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 Cytidine monophosphate (HMDB00095)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:41
Accession Number HMDB00095
Secondary Accession Numbers Not Available
Common Name Cytidine monophosphate
Description Cytidine monophosphate, also known as 5'-cytidylic acid and abbreviated CMP, is a nucleotide that is found in RNA. It is an ester of phosphoric acid with the nucleoside cytidine. CMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase cytosine.
Synonyms
  1. 5'-CMP
  2. 5Cytidylate
  3. 5Cytidylic acid
  4. CMP
  5. Cytidine 5'-monophosphate
  6. Cytidine 5'-monophosphorate
  7. Cytidine 5'-monophosphoric acid
  8. Cytidine 5'-phosphate
  9. Cytidine 5'-phosphorate
  10. Cytidine 5'-phosphoric acid
  11. Cytidine mono(dihydrogen phosphate)
  12. Cytidine monophosphate
  13. Cytidylate
  14. Cytidylic acid
Chemical IUPAC Name [5-(4-amino-2-oxo-pyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxyphosphonic acid
Chemical Formula C9H14N3O8P
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
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Ganglioside biosynthesis
  • Component of Globoside metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Keratan sulfate biosynthesis
  • Component of N-Glycan biosynthesis
  • Component of O-Glycan biosynthesis
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 323.197
Monoisotopic Molecular Weight 323.051849
Isomeric SMILES NC1=NC(=O)N(C=C1)[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O
Canonical SMILES NC1=NC(=O)N(C=C1)C1OC(COP(O)(O)=O)C(O)C1O
KEGG Compound ID C00055 Link Image
BioCyc ID CMP Link Image
BiGG ID 33689 Link Image
Wikipedia Link Cytidine monophosphate Link Image
NuGOwiki Link HMDB00095 Link Image
Metagene Link HMDB00095 Link Image
METLIN ID 5143 Link Image
PubChem Compound 6131 Link Image
PubChem Substance 825871 Link Image
ChEBI ID 17361 Link Image
CAS Registry Number 63-37-6
InChI Identifier InChI=1/C9H14N3O8P/c10-5-1-2-12(9(15)11-5)8-7(14)6(13)4(20-8)3-19-21(16,17)18/h1-2,4,6-8,13-14H,3H2,(H2,10,11,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
Synthesis Reference Zhou, Jingkang. Method for preparing cytidine 5'-monophosphate. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 12 pp.
Melting Point (Experimental) 233 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 98.6 mg/mL [MEYLAN,WM et al. (1996)]; 16.3 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.05 [Predicted by ALOGPS]; -4.2 [Predicted by PubChem via XLOGP]; -2.75 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location
Tissue References
All Tissues
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phosphatidylinositol Phosphate Metabolism SMP00463 Link Image map00562 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Hirono A, Fujii H, Miyajima H, Kawakatsu T, Hiyoshi Y, Miwa S: Three families with hereditary hemolytic anemia and pyrimidine 5'-nucleotidase deficiency: electrophoretic and kinetic studies. Clin Chim Acta. 1983 May 30;130(2):189-97. [PubMed Link Image]
  2. Okahira S, Nishikawa F, Nishikawa S, Akazawa T, Seya T, Matsumoto M: Interferon-beta induction through toll-like receptor 3 depends on double-stranded RNA structure. DNA Cell Biol. 2005 Oct;24(10):614-23. [PubMed Link Image]
  3. Daunter B, Newlands J: Seminal plasma biochemistry II: seminal plasma and spermatozoal cytidine monophosphate-sialic acid synthetase and sialyltransferase activities. Andrologia. 1981 May-Jun;13(3):215-24. [PubMed Link Image]
  4. Schmukler M, Jewett PB, Levy CC: The effects of polyamines on a residue-specific human plasma ribonuclease. J Biol Chem. 1975 Mar 25;250(6):2206-12. [PubMed Link Image]
  5. Paglia DE, Valentine WN, Keitt AS, Brockway RA, Nakatani M: Pyrimidine nucleotidase deficiency with active dephosphorylation of dTMP: evidence for existence of thymidine nucleotidase in human erythrocytes. Blood. 1983 Nov;62(5):1147-9. [PubMed Link Image]
  6. Yates AJ, Warner JK: Behavior of sugar derivatives in procedures for ganglioside isolation. Lipids. 1984 Jul;19(7):562-9. [PubMed Link Image]
  7. Li YP, Curley G, Lopez M, Chavez M, Glew R, Aragon A, Kumar H, Baca OG: Protein-tyrosine phosphatase activity of Coxiella burnetii that inhibits human neutrophils. Acta Virol. 1996 Nov-Dec;40(5-6):263-72. [PubMed Link Image]
  8. Hirono A, Fujii H, Natori H, Kurokawa I, Miwa S: Chromatographic analysis of human erythrocyte pyrimidine 5'-nucleotidase from five patients with pyrimidine 5'-nucleotidase deficiency. Br J Haematol. 1987 Jan;65(1):35-41. [PubMed Link Image]
  9. 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. Ectonucleoside triphosphate diphosphohydrolase 1
  7. Soluble calcium-activated nucleotidase 1
  8. Uridine-cytidine kinase 1
  9. CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase
  10. N-acylneuraminate cytidylyltransferase
  11. Lactosylceramide alpha-2,3-sialyltransferase
  12. Phosphatidylcholine:ceramide cholinephosphotransferase 1
  13. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
  14. Uridine-cytidine kinase 2
  15. Novel protein
  16. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
  17. Cytosolic 5'-nucleotidase III
  18. LOC129607 protein
  19. Uridine/cytidine kinase-like 1
  20. Ectonucleoside triphosphate diphosphohydrolase 8
  21. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  22. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  23. cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
  24. ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
  25. cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
  26. cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol syntha
  27. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  28. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  29. cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
  30. ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
  31. cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
  32. cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
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 5313
Enzyme 6 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 6 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 6 Gene Name ENTPD1
Enzyme 6 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 6 Number of Residues 510
Enzyme 6 Molecular Weight 57965
Enzyme 6 Theoretical pI 6.29
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 6 General Function Not Available
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 17-37 479-499
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 765256 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID S73813 Link Image
Enzyme 6 GeneCard ID ENTPD1 Link Image
Enzyme 6 GenAtlas ID ENTPD1 Link Image
Enzyme 6 HGNC ID HGNC:3363 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5314
Enzyme 7 Name Soluble calcium-activated nucleotidase 1
Enzyme 7 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 7 Gene Name CANT1
Enzyme 7 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 7 Number of Residues 401
Enzyme 7 Molecular Weight 44840
Enzyme 7 Theoretical pI 5.98
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 45-62
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 22218108 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 7 PDB ID 1S1D Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 7 GenBank Gene ID AF328554 Link Image
Enzyme 7 GeneCard ID CANT1 Link Image
Enzyme 7 GenAtlas ID CANT1 Link Image
Enzyme 7 HGNC ID HGNC:19721 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5337
Enzyme 8 Name Uridine-cytidine kinase 1
Enzyme 8 Synonyms
  1. UCK 1
  2. Uridine monophosphokinase 1
  3. Cytidine monophosphokinase 1
Enzyme 8 Gene Name UCK1
Enzyme 8 Protein Sequence >Uridine-cytidine kinase 1
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDL
EQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHR
GGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH
Enzyme 8 Number of Residues 277
Enzyme 8 Molecular Weight 31435
Enzyme 8 Theoretical pI 7.33
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 13506765 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9HA47 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UCK1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >834 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGTTCTCCGGGACGTGCGCCGAGGGAGGGACCTG
GAGCAGATTCTGACGCAGTACACCACCTTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTG
CCGACAAAGAAGTATGCCGATGTGATCATCCCGCGAGGAGTGGACAATATGGTTGCCATC
AACCTGATCGTGCAGCACATCCAGGACATTCTGAATGGTGACATCTGCAAATGGCACCGA
GGAGGGTCCAATGGGCGGAGCTACAAGCGGACCTTTTCTGAGCCAGGGGACCACCCTGGG
ATGCTGACCTCTGGCAAACGGTCACATTTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 8 GenBank Gene ID AF237290 Link Image
Enzyme 8 GeneCard ID UCK1 Link Image
Enzyme 8 GenAtlas ID UCK1 Link Image
Enzyme 8 HGNC ID HGNC:14859 Link Image
Enzyme 8 Chromosome Location 9
Enzyme 8 Locus 9q34.13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5439
Enzyme 9 Name CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase
Enzyme 9 Synonyms
  1. N-acetyllactosaminide alpha-2,3- sialyltransferase
  2. Gal beta-1,3(4GlcNAc alpha-2,3 sialyltransferase
  3. ST3N
  4. ST3GalIII
  5. Sialyltransferase 6
Enzyme 9 Gene Name ST3GAL3
Enzyme 9 Protein Sequence >CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRL
GFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARI
REFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDD
YDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLK
YIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIP
TLGSVAVTMALHGCDEVAVAGFGYDMSTPNAPLHYYETVRMAAIKESWTHNIQREKEFLR
KLVKARVITDLSSGI
Enzyme 9 Number of Residues 375
Enzyme 9 Molecular Weight 42171
Enzyme 9 Theoretical pI 9.31
Enzyme 9 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta- 1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha- 2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3- GalNAc
Enzyme 9 Pathways
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
  • Keratan sulfate biosynthesis (map00533 Link Image)
Enzyme 9 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-21
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 388015 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q11203 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name SIAT6_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1128 bp
ATGGGACTCTTGGTATTTGTGCGCAATCTGCTGCTAGCCCTCTGCCTCTTTCTGGTACTG
GGATTTTTGTATTATTCTGCGTGGAAGCTACACTTACTCCAGTGGGAGGAGGACTCCAAT
TCAGTGGTTCTTTCCTTTGACTCCGCTGGACAAACACTAGGCTCAGAGTATGATCGGTTG
GGCTTCCTCCTGAATCTGGACTCTAAACTGCCTGCTGAATTAGCCACCAAGTACGCAAAC
TTTTCAGAGGGAGCTTGCAAGCCTGGCTATGCTTCAGCCTTGATGACGGCCATCTTCCCC
CGGTTCTCCAAGCCAGCACCCATGTTCCTGGATGACTCCTTTCGCAAGTGGGCTAGAATC
CGGGAGTTCGTGCCGCCTTTTGGGATCAAAGGTCAAGACAATCTGATCAAAGCCATCTTG
TCAGTCACCAAAGAGTACCGCCTGACCCCTGCCTTGGACAGCCTCCGCTGCCGCCGCTGC
ATCATCGTGGGCAATGGAGGCGTTCTTGCCAACAAGTCTCTGGGGTCACGAATTGACGAC
TATGACATTGTGGTGAGACTGAATTCAGCACCAGTGAAAGGCTTTGAGAAGGACGTGGGC
AGCAAAACGACACTGCGCATCACCTACCCCGAGGGCGCCATGCAGCGGCCTGAGCAGTAC
GAGCGCGATTCTCTCTTTGTCCTCGCCGGCTTCAAGTGGCAGGACTTTAAGTGGTTGAAA
TACATCGTCTACAAGGAGAGAGTGAGTGCATCGGATGGCTTCTGGAAATCTGTGGCCACT
CGAGTGCCCAAGGAGCCCCCTGAGATTCGAATCCTCAACCCATATTTCATCCAGGAGGCC
GCCTTCACCCTCATTGGCCTGCCCTTCAACAATGGCCTCATGGGCCGGGGGAACATCCCT
ACCCTTGGCAGTGTGGCAGTGACCATGGCACTACACGGCTGTGACGAGGTGGCAGTCGCA
GGATTTGGCTATGACATGAGCACACCCAACGCACCCCTGCACTACTATGAGACCGTTCGC
ATGGCAGCCATCAAAGAGTCCTGGACGCACAATATCCAGCGAGAGAAAGAGTTTCTGCGG
AAGCTGGTGAAAGCTCGCGTCATCACTGATCTAAGCAGTGGCATCTGA
Enzyme 9 GenBank Gene ID L23768 Link Image
Enzyme 9 GeneCard ID ST3GAL3 Link Image
Enzyme 9 GenAtlas ID ST3GAL3 Link Image
Enzyme 9 HGNC ID HGNC:10866 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p34.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Kitagawa H, Paulson JC: Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase. Biochem Biophys Res Commun. 1993 Jul 15;194(1):375-82. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5636
Enzyme 10 Name N-acylneuraminate cytidylyltransferase
Enzyme 10 Synonyms
  1. CMP-N- acetylneuraminic acid synthetase
  2. CMP-NeuNAc synthetase
Enzyme 10 Gene Name CMAS
Enzyme 10 Protein Sequence >N-acylneuraminate cytidylyltransferase
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK
Enzyme 10 Number of Residues 434
Enzyme 10 Molecular Weight 48380
Enzyme 10 Theoretical pI 8.02
Enzyme 10 GO Classification
Function
Process
  • carbohydrate biosynthesis
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN)
Enzyme 10 Pathways
Enzyme 10 Reactions
  • CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 22085790 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q8NFW8 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NEUA_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1305 bp
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATYATAATGAGGKTGACATTGTAGGA
AATATTCAAGCTACTTCTYCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGKTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCCTACGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAAGTTAATAATTCATGCCAAAAATAG
Enzyme 10 GenBank Gene ID AF397212 Link Image
Enzyme 10 GeneCard ID CMAS Link Image
Enzyme 10 GenAtlas ID CMAS Link Image
Enzyme 10 HGNC ID HGNC:18290 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6051
Enzyme 11 Name Lactosylceramide alpha-2,3-sialyltransferase
Enzyme 11 Synonyms
  1. CMP- NeuAc:lactosylceramide alpha-2,3-sialyltransferase
  2. Ganglioside GM3 synthase
  3. ST3Gal V
  4. Sialyltransferase 9
Enzyme 11 Gene Name ST3GAL5
Enzyme 11 Protein Sequence >Lactosylceramide alpha-2,3-sialyltransferase
MRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVL
QKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLE
LLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGN
KTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVA
EKIPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEV
SLAGFGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDR
EF
Enzyme 11 Number of Residues 362
Enzyme 11 Molecular Weight 41736
Enzyme 11 Theoretical pI 8.62
Enzyme 11 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Catalyzes the formation of ganglioside GM3 (alpha-N- acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D- glucosylceramide)
Enzyme 11 Pathways
Enzyme 11 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-32
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3779139 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9UNP4 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SIAT9_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1089 bp
ATGAGAAGGCCCAGCTTGTTATTAAAAGACATCCTCAAATGTACATTGCTTGTGTTTGGA
GTGTGGATCCTTTATATCCTCAAGTTAAATTATACTACTGAAGAATGTGACATGAAAAAA
ATGCATTATGTGGACCCTGACCGTGTAAAGAGAGCTCAGAAATATGCTCAGCAAGTCTTG
CAGAAGGAATGTCGTCCCAAGTTTGCCAAGACATCAATGGCGCTGTTATTTGAGCACAGG
TATAGCGTGGACTTACTCCCTTTTGTGCAGAAGGCCCCCAAAGACAGTGAAGCTGAGTCC
AAGTACGATCCTCCTTTTGGGTTCCGGAAGTTCTCCAGTAAAGTCCAGACCCTCTTGGAA
CTCTTGCCAGAGCACGACCTCCCTGAACACTTGAAAGCCAAGACCTGTCGGCGCTGTGTG
GTTATTGGAAGCGGAGGAATACTGCACGGATTAGAACTGGGCCACACCCTGAACCAGTTC
GATGTTGTGATAAGGTTAAACAGTGCACCAGTTGAGGGATATTCAGAACATGTTGGAAAT
AAAACTACTATAAGGATGACTTATCCAGAGGGCGCACCACTGTCTGACCTTGAATATTAT
TCCAATGACTTATTTGTTGCTGTTTTATTTAAGAGTGTTGATTTCAACTGGCTTCAAGCA
ATGGTAAAAAAGGAAACCCTGCCATTCTGGGTACGACTCTTCTTTTGGAAGCAGGTGGCA
GAAAAAATCCCACTGCAGCCAAAACATTTCAGGATTTTGAATCCAGTTATCATCAAAGAG
ACTGCCTTTGACATCCTTCAGTACTCAGAGCCTCAGTCAAGGTTCTGGGGCCGAGATAAG
AACGTCCCCACAATCGGTGTCATTGCCGTTGTCTTAGCCACACATCTGTGCGATGAAGTC
AGTTTGGCGGGTTTTGGATATGACCTCAATCAACCCAGAACACCTTTGCACTACTTCGAC
AGTCAATGCATGGCTGCTATGAACTTTCAGACCATGCATAATGTGACAACGGAAACCAAG
TTCCTCTTAAAGCTGGTCAAAGAGGGAGTGGTGAAAGATCTCAGTGGAGGCATTGATCGT
GAATTTTGA
Enzyme 11 GenBank Gene ID AB018356 Link Image
Enzyme 11 GeneCard ID ST3GAL5 Link Image
Enzyme 11 GenAtlas ID ST3GAL5 Link Image
Enzyme 11 HGNC ID HGNC:10872 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2p11.2
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ishii A, Ohta M, Watanabe Y, Matsuda K, Ishiyama K, Sakoe K, Nakamura M, Inokuchi J, Sanai Y, Saito M: Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase. J Biol Chem. 1998 Nov 27;273(48):31652-5. [PubMed Link Image]
  2. 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6054
Enzyme 12 Name Phosphatidylcholine:ceramide cholinephosphotransferase 1
Enzyme 12 Synonyms
  1. Transmembrane protein 23
  2. Sphingomyelin synthase 1
  3. Protein Mob
Enzyme 12 Gene Name TMEM23
Enzyme 12 Protein Sequence >Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
Enzyme 12 Number of Residues 419
Enzyme 12 Molecular Weight 49208
Enzyme 12 Theoretical pI 8.51
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Bidirectional lipid cholinephosphotransferases capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 142-162 190-210 221-241 282-302 310-330
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 30908857 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q86VZ5 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name SMS1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAACGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
Enzyme 12 GenBank Gene ID AY280959 Link Image
Enzyme 12 GeneCard ID TMEM23 Link Image
Enzyme 12 GenAtlas ID TMEM23 Link Image
Enzyme 12 HGNC ID HGNC:29799 Link Image
Enzyme 12 Chromosome Location 10
Enzyme 12 Locus 10q11.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 7696
Enzyme 13 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
Enzyme 13 Synonyms
  1. Beta-galactoside alpha-2,3-sialyltransferase
  2. Alpha 2,3-ST
  3. Gal-NAc6S
  4. Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
  5. ST3GalIA
  6. ST3O
  7. ST3GalA.1
  8. SIAT4-A
  9. ST3Gal I
  10. SIATFL
Enzyme 13 Gene Name ST3GAL1
Enzyme 13 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCT
CTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKEL
FRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEAD
VGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVK
QDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHY
WENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
Enzyme 13 Number of Residues 340
Enzyme 13 Molecular Weight 39075
Enzyme 13 Theoretical pI 9.45
Enzyme 13 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O- linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values
Enzyme 13 Pathways
Enzyme 13 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-31
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 522197 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q11201 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name SIA4A_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1023 bp
ATGGTGACCCTGCGGAAGAGGACCCTGAAAGTCGTCACCTTCCTCGTGCTCTTCATCTTC
CTCACCTCCTTCTTCCTGAACTACTCCCACACCATGGTGGCCACCACCTGGTTCCCCAAG
CAGATGGTCCTGGAGCTCTCCGAGAACCTGAAGAGACTGATCAAGCACAGGCCTTGCACC
TGCACCCACTGCATCGGGCAGCGCAAGCTCTCGGCCTGGTTCGATGAGAGGTTCAACCAG
ACCATGCAGCCGCTGCTGACTGCCCAGAACGCGCTCTTGGAGGACGACACCTACCGATGG
TGGCTGAGGCTCCAGCGGGAGAAGAAGCCCAATAACTTGAATGACACCATCAAGGAGCTG
TTCAGAGTGGTGCCTGGGAATGTGGACCCTATGCTGGAGAAGAGGTCGGTGGGCTGCCGG
CGCTGCGCCGTTGTGGGCAACTCGGGCAACCTGAGGGAGTCTTCTTATGGGCCTGAGATA
GACAGTCACGACTTTGTCCTCAGGATGAACAAGGCGCCCACGGCAGGGTTTGAAGCTGAT
GTTGGGACCAAGACCACCCACCATCTGGTGTACCCTGAGAGCTTCCGGGAGCTGGGAGAT
AATGTCAGCATGATCCTGGTGCCCTTCAAGACCATCGACTTGGAGTGGGTGGTGAGCGCC
ATCACCACGGGCACCATTTCCCACACCTACATCCCGGTTCCTGCAAAGATCAGAGTGAAA
CAGGATAAGATCCTGATCTACCACCCAGCCTTCATCAAGTATGTCTTTGACAACTGGCTG
CAAGGGCACGGGCGATACCCATCTACCGGCATCCTCTCGGTCATCTTCTCAATGCATGTC
TGCGATGAGGTGGACTTGTACGGCTTCGGGGCAGACAGCAAAGGGAACTGGCACCACTAC
TGGGAGAACAACCCATCCGCGGGGGCTTTTCGCAAGACGGGGGTGCACGATGCAGACTTT
GAGTCTAACGTGACGGCCACCTTGGCCTCCATCAATAAAATCCGGATCTTCAAGGGGAGA
TGA
Enzyme 13 GenBank Gene ID L29555 Link Image
Enzyme 13 GeneCard ID ST3GAL1 Link Image
Enzyme 13 GenAtlas ID ST3GAL1 Link Image
Enzyme 13 HGNC ID HGNC:10862 Link Image
Enzyme 13 Chromosome Location 8
Enzyme 13 Locus 8q24.22
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Kitagawa H, Paulson JC: Differential expression of five sialyltransferase genes in human tissues. J Biol Chem. 1994 Jul 8;269(27):17872-8. [PubMed Link Image]
  2. Chang ML, Eddy RL, Shows TB, Lau JT: Three genes that encode human beta-galactoside alpha 2,3-sialyltransferases. Structural analysis and chromosomal mapping studies. Glycobiology. 1995 May;5(3):319-25. [PubMed Link Image]
  3. Shang J, Qiu R, Wang J, Liu J, Zhou R, Ding H, Yang S, Zhang S, Jin C: Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-sialyltransferase from human fetal liver. Eur J Biochem. 1999 Oct;265(2):580-8. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8075
Enzyme 14 Name Uridine-cytidine kinase 2
Enzyme 14 Synonyms
  1. UCK 2
  2. Uridine monophosphokinase 2
  3. Cytidine monophosphokinase 2
Enzyme 14 Gene Name UCK2
Enzyme 14 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 14 Number of Residues 261
Enzyme 14 Molecular Weight 29299
Enzyme 14 Theoretical pI 6.68
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Nucleotide transport and metabolism
Enzyme 14 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 1655420 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 14 PDB ID 1XRJ Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
Enzyme 14 GenBank Gene ID D78335 Link Image
Enzyme 14 GeneCard ID UCK2 Link Image
Enzyme 14 GenAtlas ID UCK2 Link Image
Enzyme 14 HGNC ID HGNC:12562 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q23
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed Link Image]
  2. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  3. Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8529
Enzyme 15 Name Novel protein
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name RP11-163G10.1
Enzyme 15 Protein Sequence >Novel protein
MFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLE
TDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEE
KIVDNLQSRHTAFIGDRN
Enzyme 15 Number of Residues 138
Enzyme 15 Molecular Weight 15645
Enzyme 15 Theoretical pI 5.71
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Coenzyme 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 Not Available
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 55665116 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q5VVM0 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q5VVM0_HUMAN Link Image
Enzyme 15 PDB ID 1P9O Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >936 bp
ATGGCGGAAATGGATCCGGTAGCCGAGTTCCCCCAGCCTCCCGGTGCTGCGCGCTGGGCT
GAGGTTATGGCTCGCTTCGCGGCCAGGCTGGGCGCGCAGGGCCGGCGGGTGGTGTTGGTT
ACGTCAGGCGGCACCAAGGTCCCACTGGAAGCGCGGCCGGTGCGCTTCCTGGACAACTTC
AGCAGCGGGCGGCGCGGTGCAACCTCGGCCGAGGCCTTCCTAGCCGCCGGCTACGGGGTC
CTGTTCTTGTATCGCGCTCGCTCTGCCTTCCCCTATGCCCACCGCTTCCCACCCCAGACT
TGGCTGTCCGCTCTGCGGCCTTCGGGCCCAGCCCTTTCGGGCTTGCTGAGCCTGGAGGCC
GAGGAGAATGCACTTCCGGGTTTTGCTGAGGCTCTGAGGAGCTACCAGGAGGCTGCGGCT
GCAGGCACCTTCCTGGCAGTAGAGTTCACCACTTTGGCGGACTATTTGCATCTGTTGCAG
GCTGCGGCCCAGGCACTCAATCCGCTAGGCCCTTCTGCGATGTTTTACCTGGCTGCGGCT
GTGTCAGATTTCTATGTTCCTGTCTCTGAAATGCCTGAACACAAGATCCAGTCATCTGGG
GGCCCACTGCAGATAACAATGAAGATGGTGCCAAAACTGCTTTCTCCTTTGGTTAAAGAT
TGGGCTCCCAAAGCATTTATAATTTCCTTTAAGTTGGAGACTGACCCCGCCATTGTAATT
AATCGAGCTCGGAAGGCTTTGGAAATTTATCAGCATCAAGTGGTGGTGGCTAATATCCTT
GAGTCACGACAGTCCTTTGTGTTTATTGTAACCAAAGACTCGGAAACCAAGTTATTGCTA
TCAGAGGAAGAAATAGAAAAAGGCGTAGAGATAGAAGAGAAGATAGTGGATAATCTTCAG
TCTCGACACACAGCTTTTATAGGTGACAGAAACTGA
Enzyme 15 GenBank Gene ID AL445669 Link Image
Enzyme 15 GeneCard ID RP11-163G10.1 Link Image
Enzyme 15 GenAtlas ID RP11-163G10.1 Link Image
Enzyme 15 HGNC ID HGNC:25686 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8660
Enzyme 16 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
Enzyme 16 Synonyms
  1. Beta-galactoside alpha-2,3-sialyltransferase
  2. Alpha 2,3-sialyltransferase IV
  3. Alpha 2,3-ST
  4. Gal-NAc6S
  5. STZ
  6. SIAT4-C
  7. ST3Gal III
  8. SAT-3
  9. ST-4
Enzyme 16 Gene Name ST3GAL4
Enzyme 16 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFG
NYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRC
VVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVE
NNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIA
ADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQIT
LKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF
Enzyme 16 Number of Residues 333
Enzyme 16 Molecular Weight 38046
Enzyme 16 Theoretical pI 9.88
Enzyme 16 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function It may catalyze the formation of the NeuAc-alpha-2,3- Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-26
Enzyme 16 Transmembrane Regions
  • 9-26
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 431315 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q11206 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name SIA4C_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >999 bp
ATGTGTCCTGCAGGCTGGAAGCTCCTGGCCATGTTGGCTCTGGTCCTGGTCGTCATGGTG
TGGTATTCCATCTCCCGGGAAGACAGGTACATCGAGCTTTTTTATTTTCCCATCCCAGAG
AAGAAGGAGCCGTGCCTCCAGGGTGAGGCAGAGAGCAAGGCCTCTAAGCTCTTTGGCAAC
TACTCCCGGGATCAGCCCATCTTCCTGCGGCTTGAGGATTATTTCTGGGTCAAGACGCCA
TCTGCTTACGAGCTGCCCTATGGGACCAAGGGGAGTGAGGATCTGCTCCTCCGGGTGCTA
GCCATCACCAGCTCCTCCATCCCCAAGAACATCCAGAGCCTCAGGTGCCGCCGCTGTGTG
GTCGTGGGGAACGGGCACCGGCTGCGGAACAGCTCACTGGGAGATGCCATCAACAAGTAC
GATGTGGTCATCAGATTGAACAATGCCCCAGTGGCTGGCTATGAGGGTGACGTGGGCTCC
AAGACCACCATGCGTCTCTTCTACCCTGAATCTGCCCACTTCGACCCCAAAGTAGAAAAC
AACCCAGACACACTCCTCGTCCTGGTAGCTTTCAAGGCAATGGACTTCCACTGGATTGAG
ACCATCCTGAGTGATAAGAAGCGGGTGCGAAAGGGTTTCTGGAAACAGCCTCCCCTCATC
TGGGATGTCAATCCTAAACAGATTCGGATTCTCAACCCCTTCTTCATGGAGATTGCAGCT
GACAAACTGCTGAGCCTGCCAATGCAACAGCCACGGAAGATTAAGCAGAAGCCCACCACG
GGCCTGTTGGCCATCACGCTGGCCCTCCACCTCTGTGACTTGGTGCACATTGCCGGCTTT
GGCTACCCAGACGCCTACAACAAGAAGCAGACCATTCACTACTATGAGCAGATCACGCTC
AAGTCCATGGCGGGGTCAGGCCATAATGTCTCCCAAGAGGCCCTGGCCATTAAGCGGATG
CTGGAGATGGGAGCTATCAAGAACCTCACGTCCTTCTGA
Enzyme 16 GenBank Gene ID L23767 Link Image
Enzyme 16 GeneCard ID ST3GAL4 Link Image
Enzyme 16 GenAtlas ID ST3GAL4 Link Image
Enzyme 16 HGNC ID HGNC:10864 Link Image
Enzyme 16 Chromosome Location 11
Enzyme 16 Locus 11q23-q24
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Kitagawa H, Mattei MG, Paulson JC: Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase. J Biol Chem. 1996 Jan 12;271(2):931-8. [PubMed Link Image]
  2. Kitagawa H, Paulson JC: Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J Biol Chem. 1994 Jan 14;269(2):1394-401. [PubMed Link Image]
  3. Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M: Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection. J Biol Chem. 1993 Oct 25;268(30):22782-7. [PubMed Link Image]
  4. Basu SS, Basu M, Li Z, Basu S: Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line. Biochemistry. 1996 Apr 23;35(16):5166-74. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8749
Enzyme 17 Name Cytosolic 5'-nucleotidase III
Enzyme 17 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 17 Gene Name NT5C3
Enzyme 17 Protein Sequence >Cytosolic 5'-nucleotidase III
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 17 Number of Residues 336
Enzyme 17 Molecular Weight 37949
Enzyme 17 Theoretical pI 7.15
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 17 Pathways
Enzyme 17 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-32
Enzyme 17 Transmembrane Regions
  • 13-35
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 11245474 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >861 bp
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 17 GenBank Gene ID AF312735 Link Image
Enzyme 17 GeneCard ID NT5C3 Link Image
Enzyme 17 GenAtlas ID NT5C3 Link Image
Enzyme 17 HGNC ID HGNC:17820 Link Image
Enzyme 17 Chromosome Location 7
Enzyme 17 Locus 7p14.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 13097
Enzyme 18 Name LOC129607 protein
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name LOC129607
Enzyme 18 Protein Sequence >LOC129607 protein
RGPLSGPLLGRRGVCAGAMAPPRRFVLELPDCTLAHFALGADAPGDADAPDPRLAALLGP
PERSYSLCVPVTPDAGCGARVRAARLHQRLLHQLRRGPFQRCQLLRLLCYCPGGQAGGAQ
QGFLLRDPLDDPDTRQALLELLGACQEAPRPHLGEFEADPRGQLWQRLWEVQDGRRLQVG
CAQVVPVPEPPLHPVVPDLPSSVVFPDREAARAVLEECTSFIPEARAVLDLVDQCPKQIQ
KGKFQVVAIEGLDATGKTTVTQSVADSLKAVLLKSPPSCIGQWRKIFDDEPTIIRRAFYS
LGNYIVASEIAKESAKSPVIVDRYWHSTATYAIATEVSGGLQHLPPAHHPVYQWPEDLLK
PDLILLLTVSPEERLQRLQGRGMEKTREEAELEANSVFRQKVEMSYQRMENPGCHVVDAS
PSREKVLQTVLSLIQNSFSGP
Enzyme 18 Number of Residues 441
Enzyme 18 Molecular Weight 48417
Enzyme 18 Theoretical pI 6.83
Enzyme 18 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 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 59808649 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q5EBM0 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q5EBM0_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID BC089425 Link Image
Enzyme 18 GeneCard ID Q5EBM0 Link Image
Enzyme 18 GenAtlas ID CMPK2 Link Image
Enzyme 18 HGNC ID HGNC:27015 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 13098
Enzyme 19 Name Uridine/cytidine kinase-like 1
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name UCKL1
Enzyme 19 Protein Sequence >Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 19 Number of Residues 548
Enzyme 19 Molecular Weight 61142
Enzyme 19 Theoretical pI 7.40
Enzyme 19 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 19 General Function Nucleotide transport and metabolism
Enzyme 19 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 19 Pathways
Enzyme 19 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964] ALL_REAC R00964
  • (other) R00513 R00516 R00517 R00962 R00967 R00968 R00970 R01548 R01549 R01880 R02091 R02096 R02097 R02327 R02332 R02371 R02372
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 38228699 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AJ605558 Link Image
Enzyme 19 GeneCard ID Q9NWZ5 Link Image
Enzyme 19 GenAtlas ID UCKL1 Link Image
Enzyme 19 HGNC ID HGNC:15938 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [PubMed Link Image]
  2. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 13379
Enzyme 20 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 20 Synonyms
  1. NTPDase 8
  2. NTPDase8
  3. E-NTPDase 8
Enzyme 20 Gene Name ENTPD8
Enzyme 20 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 20 Number of Residues 495
Enzyme 20 Molecular Weight 53904
Enzyme 20 Theoretical pI 4.96
Enzyme 20 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 20 General Function Not Available
Enzyme 20 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 20 Pathways
Enzyme 20 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 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 9-29 472-492
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 59003409 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 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 20 GenBank Gene ID AY903953 Link Image
Enzyme 20 GeneCard ID Q5MY95 Link Image
Enzyme 20 GenAtlas ID ENTPD8 Link Image
Enzyme 20 HGNC ID HGNC:24860 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 15061
Enzyme 21 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name Not Available
Enzyme 21 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 21 Number of Residues 561
Enzyme 21 Molecular Weight 64960
Enzyme 21 Theoretical pI 6.05
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function Not Available
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 158256766 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AK291667 Link Image
Enzyme 21 GeneCard ID A8K6K2 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs Not Available
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 15200
Enzyme 22 Name Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name UCK1
Enzyme 22 Protein Sequence >Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 22 Number of Residues 201
Enzyme 22 Molecular Weight 22761
Enzyme 22 Theoretical pI 6.23
Enzyme 22 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Nucleotide transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 57162360 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 22 GenBank Gene ID AL358781 Link Image
Enzyme 22 GeneCard ID Q5JT13 Link Image
Enzyme 22 GenAtlas ID UCK1 Link Image
Enzyme 22 HGNC ID HGNC:14859 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 15201
Enzyme 23 Name cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name ST6GAL1
Enzyme 23 Protein Sequence >cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
MIHTNLKKKFSCCVLVFLLFAVICVWKEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDS
QSVSSSSTQDPHRGRQTLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMN
KYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRTKAGP
WGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTE
KRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQM
PWELWDILQEISPEEIQPNPPSSGMLGIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFF
DSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC
Enzyme 23 Number of Residues 406
Enzyme 23 Molecular Weight 46605
Enzyme 23 Theoretical pI 9.35
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function Not Available
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 158259219 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID A8KA14 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name A8KA14_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1221 bp
ATGATTCACACCAACCTGAAGAAAAAGTTCAGCTGCTGCGTCCTGGTCTTTCTTCTGTTT
GCAGTCATCTGTGTGTGGAAGGAAAAGAAGAAAGGGAGTTACTATGATTCCTTTAAATTG
CAAACCAAGGAATTCCAGGTGTTAAAGAGTCTGGGGAAATTGGCCATGGGGTCTGATTCC
CAGTCTGTATCCTCAAGCAGCACCCAGGACCCCCACAGGGGCCGCCAGACCCTCGGCAGT
CTCAGAGGCCTAGCCAAGGCCAAACCAGAGGCCTCCTTCCAGGTGTGGAACAAGGACAGC
TCTTCCAAAAACCTTATCCCTAGGCTGCAAAAGATCTGGAAGAATTACCTAAGCATGAAC
AAGTACAAAGTGTCCTACAAGGGGCCAGGACCAGGCATCAAGTTCAGTGCAGAGGCCCTG
CGCTGCCACCTCCGGGACCATGTGAATGTATCCATGGTAGAGGTCACAGATTTTCCCTTC
AATACCTCTGAATGGGAGGGTTATCTGCCCAAGGAGAGCATTAGGACCAAGGCTGGGCCT
TGGGGCAGGTGTGCTGTTGTGTCGTCAGCGGGATCTCTGAAGTCCTCCCAACTAGGCAGA
GAAATCGATGATCATGACGCAGTCCTGAGGTTTAATGGGGCACCCACAGCCAACTTCCAA
CAAGATGTGGGCACAAAAACTACCATTCGCCTGATGAACTCTCAGTTGGTTACCACAGAG
AAGCGCTTCCTCAAAGACAGTTTGTACAATGAAGGAATCCTAATTGTATGGGACCCATCT
GTATACCACTCAGATATCCCAAAGTGGTACCAGAATCCGGATTATAATTTCTTTAACAAC
TACAAGACTTATCGTAAGCTGCACCCCAATCAGCCCTTTTACATCCTCAAGCCCCAGATG
CCTTGGGAGCTATGGGACATTCTTCAAGAAATCTCCCCAGAAGAGATTCAGCCAAACCCC
CCATCCTCTGGGATGCTTGGTATCATCATCATGATGACGCTGTGTGACCAGGTGGATATT
TATGAGTTCCTCCCATCCAAGCGCAAGACTGACGTGTGCTACTACTACCAGAAGTTCTTC
GATAGTGCCTGCACGATGGGTGCCTACCACCCGCTGCTCTATGAGAAGAATTTGGTGAAG
CATCTCAACCAGGGCACAGATGAGGACATCTACCTGCTTGGAAAAGCCACACTGCCTGGC
TTCCGGACCATTCACTGCTAA
Enzyme 23 GenBank Gene ID AK292879 Link Image
Enzyme 23 GeneCard ID A8KA14 Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 15202
Enzyme 24 Name ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name ST6GALNAC4
Enzyme 24 Protein Sequence >ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYS
SVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRST
LRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQ
VYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCR
EKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWR
TE
Enzyme 24 Number of Residues 302
Enzyme 24 Molecular Weight 34201
Enzyme 24 Theoretical pI 8.65
Enzyme 24 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 55958253 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q5T9D0 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name Q5T9D0_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >909 bp
ATGAAGGCTCCGGGTCGGCTCGTGCTCATCATCCTGTGCTCCGTGGTCTTCTCTGCCGTC
TACATCCTCCTGTGCTGCTGGGCCGGCCTGCCCCTCTGCCTGGCCACCTGCCTGGACCAC
CACTTCCCCACAGGCTCCAGGCCCACTGTGCCGGGACCCCTGCACTTCAGTGGATATAGC
AGTGTGCCAGATGGGAAGCCGCTGGTCCGCGAGCCCTGCCGCAGCTGTGCCGTGGTGTCC
AGCTCCGGCCAAATGCTGGGCTCAGGCCTGGGTGCTGAGATCGACAGTGCCGAGTGCGTG
TTCCGCATGAACCAGGCGCCCACCGTGGGCTTTGAGGCGGATGTGGGCCAGCGCAGCACC
CTGCGTGTCGTCTCACACACAAGCGTGCCGCTGCTGCTGCGCAACTATTCACACTACTTC
CAGAAGGCCCGAGACACGCTCTACATGGTGTGGGGCCAGGGCAGGCACATGGACCGGGTG
CTCGGCGGCCGCACCTACCGCACGCTGCTGCAGCTCACCAGGATGTACCCCGGCCTGCAG
GTGTACACCTTCACGGAGCGCATGATGGCCTACTGCGACCAGATCTTCCAGGACGAGACG
GGCAAGAACCGGAGGCAGTCGGGCTCCTTCCTCAGCACCGGCTGGTTCACCATGATCCTC
GCGCTGGAGCTGTGTGAGGAGATCGTGGTCTATGGGATGGTCAGCGACAGCTACTGCAGG
GAGAAGAGCCACCCCTCAGTGCCTTACCACTACTTTGAGAAGGGCCGGCTAGATGAGTGT
CAGATGTACCTGGCACACGAGCAGGCGCCCCGAAGCGCCCACCGCTTCATCACTGAGAAG
GCGGTCTTCTCCCGCTGGGCCAAGAAGAGGCCCATCGTGTTCGCCCATCCGTCCTGGAGG
ACTGAGTAG
Enzyme 24 GenBank Gene ID AL157935 Link Image
Enzyme 24 GeneCard ID Q5T9D0 Link Image
Enzyme 24 GenAtlas ID ST6GALNAC4 Link Image
Enzyme 24 HGNC ID HGNC:17846 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15203
Enzyme 25 Name cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name ST8SIA1
Enzyme 25 Protein Sequence >cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQG
VLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNS
TYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGS
KSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLS
DVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSV
NMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDTSLQPTS
Enzyme 25 Number of Residues 356
Enzyme 25 Molecular Weight 40519
Enzyme 25 Theoretical pI 9.61
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function Not Available
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 158255318 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID A8K4H6 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name A8K4H6_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1071 bp
ATGAGCCCCTGCGGGCGGGCCCGGCGACAAACGTCCAGAGGGGCCATGGCTGTACTGGCG
TGGAAGTTCCCGCGGACCCGGCTGCCCATGGGAGCCAGTGCCCTCTGTGTCGTGGTCCTC
TGTTGGCTCTACATCTTCCCCGTCTACCGGCTGCCCAACGAGAAAGAGATCGTGCAGGGG
GTGCTGCAACAGGGCACGGCGTGGAGGAGGAACCAGACCGCGGCCAGAGCGTTCAGGAAA
CAAATGGAAGACTGCTGCGACCCTGCTCATCTCTTTGCTATGACTAAAATGAATTCCCCT
ATGGGGAAGAGCATGTGGTATGACGGGGAGTTTTTATACTCATTCACCATTGACAATTCA
ACTTACTCTCTCTTCCCACAGGCAACCCCATTCCAGCTGCCATTGAAGAAATGCGCGGTG
GTGGGAAATGGTGGGATTCTGAAGAAGAGTGGCTGTGGCCGTCAAATAGATGAAGCAAAT
TTTGTCATGCGATGCAATCTCCCTCCTTTGTCAAGTGAATACACTAAGGATGTTGGATCC
AAAAGTCAGTTAGTGACAGCTAATCCCAGCATAATTCGGCAAAGGTTTCAGAACCTTCTG
TGGTCCAGAAAGACATTTGTGGACAACATGAAAATCTATAACCACAGTTACATCTACATG
CCTGCCTTTTCTATGAAGACAGGAACAGAGCCATCTTTGAGGGTTTATTATACACTGTCA
GATGTTGGTGCCAATCAAACAGTGCTGTTTGCCAACCCCAACTTTCTGCGTAGCATTGGA
AAGTTCTGGAAAAGTAGAGGAATCCATGCCAAGCGCCTGTCCACAGGACTTTTTCTGGTG
AGCGCAGCTCTGGGTCTCTGTGAAGAGGTGGCCATCTATGGCTTCTGGCCCTTCTCTGTG
AATATGCATGAGCAGCCCATCAGCCACCACTACTATGACAACGTCTTACCCTTTTCTGGC
TTCCATGCCATGCCCGAGGAATTTCTCCAACTCTGGTATCTTCATAAAATCGGTGCACTG
AGAATGCAGCTGGACCCATGTGAAGATACCTCACTCCAGCCCACTTCCTAG
Enzyme 25 GenBank Gene ID AK290941 Link Image
Enzyme 25 GeneCard ID A8K4H6 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location 12
Enzyme 25 Locus 12p12.1-p11.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15204
Enzyme 26 Name cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol syntha
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name CDIPT
Enzyme 26 Protein Sequence >cDNA FLJ77674, highly similar to Homo sapiens CDP-diacylglycerol-- inositol 3-phosphatidyltransferase (phosphatidylinositol synthase) (CDIPT), transcript variant 1, mRNA (CDP-diacylglycerol--inositol 3- phosphatidyltransferase (Phosphatidylinositol synthase), isoform CRA_a)
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQG
TRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESH
KMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTA
PIALLKSLISVIHLITAARNMAALDAADRAKKK
Enzyme 26 Number of Residues 213
Enzyme 26 Molecular Weight 23539
Enzyme 26 Theoretical pI 8.13
Enzyme 26 GO Classification Not Available
Enzyme 26 General Function Lipid transport and metabolism
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function Not Available
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158254696 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K3L7 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K3L7_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >642 bp
ATGCCAGACGAAAATATCTTCCTGTTCGTGCCCAACCTCATCGGTTATGCCCGGATTGTC
TTCGCCATCATTTCTTTCTACTTCATGCCCTGCTGCCCCCTCACGGCCTCCTCCTTCTAC
CTGCTCAGCGGCCTGCTGGACGCTTTCGATGGACACGCTGCTCGCGCTCTTAATCAAGGA
ACCCGGTTTGGGGCCATGCTGGACATGCTGACGGACCGCTGCTCCACCATGTGCCTGTTG
GTCAACCTGGCCCTGCTGTACCCTGGAGCCACGCTGTTCTTCCAAATCAGCATGAGTTTG
GATGTGGCCAGTCACTGGCTGCACCTCCACAGTTCTGTGGTCCGAGGCAGTGAGAGTCAC
AAGATGATCGACTTGTCCGGGAATCCGGTGCTTCGGATCTACTACACCTCGAGGCCTGCT
CTGTTCACCTTGTGTGCTGGGAATGAGCTCTTCTACTGCCTCCTCTACCTGTTCCATTTC
TCTGAGGGACCTTTAGTTGGCTCTGTGGGACTGTTCCGGATGGGCCTCTGGGTCACTGCC
CCCATCGCCTTGCTGAAGTCGCTCATCAGCGTCATCCACCTGATCACGGCCGCCCGCAAC
ATGGCTGCCCTGGACGCAGCAGACCGCGCCAAGAAGAAGTGA
Enzyme 26 GenBank Gene ID AK290632 Link Image
Enzyme 26 GeneCard ID A8K3L7 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location 16
Enzyme 26 Locus 16p11.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16422
Enzyme 27 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name Not Available
Enzyme 27 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 27 Number of Residues 574
Enzyme 27 Molecular Weight 63396
Enzyme 27 Theoretical pI 7.04
Enzyme 27 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 27 General Function Nucleotide transport and metabolism
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AK314661 Link Image
Enzyme 27 GeneCard ID B2RBH2 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs Not Available
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16437
Enzyme 28 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name ENTPD3
Enzyme 28 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 28 Number of Residues 529
Enzyme 28 Molecular Weight 59106
Enzyme 28 Theoretical pI 6.40
Enzyme 28 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK313322 Link Image
Enzyme 28 GeneCard ID B2R8D0 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16481
Enzyme 29 Name cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name Not Available
Enzyme 29 Protein Sequence >cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
MKCSLRVWFLSVAFLLVFIMSLLFTYSHHSMATLPYLDSGALDGTHRVKLVPGYAGLQRL
SKERLSGKSCACRRCMGDAGASDWFDSHFDGNISPVWTRENMDLPPDVQRWWMMLQPQFK
SHNTNEVLEKLFQIVPGENPYRFRDPHQCRRCAVVGNSGNLRGSGYGQDVDGHNFIMRMN
QAPTVGFEQDVGSRTTHHFMYPESAKNLPANVSFVLVPFKVQDLLWIASALSTGQIRFTY
APVKSFLRVDKEKVQIYNPAFFKYIHDRWTEHHGRYPSTGMLVLFFALHVCDEVNVYGFG
ADSRGNWHHYWENNRYAGEFRKTGVHDADFEAHIIDMLAKASKIEVYRGN
Enzyme 29 Number of Residues 350
Enzyme 29 Molecular Weight 40188
Enzyme 29 Theoretical pI 8.47
Enzyme 29 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID B3KXG9 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B3KXG9_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AK127322 Link Image
Enzyme 29 GeneCard ID B3KXG9 Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs Not Available
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 16482
Enzyme 30 Name ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
Enzyme 30 Synonyms
  1. SubName: cDNA, FLJ96071, Homo sapiens alpha2,3-sialyltransferase (ST3GALVI), mRNA
Enzyme 30 Gene Name ST3GAL6
Enzyme 30 Protein Sequence >ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
Enzyme 30 Number of Residues 331
Enzyme 30 Molecular Weight 38214
Enzyme 30 Theoretical pI 9.30
Enzyme 30 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID B2RCH2 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name B2RCH2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AK315111 Link Image
Enzyme 30 GeneCard ID B2RCH2 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 16483
Enzyme 31 Name cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name CHPT1
Enzyme 31 Protein Sequence >cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
Enzyme 31 Number of Residues 406
Enzyme 31 Molecular Weight 45097
Enzyme 31 Theoretical pI 6.92
Enzyme 31 GO Classification
Function
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid biosynthesis
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 31 General Function Lipid transport and metabolism
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID B3KQM2 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name B3KQM2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AK075211 Link Image
Enzyme 31 GeneCard ID B3KQM2 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location 12
Enzyme 31 Locus 12q
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 16484
Enzyme 32 Name cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
Enzyme 32 Synonyms Not Available
Enzyme 32 Gene Name MGC26963
Enzyme 32 Protein Sequence >cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
Enzyme 32 Number of Residues 365
Enzyme 32 Molecular Weight 42281
Enzyme 32 Theoretical pI 9.00
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function Not Available
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID B2RA61 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name B2RA61_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AK314049 Link Image
Enzyme 32 GeneCard ID B2RA61 Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID Not Available
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References Not Available
Enzyme 32 Metabolite References Not Available