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Protein

Cancer-related nucleoside-triphosphatase

Gene

NTPCR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.1 Publication

Catalytic activityi

NTP + H2O = NDP + phosphate.

Kineticsi

  1. KM=5 µM for ATP1 Publication
  2. KM=46 µM for ADP1 Publication
  3. KM=4 µM for GTP1 Publication
  4. KM=6 µM for CTP1 Publication
  5. KM=7 µM for TTP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 168ATPCurated
    Nucleotide bindingi109 – 1168ATPCurated

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06064-MONOMER.
    SABIO-RKQ9BSD7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cancer-related nucleoside-triphosphatase (EC:3.6.1.15)
    Short name:
    NTPase
    Alternative name(s):
    Nucleoside triphosphate phosphohydrolase
    Gene namesi
    Name:NTPCR
    Synonyms:C1orf57
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28204. NTPCR.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141E → T: Reduced activity, especially towards ATP, GTP and TTP. 1 Publication
    Mutagenesisi116 – 1161G → H: Reduced activity, especially towards ATP, GTP and TTP. 1 Publication

    Organism-specific databases

    PharmGKBiPA142672508.

    Polymorphism and mutation databases

    BioMutaiNTPCR.
    DMDMi54036528.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 190189Cancer-related nucleoside-triphosphatasePRO_0000146711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCombined sources
    Modified residuei165 – 1651N6-acetyllysineCombined sources

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ9BSD7.
    MaxQBiQ9BSD7.
    PaxDbiQ9BSD7.
    PeptideAtlasiQ9BSD7.
    PRIDEiQ9BSD7.

    PTM databases

    iPTMnetiQ9BSD7.
    PhosphoSiteiQ9BSD7.

    Expressioni

    Gene expression databases

    BgeeiQ9BSD7.
    CleanExiHS_C1orf57.
    ExpressionAtlasiQ9BSD7. baseline and differential.
    GenevisibleiQ9BSD7. HS.

    Organism-specific databases

    HPAiHPA028125.
    HPA054304.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi124011. 19 interactions.
    IntActiQ9BSD7. 10 interactions.
    STRINGi9606.ENSP00000355587.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95Combined sources
    Helixi15 – 2814Combined sources
    Beta strandi34 – 374Combined sources
    Beta strandi40 – 423Combined sources
    Beta strandi45 – 5410Combined sources
    Beta strandi59 – 646Combined sources
    Beta strandi71 – 733Combined sources
    Beta strandi76 – 838Combined sources
    Helixi85 – 895Combined sources
    Turni90 – 967Combined sources
    Beta strandi110 – 1123Combined sources
    Turni117 – 1215Combined sources
    Helixi124 – 13411Combined sources
    Beta strandi140 – 1434Combined sources
    Helixi155 – 1595Combined sources
    Beta strandi164 – 1685Combined sources
    Beta strandi171 – 1733Combined sources
    Helixi174 – 1763Combined sources
    Helixi177 – 1859Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I3BNMR-A2-190[»]
    ProteinModelPortaliQ9BSD7.
    SMRiQ9BSD7. Positions 2-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BSD7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the THEP1 NTPase family.Curated

    Phylogenomic databases

    eggNOGiENOG410IXTM. Eukaryota.
    COG1618. LUCA.
    GeneTreeiENSGT00390000018683.
    HOVERGENiHBG058637.
    InParanoidiQ9BSD7.
    KOiK06928.
    OMAiVHKICSA.
    OrthoDBiEOG7WT42C.
    PhylomeDBiQ9BSD7.
    TreeFamiTF323592.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00796. NTPase_1.
    InterProiIPR003593. AAA+_ATPase.
    IPR004948. Nuc-triphosphatase_THEP1.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF03266. NTPase_1. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BSD7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MARHVFLTGP PGVGKTTLIH KASEVLKSSG VPVDGFYTEE VRQGGRRIGF
    60 70 80 90 100
    DVVTLSGTRG PLSRVGLEPP PGKRECRVGQ YVVDLTSFEQ LALPVLRNAD
    110 120 130 140 150
    CSSGPGQRVC VIDEIGKMEL FSQLFIQAVR QTLSTPGTII LGTIPVPKGK
    160 170 180 190
    PLALVEEIRN RKDVKVFNVT KENRNHLLPD IVTCVQSSRK
    Length:190
    Mass (Da):20,713
    Last modified:June 1, 2001 - v1
    Checksum:iB4B753F95796A210
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061G → E.
    Corresponds to variant rs12123482 [ dbSNP | Ensembl ].
    VAR_053071

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF416713 mRNA. Translation: AAL16807.1.
    BC005102 mRNA. Translation: AAH05102.1.
    CCDSiCCDS1597.1.
    RefSeqiNP_115700.1. NM_032324.1.
    UniGeneiHs.642715.

    Genome annotation databases

    EnsembliENST00000366628; ENSP00000355587; ENSG00000135778.
    GeneIDi84284.
    KEGGihsa:84284.
    UCSCiuc001hvj.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF416713 mRNA. Translation: AAL16807.1.
    BC005102 mRNA. Translation: AAH05102.1.
    CCDSiCCDS1597.1.
    RefSeqiNP_115700.1. NM_032324.1.
    UniGeneiHs.642715.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I3BNMR-A2-190[»]
    ProteinModelPortaliQ9BSD7.
    SMRiQ9BSD7. Positions 2-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124011. 19 interactions.
    IntActiQ9BSD7. 10 interactions.
    STRINGi9606.ENSP00000355587.

    PTM databases

    iPTMnetiQ9BSD7.
    PhosphoSiteiQ9BSD7.

    Polymorphism and mutation databases

    BioMutaiNTPCR.
    DMDMi54036528.

    Proteomic databases

    EPDiQ9BSD7.
    MaxQBiQ9BSD7.
    PaxDbiQ9BSD7.
    PeptideAtlasiQ9BSD7.
    PRIDEiQ9BSD7.

    Protocols and materials databases

    DNASUi84284.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000366628; ENSP00000355587; ENSG00000135778.
    GeneIDi84284.
    KEGGihsa:84284.
    UCSCiuc001hvj.2. human.

    Organism-specific databases

    CTDi84284.
    GeneCardsiNTPCR.
    HGNCiHGNC:28204. NTPCR.
    HPAiHPA028125.
    HPA054304.
    neXtProtiNX_Q9BSD7.
    PharmGKBiPA142672508.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IXTM. Eukaryota.
    COG1618. LUCA.
    GeneTreeiENSGT00390000018683.
    HOVERGENiHBG058637.
    InParanoidiQ9BSD7.
    KOiK06928.
    OMAiVHKICSA.
    OrthoDBiEOG7WT42C.
    PhylomeDBiQ9BSD7.
    TreeFamiTF323592.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06064-MONOMER.
    SABIO-RKQ9BSD7.

    Miscellaneous databases

    ChiTaRSiNTPCR. human.
    EvolutionaryTraceiQ9BSD7.
    GenomeRNAii84284.
    PROiQ9BSD7.

    Gene expression databases

    BgeeiQ9BSD7.
    CleanExiHS_C1orf57.
    ExpressionAtlasiQ9BSD7. baseline and differential.
    GenevisibleiQ9BSD7. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00796. NTPase_1.
    InterProiIPR003593. AAA+_ATPase.
    IPR004948. Nuc-triphosphatase_THEP1.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF03266. NTPase_1. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Kang L., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    3. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase."
      Placzek W.J., Almeida M.S., Wuethrich K.
      J. Mol. Biol. 367:788-801(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH THE ATP ANALOG ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLU-114 AND GLY-116.

    Entry informationi

    Entry nameiNTPCR_HUMAN
    AccessioniPrimary (citable) accession number: Q9BSD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: June 1, 2001
    Last modified: June 8, 2016
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.