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Q64523

- H2A2C_MOUSE

UniProt

Q64523 - H2A2C_MOUSE

Protein

Histone H2A type 2-C

Gene

Hist2h2ac

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

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198626. Meiotic synapsis.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A type 2-C
    Alternative name(s):
    H2a-613B
    Gene namesi
    Name:Hist2h2ac
    Synonyms:Hist2h2ab
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2448316. Hist2h2ac.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleosome Source: UniProtKB-KW
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 129128Histone H2A type 2-CPRO_0000227512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21Phosphoserine; by RPS6KA5By similarity
    Modified residuei4 – 41Citrulline; alternateBy similarity
    Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternate1 Publication
    Modified residuei6 – 61N6-acetyllysineBy similarity
    Modified residuei10 – 101N6-acetyllysineBy similarity
    Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei37 – 371N6-crotonyllysine1 Publication
    Modified residuei105 – 1051N5-methylglutamine1 Publication
    Modified residuei119 – 1191N6-crotonyllysine1 Publication
    Modified residuei120 – 1201N6-crotonyllysine; alternateBy similarity
    Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
    Modified residuei121 – 1211Phosphothreonine; by VPRBPBy similarity
    Modified residuei123 – 1231PhosphoserineBy similarity
    Modified residuei125 – 1251N6-crotonyllysineBy similarity

    Post-translational modificationi

    Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro By similarity. Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.By similarity4 Publications
    Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by VPRBP is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription By similarity.By similarity
    Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex By similarity.By similarity
    Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
    Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

    Keywords - PTMi

    Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ64523.
    PRIDEiQ64523.

    PTM databases

    PhosphoSiteiQ64523.

    Expressioni

    Gene expression databases

    BgeeiQ64523.
    CleanExiMM_HIST2H2AB.
    MM_HIST2H2AC.
    GenevestigatoriQ64523.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

    Protein-protein interaction databases

    BioGridi235095. 9 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64523.
    SMRiQ64523. Positions 14-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    GeneTreeiENSGT00730000110453.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiQ64523.
    KOiK11251.
    OMAiIAMSGRG.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiQ64523.
    TreeFamiTF300137.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00620. HISTONEH2A.
    SMARTiSM00414. H2A. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00046. HISTONE_H2A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q64523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
    YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 100
    VTIAQGGVLP NIQAVLLPKK TESHKAKSK 129
    Length:129
    Mass (Da):13,988
    Last modified:January 23, 2007 - v3
    Checksum:i358AE20D1C531724
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62673 Genomic DNA. Translation: AAB04768.1.
    AY158922 Genomic DNA. Translation: AAO06232.2.
    AY158923 Genomic DNA. Translation: AAO06233.1.
    CCDSiCCDS17634.1.
    RefSeqiNP_783593.1. NM_175662.2.
    UniGeneiMm.358954.

    Genome annotation databases

    EnsembliENSMUST00000090782; ENSMUSP00000088288; ENSMUSG00000068855.
    GeneIDi319176.
    KEGGimmu:319176.
    UCSCiuc008qmi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62673 Genomic DNA. Translation: AAB04768.1 .
    AY158922 Genomic DNA. Translation: AAO06232.2 .
    AY158923 Genomic DNA. Translation: AAO06233.1 .
    CCDSi CCDS17634.1.
    RefSeqi NP_783593.1. NM_175662.2.
    UniGenei Mm.358954.

    3D structure databases

    ProteinModelPortali Q64523.
    SMRi Q64523. Positions 14-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 235095. 9 interactions.

    PTM databases

    PhosphoSitei Q64523.

    Proteomic databases

    PaxDbi Q64523.
    PRIDEi Q64523.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090782 ; ENSMUSP00000088288 ; ENSMUSG00000068855 .
    GeneIDi 319176.
    KEGGi mmu:319176.
    UCSCi uc008qmi.1. mouse.

    Organism-specific databases

    CTDi 8338.
    MGIi MGI:2448316. Hist2h2ac.

    Phylogenomic databases

    eggNOGi COG5262.
    GeneTreei ENSGT00730000110453.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi Q64523.
    KOi K11251.
    OMAi IAMSGRG.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi Q64523.
    TreeFami TF300137.

    Enzyme and pathway databases

    Reactomei REACT_198626. Meiotic synapsis.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    NextBioi 394286.
    PROi Q64523.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q64523.
    CleanExi MM_HIST2H2AB.
    MM_HIST2H2AC.
    Genevestigatori Q64523.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00046. HISTONE_H2A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the 55-kb mouse histone gene cluster on chromosome 3."
      Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F.
      Genome Res. 6:702-714(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
    2. "The human and mouse replication-dependent histone genes."
      Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
      Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation."
      de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.
      Dev. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-120.
    4. "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation."
      Fang J., Chen T., Chadwick B., Li E., Zhang Y.
      J. Biol. Chem. 279:52812-52815(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-120.
    5. "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells."
      Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.
      Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-4.
    6. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
      Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
      Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROTONYLATION AT LYS-37 AND LYS-119.
    7. "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
      Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
      Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT GLN-105.

    Entry informationi

    Entry nameiH2A2C_MOUSE
    AccessioniPrimary (citable) accession number: Q64523
    Secondary accession number(s): Q8CGP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 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