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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-Thymidylic acid (HMDB01227)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:36
Accession Number HMDB01227
Secondary Accession Numbers Not Available
Common Name 5-Thymidylic acid
Description 5-Thymidylic acid is a thymine nucleotide. Also known as thymidine monophosphate, and abbreviated TMP, is a nucleotide that is found in DNA. It is an ester of phosphoric acid with the nucleoside thymidine. TMP consists of a phosphate group, esterified to the the pentose sugar deoxyribose moiety, and the nucleobase thymine. In mammalian cells, thymidine deprivation induces chromosome aberrations such as chromatid breaks, chromatid interchanges, and chromosome fragmentation. (PMID 3888175)
Synonyms
  1. 2'-Deoxythymidine 5'-monophosphate
  2. 5'-TMP
  3. 5'-Thymidylate
  4. 5'-Thymidylic acid
  5. 5'-dTMP
  6. 5-Methyl-dUMP
  7. DTMP
  8. Deoxy TMP
  9. Deoxyribosylthymine monophosphate
  10. Deoxythymidine 5'-monophosphate
  11. Deoxythymidine 5'-phosphate
  12. Deoxythymidine monophosphate
  13. Deoxythymidylate
  14. Deoxythymidylic acid
  15. Deoxythymydilate
  16. Deoxythymydilic acid
  17. Thymidine 5'-monophosphate
  18. Thymidine 5'-phosphate
  19. Thymidine 5'-phosphorate
  20. Thymidine 5'-phosphoric acid
  21. Thymidine 5'MP
  22. Thymidine mononucleotide
  23. Thymidine monophosphate
  24. Thymidine phosphate
  25. Thymidine-5'-monophosphorate
  26. Thymidine-5'-monophosphoric acid
  27. Thymidylate
  28. Thymidylic acid
Chemical IUPAC Name [3-hydroxy-5-(5-methyl-2,4-dioxo-pyrimidin-1-yl)-oxolan-2-yl]methoxyphosphonic acid
Chemical Formula C10H15N2O8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • DNA component
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 322.208
Monoisotopic Molecular Weight 322.056610
Isomeric SMILES CC1=CN([C@H]2C[C@H](O)[C@@H](COP(O)(O)=O)O2)C(=O)NC1=O
Canonical SMILES CC1=CN(C2CC(O)C(COP(O)(O)=O)O2)C(=O)NC1=O
KEGG Compound ID C00364 Link Image
BioCyc ID TMP Link Image
BiGG ID 34753 Link Image
Wikipedia Link dTMP Link Image
NuGOwiki Link HMDB01227 Link Image
Metagene Link HMDB01227 Link Image
METLIN ID 6092 Link Image
PubChem Compound 9700 Link Image
PubChem Substance 3655 Link Image
ChEBI ID 17013 Link Image
CAS Registry Number 365-07-1
InChI Identifier InChI=1/C10H15N2O8P/c1-5-3-12(10(15)11-9(5)14)8-2-6(13)7(20-8)4-19-21(16,17)18/h3,6-8,13H,2,4H2,1H3,(H,11,14,15)(H2,16,17,18)/t6-,7+,8+/m0/s1
Synthesis Reference Scarano, E. Enzymic formation of thymidylic acid from 5-methyl-5'-deoxycytidylic acid. Bollettino - Societa Italiana di Biologia Sperimentale (1958), 34 945.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 6.78 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.37 [Predicted by ALOGPS]; -3 [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 1CY1 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
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)
  • lysosome
  • mitochondria
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Gribaudo G, Riera L, Caposio P, Maley F, Landolfo S: Human cytomegalovirus requires cellular deoxycytidylate deaminase for replication in quiescent cells. J Gen Virol. 2003 Jun;84(Pt 6):1437-41. [PubMed Link Image]
  2. Seno T, Ayusawa D, Shimizu K, Koyama H, Takeishi K, Hori T: Thymineless death and genetic events in mammalian cells. Basic Life Sci. 1985;31:241-63. [PubMed Link Image]
  3. Terai C, Carson DA: Pyrimidine nucleotide and nucleic acid synthesis in human monocytes and macrophages. Exp Cell Res. 1991 Apr;193(2):375-81. [PubMed Link Image]
  4. Gribaudo G, Riera L, Lembo D, De Andrea M, Gariglio M, Rudge TL, Johnson LF, Landolfo S: Murine cytomegalovirus stimulates cellular thymidylate synthase gene expression in quiescent cells and requires the enzyme for replication. J Virol. 2000 Jun;74(11):4979-87. [PubMed Link Image]
  5. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. 5'(3')-deoxyribonucleotidase, mitochondrial precursor
  5. Cytosolic purine 5'-nucleotidase
  6. Thymidylate kinase
  7. Ectonucleoside triphosphate diphosphohydrolase 1
  8. Soluble calcium-activated nucleotidase 1
  9. Thymidylate synthase
  10. Thymidine kinase, cytosolic
  11. Cytosolic 5'-nucleotidase III
  12. Ectonucleoside triphosphate diphosphohydrolase 8
  13. Thymidine kinase
  14. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  15. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  16. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
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 5236
Enzyme 4 Name 5'(3')-deoxyribonucleotidase, mitochondrial precursor
Enzyme 4 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 4 Gene Name NT5M
Enzyme 4 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial precursor 
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 4 Number of Residues 228
Enzyme 4 Molecular Weight 25862
Enzyme 4 Theoretical pI 8.12
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 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 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9408106 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 4 PDB ID 1Q92 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >687 bp 
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 4 GenBank Gene ID AJ277557 Link Image
Enzyme 4 GeneCard ID NT5M Link Image
Enzyme 4 GenAtlas ID NT5M Link Image
Enzyme 4 HGNC ID HGNC:15769 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5237
Enzyme 5 Name Cytosolic purine 5'-nucleotidase
Enzyme 5 Synonyms
  1. 5'-nucleotidase cytosolic II
Enzyme 5 Gene Name NT5C2
Enzyme 5 Protein Sequence >Cytosolic purine 5'-nucleotidase 
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
Enzyme 5 Number of Residues 561
Enzyme 5 Molecular Weight 64970
Enzyme 5 Theoretical pI 6.05
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 633071 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P49902 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name 5NTC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID D38524 Link Image
Enzyme 5 GeneCard ID NT5C2 Link Image
Enzyme 5 GenAtlas ID NT5C2 Link Image
Enzyme 5 HGNC ID HGNC:8022 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q24.32-q24.33
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5312
Enzyme 6 Name Thymidylate kinase
Enzyme 6 Synonyms
  1. dTMP kinase
Enzyme 6 Gene Name DTYMK
Enzyme 6 Protein Sequence >Thymidylate kinase 
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
Enzyme 6 Number of Residues 212
Enzyme 6 Molecular Weight 23820
Enzyme 6 Theoretical pI 8.49
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • thymidylate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • dTDP biosynthesis
  • dTTP biosynthesis
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine deoxyribonucleoside diphosphate biosynthesis
  • pyrimidine deoxyribonucleoside triphosphate biosynthesis
  • pyrimidine nucleoside diphosphate biosynthesis
  • pyrimidine nucleoside triphosphate biosynthesis
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Catalyzes the conversion of dTMP to dTDP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + dTMP = ADP + dTDP
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 37206 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P23919 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DTYMK_HUMAN Link Image
Enzyme 6 PDB ID 1E9A Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >636 bp 
ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA
Enzyme 6 GenBank Gene ID X54729 Link Image
Enzyme 6 GeneCard ID DTYMK Link Image
Enzyme 6 GenAtlas ID DTYMK Link Image
Enzyme 6 HGNC ID HGNC:3061 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q37.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed Link Image]
  2. Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5313
Enzyme 7 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 7 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 7 Gene Name ENTPD1
Enzyme 7 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 7 Number of Residues 510
Enzyme 7 Molecular Weight 57965
Enzyme 7 Theoretical pI 6.29
Enzyme 7 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 17-37 479-499
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 765256 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1533 bp 
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 7 GenBank Gene ID S73813 Link Image
Enzyme 7 GeneCard ID ENTPD1 Link Image
Enzyme 7 GenAtlas ID ENTPD1 Link Image
Enzyme 7 HGNC ID HGNC:3363 Link Image
Enzyme 7 Chromosome Location 10
Enzyme 7 Locus 10q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5314
Enzyme 8 Name Soluble calcium-activated nucleotidase 1
Enzyme 8 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 8 Gene Name CANT1
Enzyme 8 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 8 Number of Residues 401
Enzyme 8 Molecular Weight 44840
Enzyme 8 Theoretical pI 5.98
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 8 Pathways
Enzyme 8 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 45-62
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 22218108 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 8 PDB ID 1S1D Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1116 bp 
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 8 GenBank Gene ID AF328554 Link Image
Enzyme 8 GeneCard ID CANT1 Link Image
Enzyme 8 GenAtlas ID CANT1 Link Image
Enzyme 8 HGNC ID HGNC:19721 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17q25.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [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. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5316
Enzyme 9 Name Thymidylate synthase
Enzyme 9 Synonyms
  1. TS
  2. TSase
Enzyme 9 Gene Name TYMS
Enzyme 9 Protein Sequence >Thymidylate synthase 
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFG
MQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDS
LGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMC
AWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHI
TGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEG
YNPHPTIKMEMAV
Enzyme 9 Number of Residues 313
Enzyme 9 Molecular Weight 35716
Enzyme 9 Theoretical pI 7.00
Enzyme 9 GO Classification
Function
  • 5,10-methylenetetrahydrofolate-dependent methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • thymidylate synthase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • dTMP biosynthesis
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine deoxyribonucleoside monophosphate biosynthesis
  • pyrimidine nucleoside monophosphate biosynthesis
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Enzyme 9 Pathways
Enzyme 9 Reactions
  • 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 37479 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P04818 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name TYSY_HUMAN Link Image
Enzyme 9 PDB ID 1JUJ Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >942 bp 
ATGCCTGTGGCCGGCTCGGAGCTGCCGCGCCGGCCCTTGCCCCCCGCCGCACAGGAGCGG
GACGCCGAGCCGCGTCCGCCGCACGGGGAGCTGCAGTACCTGGGGCAGATCCAACACATC
CTCCGCTGCGGCGTCAGGAAGGACGACCGCACGGGCACCGGCACCCTGTCGGTATTCGGC
ATGCAGGCGCGCTACAGCCTGAGAGATGAATTCCCTCTGCTGACAACCAAACGTGTGTTC
TGGAAGGGTGTTTTGGAGGAGTTGCTGTGGTTTATCAAGGGATCCACAAATGCTAAAGAG
CTGTCTTCCAAGGGAGTGAAAATCTGGGATGCCAATGGATCCCGAGACTTTTTGGACAGC
CTGGGATTCTCCACCAGAGAAGAAGGGGACTTGGGCCCAGTTTATGGCTTCCAGTGGAGG
CATTTTGGGGCAGAATACAGAGATATGGAATCAGATTATTCAGGACAGGGAGTTGACCAA
CTGCAAAGAGTGATTGACACCATCAAAACCAACCCTGACGACAGAAGAATCATCATGTGC
GCTTGGAATCCAAGAGATCTTCCTCTGATGGCGCTGCCTCCATGCCATGCCCTCTGCCAG
TTCTATGTGGTGAACAGTGAGCTGTCCTGCCAGCTGTACCAGAGATCGGGAGACATGGGC
CTCGGTGTGCCTTTCAACATCGCCAGCTACGCCCTGCTCACGTACATGATTGCGCACATC
ACGGGCCTGAAGCCAGGTGACTTTATACACACTTTGGGAGATGCACATATTTACCTGAAT
CACATCGAGCCACTGAAAATTCAGCTTCAGCGAGAACCCAGACCTTTCCCAAAGCTCAGG
ATTCTTCGAAAAGTTGAGAAAATTGATGACTTCAAAGCTGAAGACTTTCAGATTGAAGGG
TACAATCCGCATCCAACTATTAAAATGGAAATGGCTGTTTAG
Enzyme 9 GenBank Gene ID X02308 Link Image
Enzyme 9 GeneCard ID TYMS Link Image
Enzyme 9 GenAtlas ID TYMS Link Image
Enzyme 9 HGNC ID HGNC:12441 Link Image
Enzyme 9 Chromosome Location 18
Enzyme 9 Locus 18p11.32
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Nucleotide sequence of a functional cDNA for human thymidylate synthase. Nucleic Acids Res. 1985 Mar 25;13(6):2035-43. [PubMed Link Image]
  2. Kaneda S, Nalbantoglu J, Takeishi K, Shimizu K, Gotoh O, Seno T, Ayusawa D: Structural and functional analysis of the human thymidylate synthase gene. J Biol Chem. 1990 Nov 25;265(33):20277-84. [PubMed Link Image]
  3. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Human thymidylate synthase gene: isolation of phage clones which cover a functionally active gene and structural analysis of the region upstream from the translation initiation codon. J Biochem (Tokyo). 1989 Oct;106(4):575-83. [PubMed Link Image]
  4. Shimizu K, Ayusawa D, Takeishi K, Seno T: Purification and NH2-terminal amino acid sequence of human thymidylate synthase in an overproducing transformant of mouse FM3A cells. J Biochem (Tokyo). 1985 Mar;97(3):845-50. [PubMed Link Image]
  5. Davisson VJ, Sirawaraporn W, Santi DV: Expression of human thymidylate synthase in Escherichia coli. J Biol Chem. 1989 Jun 5;264(16):9145-8. [PubMed Link Image]
  6. Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM: Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. Biochemistry. 1995 Dec 19;34(50):16279-87. [PubMed Link Image]
  7. Phan J, Koli S, Minor W, Dunlap RB, Berger SH, Lebioda L: Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug. Biochemistry. 2001 Feb 20;40(7):1897-902. [PubMed Link Image]
  8. Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L: Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors. J Biol Chem. 2001 Apr 27;276(17):14170-7. Epub 2001 Jan 24. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5317
Enzyme 10 Name Thymidine kinase, cytosolic
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name TK1
Enzyme 10 Protein Sequence >Thymidine kinase, cytosolic 
MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR
YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI
VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK
YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN
Enzyme 10 Number of Residues 234
Enzyme 10 Molecular Weight 25469
Enzyme 10 Theoretical pI 8.61
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • deoxynucleoside kinase activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • thymidine kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function ATP + thymidine = ADP + thymidine 5'- phosphate
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 339709 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P04183 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name KITH_HUMAN Link Image
Enzyme 10 PDB ID 1XBT Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >705 bp 
ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG
ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC
CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC
TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG
CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG
TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT
GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG
CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC
GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG
TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG
GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG
CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA
Enzyme 10 GenBank Gene ID K02581 Link Image
Enzyme 10 GeneCard ID TK1 Link Image
Enzyme 10 GenAtlas ID TK1 Link Image
Enzyme 10 HGNC ID HGNC:11830 Link Image
Enzyme 10 Chromosome Location 17
Enzyme 10 Locus 17q23.2-q25.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Bradshaw HD Jr, Deininger PL: Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol. 1984 Nov;4(11):2316-20. [PubMed Link Image]
  2. Flemington E, Bradshaw HD Jr, Traina-Dorge V, Slagel V, Deininger PL: Sequence, structure and promoter characterization of the human thymidine kinase gene. Gene. 1987;52(2-3):267-77. [PubMed Link Image]
  3. Chang ZF, Huang DY, Chi LM: Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J Biol Chem. 1998 May 15;273(20):12095-100. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 8749
Enzyme 11 Name Cytosolic 5'-nucleotidase III
Enzyme 11 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 11 Gene Name NT5C3
Enzyme 11 Protein Sequence >Cytosolic 5'-nucleotidase III 
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 11 Number of Residues 336
Enzyme 11 Molecular Weight 37949
Enzyme 11 Theoretical pI 7.15
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 11 Pathways
Enzyme 11 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-32
Enzyme 11 Transmembrane Regions
  • 13-35
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 11245474 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >861 bp 
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 11 GenBank Gene ID AF312735 Link Image
Enzyme 11 GeneCard ID NT5C3 Link Image
Enzyme 11 GenAtlas ID NT5C3 Link Image
Enzyme 11 HGNC ID HGNC:17820 Link Image
Enzyme 11 Chromosome Location 7
Enzyme 11 Locus 7p14.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 13379
Enzyme 12 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 12 Synonyms
  1. NTPDase 8
  2. NTPDase8
  3. E-NTPDase 8
Enzyme 12 Gene Name ENTPD8
Enzyme 12 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8 
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 12 Number of Residues 495
Enzyme 12 Molecular Weight 53904
Enzyme 12 Theoretical pI 4.96
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 12 Pathways
Enzyme 12 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085] ALL_REAC R00085
  • (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 9-29 472-492
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 59003409 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1488 bp 
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCCGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTGCAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 12 GenBank Gene ID AY903953 Link Image
Enzyme 12 GeneCard ID Q5MY95 Link Image
Enzyme 12 GenAtlas ID ENTPD8 Link Image
Enzyme 12 HGNC ID HGNC:24860 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15060
Enzyme 13 Name Thymidine kinase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >Thymidine kinase 
MRPGLFKGQAPGSRRRPTAGLAVVRADSHRKEPRASGSARPAMLLWPLRGWAARALRCFG
PGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEV
LTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHS
ARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCR
EEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLQLFEQNRDRILTP
ENRKHCP
Enzyme 13 Number of Residues 307
Enzyme 13 Molecular Weight 35440
Enzyme 13 Theoretical pI 10.07
Enzyme 13 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 13 General Function Nucleotide transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 25167087 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8IZR3 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q8IZR3_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >924 bp 
ATGCGACCGGGTCTCTTTAAGGGCCAGGCGCCGGGATCCAGGCGGCGCCCAACGGCTGGA
CTAGCAGTCGTCCGCGCCGACTCGCACAGGAAGGAACCCCGGGCCTCTGGATCCGCTCGC
CCGGCTATGCTGCTGTGGCCGCTGCGGGGCTGGGCCGCCCGGGCGCTGCGCTGCTTTGGG
CCGGGAAGTCGCGGGAGCCCGGCCTCAGGCCCCGGGCCGCGGAGGGTGCAGCGCCGGGCC
TGGCCTCCCGATAAAGAACAGGAAAAAGAGAAAAAATCAGTGATCTGTGTCGAGGGCAAT
ATTGCAAGTGGGAAGACGACATGCCTGGAATTCTTCTCCAACGCGACAGACGTCGAGGTG
TTAACGGAGCCTGTGTCCAAGTGGAGAAATGTCCGTGGCCACAATCCTCTGGGCCTGATG
TACCACGATGCCTCTCGCTGGGGTCTTACGCTACAGACTTATGTGCAGCTCACCATGCTG
GACAGGCATACTCGTCCTCAGGTGTCATCTGTACGGTTGATGGAGAGGTCGATTCACAGC
GCAAGATACATTTTTGTAGAAAACCTGTATAGAAGTGGGAAGATGCCAGAAGTGGACTAT
GTAGTTCTGTCGGAATGGTTTGACTGGATCTTGAGGAACATGGACGTGTCTGTTGATTTG
ATAGTTTACCTTCGGACCAATCCTGAGACTTGTTACCAGAGGTTAAAGAAGAGATGCAGG
GAAGAGGAGAAGGTCATTCCGCTGGAATACCTGGAAGCAATTCACCATCTCCATGAGGAG
TGGCTCATCAAAGGCAGCCTTTTCCCCATGGCAGCCCCTGTTCTGGTGATTGAGGCTGAC
CACCACATGGAGAGGATGTTACAACTCTTTGAACAAAATCGGGATCGAATATTAACTCCA
GAGAATCGGAAGCATTGCCCATAG
Enzyme 13 GenBank Gene ID AF521891 Link Image
Enzyme 13 GeneCard ID Q8IZR3 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID HGNC:11831 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15061
Enzyme 14 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 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 14 Number of Residues 561
Enzyme 14 Molecular Weight 64960
Enzyme 14 Theoretical pI 6.05
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 158256766 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID AK291667 Link Image
Enzyme 14 GeneCard ID A8K6K2 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs Not Available
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16422
Enzyme 15 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name Not Available
Enzyme 15 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 15 Number of Residues 574
Enzyme 15 Molecular Weight 63396
Enzyme 15 Theoretical pI 7.04
Enzyme 15 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 15 General Function Nucleotide transport and metabolism
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AK314661 Link Image
Enzyme 15 GeneCard ID B2RBH2 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs Not Available
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16437
Enzyme 16 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name ENTPD3
Enzyme 16 Protein Sequence >cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b) 
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 16 Number of Residues 529
Enzyme 16 Molecular Weight 59106
Enzyme 16 Theoretical pI 6.40
Enzyme 16 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AK313322 Link Image
Enzyme 16 GeneCard ID B2R8D0 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available