NTPCR_HUMAN
ID NTPCR_HUMAN Reviewed; 190 AA.
AC Q9BSD7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cancer-related nucleoside-triphosphatase {ECO:0000305};
DE Short=NTPase;
DE EC=3.6.1.15 {ECO:0000269|PubMed:17291528};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase;
GN Name=NTPCR {ECO:0000312|HGNC:HGNC:28204}; Synonyms=C1orf57;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Kang L., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7]
RP STRUCTURE BY NMR IN COMPLEX WITH THE ATP ANALOG ADENOSINE
RP 5'-O-(3-THIOTRIPHOSPHATE), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, MUTAGENESIS OF GLU-114 AND GLY-116, AND CATALYTIC ACTIVITY.
RX PubMed=17291528; DOI=10.1016/j.jmb.2007.01.001;
RA Placzek W.J., Almeida M.S., Wuethrich K.;
RT "NMR structure and functional characterization of a human cancer-related
RT nucleoside triphosphatase.";
RL J. Mol. Biol. 367:788-801(2007).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
CC {ECO:0000269|PubMed:17291528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000269|PubMed:17291528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000305|PubMed:17291528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = H(+) + phosphate + TDP; Xref=Rhea:RHEA:65580,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61417, ChEBI:CHEBI:63527;
CC Evidence={ECO:0000269|PubMed:17291528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65581;
CC Evidence={ECO:0000305|PubMed:17291528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000269|PubMed:17291528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC Evidence={ECO:0000305|PubMed:17291528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17291528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:17291528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:17291528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:17291528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for ATP {ECO:0000269|PubMed:17291528};
CC KM=46 uM for ADP {ECO:0000269|PubMed:17291528};
CC KM=4 uM for GTP {ECO:0000269|PubMed:17291528};
CC KM=6 uM for CTP {ECO:0000269|PubMed:17291528};
CC KM=7 uM for TTP {ECO:0000269|PubMed:17291528};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17291528}.
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000305}.
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DR EMBL; AF416713; AAL16807.1; -; mRNA.
DR EMBL; BC005102; AAH05102.1; -; mRNA.
DR CCDS; CCDS1597.1; -.
DR RefSeq; NP_001316382.1; NM_001329453.1.
DR RefSeq; NP_115700.1; NM_032324.2.
DR PDB; 2I3B; NMR; -; A=2-190.
DR PDBsum; 2I3B; -.
DR AlphaFoldDB; Q9BSD7; -.
DR BMRB; Q9BSD7; -.
DR SMR; Q9BSD7; -.
DR BioGRID; 124011; 104.
DR IntAct; Q9BSD7; 41.
DR MINT; Q9BSD7; -.
DR STRING; 9606.ENSP00000355587; -.
DR ChEMBL; CHEMBL4295936; -.
DR GlyGen; Q9BSD7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BSD7; -.
DR PhosphoSitePlus; Q9BSD7; -.
DR BioMuta; NTPCR; -.
DR DMDM; 54036528; -.
DR EPD; Q9BSD7; -.
DR jPOST; Q9BSD7; -.
DR MassIVE; Q9BSD7; -.
DR MaxQB; Q9BSD7; -.
DR PaxDb; Q9BSD7; -.
DR PeptideAtlas; Q9BSD7; -.
DR PRIDE; Q9BSD7; -.
DR ProteomicsDB; 78879; -.
DR Antibodypedia; 34690; 155 antibodies from 27 providers.
DR DNASU; 84284; -.
DR Ensembl; ENST00000366628.10; ENSP00000355587.4; ENSG00000135778.12.
DR GeneID; 84284; -.
DR KEGG; hsa:84284; -.
DR MANE-Select; ENST00000366628.10; ENSP00000355587.4; NM_032324.3; NP_115700.1.
DR UCSC; uc001hvj.2; human.
DR CTD; 84284; -.
DR DisGeNET; 84284; -.
DR GeneCards; NTPCR; -.
DR HGNC; HGNC:28204; NTPCR.
DR HPA; ENSG00000135778; Low tissue specificity.
DR neXtProt; NX_Q9BSD7; -.
DR OpenTargets; ENSG00000135778; -.
DR PharmGKB; PA142672508; -.
DR VEuPathDB; HostDB:ENSG00000135778; -.
DR eggNOG; ENOG502QVJ8; Eukaryota.
DR GeneTree; ENSGT00390000018683; -.
DR HOGENOM; CLU_103145_1_0_1; -.
DR InParanoid; Q9BSD7; -.
DR OMA; GAMEFKC; -.
DR OrthoDB; 1401569at2759; -.
DR PhylomeDB; Q9BSD7; -.
DR TreeFam; TF323592; -.
DR BioCyc; MetaCyc:HS06064-MON; -.
DR PathwayCommons; Q9BSD7; -.
DR SABIO-RK; Q9BSD7; -.
DR SignaLink; Q9BSD7; -.
DR BioGRID-ORCS; 84284; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; NTPCR; human.
DR EvolutionaryTrace; Q9BSD7; -.
DR GenomeRNAi; 84284; -.
DR Pharos; Q9BSD7; Tbio.
DR PRO; PR:Q9BSD7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BSD7; protein.
DR Bgee; ENSG00000135778; Expressed in pancreatic ductal cell and 180 other tissues.
DR ExpressionAtlas; Q9BSD7; baseline and differential.
DR Genevisible; Q9BSD7; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..190
FT /note="Cancer-related nucleoside-triphosphatase"
FT /id="PRO_0000146711"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 106
FT /note="G -> E (in dbSNP:rs12123482)"
FT /id="VAR_053071"
FT MUTAGEN 114
FT /note="E->T: Reduced activity, especially towards ATP, GTP
FT and TTP."
FT /evidence="ECO:0000269|PubMed:17291528"
FT MUTAGEN 116
FT /note="G->H: Reduced activity, especially towards ATP, GTP
FT and TTP."
FT /evidence="ECO:0000269|PubMed:17291528"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2I3B"
FT TURN 90..96
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2I3B"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:2I3B"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2I3B"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:2I3B"
SQ SEQUENCE 190 AA; 20713 MW; B4B753F95796A210 CRC64;
MARHVFLTGP PGVGKTTLIH KASEVLKSSG VPVDGFYTEE VRQGGRRIGF DVVTLSGTRG
PLSRVGLEPP PGKRECRVGQ YVVDLTSFEQ LALPVLRNAD CSSGPGQRVC VIDEIGKMEL
FSQLFIQAVR QTLSTPGTII LGTIPVPKGK PLALVEEIRN RKDVKVFNVT KENRNHLLPD
IVTCVQSSRK
