|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5312 |
| Enzyme 1 Name |
Thymidylate kinase |
| Enzyme 1 Synonyms |
- 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 |
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
37206  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P23919  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DTYMK_HUMAN  |
| Enzyme 1 PDB ID |
1E9A  |
| 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  |
| Enzyme 1 GeneCard ID |
DTYMK  |
| Enzyme 1 GenAtlas ID |
DTYMK  |
| Enzyme 1 HGNC ID |
HGNC:3061  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2q37.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5313 |
| Enzyme 2 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 2 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase
- ATPDase
- Lymphoid cell activation antigen
- Ecto-apyrase
- 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
765256  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
ENTPD1  |
| Enzyme 2 GenAtlas ID |
ENTPD1  |
| Enzyme 2 HGNC ID |
HGNC:3363  |
| Enzyme 2 Chromosome Location |
10 |
| Enzyme 2 Locus |
10q24 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5314 |
| Enzyme 3 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 3 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative NF-kappa-B-activating protein 107
- 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 |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
22218108  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 3 PDB ID |
1S1D  |
| 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  |
| Enzyme 3 GeneCard ID |
CANT1  |
| Enzyme 3 GenAtlas ID |
CANT1  |
| Enzyme 3 HGNC ID |
HGNC:19721  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q25.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5338 |
| Enzyme 4 Name |
Nucleoside diphosphate kinase, mitochondrial precursor |
| Enzyme 4 Synonyms |
- NDP kinase, mitochondrial
- NDK
- nm23-H4
- Nucleoside diphosphate kinase D
- 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 |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
1945762  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 4 PDB ID |
1EHW  |
| 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  |
| Enzyme 4 GeneCard ID |
NME4  |
| Enzyme 4 GenAtlas ID |
NME4  |
| Enzyme 4 HGNC ID |
HGNC:7852  |
| Enzyme 4 Chromosome Location |
16 |
| Enzyme 4 Locus |
16p13.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5341 |
| Enzyme 5 Name |
Nucleoside diphosphate kinase A |
| Enzyme 5 Synonyms |
- NDK A
- NDP kinase A
- Tumor metastatic process-associated protein
- Metastasis inhibition factor nm23
- nm23-H1
- Granzyme A-activated DNase
- 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 |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
35068  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 5 PDB ID |
1JXV  |
| 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  |
| Enzyme 5 GeneCard ID |
NME1  |
| Enzyme 5 GenAtlas ID |
NME1  |
| Enzyme 5 HGNC ID |
HGNC:7849  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17q21.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5342 |
| Enzyme 6 Name |
Nucleoside diphosphate kinase 7 |
| Enzyme 6 Synonyms |
- NDK 7
- NDP kinase 7
- 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 |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
4960169  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9Y5B8  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
NDK7_HUMAN  |
| 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  |
| Enzyme 6 GeneCard ID |
NME7  |
| Enzyme 6 GenAtlas ID |
NME7  |
| Enzyme 6 HGNC ID |
HGNC:20461  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
1q24 |
| Enzyme 6 SNPs |
SNPJam Report  |
| 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 |
- NDK B
- NDP kinase B
- nm23-H2
- 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 |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
4467843  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 7 PDB ID |
1NSK  |
| 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  |
| Enzyme 7 GeneCard ID |
NME2  |
| Enzyme 7 GenAtlas ID |
NME2  |
| Enzyme 7 HGNC ID |
HGNC:7850  |
| Enzyme 7 Chromosome Location |
17 |
| Enzyme 7 Locus |
17q21.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5345 |
| Enzyme 8 Name |
Nucleoside diphosphate kinase 3 |
| Enzyme 8 Synonyms |
- NDK 3
- NDP kinase 3
- Nucleoside diphosphate kinase C
- NDPKC
- nm23-H3
- 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 |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
1051256  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q13232  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NDK3_HUMAN  |
| 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  |
| Enzyme 8 GeneCard ID |
NME3  |
| Enzyme 8 GenAtlas ID |
NME3  |
| Enzyme 8 HGNC ID |
HGNC:7851  |
| Enzyme 8 Chromosome Location |
16 |
| Enzyme 8 Locus |
16q13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5346 |
| Enzyme 9 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 9 Synonyms |
- NDK 6
- NDP kinase 6
- nm23-H6
- Inhibitor of p53-induced apoptosis-alpha
- 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 |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
3228530  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| 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  |
| Enzyme 9 GeneCard ID |
NME6  |
| Enzyme 9 GenAtlas ID |
NME6  |
| Enzyme 9 HGNC ID |
HGNC:20567  |
| Enzyme 9 Chromosome Location |
3 |
| Enzyme 9 Locus |
3p21 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6159 |
| Enzyme 10 Name |
Ectonucleoside triphosphate diphosphohydrolase 4 |
| Enzyme 10 Synonyms |
- NTPDase 4
- Uridine-diphosphatase
- UDPase
- 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 |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
3153211  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9Y227  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ENTP4_HUMAN  |
| 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  |
| Enzyme 10 GeneCard ID |
ENTPD4  |
| Enzyme 10 GenAtlas ID |
ENTPD4  |
| Enzyme 10 HGNC ID |
HGNC:14573  |
| Enzyme 10 Chromosome Location |
8 |
| Enzyme 10 Locus |
8p21.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6160 |
| Enzyme 11 Name |
Ectonucleoside triphosphate diphosphohydrolase 6 |
| Enzyme 11 Synonyms |
- NTPDase 6
- 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 |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
3335098  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O75354  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
ENTP6_HUMAN  |
| 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  |
| Enzyme 11 GeneCard ID |
ENTPD6  |
| Enzyme 11 GenAtlas ID |
ENTPD6  |
| Enzyme 11 HGNC ID |
HGNC:3368  |
| Enzyme 11 Chromosome Location |
20 |
| Enzyme 11 Locus |
20p11.2-p11.22 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6161 |
| Enzyme 12 Name |
Ectonucleoside triphosphate diphosphohydrolase 5 precursor |
| Enzyme 12 Synonyms |
- NTPDase 5
- Nucleoside diphosphatase
- CD39 antigen-like 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 |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
3335102  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O75356  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
ENTP5_HUMAN  |
| 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  |
| Enzyme 12 GeneCard ID |
ENTPD5  |
| Enzyme 12 GenAtlas ID |
ENTPD5  |
| Enzyme 12 HGNC ID |
HGNC:3367  |
| Enzyme 12 Chromosome Location |
14 |
| Enzyme 12 Locus |
14q24 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
|
| 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
)
- Nucleotide Sugars Metabolism (map00520
)
- Polyketide sugar unit biosynthesis (map00523
)
- Streptomycin biosynthesis (map00521
)
|
| Enzyme 13 Reactions |
- dTDP-glucose = dTDP-4-dehydro-6-deoxy-D-glucose + H2O
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
4128133  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O95455  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
TGDS_HUMAN  |
| 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  |
| Enzyme 13 GeneCard ID |
TGDS  |
| Enzyme 13 GenAtlas ID |
TGDS  |
| Enzyme 13 HGNC ID |
HGNC:20324  |
| Enzyme 13 Chromosome Location |
13 |
| Enzyme 13 Locus |
13q32.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| 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 |
- PNPase 1
- Polynucleotide phosphorylase-like protein
- PNPase old-35
- 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 |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
20372922  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q8TCS8  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PNPT1_HUMAN  |
| 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  |
| Enzyme 14 GeneCard ID |
PNPT1  |
| Enzyme 14 GenAtlas ID |
PNPT1  |
| Enzyme 14 HGNC ID |
HGNC:23166  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2p15 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
8075 |
| Enzyme 15 Name |
Uridine-cytidine kinase 2 |
| Enzyme 15 Synonyms |
- UCK 2
- Uridine monophosphokinase 2
- 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 |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
1655420  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 15 PDB ID |
1XRJ  |
| 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  |
| Enzyme 15 GeneCard ID |
UCK2  |
| Enzyme 15 GenAtlas ID |
UCK2  |
| Enzyme 15 HGNC ID |
HGNC:12562  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1q23 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- 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
]
- 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
]
- 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
]
|
| 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 |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
38228699  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
AJ605558  |
| Enzyme 16 GeneCard ID |
Q9NWZ5  |
| Enzyme 16 GenAtlas ID |
UCKL1  |
| Enzyme 16 HGNC ID |
HGNC:15938  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
13379 |
| Enzyme 17 Name |
Ectonucleoside triphosphate diphosphohydrolase 8 |
| Enzyme 17 Synonyms |
- NTPDase 8
- NTPDase8
- 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 |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
59003409  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q5MY95  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
ENTP8_HUMAN  |
| 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  |
| Enzyme 17 GeneCard ID |
Q5MY95  |
| Enzyme 17 GenAtlas ID |
ENTPD8  |
| Enzyme 17 HGNC ID |
HGNC:24860  |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- 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
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
14489 |
| Enzyme 18 Name |
Putative nucleoside diphosphate kinase |
| Enzyme 18 Synonyms |
- NDK
- 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 |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
2935619  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O60361  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
NDK8_HUMAN  |
| Enzyme 18 PDB ID |
1NSK  |
| 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  |
| Enzyme 18 GeneCard ID |
O60361  |
| Enzyme 18 GenAtlas ID |
NME2P1  |
| Enzyme 18 HGNC ID |
HGNC:31358  |
| Enzyme 18 Chromosome Location |
12 |
| Enzyme 18 Locus |
12q24.31 |
| Enzyme 18 SNPs |
SNPJam Report  |
| 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 |
- 8-oxo-dGTPase NUDT15
- Nucleoside diphosphate-linked moiety X motif 15
- 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 |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
7023325  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NV35  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
NUD15_HUMAN  |
| 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  |
| Enzyme 19 GeneCard ID |
Q9NV35  |
| Enzyme 19 GenAtlas ID |
NUDT15  |
| Enzyme 19 HGNC ID |
HGNC:23063  |
| Enzyme 19 Chromosome Location |
13 |
| Enzyme 19 Locus |
13q14.2 |
| Enzyme 19 SNPs |
SNPJam Report  |
| 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 |
- 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 |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P0C025  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
NUD17_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AL160282  |
| Enzyme 20 GeneCard ID |
P0C025  |
| Enzyme 20 GenAtlas ID |
NUDT17  |
| Enzyme 20 HGNC ID |
HGNC:26618  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| 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 |
- 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 |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
34530231  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q6ZVK8  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
Q6ZVK8_HUMAN  |
| 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  |
| Enzyme 21 GeneCard ID |
Q6ZVK8  |
| Enzyme 21 GenAtlas ID |
NUDT18  |
| Enzyme 21 HGNC ID |
HGNC:26194  |
| 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 |
- 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 |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
34529139  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q8WV74  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
NUDT8_HUMAN  |
| 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  |
| Enzyme 22 GeneCard ID |
Q8WV74  |
| Enzyme 22 GenAtlas ID |
NUDT8  |
| Enzyme 22 HGNC ID |
HGNC:8055  |
| Enzyme 22 Chromosome Location |
11 |
| Enzyme 22 Locus |
11q13.2 |
| Enzyme 22 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
158254838  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| 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  |
| Enzyme 23 GeneCard ID |
A8K3T6  |
| 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  |
| 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 |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
57162360  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| 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  |
| Enzyme 24 GeneCard ID |
Q5JT13  |
| Enzyme 24 GenAtlas ID |
UCK1  |
| Enzyme 24 HGNC ID |
HGNC:14859  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| 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 |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
B2R8D0  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
B2R8D0_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AK313322  |
| Enzyme 25 GeneCard ID |
B2R8D0  |
| 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  |
| 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 |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
123243687  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A2IDD0  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A2IDD0_HUMAN  |
| Enzyme 26 PDB ID |
1EHW  |
| 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  |
| Enzyme 26 GeneCard ID |
NME4  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
HGNC:7852  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
16p13.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |