weight 40765
Enzyme 11 Theoretical pI 5.80
Enzyme 11 GO Classification
Function
  • adenosine deaminase activity
  • catalytic activity
  • deaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 11 General Function Replication, recombination and repair
Enzyme 11 Specific Function Adenosine + H(2)O = inosine + NH(3)
Enzyme 11 Pathways
Enzyme 11 Reactions
  • adenosine + H2O = inosine + ammonia
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 28380 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00813 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ADA_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1092 bp
ATGGCCCAGACGCCCGCCTTCGACAAGCCCAAAGTAGAACTGCATGTCCACCTAGACGGA
TCCATCAAGCCTGAAACCATCTTATACTATGGCAGGAGGAGAGGGATCGCCCTCCCAGCT
AACACAGCAGAGGGGCTGCTGAACGTCATTGGCATGGACAAGCCGCTCACCCTTCCAGAC
TTCCTGGCCAAGTTTGACTACTACATGCCTGCTATCGCGGGCTGCCGGGAGGCTATCAAA
AGGATCGCCTATGAGTTTGTAGAGATGAAGGCCAAAGAGGGCGTGGTGTATGTGGAGGTG
CGGTACAGTCCGCACCTGCTGGCCAACTCCAAAGTGGAGCCAATCCCCTGGAACCAGGCT
GAAGGGGACCTCACCCCAGACGAGGTGGTGGCCCTAGTGGGCCAGGGCCTGCAGGAGGGG
GAGCGAGACTTCGGGGTCAAGGCCCGGTCCATCCTGTGCTGCATGCGCCACCAGCCCAAC
TGGTCCCCCAAGGTGGTGGAGCTGTGTAAGAAGTACCAGCAGCAGACCGTGGTGGCCATT
GACCTGGCTGGAGATGAGACCATCCCAGGAAGCAGCCTCTTGCCTGGACATGTCCAGGCC
TACCAGGAGGCTGTGAAGAGCGGCATTCACCGTACTGTCCACGCCGGGGAGGTGGGCTCG
GCCGAAGTAGTAAAAGAGGCTGTGGACATACTCAAGACAGAGCGGCTGGGACACGGCTAC
CACACCCTGGAAGACCAGGCCCTTTATAACAGGCTGCGGCAGGAAAACATGCACTTCGAG
ATCTGCCCCTGGTCCAGCTACCTCACTGGTGCCTGGAAGCCGGACACGGAGCATGCAGTC
ATTCGGCTCAAAAATGACCAGGCTAACTACTCGCTCAACACAGATGACCCGCTCATCTTC
AAGTCCACCCTGGACACTGATTACCAGATGACCAAACGGGACATGGGCTTTACTGAAGAG
GAGTTTAAAAGGCTGAACATCAATGCGGCCAAATCTAGTTTCCTCCCAGAAGATGAAAAG
AGGGAGCTTCTCGACCTGCTCTATAAAGCCTATGGGATGCCACCTTCAGCCTCTGCAGGG
CAGAACCTCTGA
Enzyme 11 GenBank Gene ID X02994 Link Image
Enzyme 11 GeneCard ID ADA Link Image
Enzyme 11 GenAtlas ID ADA Link Image
Enzyme 11 HGNC ID HGNC:186 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20q12-q13.11
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Daddona PE, Shewach DS, Kelley WN, Argos P, Markham AF, Orkin SH: Human adenosine deaminase. cDNA and complete primary amino acid sequence. J Biol Chem. 1984 Oct 10;259(19):12101-6. [PubMed Link Image]
  2. Wiginton DA, Adrian GS, Hutton JJ: Sequence of human adenosine deaminase cDNA including the coding region and a small intron. Nucleic Acids Res. 1984 Mar 12;12(5):2439-46. [PubMed Link Image]
  3. Valerio D, Duyvesteyn MG, Dekker BM, Weeda G, Berkvens TM, van der Voorn L, van Ormondt H, van der Eb AJ: Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. EMBO J. 1985 Feb;4(2):437-43. [PubMed Link Image]
  4. Wiginton DA, Kaplan DJ, States JC, Akeson AL, Perme CM, Bilyk IJ, Vaughn AJ, Lattier DL, Hutton JJ: Complete sequence and structure of the gene for human adenosine deaminase. Biochemistry. 1986 Dec 16;25(25):8234-44. [PubMed Link Image]
  5. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  6. Orkin SH, Daddona PE, Shewach DS, Markham AF, Bruns GA, Goff SC, Kelley WN: Molecular cloning of human adenosine deaminase gene sequences. J Biol Chem. 1983 Nov 10;258(21):12753-6. [PubMed Link Image]
  7. Hirschhorn R, Yang DR, Israni A: An Asp8Asn substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA 2 allozyme): occurrence on different chromosomal backgrounds and apparent intragenic crossover. Ann Hum Genet. 1994 Jan;58(Pt 1):1-9. [PubMed Link Image]
  8. Adrian GS, Wiginton DA, Hutton JJ: Structure of adenosine deaminase mRNAs from normal and adenosine deaminase-deficient human cell lines. Mol Cell Biol. 1984 Sep;4(9):1712-7. [PubMed Link Image]
  9. Bonthron DT, Markham AF, Ginsburg D, Orkin SH: Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency. J Clin Invest. 1985 Aug;76(2):894-7. [PubMed Link Image]
  10. Akeson AL, Wiginton DA, Dusing MR, States JC, Hutton JJ: Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts. J Biol Chem. 1988 Nov 5;263(31):16291-6. [PubMed Link Image]
  11. Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH: Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency. J Clin Invest. 1989 Feb;83(2):497-501. [PubMed Link Image]
  12. Hirschhorn R: Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions. Hum Mutat. 1992;1(2):166-8. [PubMed Link Image]
  13. Santisteban I, Arredondo-Vega FX, Kelly S, Mary A, Fischer A, Hummell DS, Lawton A, Sorensen RU, Stiehm ER, Uribe L, et al.: Novel splicing, missense, and deletion mutations in seven adenosine deaminase-deficient patients with late/delayed onset of combined immunodeficiency disease. Contribution of genotype to phenotype. J Clin Invest. 1993 Nov;92(5):2291-302. [PubMed Link Image]
  14. Yang DR, Huie ML, Hirschhorn R: Homozygosity for a missense mutation (G20R) associated with neonatal onset adenosine deaminase-deficient severe combined immunodeficiency (ADA-SCID). Clin Immunol Immunopathol. 1994 Feb;70(2):171-5. [PubMed Link Image]
  15. Santisteban I, Arredondo-Vega FX, Kelly S, Loubser M, Meydan N, Roifman C, Howell PL, Bowen T, Weinberg KI, Schroeder ML, et al.: Three new adenosine deaminase mutations that define a splicing enhancer and cause severe and partial phenotypes: implications for evolution of a CpG hotspot and expression of a transduced ADA cDNA. Hum Mol Genet. 1995 Nov;4(11):2081-7. [PubMed Link Image]
  16. Santisteban I, Arredondo-Vega FX, Kelly S, Debre M, Fischer A, Perignon JL, Hilman B, elDahr J, Dreyfus DH, Gelfand EW, et al.: Four new adenosine deaminase mutations, altering a zinc-binding histidine, two conserved alanines, and a 5' splice site. Hum Mutat. 1995;5(3):243-50. [PubMed Link Image]
  17. Hirschhorn R, Borkowsky W, Jiang CK, Yang DR, Jenkins T: Two newly identified mutations (Thr233Ile and Leu152Met) in partially adenosine deaminase-deficient (ADA-) individuals that result in differing biochemical and metabolic phenotypes. Hum Genet. 1997 Jul;100(1):22-9. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6980
Enzyme 12 Name Adenosine A1 receptor
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name ADORA1
Enzyme 12 Protein Sequence >Adenosine A1 receptor
MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGA
LVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVT
PRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYM
VYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALIL
FLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFL
KIWNDHFRCQPAPPIDEDLPEERPDD
Enzyme 12 Number of Residues 326
Enzyme 12 Molecular Weight 36512
Enzyme 12 Theoretical pI 8.75
Enzyme 12 GO Classification
Function
  • A1 adenosine receptor activity, G-protein coupled
  • G-protein coupled receptor activity
  • adenosine receptor activity, G-protein coupled
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide 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 12 General Function Not Available
Enzyme 12 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-33
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 256155 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P30542 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name AA1R_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >981 bp
ATGCCGCCCTCCATCTCAGCTTTCCAGGCCGCCTACATCGGCATCGAGGTGCTCATCGCC
CTGGTCTCTGTGCCCGGGAACGTGCTGGTGATCTGGGCGGTGAAGGTGAACCAGGCGCTG
CGGGATGCCACCTTCTGCTTCATCGTGTCGCTGGCGGTGGCTGATGTGGCCGTGGGTGCC
CTGGTCATCCCCCTCGCCATCCTCATCAACATTGGGCCACAGACCTACTTCCACACCTGC
CTCATGGTTGCCTGTCCGGTCCTCATCCTCACCCAGAGCTCCATCCTGGCCCTGCTGGCA
ATTGCGGTGGACCGCTACCTCCGGGTCAAGATCCCTCTCCGGTACAAGATGGTGGTGACC
CCCCGGAGGGCGGCGGTGGCCATAGCCGGCTGCTGGATCCTCTCCTTCGTGGTGGGACTG
ACCCCTATGTTTGGCTGGAACAATCTGAGTGCGGTGGAGCGGGCCTGGGCAGCCAACGGC
AGCATGGGGGAGCCCGTGATCAAGTGCGAGTTCGAGAAGGTCATCAGCATGGAGTACATG
GTCTACTTCAACTTCTTTGTGTGGGTGCTCCCCCCGCTTCTCCTCATGGTCCTCATCTAC
CTGGAGGTCTTCTACCTAATCCGCAAGCAGCTCAACAAGAAGGTGTCGGCCTCCTCCGGC
GACCCGCAGAAGTACTATGGGAAGGAGCTGAAGATCGCCAAGTCGCTGGCCCTCATCCTC
TTCCTCTTTGCCCTCAGCTGGCTGCCTTTGCACATCCTCAACTGCATCACCCTCTTCTGC
CCGTCCTGCCACAAGCCCAGCATCCTTACCTACATTGCCATCTTCCTCACGCACGGCAAC
TCGGCCATGAACCCCATTGTCTATGCCTTCCGCATCCAGAAGTTCCGCGTCACCTTCCTT
AAGATTTGGAATGACCATTTCCGCTGCCAGCCTGCACCTCCCATTGACGAGGATCTCCCA
GAAGAGAGGCCTGATGACTAG
Enzyme 12 GenBank Gene ID S45235 Link Image
Enzyme 12 GeneCard ID ADORA1 Link Image
Enzyme 12 GenAtlas ID ADORA1 Link Image
Enzyme 12 HGNC ID HGNC:262 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1q32.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Libert F, Van Sande J, Lefort A, Czernilofsky A, Dumont JE, Vassart G, Ensinger HA, Mendla KD: Cloning and functional characterization of a human A1 adenosine receptor. Biochem Biophys Res Commun. 1992 Sep 16;187(2):919-26. [PubMed Link Image]
  2. Townsend-Nicholson A, Shine J: Molecular cloning and characterisation of a human brain A1 adenosine receptor cDNA. Brain Res Mol Brain Res. 1992 Dec;16(3-4):365-70. [PubMed Link Image]
  3. Ren H, Stiles GL: Characterization of the human A1 adenosine receptor gene. Evidence for alternative splicing. J Biol Chem. 1994 Jan 28;269(4):3104-10. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6982
Enzyme 13 Name Adenosine A2a receptor
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name ADORA2A
Enzyme 13 Protein Sequence >Adenosine A2a receptor
MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAI
PFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTR
AKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYF
NFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVG
LFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFR
KIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNG
YALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS
Enzyme 13 Number of Residues 412
Enzyme 13 Molecular Weight 44708
Enzyme 13 Theoretical pI 8.05
Enzyme 13 GO Classification
Function
  • A2A adenosine receptor activity, G-protein coupled
  • G-protein coupled receptor activity
  • adenosine receptor activity, G-protein coupled
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide 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 13 General Function Not Available
Enzyme 13 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-30
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 177892 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P29274 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name AA2AR_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1230 bp
ATGGGCTCCTCGGTGTACATCACGGTGGAGCTGGCCATTGCTGTGCTGGCCATCCTGGGC
AATGTGCTGGTGTGCTGGGCCGTGTGGCTCAACAGCAACCTGCAGAACGTCACCAACTAC
TTTGTGGTGTCACTGGCGGCGGCCGACATCGCAGTGGGTGTGCTCGCCATCCCCTTTGCC
ATCACCATCAGCACCGGGTTCTGCGCTGCCTGCCACGGCTGCCTCTTCATTGCCTGCTTC
GTCCTGGTCCTCACGCAGAGCTCCATCTTCAGTCTCCTGGCCATCGCCATTGACCGCTAC
ATTGCCATCCGCATCCCGCTCCGGTACAATGGCTTGGTGACCGGCACGAGGGCTAAGGGC
ATCATTGCCATCTGCTGGGTGCTGTCGTTTGCCATCGGCCTGACTCCCATGCTAGGTTGG
AACAACTGCGGTCAGCCAAAGGAGGGCAAGAACCACTCCCAGGGCTGCGGGGAGGGCCAA
GTGGCCTGTCTCTTTGAGGATGTGGTCCCCATGAACTACATGGTGTACTTCAACTTCTTT
GCCTGTGTGCTGGTGCCCCTGCTGCTCATGCTGGGTGTCTATTTGCGGATCTTCCTGGCG
GCGCGACGACAGCTGAAGCAGATGGAGAGCCAGCCTCTGCCGGGGGAGCGGGCACGGTCC
ACACTGCAGAAGGAGGTCCATGCTGCCAAGTCACTGGCCATCATTGTGGGGCTCTTTGCC
CTCTGCTGGCTGCCCCTACACATCATCAACTGCTTCACTTTCTTCTGCCCCGACTGCAGC
CACGCCCCTCTCTGGCTCATGTACCTGGCCATCGTCCTCTCCCACACCAATTCGGTTGTG
AATCCCTTCATCTACGCCTACCGTATCCGCGAGTTCCGCCAGACCTTCCGCAAGATCATT
CGCAGCCACGTCCTGAGGCAGCAAGAACCTTTCAAGGCAGCTGGCACCAGTGCCCGGGTC
TTGGCAGCTCATGGCAGTGACGGAGAGCAGGTCAGCCTCCGTCTCAACGGCCACCCGCCA
GGAGTGTGGGCCAACGGCAGTGCTCCCCACCCTGAGCGGAGGCCCAATGGCTATGCCCTG
GGGCTGGTGAGTGGAGGGAGTGCCCAAGAGTCCCAGGGGAACACGGGCCTCCCAGACGTG
GAGCTCCTTAGCCATGAGCTCAAGGGAGTGTGCCCAGAGCCCCCTGGCCTAGATGACCCC
CTGGCCCAGGATGGAGCAGGAGTGTCCTGA
Enzyme 13 GenBank Gene ID M97370 Link Image
Enzyme 13 GeneCard ID ADORA2A Link Image
Enzyme 13 GenAtlas ID ADORA2A Link Image
Enzyme 13 HGNC ID HGNC:263 Link Image
Enzyme 13 Chromosome Location 22
Enzyme 13 Locus 22q11.23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Furlong TJ, Pierce KD, Selbie LA, Shine J: Molecular characterization of a human brain adenosine A2 receptor. Brain Res Mol Brain Res. 1992 Sep;15(1-2):62-6. [PubMed Link Image]
  2. Le F, Townsend-Nicholson A, Baker E, Sutherland GR, Schofield PR: Characterization and chromosomal localization of the human A2a adenosine receptor gene: ADORA2A. Biochem Biophys Res Commun. 1996 Jun 14;223(2):461-7. [PubMed Link Image]
  3. Kim J, Wess J, van Rhee AM, Schoneberg T, Jacobson KA: Site-directed mutagenesis identifies residues involved in ligand recognition in the human A2a adenosine receptor. J Biol Chem. 1995 Jun 9;270(23):13987-97. [PubMed Link Image]
  4. 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]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6985
Enzyme 14 Name Adenosine A3 receptor
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name ADORA3
Enzyme 14 Protein Sequence >Adenosine A3 receptor
MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIA
VGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKR
VTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYF
SFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFA
LSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKAC
VVCHPSDSLDTSIEKNSE
Enzyme 14 Number of Residues 318
Enzyme 14 Molecular Weight 36185
Enzyme 14 Theoretical pI 9.04
Enzyme 14 GO Classification
Function
  • A3 adenosine receptor activity, G-protein coupled
  • G-protein coupled receptor activity
  • adenosine receptor activity, G-protein coupled
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide 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 14 General Function Not Available
Enzyme 14 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Possible role in reproduction
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 15-37 49-72 85-106 127-148 178-198 232-255 262-284
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 349449 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P33765 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name AA3R_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >957 bp
ATGCCCAACAACAGCACTACTCTGTCATTGGCCAATGTTACCTACATCACCATGGAAATT
TTCATTGGACTCTGCGCCATAGTGGGCAACGTGCTGGTCATCTGCGTGGTCAAGCTGAAC
CCCAGCCTGCAGACCACCACCTTCTATTTCATTGTCTCTCTAGCCCTGGCTGACATTGCT
GTTGGGGTGCTGGTCATGCCTTTGGCCATTGTTGTCAGCCTGGGCATCACAATCCACTTC
TACAGCTGCCTTTTTATGACTTGCCTACTGCTTATCTTTACCCACGCCTCCATCATGTCC
TTGCTGGCCATCGCTGTGGACCGATACTTGCGGGTCAAGCTTACCGTCAGATACAAGAGG
GTCACCACTCACAGAAGAATATGGCTGGCCCTGGGCCTTTGCTGGCTGGTGTCATTCCTG
GTGGGATTGACCCCCATGTTTGGCTGGAACATGAAACTGACCTCAGAGTACCACAGAAAT
GTCACCTTCCTTTCATGCCAATTTGTTTCCGTCATGAGAATGGACTACATGGTATACTTC
AGCTTCCTCACCTGGATTTTCATCCCCCTGGTTGTCATGTGCGCCATCTATCTTGACATC
TTTTACATCATTCGGAACAAACTCAGTCTGAACTTATCTAACTCCAAAGAGACAGGTGCA
TTTTATGGACGGGAGTTCAAGACGGCTAAGTCCTTGTTTCTGGTTCTTTTCTTGTTTGCT
CTGTCATGGCTGCCTTTATCTATCATCAACTGCATCATCTACTTTAATGGTGAGGTACCA
CAGCTTGTGCTGTACATGGGCATCCTGCTGTCCCATGCCAACTCCATGATGAACCCTATC
GTCTATGCCTATAAAATAAAGAAGTTCAAGGAAACCTACCTTTTGATCCTCAAAGCCTGT
GTGGTCTGCCATCCCTCTGATTCTTTGGACACAAGCATTGAGAAGAATTCTGAGTAG
Enzyme 14 GenBank Gene ID L20463 Link Image
Enzyme 14 GeneCard ID ADORA3 Link Image
Enzyme 14 GenAtlas ID ADORA3 Link Image
Enzyme 14 HGNC ID HGNC:268 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1p13.2
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Sajjadi FG, Firestein GS: cDNA cloning and sequence analysis of the human A3 adenosine receptor. Biochim Biophys Acta. 1993 Oct 7;1179(1):105-7. [PubMed Link Image]
  2. Salvatore CA, Jacobson MA, Taylor HE, Linden J, Johnson RG: Molecular cloning and characterization of the human A3 adenosine receptor. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10365-9. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6986
Enzyme 15 Name Adenosine A2b receptor
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name ADORA2B
Enzyme 15 Protein Sequence >Adenosine A2b receptor
MLLETQDALYVALELVIAALSVAGNVLVCAAVGTANTLQTPTNYFLVSLAAADVAVGLFA
IPFAITISLGFCTDFYGCLFLACFVLVLTQSSIFSLLAVAVDRYLAICVPLRYKSLVTGT
RARGVIAVLWVLAFGIGLTPFLGWNSKDSATNNCTEPWDGTTNESCCLVKCLFENVVPMS
YMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTELMDHSRTTLQREIHAAKSLAMIV
GIFALCWLPVHAVNCVTLFQPAQGKNKPKWAMNMAILLSHANSVVNPIVYAYRNRDFRYT
FHKIISRYLLCQADVKSGNGQAGVQPALGVGL
Enzyme 15 Number of Residues 332
Enzyme 15 Molecular Weight 36333
Enzyme 15 Theoretical pI 8.31
Enzyme 15 GO Classification
Function
  • A2B adenosine receptor activity, G-protein coupled
  • G-protein coupled receptor activity
  • adenosine receptor activity, G-protein coupled
  • nucleotide receptor activity, G-protein coupled
  • purinergic nucleotide 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 15 General Function Not Available
Enzyme 15 Specific Function Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 9-31 45-67 79-101 122-144 179-203 236-259 268-291
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 178150 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P29275 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name AA2BR_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >999 bp
ATGCTGCTGGAGACACAGGACGCGCTGTACGTGGCGCTGGAGCTGGTCATCGCCGCGCTT
TCGGTGGCGGGCAACGTGCTGGTGTGCGCCGCGGTGGGCACGGCGAACACTCTGCAGACG
CCCACCAACTACTTCCTGGTGTCCCTGGCTGCGGCCGACGTGGCCGTGGGGCTCTTCGCC
ATCCCCTTTGCCATCACCATCAGCCTGGGCTTCTGCACTGACTTCTACGGCTGCCTCTTC
CTCGCCTGCTTCGTGCTGGTGCTCACGCAGAGCTCCATCTTCAGCCTTCTGGCCGTGGCA
GTCGACAGATACCTGGCCATCTGTGTCCCGCTCAGGTATAAAAGTTTGGTCACGGGGACC
CGAGCAAGAGGGGTCATTGCTGTCCTCTGGGTCCTTGCCTTTGGCATCGGATTGACTCCA
TTCCTGGGGTGGAACAGTAAAGACAGTGCCACCAACAACTGCACAGAACCCTGGGATGGA
ACCACGAATGAAAGCTGCTGCCTTGTGAAGTGTCTCTTTGAGAATGTGGTCCCCATGAGC
TACATGGTATATTTCAATTTCTTTGGGTGTGTTCTGCCCCCACTGCTTATAATGCTGGTG
ATCTACATTAAGATCTTCCTGGTGGCCTGCAGGCAGCTTCAGCGCACTGAGCTGATGGAC
CACTCGAGGACCACCCTCCAGCGGGAGATCCATGCAGCCAAGTCACTGGCCATGATTGTG
GGGATTTTTGCCCTGTGCTGGTTACCTGTGCATGCTGTTAACTGTGTCACTCTTTTCCAG
CCAGCTCAGGGTAAAAATAAGCCCAAGTGGGCAATGAATATGGCCATTCTTCTGTCACAT
GCCAATTCAGTTGTCAATCCCATTGTCTATGCTTACCGGAACCGAGACTTCCGCTACACT
TTTCACAAAATTATCTCCAGGTATCTTCTCTGCCAAGCAGATGTCAAGAGTGGGAATGGT
CAGGCTGGGGTACAGCCTGCTCTCGGTGTGGGCCTATGA
Enzyme 15 GenBank Gene ID M97759 Link Image
Enzyme 15 GeneCard ID ADORA2B Link Image
Enzyme 15 GenAtlas ID ADORA2B Link Image
Enzyme 15 HGNC ID HGNC:264 Link Image
Enzyme 15 Chromosome Location 17
Enzyme 15 Locus 17p12-p11.2
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Pierce KD, Furlong TJ, Selbie LA, Shine J: Molecular cloning and expression of an adenosine A2b receptor from human brain. Biochem Biophys Res Commun. 1992 Aug 31;187(1):86-93. [PubMed Link Image]
  2. Jacobson MA, Johnson RG, Luneau CJ, Salvatore CA: Cloning and chromosomal localization of the human A2b adenosine receptor gene (ADORA2B) and its pseudogene. Genomics. 1995 May 20;27(2):374-6. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8749
Enzyme 16 Name Cytosolic 5'-nucleotidase III
Enzyme 16 Synonyms
  1. cN-III
  2. Pyrimidine 5'- nucleotidase 1
  3. P5'N-1
  4. P5N-1
  5. PN-I
  6. Uridine 5'-monophosphate hydrolase 1
  7. p36
Enzyme 16 Gene Name NT5C3
Enzyme 16 Protein Sequence >Cytosolic 5'-nucleotidase III
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 16 Number of Residues 336
Enzyme 16 Molecular Weight 37949
Enzyme 16 Theoretical pI 7.15
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 16 Pathways
Enzyme 16 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-32
Enzyme 16 Transmembrane Regions
  • 13-35
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 11245474 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >861 bp
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 16 GenBank Gene ID AF312735 Link Image
Enzyme 16 GeneCard ID NT5C3 Link Image
Enzyme 16 GenAtlas ID NT5C3 Link Image
Enzyme 16 HGNC ID HGNC:17820 Link Image
Enzyme 16 Chromosome Location 7
Enzyme 16 Locus 7p14.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  4. Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8826
Enzyme 17 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Enzyme 17 Synonyms
  1. PAPS transporter 1
  2. Solute carrier family 35 member B2
  3. Putative MAPK-activating protein PM15
  4. Putative NF-kappa-B-activating protein 48
Enzyme 17 Gene Name SLC35B2
Enzyme 17 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 1
MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYF
RRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQ
VSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHG
APMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEY
LTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSV
QMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIG
QFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGK
KAVPVESPVQKV
Enzyme 17 Number of Residues 432
Enzyme 17 Molecular Weight 47515
Enzyme 17 Theoretical pI 9.40
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF- kappa-B and MAPK pathways
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-20
Enzyme 17 Transmembrane Regions
  • 5-25 40-60 109-129 154-174 238-258 265-285 299-319 353-373 387-407
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 32480471 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q8TB61 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name S35B2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1299 bp
ATGGACGCCAGATGGTGGGCAGTGGTGGTGCTGGCTGCGTTCCCCTCCCTAGGGGCAGGT
GGGGAGACTCCCGAAGCCCCTCCGGAGTCATGGACCCAGCTATGGTTCTTCCGATTTGTG
GTGAATGCTGCTGGCTATGCCAGCTTTATGGTACCTGGCTACCTCCTGGTGCAGTACTTC
AGGCGGAAGAACTACCTGGAGACCGGTAGGGGCCTCTGCTTTCCCCTGGTGAAAGCTTGT
GTGTTTGGCAATGAGCCCAAGGCCTCTGATGAGGTTCCCCTGGCGCCCCGAACAGAGGCG
GCAGAGACCACCCCGATGTGGCAGGCCCTGAAGCTGCTCTTCTGTGCCACAGGGCTCCAG
GTGTCTTATCTGACTTGGGGTGTGCTGCAGGAAAGAGTGATGACCCGCAGCTATGGGGCC
ACAGCCACATCACCGGGTGAGCGCTTTACGGACTCGCAGTTCCTGGTGCTAATGAACCGA
GTGCTGGCACTGATTGTGGCTGGCCTCTCCTGTGTTCTCTGCAAGCAGCCCCGGCATGGG
GCACCCATGTACCGGTACTCCTTTGCCAGCCTGTCCAATGTGCTTAGCAGCTGGTGCCAA
TACGAAGCTCTTAAGTTCGTCAGCTTCCCCACCCAGGTGCTGGCCAAGGCCTCTAAGGTG
ATCCCTGTCATGCTGATGGGAAAGCTTGTGTCTCGGCGCAGCTACGAACACTGGGAGTAC
CTGACAGCCACCCTCATCTCCATTGGGGTCAGCATGTTTCTGCTATCCAGCGGACCAGAG
CCCCGCAGCTCCCCAGCCACCACACTCTCAGGCCTCATCTTACTGGCAGGTTATATTGCT
TTTGACAGCTTCACCTCAAACTGGCAGGATGCCCTGTTTGCCTATAAGATGTCATCGGTG
CAGATGATGTTTGGGGTCAATTTCTTCTCCTGCCTCTTCACAGTGGGCTCACTGCTAGAA
CAGGGGGCCCTACTGGAGGGAACCCGCTTCATGGGGCGACACAGTGAGTTTGCTGCCCAT
GCCCTGCTACTCTCCATCTGCTCCGCATGTGGCCAGCTCTTCATCTTTTACACCATTGGG
CAGTTTGGGGCTGCCGTCTTCACCATCATCATGACCCTCCGCCAGGCCTTTGCCATCCTT
CTTTCCTGCCTTCTCTATGGCCACACTGTCACTGTGGTGGGAGGGCTGGGGGTGGCTGTG
GTCTTTGCTGCCCTCCTGCTCAGAGTCTACGCGCGGGGCCGTCTAAAGCAACGGGGAAAG
AAGGCTGTGCCTGTTGAGTCTCCTGTGCAGAAGGTTTGA
Enzyme 17 GenBank Gene ID AB106538 Link Image
Enzyme 17 GeneCard ID SLC35B2 Link Image
Enzyme 17 GenAtlas ID SLC35B2 Link Image
Enzyme 17 HGNC ID HGNC:16872 Link Image
Enzyme 17 Chromosome Location 6
Enzyme 17 Locus 6p12.1-p11.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Kamiyama S, Suda T, Ueda R, Suzuki M, Okubo R, Kikuchi N, Chiba Y, Goto S, Toyoda H, Saigo K, Watanabe M, Narimatsu H, Jigami Y, Nishihara S: Molecular cloning and identification of 3'-phosphoadenosine 5'-phosphosulfate transporter. J Biol Chem. 2003 Jul 11;278(28):25958-63. Epub 2003 Apr 25. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 13068
Enzyme 18 Name cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
Enzyme 18 Synonyms
  1. AHCY, mRNA
  2. S-adenosylhomocysteine hydrolase, isoform CRA_a
Enzyme 18 Gene Name AHCY
Enzyme 18 Protein Sequence >cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 18 Number of Residues 432
Enzyme 18 Molecular Weight 47717
Enzyme 18 Theoretical pI 6.29
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Coenzyme transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158261867 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K307 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K307_HUMAN Link Image
Enzyme 18 PDB ID 1LI4 Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AK290422 Link Image
Enzyme 18 GeneCard ID A8K307 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 15061
Enzyme 19 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name Not Available
Enzyme 19 Protein Sequence >cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
Enzyme 19 Number of Residues 561
Enzyme 19 Molecular Weight 64960
Enzyme 19 Theoretical pI 6.05
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function Not Available
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 158256766 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1686 bp
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 19 GenBank Gene ID AK291667 Link Image
Enzyme 19 GeneCard ID A8K6K2 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs Not Available
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16422
Enzyme 20 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name Not Available
Enzyme 20 Protein Sequence >cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
Enzyme 20 Number of Residues 574
Enzyme 20 Molecular Weight 63396
Enzyme 20 Theoretical pI 7.04
Enzyme 20 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 20 General Function Nucleotide transport and metabolism
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AK314661 Link Image
Enzyme 20 GeneCard ID B2RBH2 Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs Not Available
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 17072
Enzyme 21 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 21 Synonyms
  1. PAPS transporter 2
  2. Solute carrier family 35 member B3
  3. 3'-phosphoadenosine 5'-phosphosulfate transporter
Enzyme 21 Gene Name SLC35B3
Enzyme 21 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 2
MDLTQQAKDIQNITVQETNKNNSESIECSKITMDLKFNNSRKYISITVPSKTQTMSPHIK
SVDDVVVLGMNLSKFNKLTQFFICVAGVFVFYLIYGYLQELIFSVEGFKSCGWYLTLVQF
AFYSIFGLIELQLIQDKRRRIPGKTYMIIAFLTVGTMGLSNTSLGYLNYPTQVIFKCCKL
IPVMLGGVFIQGKRYNVADVSAAICMSLGLIWFTLADSTTAPNFNLTGVVLISLALCADA
VIGNVQEKAMKLHNASNSEMVLYSYSIGFVYILLGLTCTSGLGPAVTFCAKNPVRTYGYA
FLFSLTGYFGISFVLALIKIFGALIAVTVTTGRKAMTIVLSFIFFAKPFTFQYVWSGLLV
VLGIFLNVYSKNMDKIRLPSLYDLINKSVEARKSRTLAQTV
Enzyme 21 Number of Residues 401
Enzyme 21 Molecular Weight 44593
Enzyme 21 Theoretical pI 9.58
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 78-98 114-134 147-167 170-190 196-216 223-243 267-287 298-317 324-346 349-369
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID Q9H1N7 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name S35B3_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AB231931 Link Image
Enzyme 21 GeneCard ID Q9H1N7 Link Image
Enzyme 21 GenAtlas ID SLC35B3 Link Image
Enzyme 21 HGNC ID HGNC:21601 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available