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Protein

Cancer-related nucleoside-triphosphatase homolog

Gene

Ntpcr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

NTP + H2O = NDP + phosphate.

Regions

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cancer-related nucleoside-triphosphatase homolog (EC:3.6.1.15)
Short name:
NTPase
Alternative name(s):
Nucleoside triphosphate phosphohydrolase
Gene namesi
Name:Ntpcr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1913816. Ntpcr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 190189Cancer-related nucleoside-triphosphatase homologPRO_0000146712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CQA9.
MaxQBiQ9CQA9.
PaxDbiQ9CQA9.
PRIDEiQ9CQA9.

PTM databases

PhosphoSiteiQ9CQA9.

Expressioni

Gene expression databases

BgeeiQ9CQA9.
CleanExiMM_2310079N02RIK.
ExpressionAtlasiQ9CQA9. baseline and differential.
GenevisibleiQ9CQA9. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034313.

Structurei

3D structure databases

ProteinModelPortaliQ9CQA9.
SMRiQ9CQA9. Positions 2-189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the THEP1 NTPase family.Curated

Phylogenomic databases

eggNOGiENOG410IXTM. Eukaryota.
COG1618. LUCA.
GeneTreeiENSGT00390000018683.
HOVERGENiHBG058637.
InParanoidiQ9CQA9.
KOiK06928.
OMAiVHKICSA.
PhylomeDBiQ9CQA9.
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.

Q9CQA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRHVFLTGP PGVGKTTLIQ KAIEVLQSSG LPVDGFYTQE VRQEGKRIGF
60 70 80 90 100
DVVTLSGAQG PLSRVGSQPL PGKPECRVGQ YVVNLDSFEQ LALPVLRNAG
110 120 130 140 150
SSCGPKHRVC IIDEIGKMEL FSQPFIQAVR QMLSTPGIIV VGTIPVPKGK
160 170 180 190
PLALVEEIRK RRDVKVFNVT RDNRNSLLPD IVAVVQSSRT
Length:190
Mass (Da):20,667
Last modified:June 1, 2001 - v1
Checksum:iA6B9C6DFDFB06813
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006433 mRNA. Translation: BAB24586.1.
AK010229 mRNA. Translation: BAB26783.1.
AK010823 mRNA. Translation: BAB27206.1.
AK019321 mRNA. Translation: BAB31665.1.
BC025168 mRNA. Translation: AAH25168.1.
CCDSiCCDS22781.1.
RefSeqiNP_001297617.1. NM_001310688.1.
NP_079912.1. NM_025636.5.
UniGeneiMm.25296.

Genome annotation databases

EnsembliENSMUST00000034313; ENSMUSP00000034313; ENSMUSG00000031851.
GeneIDi66566.
KEGGimmu:66566.
UCSCiuc009nyk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006433 mRNA. Translation: BAB24586.1.
AK010229 mRNA. Translation: BAB26783.1.
AK010823 mRNA. Translation: BAB27206.1.
AK019321 mRNA. Translation: BAB31665.1.
BC025168 mRNA. Translation: AAH25168.1.
CCDSiCCDS22781.1.
RefSeqiNP_001297617.1. NM_001310688.1.
NP_079912.1. NM_025636.5.
UniGeneiMm.25296.

3D structure databases

ProteinModelPortaliQ9CQA9.
SMRiQ9CQA9. Positions 2-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034313.

PTM databases

PhosphoSiteiQ9CQA9.

Proteomic databases

EPDiQ9CQA9.
MaxQBiQ9CQA9.
PaxDbiQ9CQA9.
PRIDEiQ9CQA9.

Protocols and materials databases

DNASUi66566.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034313; ENSMUSP00000034313; ENSMUSG00000031851.
GeneIDi66566.
KEGGimmu:66566.
UCSCiuc009nyk.2. mouse.

Organism-specific databases

CTDi84284.
MGIiMGI:1913816. Ntpcr.

Phylogenomic databases

eggNOGiENOG410IXTM. Eukaryota.
COG1618. LUCA.
GeneTreeiENSGT00390000018683.
HOVERGENiHBG058637.
InParanoidiQ9CQA9.
KOiK06928.
OMAiVHKICSA.
PhylomeDBiQ9CQA9.
TreeFamiTF323592.

Miscellaneous databases

NextBioi322018.
PROiQ9CQA9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQA9.
CleanExiMM_2310079N02RIK.
ExpressionAtlasiQ9CQA9. baseline and differential.
GenevisibleiQ9CQA9. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hippocampus, Testis and Tongue.
  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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNTPCR_MOUSE
AccessioniPrimary (citable) accession number: Q9CQA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.