|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5338 |
| Enzyme 1 Name |
Nucleoside diphosphate kinase, mitochondrial precursor |
| Enzyme 1 Synonyms |
- NDP kinase, mitochondrial
- NDK
- nm23-H4
- Nucleoside diphosphate kinase D
- NDPKD
|
| Enzyme 1 Gene Name |
NME4 |
| Enzyme 1 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 1 Number of Residues |
187 |
| Enzyme 1 Molecular Weight |
20659 |
| Enzyme 1 Theoretical pI |
10.75 |
| Enzyme 1 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 1 General Function |
Nucleotide transport and metabolism |
| Enzyme 1 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1945762  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O00746  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN  |
| Enzyme 1 PDB ID |
1EHW  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 1 GenBank Gene ID |
Y07604  |
| Enzyme 1 GeneCard ID |
NME4  |
| Enzyme 1 GenAtlas ID |
NME4  |
| Enzyme 1 HGNC ID |
HGNC:7852  |
| Enzyme 1 Chromosome Location |
16 |
| Enzyme 1 Locus |
16p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5341 |
| Enzyme 2 Name |
Nucleoside diphosphate kinase A |
| Enzyme 2 Synonyms |
- NDK A
- NDP kinase A
- Tumor metastatic process-associated protein
- Metastasis inhibition factor nm23
- nm23-H1
- Granzyme A-activated DNase
- GAAD
|
| Enzyme 2 Gene Name |
NME1 |
| Enzyme 2 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 2 Number of Residues |
152 |
| Enzyme 2 Molecular Weight |
17149 |
| Enzyme 2 Theoretical pI |
6.11 |
| Enzyme 2 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 2 General Function |
Nucleotide transport and metabolism |
| Enzyme 2 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
35068  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P15531  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN  |
| Enzyme 2 PDB ID |
1JXV  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
|
| Enzyme 2 GenBank Gene ID |
X17620  |
| Enzyme 2 GeneCard ID |
NME1  |
| Enzyme 2 GenAtlas ID |
NME1  |
| Enzyme 2 HGNC ID |
HGNC:7849  |
| Enzyme 2 Chromosome Location |
17 |
| Enzyme 2 Locus |
17q21.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5344 |
| Enzyme 3 Name |
Nucleoside diphosphate kinase B |
| Enzyme 3 Synonyms |
- NDK B
- NDP kinase B
- nm23-H2
- C-myc purine-binding transcription factor PUF
|
| Enzyme 3 Gene Name |
NME2 |
| Enzyme 3 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 3 Number of Residues |
152 |
| Enzyme 3 Molecular Weight |
17298 |
| Enzyme 3 Theoretical pI |
8.69 |
| Enzyme 3 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 3 General Function |
Nucleotide transport and metabolism |
| Enzyme 3 Specific Function |
Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
4467843  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22392  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN  |
| Enzyme 3 PDB ID |
1NSK  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 3 GenBank Gene ID |
X58965  |
| Enzyme 3 GeneCard ID |
NME2  |
| Enzyme 3 GenAtlas ID |
NME2  |
| Enzyme 3 HGNC ID |
HGNC:7850  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5346 |
| Enzyme 4 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 4 Synonyms |
- NDK 6
- NDP kinase 6
- nm23-H6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
|
| Enzyme 4 Gene Name |
NME6 |
| Enzyme 4 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 4 Number of Residues |
186 |
| Enzyme 4 Molecular Weight |
21142 |
| Enzyme 4 Theoretical pI |
8.49 |
| 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. 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 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 |
3228530  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O75414  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 4 GenBank Gene ID |
AF051941  |
| Enzyme 4 GeneCard ID |
NME6  |
| Enzyme 4 GenAtlas ID |
NME6  |
| Enzyme 4 HGNC ID |
HGNC:20567  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5668 |
| Enzyme 5 Name |
Inosine triphosphate pyrophosphatase |
| Enzyme 5 Synonyms |
- ITPase
- Inosine triphosphatase
- Putative oncogene protein hlc14-06-p
|
| Enzyme 5 Gene Name |
ITPA |
| Enzyme 5 Protein Sequence |
>Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
|
| Enzyme 5 Number of Residues |
194 |
| Enzyme 5 Molecular Weight |
21446 |
| Enzyme 5 Theoretical pI |
5.34 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Nucleotide transport and metabolism |
| Enzyme 5 Specific Function |
Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- A nucleoside triphosphate + H2O = a nucleotide + diphosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
13398328  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9BY32  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ITPA_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
|
| Enzyme 5 GenBank Gene ID |
AF219116  |
| Enzyme 5 GeneCard ID |
ITPA  |
| Enzyme 5 GenAtlas ID |
ITPA  |
| Enzyme 5 HGNC ID |
HGNC:6176  |
| Enzyme 5 Chromosome Location |
20 |
| Enzyme 5 Locus |
20p |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [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
]
- Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed
]
- Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5669 |
| Enzyme 6 Name |
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial precursor |
| Enzyme 6 Synonyms |
- dUTPase
- dUTP pyrophosphatase
|
| Enzyme 6 Gene Name |
DUT |
| Enzyme 6 Protein Sequence |
>Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial precursor
MTPLCPRPALCYHFLTSLLRSAMQNARGTAEGRSRGTLRARPAPRPPAAQHGIPRPLSSA
GRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLS
EHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKH
FIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTE
RGSGGFGSTGKN
|
| Enzyme 6 Number of Residues |
252 |
| Enzyme 6 Molecular Weight |
26707 |
| Enzyme 6 Theoretical pI |
10.01 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
- cellular metabolism
- dUTP metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine deoxyribonucleoside triphosphate metabolism
- pyrimidine nucleoside triphosphate metabolism
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 6 General Function |
Nucleotide transport and metabolism |
| Enzyme 6 Specific Function |
This enzyme is involved in nucleotide metabolism:it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- dUTP + H2O = dUMP + diphosphate
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
2443580  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P33316  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
DUT_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>759 bp
ATGACTCCCCTCTGCCCTCGCCCCGCGCTCTGCTACCATTTCCTTACGTCTCTGCTTCGC
TCAGCGATGCAAAACGCGCGAGGCACGGCAGAGGGCCGAAGCCGCGGTACTCTCCGGGCC
AGGCCCGCCCCTCGGCCGCCGGCCGCGCAGCACGGGATTCCCCGGCCGCTGTCCAGCGCT
GGCCGCCTGAGCCAAGGCTGCCGCGGAGCCAGTACAGTCGGGGCCGCTGGCTGGAAGGGC
GAGCTTCCTAAGGCGGGGGGAAGCCCGGCGCCGGGGCCGGAGACACCCGCCATTTCACCC
AGTAAGCGGGCCCGGCCTGCGGAGGTGGGCGGCATGCAGCTCCGCTTTGCCCGGCTCTCC
GAGCACGCCACGGCCCCCACCCGGGGCTCCGCGCGCGCCGCGGGCTACGACCTGTACAGT
GCCTATGATTACACAATACCACCTATGGAGAAAGCTGTTGTGAAAACGGACATTCAGATA
GCGCTCCCTTCTGGGTGTTATGGAAGAGTGGCTCCACGGTCAGGCTTGGCTGCAAAACAC
TTTATTGATGTAGGAGCTGGTGTCATAGATGAAGATTATAGAGGAAATGTTGGTGTTGTA
CTGTTTAATTTTGGCAAAGAAAAGTTTGAAGTCAAAAAAGGTGATCGAATTGCACAGCTC
ATTTGCGAACGGATTTTTTATCCAGAAATAGAAGAAGTTCAAGCCTTGGATGACACCGAA
AGGGGTTCAGGAGGTTTTGGTTCCACTGGAAAGAATTAA
|
| Enzyme 6 GenBank Gene ID |
AF018432  |
| Enzyme 6 GeneCard ID |
DUT  |
| Enzyme 6 GenAtlas ID |
DUT  |
| Enzyme 6 HGNC ID |
HGNC:3078  |
| Enzyme 6 Chromosome Location |
15 |
| Enzyme 6 Locus |
15q15-q21.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Ladner RD, McNulty DE, Carr SA, Roberts GD, Caradonna SJ: Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase. J Biol Chem. 1996 Mar 29;271(13):7745-51. [PubMed
]
- McIntosh EM, Ager DD, Gadsden MH, Haynes RH: Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8020-4. [PubMed
]
- Strahler JR, Zhu XX, Hora N, Wang YK, Andrews PC, Roseman NA, Neel JV, Turka L, Hanash SM: Maturation stage and proliferation-dependent expression of dUTPase in human T cells. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4991-5. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
8075 |
| Enzyme 7 Name |
Uridine-cytidine kinase 2 |
| Enzyme 7 Synonyms |
- UCK 2
- Uridine monophosphokinase 2
- Cytidine monophosphokinase 2
|
| Enzyme 7 Gene Name |
UCK2 |
| Enzyme 7 Protein Sequence |
>Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
|
| Enzyme 7 Number of Residues |
261 |
| Enzyme 7 Molecular Weight |
29299 |
| Enzyme 7 Theoretical pI |
6.68 |
| Enzyme 7 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 7 General Function |
Nucleotide transport and metabolism |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + uridine = ADP + UMP
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
1655420  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9BZX2  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
UCK2_HUMAN  |
| Enzyme 7 PDB ID |
1XRJ  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>336 bp
ATGAAGCTTTTTGTGGATACAGATGCGGACACCCGGCTCTCACGCAGAGTATTAAGGGAC
ATCAGCGAGAGAGGCAGGGATCTTGAGCAGATTTTATCTCAGTACATTACGTTCGTCAAG
CCTGCCTTTGAGGAATTCTGCTTGCCAACAAAGCAGTATGCTGATGTGATCATCCCTAGA
GGTGCAGATAATCTGGTGGCCATCAACCTCATCGAGCAGCACATCCAGGACATCCTGAAT
GGAGGGCCCTCCAAACGGCAGACCAATGGCTGTCTCAACGGCTACACCCCTTCACGCAAG
AGGCAGGCATCGGAGTCCAGCAGCAGGCCGCATTGA
|
| Enzyme 7 GenBank Gene ID |
D78335  |
| Enzyme 7 GeneCard ID |
UCK2  |
| Enzyme 7 GenAtlas ID |
UCK2  |
| Enzyme 7 HGNC ID |
HGNC:12562  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1q23 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
13098 |
| Enzyme 8 Name |
Uridine/cytidine kinase-like 1 |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
UCKL1 |
| Enzyme 8 Protein Sequence |
>Uridine/cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
|
| Enzyme 8 Number of Residues |
548 |
| Enzyme 8 Molecular Weight |
61142 |
| Enzyme 8 Theoretical pI |
7.40 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- uridine kinase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Nucleotide transport and metabolism |
| Enzyme 8 Specific Function |
May contribute to UTP accumulation needed for blast transformation and proliferation |
| Enzyme 8 Pathways |
|
| Enzyme 8 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 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
38228699  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9NWZ5  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
UCKL1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
AJ605558  |
| Enzyme 8 GeneCard ID |
Q9NWZ5  |
| Enzyme 8 GenAtlas ID |
UCKL1  |
| Enzyme 8 HGNC ID |
HGNC:15938  |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
13099 |
| Enzyme 9 Name |
DUTP pyrophosphatase |
| Enzyme 9 Synonyms |
- DUTP pyrophosphatase, isoform CRA_b
|
| Enzyme 9 Gene Name |
DUT |
| Enzyme 9 Protein Sequence |
>DUTP pyrophosphatase
MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSA
GRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLS
EHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKH
FIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTE
RGSGGFGSTGKN
|
| Enzyme 9 Number of Residues |
252 |
| Enzyme 9 Molecular Weight |
26564 |
| Enzyme 9 Theoretical pI |
9.74 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
- cellular metabolism
- dUTP metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine deoxyribonucleoside triphosphate metabolism
- pyrimidine nucleoside triphosphate metabolism
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 9 General Function |
Nucleotide transport and metabolism |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
47123503  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q6NSA3  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
Q6NSA3_HUMAN  |
| Enzyme 9 PDB ID |
1Q5U  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
BC070339  |
| Enzyme 9 GeneCard ID |
Q6NSA3  |
| Enzyme 9 GenAtlas ID |
DUT  |
| Enzyme 9 HGNC ID |
HGNC:3078  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
15191 |
| Enzyme 10 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 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
NME7 |
| Enzyme 10 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 10 Number of Residues |
376 |
| Enzyme 10 Molecular Weight |
42492 |
| Enzyme 10 Theoretical pI |
6.44 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
Not Available |
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
158254838  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
A8K3T6  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
A8K3T6_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 10 GenBank Gene ID |
AK290701  |
| Enzyme 10 GeneCard ID |
A8K3T6  |
| Enzyme 10 GenAtlas ID |
Not Available |
| Enzyme 10 HGNC ID |
Not Available |
| Enzyme 10 Chromosome Location |
Not Available |
| Enzyme 10 Locus |
Not Available |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
15200 |
| Enzyme 11 Name |
Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e) |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
UCK1 |
| Enzyme 11 Protein Sequence |
>Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
|
| Enzyme 11 Number of Residues |
201 |
| Enzyme 11 Molecular Weight |
22761 |
| Enzyme 11 Theoretical pI |
6.23 |
| Enzyme 11 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 11 General Function |
Nucleotide transport and metabolism |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
57162360  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q5JT13  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
Q5JT13_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>807 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGTCGACCGTGTGTGAGAAGATCATGGAGTTGCTGGGACAG
AACGAGGTGGAACAGCGGCAGCGGAAGGTGGTCATCCTGAGCCAGGACAGGTTCTACAAG
GTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTGAAAGGACAGTACAATTTTGACCATCCA
GATGCCTTTGATAATGATTTGATGCACAGGACTCTGAAGAACATCGTGGAGGGCAAAACG
GTGGAGGTGCCGACCTATGATTTTGTGACACACTCAAGGTTACCAGAGACCACGGTGGTC
TACCCTGCGGACGTGGTTCTGTTTGAGGGCATCTTGGTGTTCTACAGCCAGGAGATCCGG
GACATGTTCCACCTGCGCCTCTTCGTGGACACCGACTCCGACGTCAGGCTGTCTCGAAGA
GTTCTCCGGGACGTGCGCCGAGGGAGGGACCTGGAGCAGATTCTGACGCAGTACACCACC
TTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTGCCGACAAAGAAGTATGCCGATGTGATC
ATCCCGCGAGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGAC
ATTCTGAATGGTGACATCTGCAAATGGCACCGAGGAGGGTCCAATGGGCGGAGCTACAAG
CGGACCTTTTCTGAGCCAGGGGACCACCCTGGGATGCTGACCTCTGGCAAACGGTCACAT
TTGGAGTCCAGCAGCAGACCCCACTGA
|
| Enzyme 11 GenBank Gene ID |
AL358781  |
| Enzyme 11 GeneCard ID |
Q5JT13  |
| Enzyme 11 GenAtlas ID |
UCK1  |
| Enzyme 11 HGNC ID |
HGNC:14859  |
| Enzyme 11 Chromosome Location |
Not Available |
| Enzyme 11 Locus |
Not Available |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
Not Available |
| Enzyme 11 Metabolite References |
Not Available |