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Protein

Centromere protein W

Gene

CENPW

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

Functioni

Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.By similarity5 Publications

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • CENP-A containing nucleosome assembly Source: UniProtKB
  • chromosome organization Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • kinetochore assembly Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • nucleosome assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein W
Short name:
CENP-W
Alternative name(s):
Cancer-up-regulated gene 2 protein
Gene namesi
Name:CENPW
Synonyms:C6orf173, CUG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21488. CENPW.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • kinetochore Source: UniProtKB
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165617841.

Polymorphism and mutation databases

BioMutaiCENPW.
DMDMi74741448.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8888Centromere protein WPRO_0000311183Add
BLAST

Proteomic databases

EPDiQ5EE01.
MaxQBiQ5EE01.
PaxDbiQ5EE01.
PRIDEiQ5EE01.
TopDownProteomicsiQ5EE01-1. [Q5EE01-1]

PTM databases

PhosphoSiteiQ5EE01.

Expressioni

Tissue specificityi

Highly expressed in ovary, liver, lung and pancreas and to a lower extent in breast and gastrointestinal tract cancers; such as those of the colon, rectum and stomach. Overexpressed in high grade breast invasive tumors. Expressed in many cancer cell types.2 Publications

Inductioni

Up-regulated in many cancer tissues.1 Publication

Gene expression databases

BgeeiQ5EE01.
CleanExiHS_C6orf173.
ExpressionAtlasiQ5EE01. baseline and differential.
GenevisibleiQ5EE01. HS.

Interactioni

Subunit structurei

Part of a centromere complex consisting of CENPA, CENPT and CENPW. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Interacts directly with CENPT. Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts with NPM1. Binds DNA.5 Publications

Protein-protein interaction databases

BioGridi132240. 3 interactions.
IntActiQ5EE01. 3 interactions.
STRINGi9606.ENSP00000357311.

Structurei

3D structure databases

ProteinModelPortaliQ5EE01.
SMRiQ5EE01. Positions 18-88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CENPW family.Curated

Phylogenomic databases

eggNOGiENOG410J16U. Eukaryota.
ENOG411155P. LUCA.
GeneTreeiENSGT00390000010369.
HOGENOMiHOG000060251.
InParanoidiQ5EE01.
OMAiSTTVSQR.
OrthoDBiEOG72G19W.
PhylomeDBiQ5EE01.
TreeFamiTF343285.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028847. CENP-W.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF15510. CENP-W. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5EE01-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALSTIVSQR KQIKRKAPRG FLKRVFKRKK PQLRLEKSGD LLVHLNCLLF
60 70 80
VHRLAEESRT NACASKCRVI NKEHVLAAAK VILKKSRG
Length:88
Mass (Da):10,061
Last modified:March 15, 2005 - v1
Checksum:i3BC0A6F158B1E6D9
GO
Isoform 2 (identifier: Q5EE01-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-43: V → VRFHPFSGWEWGTGEV

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:103
Mass (Da):11,835
Checksum:i5363AD93990CA973
GO

Sequence cautioni

The sequence EAW48122.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW48123.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 431V → VRFHPFSGWEWGTGEV in isoform 2. CuratedVSP_055708

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY902475 mRNA. Translation: AAW82474.1.
AC020559 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48121.1.
CH471051 Genomic DNA. Translation: EAW48122.1. Sequence problems.
CH471051 Genomic DNA. Translation: EAW48123.1. Sequence problems.
BC017928 mRNA. Translation: AAH17928.1.
BC039556 mRNA. Translation: AAH39556.1.
BC046178 mRNA. Translation: AAH46178.1.
BC062798 mRNA. Translation: AAH62798.1.
CCDSiCCDS34529.1. [Q5EE01-1]
CCDS69196.1. [Q5EE01-2]
RefSeqiNP_001012525.1. NM_001012507.3. [Q5EE01-1]
NP_001273453.1. NM_001286524.1. [Q5EE01-2]
NP_001273454.1. NM_001286525.1.
UniGeneiHs.486401.

Genome annotation databases

EnsembliENST00000368325; ENSP00000357308; ENSG00000203760. [Q5EE01-2]
ENST00000368328; ENSP00000357311; ENSG00000203760. [Q5EE01-1]
GeneIDi387103.
KEGGihsa:387103.
UCSCiuc003qao.5. human. [Q5EE01-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY902475 mRNA. Translation: AAW82474.1.
AC020559 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48121.1.
CH471051 Genomic DNA. Translation: EAW48122.1. Sequence problems.
CH471051 Genomic DNA. Translation: EAW48123.1. Sequence problems.
BC017928 mRNA. Translation: AAH17928.1.
BC039556 mRNA. Translation: AAH39556.1.
BC046178 mRNA. Translation: AAH46178.1.
BC062798 mRNA. Translation: AAH62798.1.
CCDSiCCDS34529.1. [Q5EE01-1]
CCDS69196.1. [Q5EE01-2]
RefSeqiNP_001012525.1. NM_001012507.3. [Q5EE01-1]
NP_001273453.1. NM_001286524.1. [Q5EE01-2]
NP_001273454.1. NM_001286525.1.
UniGeneiHs.486401.

3D structure databases

ProteinModelPortaliQ5EE01.
SMRiQ5EE01. Positions 18-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132240. 3 interactions.
IntActiQ5EE01. 3 interactions.
STRINGi9606.ENSP00000357311.

PTM databases

PhosphoSiteiQ5EE01.

Polymorphism and mutation databases

BioMutaiCENPW.
DMDMi74741448.

Proteomic databases

EPDiQ5EE01.
MaxQBiQ5EE01.
PaxDbiQ5EE01.
PRIDEiQ5EE01.
TopDownProteomicsiQ5EE01-1. [Q5EE01-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368325; ENSP00000357308; ENSG00000203760. [Q5EE01-2]
ENST00000368328; ENSP00000357311; ENSG00000203760. [Q5EE01-1]
GeneIDi387103.
KEGGihsa:387103.
UCSCiuc003qao.5. human. [Q5EE01-1]

Organism-specific databases

CTDi387103.
GeneCardsiCENPW.
HGNCiHGNC:21488. CENPW.
MIMi611264. gene.
neXtProtiNX_Q5EE01.
PharmGKBiPA165617841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J16U. Eukaryota.
ENOG411155P. LUCA.
GeneTreeiENSGT00390000010369.
HOGENOMiHOG000060251.
InParanoidiQ5EE01.
OMAiSTTVSQR.
OrthoDBiEOG72G19W.
PhylomeDBiQ5EE01.
TreeFamiTF343285.

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

GenomeRNAii387103.
NextBioi101198.
PROiQ5EE01.
SOURCEiSearch...

Gene expression databases

BgeeiQ5EE01.
CleanExiHS_C6orf173.
ExpressionAtlasiQ5EE01. baseline and differential.
GenevisibleiQ5EE01. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028847. CENP-W.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF15510. CENP-W. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional analysis of a novel oncogene, cancer-upregulated gene 2 (CUG2)."
    Lee S., Gang J., Jeon S.B., Choo S.H., Lee B., Kim Y.-G., Lee Y.S., Jung J., Song S.Y., Koh S.S.
    Biochem. Biophys. Res. Commun. 360:633-639(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
    Tissue: Stomach.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Kidney and Lung.
  5. "Genetic reclassification of histologic grade delineates new clinical subtypes of breast cancer."
    Ivshina A.V., George J., Senko O., Mow B., Putti T.C., Smeds J., Lindahl T., Pawitan Y., Hall P., Nordgren H., Wong J.E., Liu E.T., Bergh J., Kuznetsov V.A., Miller L.D.
    Cancer Res. 66:10292-10301(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "CCAN makes multiple contacts with centromeric DNA to provide distinct pathways to the outer kinetochore."
    Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y., McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.
    Cell 135:1039-1052(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH CENPT.
  7. "Cancer-upregulated gene 2 (CUG2), a new component of centromere complex, is required for kinetochore function."
    Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.
    Mol. Cells 27:697-701(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH CENPA AND CENPT, SUBCELLULAR LOCATION.
  8. "New centromeric component CENP-W is an RNA-associated nuclear matrix protein that interacts with nucleophosmin/B23 protein."
    Chun Y., Park B., Koh W., Lee S., Cheon Y., Kim R., Che L., Lee S.
    J. Biol. Chem. 286:42758-42769(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
  9. "Premitotic assembly of human CENPs -T and -W switches centromeric chromatin to a mitotic state."
    Prendergast L., van Vuuren C., Kaczmarczyk A., Doering V., Hellwig D., Quinn N., Hoischen C., Diekmann S., Sullivan K.F.
    PLoS Biol. 9:E1001082-E1001082(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HISTONE H3, INTERACTION WITH CENPT, SUBCELLULAR LOCATION.
  10. "CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold."
    Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T., Morikawa K., Cheeseman I.M., Fukagawa T.
    Cell 148:487-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCENPW_HUMAN
AccessioniPrimary (citable) accession number: Q5EE01
Secondary accession number(s): A6NIR0, A6NJC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 15, 2005
Last modified: April 13, 2016
This is version 104 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.