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Human Metabolome Database Version 2.5

 

Showing metabocard for dTDP (HMDB01274)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-19 11:38:51
Accession Number HMDB01274
Secondary Accession Numbers Not Available
Common Name dTDP
Description Is an intermediate in the Thymidylate kinase (EC 2.7.4.9; ATP:dTMP phosphotransferase) catalyzes the phosphorylation of dTMP (to form dTDP) in the dTTP synthesis pathway for DNA synthesis. (OMIM 188345 )
Synonyms
  1. Deoxy-tdp
  2. Deoxythymidine 5'-diphosphate
  3. Thymidine 5'-diphosphate
  4. Thymidine 5'-pyrophosphate
  5. dTDP;TDP
Chemical IUPAC Name [hydroxy-[[3-hydroxy-5-(5-methyl-2,4-dioxo-pyrimidin-1-yl)-oxolan-2-yl]methoxy]phosphoryl]oxyphosphonic acid
Chemical Formula C10H16N2O11P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 402.188
Monoisotopic Molecular Weight 402.022919
Isomeric SMILES CC1=CN([C@H]2C[C@H](O)[C@@H](COP(O)(=O)OP(O)(O)=O)O2)C(=O)NC1=O
Canonical SMILES CC1=CN(C2CC(O)C(COP(O)(=O)OP(O)(O)=O)O2)C(=O)NC1=O
KEGG Compound ID C00363 Link Image
BioCyc ID TDP Link Image
BiGG ID 34750 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01274 Link Image
Metagene Link HMDB01274 Link Image
METLIN ID 6129 Link Image
PubChem Compound 164628 Link Image
PubChem Substance 8027283 Link Image
ChEBI ID 18075 Link Image
CAS Registry Number 491-97-4
InChI Identifier InChI=1/C10H16N2O11P2/c1-5-3-12(10(15)11-9(5)14)8-2-6(13)7(22-8)4-21-25(19,20)23-24(16,17)18/h3,6-8,13H,2,4H2,1H3,(H,19,20)(H,11,14,15)(H2,16,17,18)/t6-,7+,8+/m0/s1
Synthesis Reference Rupprath, Carsten; Kopp, Maren; Hirtz, Dennis; Mueller, Rolf; Elling, Lothar. An enzyme module system for in situ regeneration of deoxythymidine 5'-diphosphate (dTDP)-activated deoxy sugars. Advanced Synthesis & Catalysis (2007), 349(8+9), 1489-1496.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 6.94 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.87 [Predicted by ALOGPS]; -4.3 [Predicted by PubChem via XLOGP]; 13.45 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
  • nucleus
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Dahlmann N: Human serum thymidine triphosphate nucleotidohydrolase: purification and properties of a new enzyme. Biochemistry. 1982 Dec 21;21(26):6634-9. [PubMed Link Image]
  2. Xu Y, Singh KV, Qin X, Murray BE, Weinstock GM: Analysis of a gene cluster of Enterococcus faecalis involved in polysaccharide biosynthesis. Infect Immun. 2000 Feb;68(2):815-23. [PubMed Link Image]
  3. Vallon O: New sequence motifs in flavoproteins: evidence for common ancestry and tools to predict structure. Proteins. 2000 Jan 1;38(1):95-114. [PubMed Link Image]
  4. Sheu SJ, Wu SN: Mechanism of inhibitory actions of oxidizing agents on calcium-activated potassium current in cultured pigment epithelial cells of the human retina. Invest Ophthalmol Vis Sci. 2003 Mar;44(3):1237-44. [PubMed Link Image]
  5. Costantini P, Belzacq AS, Vieira HL, Larochette N, de Pablo MA, Zamzami N, Susin SA, Brenner C, Kroemer G: Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene. 2000 Jan 13;19(2):307-14. [PubMed Link Image]
  6. Ramaswamy SV, Amin AG, Goksel S, Stager CE, Dou SJ, El Sahly H, Moghazeh SL, Kreiswirth BN, Musser JM: Molecular genetic analysis of nucleotide polymorphisms associated with ethambutol resistance in human isolates of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 2000 Feb;44(2):326-36. [PubMed Link Image]
  7. Tomioka H: [Prospects for development of new antituberculous drugs] Kekkaku. 2002 Aug;77(8):573-84. [PubMed Link Image]
  8. Kuo SY, Jiann BP, Lu YC, Chang HT, Chen WC, Huang JK, Jan CR: Thiol oxidation by 2,2'-dithiodipyridine induced calcium mobilization in MG63 human osteosarcoma cells. Life Sci. 2003 Feb 28;72(15):1733-43. [PubMed Link Image]
  9. Riener CK, Kada G, Gruber HJ: Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine. Anal Bioanal Chem. 2002 Jul;373(4-5):266-76. Epub 2002 Jun 6. [PubMed Link Image]
  10. Ahmed IH, Manning G, Wassenaar TM, Cawthraw S, Newell DG: Identification of genetic differences between two Campylobacter jejuni strains with different colonization potentials. Microbiology. 2002 Apr;148(Pt 4):1203-12. [PubMed Link Image]
  11. Kuo SY, Ho CM, Chen WC, Jan CR: Sulfhydryl modification by 4,4'-dithiodipyridine induces calcium mobilization in human osteoblast-like cells. Arch Toxicol. 2003 Nov;77(11):630-7. Epub 2003 Aug 20. [PubMed Link Image]
  12. Bialkowski K, Kasprzak KS: Inhibition of 8-oxo-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase (8-oxo-dGTPase) activity of the antimutagenic human MTH1 protein by nucleoside 5'-diphosphates. Free Radic Biol Med. 2003 Sep 15;35(6):595-602. [PubMed Link Image]
Metabolic Enzymes
  1. Thymidylate kinase
  2. Ectonucleoside triphosphate diphosphohydrolase 1
  3. Soluble calcium-activated nucleotidase 1
  4. Nucleoside diphosphate kinase, mitochondrial precursor
  5. Nucleoside diphosphate kinase A
  6. Nucleoside diphosphate kinase 7
  7. Nucleoside diphosphate kinase B
  8. Nucleoside diphosphate kinase 3
  9. Nucleoside diphosphate kinase 6
  10. Ectonucleoside triphosphate diphosphohydrolase 4
  11. Ectonucleoside triphosphate diphosphohydrolase 6
  12. Ectonucleoside triphosphate diphosphohydrolase 5 precursor
  13. dTDP-D-glucose 4,6-dehydratase
  14. Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
  15. Uridine-cytidine kinase 2
  16. Uridine/cytidine kinase-like 1
  17. Ectonucleoside triphosphate diphosphohydrolase 8
  18. Putative nucleoside diphosphate kinase
  19. Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
  20. Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
  21. Nucleoside diphosphate-linked moiety X motif 18
  22. Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
  23. cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
  24. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  25. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  26. Nucleoside diphosphate kinase
Enzyme 1 [top]
Enzyme 1 ID 5312
Enzyme 1 Name Thymidylate kinase
Enzyme 1 Synonyms
  1. dTMP kinase
Enzyme 1 Gene Name DTYMK
Enzyme 1 Protein Sequence >Thymidylate kinase
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
Enzyme 1 Number of Residues 212
Enzyme 1 Molecular Weight 23820
Enzyme 1 Theoretical pI 8.49
Enzyme 1 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 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function Catalyzes the conversion of dTMP to dTDP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + dTMP = ADP + dTDP
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 37206 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P23919 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DTYMK_HUMAN Link Image
Enzyme 1 PDB ID 1E9A Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >636 bp
ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA
Enzyme 1 GenBank Gene ID X54729 Link Image
Enzyme 1 GeneCard ID DTYMK Link Image
Enzyme 1 GenAtlas ID DTYMK Link Image
Enzyme 1 HGNC ID HGNC:3061 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q37.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed Link Image]
  2. Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5313
Enzyme 2 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 2 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 2 Gene Name ENTPD1
Enzyme 2 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 2 Number of Residues 510
Enzyme 2 Molecular Weight 57965
Enzyme 2 Theoretical pI 6.29
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 2 General Function Not Available
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 17-37 479-499
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 765256 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID S73813 Link Image
Enzyme 2 GeneCard ID ENTPD1 Link Image
Enzyme 2 GenAtlas ID ENTPD1 Link Image
Enzyme 2 HGNC ID HGNC:3363 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5314
Enzyme 3 Name Soluble calcium-activated nucleotidase 1
Enzyme 3 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 3 Gene Name CANT1
Enzyme 3 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 3 Number of Residues 401
Enzyme 3 Molecular Weight 44840
Enzyme 3 Theoretical pI 5.98
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 45-62
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 22218108 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 3 PDB ID 1S1D Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 3 GenBank Gene ID AF328554 Link Image
Enzyme 3 GeneCard ID CANT1 Link Image
Enzyme 3 GenAtlas ID CANT1 Link Image
Enzyme 3 HGNC ID HGNC:19721 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5338
Enzyme 4 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 4 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 4 Gene Name NME4
Enzyme 4 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 4 Number of Residues 187
Enzyme 4 Molecular Weight 20659
Enzyme 4 Theoretical pI 10.75
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
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 1945762 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 4 PDB ID 1EHW Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 4 GenBank Gene ID Y07604 Link Image
Enzyme 4 GeneCard ID NME4 Link Image
Enzyme 4 GenAtlas ID NME4 Link Image
Enzyme 4 HGNC ID HGNC:7852 Link Image
Enzyme 4 Chromosome Location 16
Enzyme 4 Locus 16p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5341
Enzyme 5 Name Nucleoside diphosphate kinase A
Enzyme 5 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 5 Gene Name NME1
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17149
Enzyme 5 Theoretical pI 6.11
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 35068 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 5 PDB ID 1JXV Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 5 GenBank Gene ID X17620 Link Image
Enzyme 5 GeneCard ID NME1 Link Image
Enzyme 5 GenAtlas ID NME1 Link Image
Enzyme 5 HGNC ID HGNC:7849 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  5. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  6. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  7. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  8. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  9. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  10. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5342
Enzyme 6 Name Nucleoside diphosphate kinase 7
Enzyme 6 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 6 Gene Name NME7
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 6 Number of Residues 376
Enzyme 6 Molecular Weight 42492
Enzyme 6 Theoretical pI 6.44
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4960169 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 6 GenBank Gene ID AF153191 Link Image
Enzyme 6 GeneCard ID NME7 Link Image
Enzyme 6 GenAtlas ID NME7 Link Image
Enzyme 6 HGNC ID HGNC:20461 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5344
Enzyme 7 Name Nucleoside diphosphate kinase B
Enzyme 7 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 7 Gene Name NME2
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 7 Number of Residues 152
Enzyme 7 Molecular Weight 17298
Enzyme 7 Theoretical pI 8.69
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4467843 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 7 PDB ID 1NSK Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 7 GenBank Gene ID X58965 Link Image
Enzyme 7 GeneCard ID NME2 Link Image
Enzyme 7 GenAtlas ID NME2 Link Image
Enzyme 7 HGNC ID HGNC:7850 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q21.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  2. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  5. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5345
Enzyme 8 Name Nucleoside diphosphate kinase 3
Enzyme 8 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. Nucleoside diphosphate kinase C
  4. NDPKC
  5. nm23-H3
  6. DR-nm23
Enzyme 8 Gene Name NME3
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 8 Number of Residues 169
Enzyme 8 Molecular Weight 19015
Enzyme 8 Theoretical pI 7.97
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1051256 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >507 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 8 GenBank Gene ID U29656 Link Image
Enzyme 8 GeneCard ID NME3 Link Image
Enzyme 8 GenAtlas ID NME3 Link Image
Enzyme 8 HGNC ID HGNC:7851 Link Image
Enzyme 8 Chromosome Location 16
Enzyme 8 Locus 16q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5346
Enzyme 9 Name Nucleoside diphosphate kinase 6
Enzyme 9 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 9 Gene Name NME6
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 9 Number of Residues 186
Enzyme 9 Molecular Weight 21142
Enzyme 9 Theoretical pI 8.49
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-24
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3228530 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 9 GenBank Gene ID AF051941 Link Image
Enzyme 9 GeneCard ID NME6 Link Image
Enzyme 9 GenAtlas ID NME6 Link Image
Enzyme 9 HGNC ID HGNC:20567 Link Image
Enzyme 9 Chromosome Location 3
Enzyme 9 Locus 3p21
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6159
Enzyme 10 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 10 Synonyms
  1. NTPDase 4
  2. Uridine-diphosphatase
  3. UDPase
  4. Lysosomal apyrase-like protein of 70 kDa
Enzyme 10 Gene Name ENTPD4
Enzyme 10 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 10 Number of Residues 616
Enzyme 10 Molecular Weight 70256
Enzyme 10 Theoretical pI 8.39
Enzyme 10 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP
Enzyme 10 Pathways
Enzyme 10 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 34-54 560-580
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3153211 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1830 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGG
CGACTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCT
ACAGACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGG
TCTCGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGAT
ATCAGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATT
TCAGAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTT
GCTGCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACG
GCTGGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACC
GATATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGG
AAACAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCAT
ATTGAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAA
GCCATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATA
GCGTACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTG
GGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGG
TTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAA
AAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCC
TGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGA
GGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAAC
GAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAA
TTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGAC
TACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTACTGTGCAACAAAGTGGTCCATT
TTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAG
TATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCT
GTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACC
CTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGAGACATCCAGCAGGAGGCC
TTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTTGTCTACAACCACTACCTGTTC
TCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTGTACCTGCTGCGGCTGCGGCGC
ATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCCCTCTGGATGGAGGAGGGCCTT
CCCGCCCAGAATGCCCCAGGGACCTTGTGA
Enzyme 10 GenBank Gene ID AF016032 Link Image
Enzyme 10 GeneCard ID ENTPD4 Link Image
Enzyme 10 GenAtlas ID ENTPD4 Link Image
Enzyme 10 HGNC ID HGNC:14573 Link Image
Enzyme 10 Chromosome Location 8
Enzyme 10 Locus 8p21.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed Link Image]
  2. Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed Link Image]
  3. Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6160
Enzyme 11 Name Ectonucleoside triphosphate diphosphohydrolase 6
Enzyme 11 Synonyms
  1. NTPDase 6
  2. CD39 antigen-like 2
Enzyme 11 Gene Name ENTPD6
Enzyme 11 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 6
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
Enzyme 11 Number of Residues 484
Enzyme 11 Molecular Weight 53248
Enzyme 11 Theoretical pI 9.52
Enzyme 11 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP
Enzyme 11 Pathways
Enzyme 11 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 40-60
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3335098 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O75354 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ENTP6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1455 bp
ATGAAAAAAGGTATCCGTTATGAAACTTCCAGAAAAACGAGCTACATTTTTCAGCAGCCG
CAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGCCTGCGGGTG
GCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTTGCCTACATC
AAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCAGCCCCGGGG
GCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGGCACGAGGTC
TTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTCTTCCAGTTC
ACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCAGTGAAGCCA
GGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGGGAACTACTG
GATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTGGTCCTCAAG
GCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTGCAGAAGGTG
AAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCCATCATGAAC
GGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGCAGCTTGAAA
ACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACTCAGATCGCC
TTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTGACGGCACTG
CGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTCGGGCTGATG
TCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGATGGAAAGGAG
TTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCAGAAGTCACG
TACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCTGCCAGAGTG
TCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTGGACTTCTAT
GCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCGGAGAAGGGA
GGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGGACCCTGGAG
ACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGCCTGCTACTC
CAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATTGACAATGTT
GAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAACAGACAGAAG
AGTCCAGCCTCATAG
Enzyme 11 GenBank Gene ID AF039916 Link Image
Enzyme 11 GeneCard ID ENTPD6 Link Image
Enzyme 11 GenAtlas ID ENTPD6 Link Image
Enzyme 11 HGNC ID HGNC:3368 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20p11.2-p11.22
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [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]
  3. Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE: CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry. 2000 Oct 24;39(42):12916-23. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6161
Enzyme 12 Name Ectonucleoside triphosphate diphosphohydrolase 5 precursor
Enzyme 12 Synonyms
  1. NTPDase 5
  2. Nucleoside diphosphatase
  3. CD39 antigen-like 4
  4. ER-UDPase
Enzyme 12 Gene Name ENTPD5
Enzyme 12 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5 precursor
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 12 Number of Residues 428
Enzyme 12 Molecular Weight 47518
Enzyme 12 Theoretical pI 6.29
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Likely to promote reglycosylation reactions involved in glycoproteins folding and quality control in the endoplasmic reticulum. Hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-20
Enzyme 12 Transmembrane Regions
  • 29-51
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 3335102 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O75356 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ENTP5_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACTTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 12 GenBank Gene ID AF039918 Link Image
Enzyme 12 GeneCard ID ENTPD5 Link Image
Enzyme 12 GenAtlas ID ENTPD5 Link Image
Enzyme 12 HGNC ID HGNC:3367 Link Image
Enzyme 12 Chromosome Location 14
Enzyme 12 Locus 14q24
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6190
Enzyme 13 Name dTDP-D-glucose 4,6-dehydratase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name TGDS
Enzyme 13 Protein Sequence >dTDP-D-glucose 4,6-dehydratase
MSAACWEEPWGLPGGFAKRVLVTGGAGFIASHMIVSLVEDYPNYMIINLDKLDYCASLKN
LETISNKQNYKFIQGDICDSHFVKLLFETEKIDIVLHFAAQTHVDLSFVRAFEFTYVNVY
GTHVLVSAAHEARVEKFIYVSTDEVYGGSLDKEFDESSPKQPTNPYASSKAAAECFVQSY
WEQYKFPVVITRSSNVYGPHQYPEKVIPKFISLLQHNRKCCIHGSGLQTRNFLYATDVVE
AFLTVLKKGKPGEIYNIGTNFEMSVVQLAKELIQLIKETNSESEMENWVDYVNDRPTNDM
RYPMKSEKIHGLGWRPKVPWKEGIKKTIEWYRENFHNWKNVEKALEPFPV
Enzyme 13 Number of Residues 350
Enzyme 13 Molecular Weight 40214
Enzyme 13 Theoretical pI 6.59
Enzyme 13 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 13 General Function Cell wall/membrane/envelope biogenesis
Enzyme 13 Specific Function dTDP-glucose = dTDP-4-dehydro-6-deoxy-D- glucose + H(2)O
Enzyme 13 Pathways
  • Biosynthesis of vancomycin group antibiotics (map01055 Link Image)
  • Nucleotide Sugars Metabolism (map00520 Link Image)
  • Polyketide sugar unit biosynthesis (map00523 Link Image)
  • Streptomycin biosynthesis (map00521 Link Image)
Enzyme 13 Reactions
  • dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 4128133 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O95455 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name TGDS_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1053 bp
ATGTCGGCGGCGTGTTGGGAGGAACCGTGGGGTCTTCCCGGCGGCTTTGCGAAGCGGGTC
CTGGTGACCGGCGGTGCTGGTTTCATTGCATCACATATGATTGTCTCTTTAGTGGAAGAT
TATCCAAACTATATGATCATAAATCTAGACAAGCTGGATTACTGTGCAAGCTTGAAGAAT
CTTGAAACCATTTCTAACAAACAGAACTACAAATTTATACAGGGTGACATATGTGATTCT
CACTTTGTGAAACTGCTTTTTGAAACAGAGAAAATAGATATAGTACTACATTTTGCCGCA
CAAACACATGTAGATCTTTCATTCGTACGTGCCTTTGAGTTTACCTATGTTAATGTTTAT
GGCACTCACGTTTTGGTAAGTGCTGCTCATGAAGCCAGAGTGGAGAAGTTTATTTATGTC
AGCACAGATGAAGTATATGGTGGCAGTCTTGATAAGGAATTTGATGAATCTTCACCCAAA
CAACCTACAAATCCTTATGCATCATCTAAAGCAGCTGCTGAATGTTTTGTACAGTCTTAC
TGGGAACAATATAAGTTTCCAGTTGTCATCACAAGAAGCAGTAATGTTTATGGACCACAT
CAATATCCAGAAAAGGTTATTCCAAAATTTATATCTTTGCTACAGCACAACAGGAAATGT
TGCATTCATGGGTCAGGGCTTCAAACAAGAAACTTCCTTTATGCTACTGATGTTGTAGAA
GCATTTCTCACTGTCCTCAAAAAAGGGAAACCAGGTGAAATTTATAACATCGGAACCAAT
TTTGAAATGTCAGTTGTCCAGCTTGCCAAAGAACTAATACAACTGATCAAAGAGACCAAT
TCAGAGTCTGAAATGGAAAATTGGGTTGATTATGTTAATGATAGACCCACCAATGACATG
AGATACCCAATGAAGTCAGAAAAAATACATGGCTTAGGATGGAGACCTAAAGTGCCTTGG
AAAGAAGGAATAAAGAAAACAATTGAATGGTACAGAGAGAATTTTCACAACTGGAAGAAT
GTGGAAAAGGCATTAGAACCCTTTCCGGTATAA
Enzyme 13 GenBank Gene ID AJ006068 Link Image
Enzyme 13 GeneCard ID TGDS Link Image
Enzyme 13 GenAtlas ID TGDS Link Image
Enzyme 13 HGNC ID HGNC:20324 Link Image
Enzyme 13 Chromosome Location 13
Enzyme 13 Locus 13q32.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6586
Enzyme 14 Name Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
Enzyme 14 Synonyms
  1. PNPase 1
  2. Polynucleotide phosphorylase-like protein
  3. PNPase old-35
  4. 3'-5' RNA exonuclease OLD35
Enzyme 14 Gene Name PNPT1
Enzyme 14 Protein Sequence >Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISS
GKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRRE
IGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLS
DIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQD
FCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFT
DYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCD
GRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKD
KNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESN
GSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYN
GDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASR
KENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEA
RDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHP
TALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSS
NSQ
Enzyme 14 Number of Residues 783
Enzyme 14 Molecular Weight 85952
Enzyme 14 Theoretical pI 7.86
Enzyme 14 GO Classification
Function
  • 3'-5' exonuclease activity
  • 3'-5'-exoribonuclease activity
  • RNA binding
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • polyribonucleotide nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA catabolism
  • RNA metabolism
  • RNA processing
  • cellular metabolism
  • mRNA catabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 14 General Function Translation, ribosomal structure and biogenesis
Enzyme 14 Specific Function Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction
Enzyme 14 Pathways
Enzyme 14 Reactions
  • RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 20372922 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q8TCS8 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PNPT1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2352 bp
ATGGCGGCCTGCAGGTACTGCTGCTCGTGCCTCCGGCTCCGGCCCCTGAGCGATGGTCCT
TTCCTTCTGCCACGGCGGGATCGGGCACTCACCCAGTTGCAAGTGCGAGCACTATGGAGT
AGCGCAGGGTCTCGAGCTGTGGCCGTGGACTTAGGCAACAGGAAATTAGAAATATCTTCT
GGAAAGCTGGCCAGATTTGCAGATGGCTCTGCTGTAGTACAGTCAGGTGACACTGCAGTA
ATGGTCACAGCGGTCAGTAAAACAAAACCTTCCCCTTCCCAGTTTATGCCTTTGGTGGTT
GACTACAGACAAAAAGCTGCTGCAGCAGGTAGAATTCCCACAAACTATCTGAGAAGAGAG
GTTGGTACTTCTGATAAAGAAATTCTAACAAGTCGAATAATAGATCGTTCAATTAGACCG
CTCTTTCCAGCTGGCTACTTCTATGATACACAGGTTCTGTGTAATCTGTTAGCAGTAGAT
GGTGTAAATGAGCCTGATGTCCTAGCAATTAATGGCGCTTCCGTAGCCCTCTCATTATCA
GATATTCCTTGGAATGGACCTGTTGGGGCAGTACGAATAGGAATAATTGATGGAGAATAT
GTTGTTAACCCAACAAGAAAAGAAATGTCTTCTAGTACTTTAAATTTAGTGGTTGCTGGA
GCACCTAAAAGTCAGATTGTCATGTTGGAAGCCTCTGCAGAGAACATTTTACAGCAGGAC
TTTTGCCATGCTATCAAAGTGGGAGTGAAATATACCCAACAAATAATTCAGGGCATTCAG
CAGTTGGTAAAAGAAACTGGTGTTACCAAGAGGACACCTCAGAAGTTATTTACCCCTTCG
CCAGAGATTGTGAAATATACTCATAAACTTGCTATGGAGAGACTCTATGCAGTTTTTACA
GATTACGAGCATGACAAAGTTTCCAGAGATGAAGCTGTTAACAAAATAAGATTAGATACG
GAGGAACAACTAAAAGAAAAATTTCCAGAAGCCGATCCATATGAAATAATAGAATCCTTC
AATGTTGTTGCAAAGGAAGTTTTTAGAAGTATTGTTTTGAATGAATACAAAAGGTGCGAT
GGTCGGGATTTGACTTCACTTAGGAATGTAAGTTGTGAGGTAGATATGTTTAAAACCCTT
CATGGATCAGCATTATTTCAAAGAGGACAAACACAGGTGCTTTGTACCGTTACATTTGAT
TCATTAGAATCTGGTATTAAGTCAGATCAAGTTATAACAGCTATAAATGGGATAAAAGAT
AAAAATTTCATGCTGCACTACGAGTTTCCTCCTTATGCAACTAATGAAATTGGCAAAGTC
ACTGGTTTAAATAGAAGAGAACTTGGGCATGGTGCTCTTGCTGAGAAAGCTTTGTATCCT
GTTATTCCCCGAGATTTTCCTTTCACCATAAGAGTTACATCTGAAGTCCTAGAGTCAAAT
GGGTCATCTTCTATGGCATCTGCATGTGGCGGAAGTTTAGCATTAATGGATTCAGGGGTT
CCAATTTCATCTGCTGTTGCAGGCGTAGCAATAGGATTGGTCACCAAAACCGATCCTGAG
AAGGGTGAAATAGAAGATTATCGTTTGCTGACAGATATTTTGGGAATTGAAGATTACAAT
GGTGACATGGACTTCAAAATAGCTGGCACTAATAAAGGAATAACTGCATTACAGGCTGAT
ATTAAATTACCTGGAATACCAATAAAAATTGTGATGGAGGCTATTCAACAAGCTTCAGTG
GCAAAAAAGGAGATATTACAGATCATGAACAAAACTATTTCAAAACCTCGAGCATCTAGA
AAAGAAAATGGACCTGTTGTAGAAACTGTTCAGGTTCCATTATCAAAACGAGCAAAATTT
GTTGGACCTGGTGGCTATAACTTAAAAAAACTTCAGGCTGAAACAGGTGTAACTATTAGT
CAGGTGGATGAAGAAACGTTTTCTGTATTTGCACCAACACCCAGTGCTATGCATGAGGCA
AGAGACTTCATTACTGAAATCTGCAAGGATGATCAGGAGCAGCAATTAGAATTTGGAGCA
GTATATACCGCCACAATAACTGAAATCAGAGATACTGGTGTAATGGTAAAATTATATCCA
AATATGACTGCGGTACTGCTTCATAACACACAACTTGATCAACGAAAGATTAAACATCCT
ACTGCCCTAGGATTAGAAGTTGGCCAAGAAATTCAGGTGAAATACTTTGGACGTGACCCA
GCCGATGGAAGAATGAGGCTTTCTCGAAAAGTGCTTCAGTCGCCAGCTACAACCGTGGTC
AGAACTTTGAATGACAGAAGTAGTATTGTAATGGGAGAACCTATTTCACAGTCATCATCT
AATTCTCAGTGA
Enzyme 14 GenBank Gene ID AJ458465 Link Image
Enzyme 14 GeneCard ID PNPT1 Link Image
Enzyme 14 GenAtlas ID PNPT1 Link Image
Enzyme 14 HGNC ID HGNC:23166 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2p15
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ: Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol. 2002 Nov 1;323(4):653-63. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8075
Enzyme 15 Name Uridine-cytidine kinase 2
Enzyme 15 Synonyms
  1. UCK 2
  2. Uridine monophosphokinase 2
  3. Cytidine monophosphokinase 2
Enzyme 15 Gene Name UCK2
Enzyme 15 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 15 Number of Residues 261
Enzyme 15 Molecular Weight 29299
Enzyme 15 Theoretical pI 6.68
Enzyme 15 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 15 General Function Nucleotide transport and metabolism
Enzyme 15 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 15 Pathways
Enzyme 15 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 1655420 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 15 PDB ID 1XRJ Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
Enzyme 15 GenBank Gene ID D78335 Link Image
Enzyme 15 GeneCard ID UCK2 Link Image
Enzyme 15 GenAtlas ID UCK2 Link Image
Enzyme 15 HGNC ID HGNC:12562 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1q23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 13098
Enzyme 16 Name Uridine/cytidine kinase-like 1
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name UCKL1
Enzyme 16 Protein Sequence >Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 16 Number of Residues 548
Enzyme 16 Molecular Weight 61142
Enzyme 16 Theoretical pI 7.40
Enzyme 16 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 16 General Function Nucleotide transport and metabolism
Enzyme 16 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 16 Pathways
Enzyme 16 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 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 38228699 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AJ605558 Link Image
Enzyme 16 GeneCard ID Q9NWZ5 Link Image
Enzyme 16 GenAtlas ID UCKL1 Link Image
Enzyme 16 HGNC ID HGNC:15938 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 13379
Enzyme 17 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 17 Synonyms
  1. NTPDase 8
  2. NTPDase8
  3. E-NTPDase 8
Enzyme 17 Gene Name ENTPD8
Enzyme 17 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 17 Number of Residues 495
Enzyme 17 Molecular Weight 53904
Enzyme 17 Theoretical pI 4.96
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 17 General Function Not Available
Enzyme 17 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 17 Pathways
Enzyme 17 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 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 9-29 472-492
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 59003409 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 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 17 GenBank Gene ID AY903953 Link Image
Enzyme 17 GeneCard ID Q5MY95 Link Image
Enzyme 17 GenAtlas ID ENTPD8 Link Image
Enzyme 17 HGNC ID HGNC:24860 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 14489
Enzyme 18 Name Putative nucleoside diphosphate kinase
Enzyme 18 Synonyms
  1. NDK
  2. NDP kinase
Enzyme 18 Gene Name NME2P1
Enzyme 18 Protein Sequence >Putative nucleoside diphosphate kinase
MQCGLVGKIIKRFEQKGFRLVAMKFLPASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVA
MVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLRFK
PEELVDYKSCAHDWVYE
Enzyme 18 Number of Residues 137
Enzyme 18 Molecular Weight 15529
Enzyme 18 Theoretical pI 8.83
Enzyme 18 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331] ALL_REAC R00331 > R00124 R00156 R00330 R00570 R00722 R01137 R01857 R02093 R02326 R02331 R03530
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 2935619 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O60361 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name NDK8_HUMAN Link Image
Enzyme 18 PDB ID 1NSK Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >414 bp
ATGCAGTGCGGCCTGGTGGGCAAGATCATCAAGCGCTTCGAGCAGAAGGGGTTCCGCCTC
GTGGCCATGAAGTTCCTCCCGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTG
AAGGACCGCCCATTCTTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTCGTGGCC
ATGGTCTGGGAGGGGCTGAACGTCGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAAT
CCAGCAGATTCTAAGCCAGGCACCATTCGTGGGGACTTTTGCATTCAGGTTGGCAGGAAC
ATCATTCATGGCAGTGATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTACGGTTTAAG
CCTGAAGAACTGGTTGACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 18 GenBank Gene ID AC004263 Link Image
Enzyme 18 GeneCard ID O60361 Link Image
Enzyme 18 GenAtlas ID NME2P1 Link Image
Enzyme 18 HGNC ID HGNC:31358 Link Image
Enzyme 18 Chromosome Location 12
Enzyme 18 Locus 12q24.31
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 14500
Enzyme 19 Name Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
Enzyme 19 Synonyms
  1. 8-oxo-dGTPase NUDT15
  2. Nucleoside diphosphate-linked moiety X motif 15
  3. Nudix motif 15
Enzyme 19 Gene Name NUDT15
Enzyme 19 Protein Sequence >Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
MTASAQPRGRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEECA
QRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSEPKNVEPEKNESW
EWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVGYKGNHL
Enzyme 19 Number of Residues 164
Enzyme 19 Molecular Weight 18609
Enzyme 19 Theoretical pI 6.08
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Nucleotide transport and metabolism
Enzyme 19 Specific Function Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8- oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. Its substrate specificity in vivo however remains unclear
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 7023325 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9NV35 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name NUD15_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >495 bp
ATGACGGCCAGCGCACAGCCGCGCGGGCGGCGGCCAGGAGTCGGAGTCGGAGTCGTGGTG
ACCAGCTGCAAGCATCCGCGTTGCGTCCTCCTGGGGAAGAGGAAAGGCTCGGTTGGAGCT
GGCAGTTTCCAACTCCCTGGAGGTCATCTGGAGTTCGGTGAAACCTGGGAAGAATGTGCT
CAAAGGGAAACCTGGGAAGAAGCAGCTCTTCACCTGAAAAATGTTCACTTTGCCTCAGTT
GTGAATTCTTTCATTGAGAAGGAGAATTACCATTATGTTACTATATTAATGAAAGGAGAA
GTGGATGTGACTCATGATTCAGAACCAAAGAATGTAGAGCCTGAAAAAAATGAAAGTTGG
GAGTGGGTTCCTTGGGAAGAACTACCTCCCCTGGACCAGCTTTTCTGGGGACTGCGTTGT
TTAAAAGAACAAGGCTATGATCCATTTAAAGAAGATCTGAACCATCTGGTGGGATACAAA
GGAAATCATCTCTAG
Enzyme 19 GenBank Gene ID AK001818 Link Image
Enzyme 19 GeneCard ID Q9NV35 Link Image
Enzyme 19 GenAtlas ID NUDT15 Link Image
Enzyme 19 HGNC ID HGNC:23063 Link Image
Enzyme 19 Chromosome Location 13
Enzyme 19 Locus 13q14.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 14501
Enzyme 20 Name Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
Enzyme 20 Synonyms
  1. Nudix motif 17
Enzyme 20 Gene Name NUDT17
Enzyme 20 Protein Sequence >Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
MAEVRVQLLLSRRPESVSFARSVCGLLGAGPGLGTWPIHCSLKRGRLVLSSRPFPGASAR
LPLQRPPFCPFAALEERPRVPGAELPTDRGVDLGVAVILQSSDKTVLLTRRARTLSVSPN
LWVPPGGHVELEEELLDGGLRELWEESGLHLPQGQFSWVPLGLWESAYPPRLSWGLPKYH
HIVLYLLVISQESQQQLQARIQPNPNEVSALMWLTPDVAAAVAAAEDGTETPGLLPQDLP
PSVLAVELEEDGRARPLVLHMSTLLRMIPTMAEDKERVSTGTKFALKLWLQHLGR
Enzyme 20 Number of Residues 295
Enzyme 20 Molecular Weight 32448
Enzyme 20 Theoretical pI 6.89
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Probably mediates the hydrolysis of some nucleoside diphosphate derivatives
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID P0C025 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name NUD17_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AL160282 Link Image
Enzyme 20 GeneCard ID P0C025 Link Image
Enzyme 20 GenAtlas ID NUDT17 Link Image
Enzyme 20 HGNC ID HGNC:26618 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 14502
Enzyme 21 Name Nucleoside diphosphate-linked moiety X motif 18
Enzyme 21 Synonyms
  1. Nudix motif 18
Enzyme 21 Gene Name Not Available
Enzyme 21 Protein Sequence >Nucleoside diphosphate-linked moiety X motif 18
MRISFKAGVYVPHPTGHVTFITLWWNEKKGIWDMINSGNAIVCLRQQRDSGSRGRPRASV
TSPDCRVTVAYPGGATRPAGKMTSPSELLQTSARSGSWRAGGGWETSRAHGTDRRQKPGG
VRWAPDPCPPSSRAAPGGPAPSVNAAGRPIRAGRGAAQPISGQSSRALPRSRALPRSREL
PARCRRDWERAPQRTLARGSAQSVCEDPARRPPGDPMASEGLAGALASVLAGQGSSVHSC
DSAPAGEPPAPVRLRKNVCYVVLAVFLSEQDEVLLIQEAKRECRGSWYLPAGRMEPGETI
VEALQREVKEEAGLHCEPETLLSVEERGPSWVRFVFLARPTGGILKTSKEADAESLQAAW
YPRTSLPTPLRAHDILHLVELAAQYRQQARHPLILPQELPCDLVCQRLVATFTSAQTVWV
LVGTVGMPHLPVTACGLDPVEQRGGMKMAVLRLLQECLTLHHLVVEIKGLLGLQHLGRDH
SDGICLNVLVTVAFRSPGIQDEPPKVRGENFSWWKVMEEDLQSQLLQRLQGSSVVPVNR
Enzyme 21 Number of Residues 539
Enzyme 21 Molecular Weight 58665
Enzyme 21 Theoretical pI 9.42
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Nucleotide transport and metabolism
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 34530231 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q6ZVK8 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name Q6ZVK8_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1620 bp
ATGCGAATCTCCTTCAAGGCAGGGGTTTATGTCCCCCACCCCACGGGCCATGTGACATTT
ATAACTCTTTGGTGGAATGAGAAGAAAGGTATTTGGGATATGATCAACTCCGGCAATGCC
ATTGTGTGTTTACGGCAACAGCGGGACAGTGGTTCCAGGGGGCGGCCCCGGGCCTCCGTG
ACGTCACCGGATTGTCGCGTCACCGTCGCCTACCCCGGCGGCGCAACGCGCCCTGCAGGA
AAGATGACGTCACCGTCGGAGCTCCTGCAGACCAGTGCGCGCTCGGGGAGTTGGCGAGCG
GGTGGCGGCTGGGAGACGTCCCGAGCGCACGGGACTGACAGGCGGCAGAAGCCGGGCGGG
GTCCGCTGGGCTCCGGACCCGTGCCCCCCCAGTTCCAGGGCGGCCCCGGGCGGCCCCGCC
CCCTCGGTGAATGCCGCGGGCCGGCCAATCCGGGCAGGCCGCGGCGCCGCGCAGCCTATC
AGCGGCCAGAGCTCGCGTGCGCTTCCGCGTTCGCGTGCGCTTCCGCGTTCTCGTGAGCTC
CCGGCCCGCTGCCGCAGGGACTGGGAGCGGGCTCCGCAGCGCACTCTAGCCCGCGGCTCG
GCTCAGTCGGTCTGCGAGGATCCGGCCCGCCGCCCCCCGGGGGACCCGATGGCCTCGGAG
GGCCTGGCGGGGGCGCTGGCTTCCGTGCTGGCTGGCCAGGGGTCCAGCGTGCACAGCTGC
GACTCGGCGCCGGCCGGGGAGCCGCCGGCGCCCGTGCGGCTGCGGAAGAACGTGTGCTAC
GTGGTGCTGGCCGTGTTCCTCAGCGAGCAGGATGAGGTGCTACTGATCCAGGAGGCCAAG
AGGGAGTGCCGGGGGTCGTGGTACCTGCCTGCGGGGAGAATGGAGCCAGGGGAGACCATC
GTGGAGGCGCTGCAGCGGGAGGTGAAGGAGGAGGCGGGGCTGCACTGTGAGCCCGAGACA
CTGCTGTCCGTGGAGGAGCGGGGCCCCTCCTGGGTCCGCTTCGTGTTCCTCGCTCGCCCC
ACAGGTGGAATTCTCAAGACTTCCAAGGAGGCCGATGCGGAGTCCCTGCAGGCTGCCTGG
TACCCACGGACCTCCCTGCCCACTCCGCTGCGAGCCCATGACATCCTGCACCTGGTTGAA
CTAGCCGCCCAGTATCGCCAGCAAGCCAGGCACCCTCTCATTCTGCCCCAAGAGCTACCC
TGTGATCTGGTCTGCCAGCGGCTCGTGGCTACCTTTACCAGCGCCCAGACAGTGTGGGTG
TTAGTGGGCACAGTGGGGATGCCTCACTTGCCTGTCACTGCCTGTGGCCTCGACCCTGTG
GAGCAGAGGGGTGGCATGAAGATGGCCGTCCTGCGGCTGCTGCAGGAGTGTCTGACCCTG
CACCACTTGGTGGTGGAGATCAAGGGGTTGCTTGGACTGCAGCACCTGGGCCGAGATCAC
AGTGATGGCATCTGTTTGAATGTGCTGGTGACCGTGGCTTTTCGGAGCCCAGGGATCCAG
GATGAACCCCCAAAAGTTCGGGGTGAGAACTTCTCTTGGTGGAAGGTGATGGAGGAAGAC
CTGCAAAGCCAGCTCCTCCAGCGGCTTCAGGGATCCTCTGTTGTCCCAGTGAACAGATAG
Enzyme 21 GenBank Gene ID AK124446 Link Image
Enzyme 21 GeneCard ID Q6ZVK8 Link Image
Enzyme 21 GenAtlas ID NUDT18 Link Image
Enzyme 21 HGNC ID HGNC:26194 Link Image
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 14507
Enzyme 22 Name Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
Enzyme 22 Synonyms
  1. Nudix motif 8
Enzyme 22 Gene Name NUDT8
Enzyme 22 Protein Sequence >Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
MLPDCLSAEGELRCRRLLAGATARLRARPASAAVLVPLCSVRGVPALLYTLRSSRLTGRH
KGDVSFPGGKCDPADQDVVHTALRETREELGLAVPEEHVWGLLRPVYDPQKATVVPVLAG
VGPLDPQSLRPNSEEVDEVFALPLAHLLQTQNQGYTHFCRGGHFRYTLPVFLHGPHRVWG
LTAVITEFALQLLAPGTYQPRLAGLTCSGAEGLARPKQPLASPCQASSTPGLNKGL
Enzyme 22 Number of Residues 236
Enzyme 22 Molecular Weight 25371
Enzyme 22 Theoretical pI 8.50
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Replication, recombination and repair
Enzyme 22 Specific Function Probably mediates the hydrolysis of some nucleoside diphosphate derivatives
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 34529139 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8WV74 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name NUDT8_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >711 bp
ATGCTGCCCGACTGCCTGTCGGCCGAGGGCGAGCTGCGCTGCCGCCGGCTGCTGGCAGGG
GCCACGGCCCGGCTCCGCGCGCGGCCCGCGTCGGCCGCGGTGCTCGTGCCGCTCTGCTCA
GTGCGTGGGGTCCCGGCGCTGCTGTACACGCTGCGGTCCAGCCGCCTGACCGGGAGGCAC
AAGGGCGACGTCAGTTTCCCAGGCGGCAAGTGCGACCCGGCTGACCAAGATGTGGTGCAC
ACGGCCCTGCGGGAAACCCGGGAGGAGCTGGGCCTGGCAGTGCCCGAGGAGCACGTGTGG
GGCCTGCTGCGGCCTGTGTATGATCCGCAAAAGGCCACCGTGGTGCCAGTGCTTGCTGGT
GTAGGCCCACTGGATCCCCAGAGCCTCAGGCCCAACTCGGAGGAGGTAGATGAGGTGTTT
GCACTGCCGCTGGCCCACCTGCTGCAGACGCAGAATCAGGGCTATACCCACTTCTGCCGG
GGTGGCCACTTCCGCTACACACTACCCGTCTTCCTGCATGGACCACACCGGGTCTGGGGC
CTCACAGCTGTCATCACTGAGTTTGCCCTGCAGCTGCTGGCACCTGGTACCTACCAGCCC
CGCCTGGCCGGCCTGACCTGCTCAGGGGCTGAGGGTCTGGCCCGCCCTAAGCAGCCCCTG
GCTTCACCCTGTCAGGCCAGCTCCACTCCAGGACTGAATAAAGGTCTTTGA
Enzyme 22 GenBank Gene ID AK123561 Link Image
Enzyme 22 GeneCard ID Q8WV74 Link Image
Enzyme 22 GenAtlas ID NUDT8 Link Image
Enzyme 22 HGNC ID HGNC:8055 Link Image
Enzyme 22 Chromosome Location 11
Enzyme 22 Locus 11q13.2
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 15191
Enzyme 23 Name cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name NME7
Enzyme 23 Protein Sequence >cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 23 Number of Residues 376
Enzyme 23 Molecular Weight 42492
Enzyme 23 Theoretical pI 6.44
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Nucleotide transport and metabolism
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 158254838 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 23 GenBank Gene ID AK290701 Link Image
Enzyme 23 GeneCard ID A8K3T6 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 15200
Enzyme 24 Name Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name UCK1
Enzyme 24 Protein Sequence >Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 24 Number of Residues 201
Enzyme 24 Molecular Weight 22761
Enzyme 24 Theoretical pI 6.23
Enzyme 24 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 24 General Function Nucleotide transport and metabolism
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 57162360 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 24 GenBank Gene ID AL358781 Link Image
Enzyme 24 GeneCard ID Q5JT13 Link Image
Enzyme 24 GenAtlas ID UCK1 Link Image
Enzyme 24 HGNC ID HGNC:14859 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 16437
Enzyme 25 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name ENTPD3
Enzyme 25 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 25 Number of Residues 529
Enzyme 25 Molecular Weight 59106
Enzyme 25 Theoretical pI 6.40
Enzyme 25 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
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
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AK313322 Link Image
Enzyme 25 GeneCard ID B2R8D0 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
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 17697
Enzyme 26 Name Nucleoside diphosphate kinase
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name NME4
Enzyme 26 Protein Sequence >Nucleoside diphosphate kinase
MKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSA
EAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
Enzyme 26 Number of Residues 117
Enzyme 26 Molecular Weight 12978.5
Enzyme 26 Theoretical pI 6.80
Enzyme 26 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 26 General Function Nucleotide transport and metabolism
Enzyme 26 Specific Function ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 123243687 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A2IDD0 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A2IDD0_HUMAN Link Image
Enzyme 26 PDB ID 1EHW Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >471 bp
ATGGCGCTGAAAGCAAAGAAGGAAGCTCCTGCCTCTCCTGAAGCCGAAGCCAAAGCGAAG
GCTTTAAAGGCCAAGAAGGCAGCGTTGAAAGGTGTCCACAGCCACATAAAAAAGAAGACC
CGCACGTCACTCACCTTCCAGCGGCCCAAGACACTGCGACGCCGGAGGCGGCCTGAATAT
CCTTGGAAGAGCACCCCCAGGAGAAACAAGCTTGGCCACTATGCTGTCATCAAGTTTCCG
CTGACCACGGAGTCGGCCGTGAAGAGGACAGAAGAAAACAACACGCTTTTGTTCACTGTG
GATGTTAAAGCCAACAAGCACCAGATCAAACAGGCTGTGAAGAAGCTCTATGACGGTGAT
GTGGCCGAGGTCACCACCCTGATTCCGCCTGATGGAGAGAAGAAGGCATGTGTTCGACTG
GCTCCTGATTACGATGCGTTGGATGTTGCCAACAAAATTGGGATCATCTAA
Enzyme 26 GenBank Gene ID Z97634 Link Image
Enzyme 26 GeneCard ID NME4 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID HGNC:7852 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 16p13.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available