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O35216 (CENPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone H3-like centromeric protein A
Alternative name(s):
Centromere protein A
Short name=CENP-A
Gene names
Name:Cenpa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length134 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro) By similarity.

Subunit structure

Forms a nucleosome-like histone octamer containing two molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and two H2A-H2B heterodimers. Nucleosomes containing CENPA also contain histone H2A variants such as macroH2A H2AFY and H2A.Z/H2AFZ. The CENPA-H4 heterotetramer is more compact and structurally more rigid than corresponding H3-H4 heterotetramers. Heterotrimer composed of HJURP, CENPA and histone H4, where HJURP interacts with the dimer formed by CENPA and histone H4 and prevents tetramerization of CENPA and H4. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. Interacts (via CATD domain) with HJURP; the interaction is direct and is required for its localization to centromeres. Interacts with CENPC, CENPN and CENPT; interaction is direct. Part of a centromere complex consisting of CENPA, CENPT and CENPW By similarity.

Subcellular location

Nucleus. Chromosome › centromere › kinetochore. Note: Localizes exclusively in the kinetochore domain of centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height By similarity.

Domain

The CATD (CENPA targeting domain) region is responsible for the more compact structure of nucleosomes containing CENPA and is necessary and sufficient to mediate the localization into centromeres By similarity.

Post-translational modification

Poly-ADP-ribosylated by PARP1. Ref.4

Sequence similarities

Belongs to the histone H3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 134134Histone H3-like centromeric protein A
PRO_0000221374

Regions

Region35 – 134100H3-like
Region69 – 11042CATD

Amino acid modifications

Modified residue161Phosphoserine By similarity
Modified residue221Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O35216 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0381FA6492E43C3D

FASTA13415,509
        10         20         30         40         50         60 
MGPRRKPQTP RRRPSSPAPG PSRQSSSVGS QTLRRRQKFM WLKEIKTLQK STDLLFRKKP 

        70         80         90        100        110        120 
FSMVVREICE KFSRGVDFWW QAQALLALQE AAEAFLIHLF EDAYLLSLHA GRVTLFPKDI 

       130 
QLTRRIRGFE GGLP

« Hide

References

« Hide 'large scale' references
[1]"Gene structure and sequence analysis of mouse centromere proteins A and C."
Kalitsis P., Macdonald A.C., Newson A.J., Hudson D.F., Choo K.H.A.
Genomics 47:108-114(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and C57BL/6J.
[2]"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. expand/collapse author list , 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 and NOD.
Tissue: Eye and Thymus.
[3]"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: Czech II.
Tissue: Mammary gland.
[4]"Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated."
Saxena A., Saffery R., Wong L.H., Kalitsis P., Choo K.H.
J. Biol. Chem. 277:26921-26926(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POLY-ADP-RIBOSYLATION BY PARP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF012709 mRNA. Translation: AAC39957.1.
AF012710 Genomic DNA. Translation: AAC39958.1.
AK010718 mRNA. Translation: BAB27140.1.
AK011399 mRNA. Translation: BAB27591.1.
AK053763 mRNA. Translation: BAC35512.1.
AK089033 mRNA. Translation: BAC40710.1.
BC011038 mRNA. Translation: AAH11038.1.
IPIIPI00128526.
RefSeqNP_031707.1. NM_007681.2.
UniGeneMm.290563.

3D structure databases

ProteinModelPortalO35216.
SMRO35216. Positions 54-128.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000122831.

PTM databases

PhosphoSiteO35216.

Proteomic databases

PRIDEO35216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000144742; ENSMUSP00000122831; ENSMUSG00000029177.
GeneID12615.
KEGGmmu:12615.
UCSCuc008wvt.1. mouse.

Organism-specific databases

CTD1058.
MGIMGI:88375. Cenpa.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00690000102181.
HOVERGENHBG001172.
InParanoidO35216.
KOK11495.
OMALVREICV.
OrthoDBEOG4MPHRS.

Gene expression databases

ArrayExpressO35216.
BgeeO35216.
CleanExMM_CENPA.
GenevestigatorO35216.
GermOnlineENSMUSG00000029177. Mus musculus.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
PROSITEPS00959. HISTONE_H3_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio281778.
SOURCESearch...

Entry information

Entry nameCENPA_MOUSE
AccessionPrimary (citable) accession number: O35216
Secondary accession number(s): Q545C9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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