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P0DJH6 (CENPW_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein W

Short name=CENP-W
Gene names
Name:CENPW
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length76 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4

Subunit structure

Part of a centromere complex consisting of CENPA, CENPT and CENPW By similarity. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts directly with CENPT. Binds DNA. Ref.2 Ref.3 Ref.4

Subcellular location

Nucleus. Chromosomecentromerekinetochore. Note: Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore. Ref.2 Ref.4

Miscellaneous

Association with CENPA-containing complexes may be indirect and due to the proximity of centromeric nucleosomes containing histone H3 with those containing CENPA.

Sequence similarities

Belongs to the CENPW family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CENPTF1NPG54EBI-2132287,EBI-2132248

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Centromere protein W
PRO_0000417384

Experimental info

Mutagenesis71R → A: Lethal mitotic defects; when associated with A-22 and A-75. Lethal mitotic defects; when associated with A-11; A-12; A-22; A-54 and A-56. Lethal mitotic defects; when associated with A-11; A-12; A-22 and A-75. Ref.2 Ref.4
Mutagenesis111R → A: Lethal mitotic defects; when associated with A-7; A-12; A-22; A-54 and A-56. Lethal mitotic defects; when associated with A-7; A-12; A-22 and A-75. Ref.2 Ref.4
Mutagenesis121K → A: Lethal mitotic defects; when associated with A-7; A-11; A-22; A-54 and A-56. Lethal mitotic defects; when associated with A-7; A-11; A-22 and A-75. Ref.2 Ref.4
Mutagenesis221R → A: Lethal mitotic defects; when associated with A-7 and A-75. Lethal mitotic defects; when associated with A-7; A-11; A-12; A-54 and A-56. Lethal mitotic defects; when associated with A-7; A-11; A-12 and A-75. Ref.2 Ref.4
Mutagenesis541K → A: Lethal mitotic defects; when associated with A-7; A-11; A-12; A-22; and A-56. Ref.4
Mutagenesis561K → A: Lethal mitotic defects; when associated with A-7; A-11; A-12; A-22 and A-54. Ref.4
Mutagenesis751R → A: Lethal mitotic defects; when associated with A-7 and A-22. Lethal mitotic defects; when associated with A-7; A-11; A-12 and A-22. Ref.2

Secondary structure

......... 76
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0DJH6 [UniParc].

Last modified May 16, 2012. Version 1.
Checksum: B34E201BEBDE72F7

FASTA768,743
        10         20         30         40         50         60 
MRRTVPRGTL RKIIKKHKPH LRLAANTDLL VHLSFLLFLH RLAEEARTNA FENKSKIIKP 

        70 
EHTIAAAKVI LKKSRG 

« Hide

References

« Hide 'large scale' references
[1]"A comprehensive collection of chicken cDNAs."
Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E., Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.
Curr. Biol. 12:1965-1969(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: White Leghorn Hisex.
[2]"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: FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-7; ARG-11; LYS-12; ARG-22 AND ARG-75, SUBCELLULAR LOCATION.
[3]"Spindle microtubules generate tension-dependent changes in the distribution of inner kinetochore proteins."
Suzuki A., Hori T., Nishino T., Usukura J., Miyagi A., Morikawa K., Fukagawa T.
J. Cell Biol. 193:125-140(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CENPT.
[4]"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: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-7; ARG-11; LYS-12; ARG-22; LYS-54 AND LYS-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BU413473 mRNA. No translation available.
RefSeqNP_001264662.1. NM_001277733.1.
UniGeneGga.16138.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B0CX-ray2.20W2-76[»]
3B0DX-ray2.20C/W2-76[»]
3VH5X-ray2.40W2-76[»]
3VH6X-ray3.35W2-76[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0DJH6. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID421716.
KEGGgga:421716.

Organism-specific databases

CTD387103.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR028847. CENP-W.
IPR009072. Histone-fold.
[Graphical view]
PfamPF15510. CENP-W. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCENPW_CHICK
AccessionPrimary (citable) accession number: P0DJH6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: May 16, 2012
Last modified: July 9, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references