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O35216

- CENPA_MOUSE

UniProt

O35216 - CENPA_MOUSE

Protein

Histone H3-like centromeric protein A

Gene

Cenpa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    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.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. establishment of mitotic spindle orientation Source: Ensembl
    2. kinetochore assembly Source: Ensembl
    3. nucleosome assembly Source: InterPro
    4. protein localization to chromosome, centromeric region Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3-like centromeric protein A
    Alternative name(s):
    Centromere protein A
    Short name:
    CENP-A
    Gene namesi
    Name:Cenpa
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:88375. Cenpa.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore
    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.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: MGI
    2. condensed chromosome inner kinetochore Source: MGI
    3. condensed nuclear chromosome kinetochore Source: Ensembl
    4. nucleosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 134134Histone H3-like centromeric protein APRO_0000221374Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161PhosphoserineBy similarity
    Modified residuei22 – 221PhosphoserineBy similarity

    Post-translational modificationi

    Poly-ADP-ribosylated by PARP1.

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein

    Proteomic databases

    PRIDEiO35216.

    PTM databases

    PhosphoSiteiO35216.

    Expressioni

    Gene expression databases

    ArrayExpressiO35216.
    BgeeiO35216.
    CleanExiMM_CENPA.
    GenevestigatoriO35216.

    Interactioni

    Subunit structurei

    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 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.By similarity

    Protein-protein interaction databases

    IntActiO35216. 1 interaction.
    MINTiMINT-237454.
    STRINGi10090.ENSMUSP00000122831.

    Structurei

    3D structure databases

    ProteinModelPortaliO35216.
    SMRiO35216. Positions 54-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 134100H3-likeAdd
    BLAST
    Regioni69 – 11042CATDAdd
    BLAST

    Domaini

    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

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00730000110760.
    HOVERGENiHBG001172.
    InParanoidiO35216.
    KOiK11495.
    OMAiLVREICV.
    PhylomeDBiO35216.
    TreeFamiTF354293.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view]
    PANTHERiPTHR11426. PTHR11426. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00622. HISTONEH3.
    SMARTiSM00428. H3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O35216-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPRRKPQTP RRRPSSPAPG PSRQSSSVGS QTLRRRQKFM WLKEIKTLQK    50
    STDLLFRKKP FSMVVREICE KFSRGVDFWW QAQALLALQE AAEAFLIHLF 100
    EDAYLLSLHA GRVTLFPKDI QLTRRIRGFE GGLP 134
    Length:134
    Mass (Da):15,509
    Last modified:January 1, 1998 - v1
    Checksum:i0381FA6492E43C3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS19162.1.
    RefSeqiNP_031707.1. NM_007681.2.
    UniGeneiMm.290563.

    Genome annotation databases

    EnsembliENSMUST00000144742; ENSMUSP00000122831; ENSMUSG00000029177.
    GeneIDi12615.
    KEGGimmu:12615.
    UCSCiuc008wvt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS19162.1.
    RefSeqi NP_031707.1. NM_007681.2.
    UniGenei Mm.290563.

    3D structure databases

    ProteinModelPortali O35216.
    SMRi O35216. Positions 54-128.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35216. 1 interaction.
    MINTi MINT-237454.
    STRINGi 10090.ENSMUSP00000122831.

    PTM databases

    PhosphoSitei O35216.

    Proteomic databases

    PRIDEi O35216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000144742 ; ENSMUSP00000122831 ; ENSMUSG00000029177 .
    GeneIDi 12615.
    KEGGi mmu:12615.
    UCSCi uc008wvt.1. mouse.

    Organism-specific databases

    CTDi 1058.
    MGIi MGI:88375. Cenpa.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00730000110760.
    HOVERGENi HBG001172.
    InParanoidi O35216.
    KOi K11495.
    OMAi LVREICV.
    PhylomeDBi O35216.
    TreeFami TF354293.

    Enzyme and pathway databases

    Reactomei REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Miscellaneous databases

    NextBioi 281778.
    PROi O35216.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35216.
    Bgeei O35216.
    CleanExi MM_CENPA.
    Genevestigatori O35216.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view ]
    PANTHERi PTHR11426. PTHR11426. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00622. HISTONEH3.
    SMARTi SM00428. H3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiCENPA_MOUSE
    AccessioniPrimary (citable) accession number: O35216
    Secondary accession number(s): Q545C9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 107 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

    External Data

    Dasty 3