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Showing Protein Cancer-related nucleoside-triphosphatase (HMDBP10641)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP10641
Secondary Accession Numbers
  • 16871
Name Cancer-related nucleoside-triphosphatase
Synonyms
  1. NTPase
  2. Nucleoside triphosphate phosphohydrolase
Gene Name NTPCR
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
Pathways
  • Purine metabolism
  • Thiamine metabolism
  • Thiamine Metabolism
Reactions
NTP + Water → NDP + Phosphate details
Adenosine triphosphate + Water → ADP + Phosphate details
Thiamine pyrophosphate + Water → Thiamine monophosphate + Phosphate details
GO Classification
Function
binding
nucleotide binding
catalytic activity
hydrolase activity
transferase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
nucleoside-triphosphatase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Molecular Function
nucleotide phosphatase activity
transferase activity
nucleoside-triphosphatase activity
ATP binding
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location 1
Locus 1q42.2
SNPs C1orf57
Gene Sequence 
>573 bp
ATGGCCCGGCACGTGTTCCTAACGGGGCCCCCAGGAGTTGGAAAAACAACATTGATCCAT
AAAGCCAGTGAGGTTTTAAAATCCTCTGGTGTGCCTGTTGATGGATTTTATACCGAAGAA
GTCAGACAGGGAGGGAGAAGAATAGGATTCGATGTCGTCACGTTGTCCGGCACCCGGGGG
CCTTTATCGAGAGTTGGGTTAGAGCCTCCACCTGGAAAACGTGAATGCCGAGTTGGGCAG
TATGTGGTCGACCTGACTTCTTTTGAGCAGTTGGCACTACCCGTCTTGAGGAATGCCGAC
TGCAGCAGTGGCCCAGGGCAAAGAGTGTGCGTCATCGATGAGATTGGGAAGATGGAGCTC
TTCAGTCAGCTTTTCATTCAAGCTGTTCGTCAGACGCTGTCTACCCCAGGGACTATAATC
CTTGGCACAATCCCAGTTCCTAAAGGAAAGCCACTGGCTCTTGTAGAAGAAATCAGAAAC
AGAAAGGATGTGAAGGTGTTTAATGTCACCAAGGAAAACAGAAACCACCTTCTGCCAGAT
ATCGTGACGTGCGTGCAGAGCAGCAGGAAGTGA
Protein Properties
Number of Residues 190
Molecular Weight 20712.935
Theoretical pI 9.535
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Nucleoside-triphosphatase C1orf57
MARHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTLSGTRG
PLSRVGLEPPPGKRECRVGQYVVDLTSFEQLALPVLRNADCSSGPGQRVCVIDEIGKMEL
FSQLFIQAVRQTLSTPGTIILGTIPVPKGKPLALVEEIRNRKDVKVFNVTKENRNHLLPD
IVTCVQSSRK
GenBank ID Protein 16303796
UniProtKB/Swiss-Prot ID Q9BSD7
UniProtKB/Swiss-Prot Entry Name CA057_HUMAN
PDB IDs
GenBank Gene ID AF416713
GeneCard ID C1orf57
GenAtlas ID C1orf57
HGNC ID HGNC:28204
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Placzek WJ, Almeida MS, Wuthrich K: NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase. J Mol Biol. 2007 Mar 30;367(3):788-801. Epub 2007 Jan 9. [PubMed:17291528 ]