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CENPW_HUMAN
ID   CENPW_HUMAN             Reviewed;          88 AA.
AC   Q5EE01; A6NIR0; A6NJC2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Centromere protein W;
DE            Short=CENP-W;
DE   AltName: Full=Cancer-up-regulated gene 2 protein;
GN   Name=CENPW; Synonyms=C6orf173, CUG2;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Stomach;
RX   PubMed=17610844; DOI=10.1016/j.bbrc.2007.06.102;
RA   Lee S., Gang J., Jeon S.B., Choo S.H., Lee B., Kim Y.-G., Lee Y.S.,
RA   Jung J., Song S.Y., Koh S.S.;
RT   "Molecular cloning and functional analysis of a novel oncogene, cancer-
RT   upregulated gene 2 (CUG2).";
RL   Biochem. Biophys. Res. Commun. 360:633-639(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Lung;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17079448; DOI=10.1158/0008-5472.can-05-4414;
RA   Ivshina A.V., George J., Senko O., Mow B., Putti T.C., Smeds J.,
RA   Lindahl T., Pawitan Y., Hall P., Nordgren H., Wong J.E., Liu E.T.,
RA   Bergh J., Kuznetsov V.A., Miller L.D.;
RT   "Genetic reclassification of histologic grade delineates new clinical
RT   subtypes of breast cancer.";
RL   Cancer Res. 66:10292-10301(2006).
RN   [6]
RP   SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CENPT.
RX   PubMed=19070575; DOI=10.1016/j.cell.2008.10.019;
RA   Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y.,
RA   McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.;
RT   "CCAN makes multiple contacts with centromeric DNA to provide distinct
RT   pathways to the outer kinetochore.";
RL   Cell 135:1039-1052(2008).
RN   [7]
RP   FUNCTION, INTERACTION WITH CENPT, AND SUBCELLULAR LOCATION.
RX   PubMed=19533040; DOI=10.1007/s10059-009-0083-2;
RA   Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.;
RT   "Cancer-upregulated gene 2 (CUG2), a new component of centromere complex,
RT   is required for kinetochore function.";
RL   Mol. Cells 27:697-701(2009).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPM1.
RX   PubMed=22002061; DOI=10.1074/jbc.m111.228411;
RA   Chun Y., Park B., Koh W., Lee S., Cheon Y., Kim R., Che L., Lee S.;
RT   "New centromeric component CENP-W is an RNA-associated nuclear matrix
RT   protein that interacts with nucleophosmin/B23 protein.";
RL   J. Biol. Chem. 286:42758-42769(2011).
RN   [9]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH HISTONE H3, INTERACTION WITH
RP   CENPT, AND SUBCELLULAR LOCATION.
RX   PubMed=21695110; DOI=10.1371/journal.pbio.1001082;
RA   Prendergast L., van Vuuren C., Kaczmarczyk A., Doering V., Hellwig D.,
RA   Quinn N., Hoischen C., Diekmann S., Sullivan K.F.;
RT   "Premitotic assembly of human CENPs -T and -W switches centromeric
RT   chromatin to a mitotic state.";
RL   PLoS Biol. 9:E1001082-E1001082(2011).
RN   [10]
RP   FUNCTION, INTERACTION WITH CENPS; CENPT AND CEPNX, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=22304917; DOI=10.1016/j.cell.2011.11.061;
RA   Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T.,
RA   Morikawa K., Cheeseman I.M., Fukagawa T.;
RT   "CENP-T-W-S-X forms a unique centromeric chromatin structure with a
RT   histone-like fold.";
RL   Cell 148:487-501(2012).
CC   -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC       complex that plays a central role in assembly of kinetochore proteins,
CC       mitotic progression and chromosome segregation (By similarity). The
CC       CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex
CC       and may be involved in incorporation of newly synthesized CENPA into
CC       centromeres (By similarity). Part of a nucleosome-associated complex
CC       that binds specifically to histone H3-containing nucleosomes at the
CC       centromere, as opposed to nucleosomes containing CENPA. Component of
CC       the heterotetrameric CENP-T-W-S-X complex that binds and supercoils
CC       DNA, and plays an important role in kinetochore assembly. CENPW has a
CC       fundamental role in kinetochore assembly and function. It is one of the
CC       inner kinetochore proteins, with most further proteins binding
CC       downstream. Required for normal chromosome organization and normal
CC       progress through mitosis. {ECO:0000250, ECO:0000269|PubMed:19070575,
CC       ECO:0000269|PubMed:19533040, ECO:0000269|PubMed:21695110,
CC       ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22304917}.
CC   -!- SUBUNIT: Heterodimer with CENPT; this dimer coassembles with CENPS-
CC       CENPX heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC       complex, which is a subcomplex of the large constitutive centromere-
CC       associated network (CCAN, also known as the interphase centromere
CC       complex or ICEN) (PubMed:19070575, PubMed:19533040, PubMed:21695110,
CC       PubMed:22304917). Interacts with NPM1 (PubMed:22002061).
CC       {ECO:0000269|PubMed:19070575, ECO:0000269|PubMed:19533040,
CC       ECO:0000269|PubMed:21695110, ECO:0000269|PubMed:22002061,
CC       ECO:0000269|PubMed:22304917}.
CC   -!- INTERACTION:
CC       Q5EE01; Q96BT3: CENPT; NbExp=6; IntAct=EBI-5529625, EBI-719918;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17610844}.
CC       Chromosome, centromere {ECO:0000269|PubMed:19070575,
CC       ECO:0000269|PubMed:19533040, ECO:0000269|PubMed:22304917}. Chromosome,
CC       centromere, kinetochore {ECO:0000269|PubMed:19070575,
CC       ECO:0000269|PubMed:22304917}. Nucleus matrix
CC       {ECO:0000269|PubMed:22002061}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:22002061}. Note=Constitutively localizes to
CC       centromeres throughout the cell cycle, and to the inner kinetochore
CC       during mitosis. {ECO:0000250|UniProtKB:P0DJH6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5EE01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5EE01-2; Sequence=VSP_055708;
CC   -!- TISSUE SPECIFICITY: Highly expressed in ovary, liver, lung and pancreas
CC       and to a lower extent in breast and gastrointestinal tract cancers;
CC       such as those of the colon, rectum and stomach. Overexpressed in high
CC       grade breast invasive tumors. Expressed in many cancer cell types.
CC       {ECO:0000269|PubMed:17079448, ECO:0000269|PubMed:17610844}.
CC   -!- SIMILARITY: Belongs to the CENP-W/WIP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW48122.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW48123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY902475; AAW82474.1; -; mRNA.
DR   EMBL; AC020559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48121.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48122.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471051; EAW48123.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC017928; AAH17928.1; -; mRNA.
DR   EMBL; BC039556; AAH39556.1; -; mRNA.
DR   EMBL; BC046178; AAH46178.1; -; mRNA.
DR   EMBL; BC062798; AAH62798.1; -; mRNA.
DR   CCDS; CCDS34529.1; -. [Q5EE01-1]
DR   CCDS; CCDS69196.1; -. [Q5EE01-2]
DR   RefSeq; NP_001012525.1; NM_001012507.3. [Q5EE01-1]
DR   RefSeq; NP_001273453.1; NM_001286524.1. [Q5EE01-2]
DR   RefSeq; NP_001273454.1; NM_001286525.1.
DR   RefSeq; XP_016866334.1; XM_017010845.1.
DR   AlphaFoldDB; Q5EE01; -.
DR   SMR; Q5EE01; -.
DR   BioGRID; 132240; 33.
DR   ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR   CORUM; Q5EE01; -.
DR   IntAct; Q5EE01; 4.
DR   iPTMnet; Q5EE01; -.
DR   PhosphoSitePlus; Q5EE01; -.
DR   BioMuta; CENPW; -.
DR   DMDM; 74741448; -.
DR   EPD; Q5EE01; -.
DR   jPOST; Q5EE01; -.
DR   MassIVE; Q5EE01; -.
DR   MaxQB; Q5EE01; -.
DR   PaxDb; Q5EE01; -.
DR   PeptideAtlas; Q5EE01; -.
DR   PRIDE; Q5EE01; -.
DR   ProteomicsDB; 62772; -. [Q5EE01-1]
DR   TopDownProteomics; Q5EE01-1; -. [Q5EE01-1]
DR   Antibodypedia; 32744; 70 antibodies from 23 providers.
DR   DNASU; 387103; -.
DR   Ensembl; ENST00000368325.5; ENSP00000357308.1; ENSG00000203760.9. [Q5EE01-2]
DR   Ensembl; ENST00000368328.5; ENSP00000357311.4; ENSG00000203760.9. [Q5EE01-1]
DR   GeneID; 387103; -.
DR   KEGG; hsa:387103; -.
DR   MANE-Select; ENST00000368328.5; ENSP00000357311.4; NM_001012507.4; NP_001012525.1.
DR   UCSC; uc003qao.5; human. [Q5EE01-1]
DR   CTD; 387103; -.
DR   DisGeNET; 387103; -.
DR   GeneCards; CENPW; -.
DR   HGNC; HGNC:21488; CENPW.
DR   HPA; ENSG00000203760; Tissue enhanced (bone marrow, testis).
DR   MIM; 611264; gene.
DR   neXtProt; NX_Q5EE01; -.
DR   OpenTargets; ENSG00000203760; -.
DR   PharmGKB; PA165617841; -.
DR   VEuPathDB; HostDB:ENSG00000203760; -.
DR   GeneTree; ENSGT00390000010369; -.
DR   HOGENOM; CLU_178644_1_0_1; -.
DR   InParanoid; Q5EE01; -.
DR   OMA; IIKKDHV; -.
DR   OrthoDB; 1578618at2759; -.
DR   PhylomeDB; Q5EE01; -.
DR   TreeFam; TF343285; -.
DR   PathwayCommons; Q5EE01; -.
DR   Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   SignaLink; Q5EE01; -.
DR   SIGNOR; Q5EE01; -.
DR   BioGRID-ORCS; 387103; 782 hits in 1097 CRISPR screens.
DR   ChiTaRS; CENPW; human.
DR   GenomeRNAi; 387103; -.
DR   Pharos; Q5EE01; Tbio.
DR   PRO; PR:Q5EE01; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q5EE01; protein.
DR   Bgee; ENSG00000203760; Expressed in oocyte and 148 other tissues.
DR   ExpressionAtlas; Q5EE01; baseline and differential.
DR   Genevisible; Q5EE01; HS.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; TAS:UniProtKB.
DR   GO; GO:0051276; P:chromosome organization; IMP:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0051382; P:kinetochore assembly; IMP:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR028847; CENP-W.
DR   InterPro; IPR009072; Histone-fold.
DR   Pfam; PF15510; CENP-W; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW   DNA-binding; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..88
FT                   /note="Centromere protein W"
FT                   /id="PRO_0000311183"
FT   VAR_SEQ         43
FT                   /note="V -> VRFHPFSGWEWGTGEV (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055708"
SQ   SEQUENCE   88 AA;  10061 MW;  3BC0A6F158B1E6D9 CRC64;
     MALSTIVSQR KQIKRKAPRG FLKRVFKRKK PQLRLEKSGD LLVHLNCLLF VHRLAEESRT
     NACASKCRVI NKEHVLAAAK VILKKSRG
 
 
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