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Q8CGP6

- H2A1H_MOUSE

UniProt

Q8CGP6 - H2A1H_MOUSE

Protein

Histone H2A type 1-H

Gene

Hist1h2ah

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_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A type 1-H
    Gene namesi
    Name:Hist1h2ah
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:2448295. Hist1h2ah.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    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 – 128127Histone H2A type 1-HPRO_0000227504Add
    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
    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 residuei126 – 1261N6-crotonyllysineBy similarity

    Post-translational modificationi

    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
    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
    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

    PaxDbiQ8CGP6.
    PRIDEiQ8CGP6.

    Expressioni

    Gene expression databases

    BgeeiQ8CGP6.
    CleanExiMM_HIST1H2AH.
    GenevestigatoriQ8CGP6.

    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

    IntActiQ8CGP6. 1 interaction.
    MINTiMINT-4606203.
    STRINGi10090.ENSMUSP00000089336.

    Structurei

    Secondary structure

    1
    128
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 225
    Helixi28 – 3710
    Beta strandi42 – 443
    Helixi48 – 7326
    Beta strandi77 – 793
    Helixi81 – 9010
    Helixi92 – 976
    Turni98 – 1003
    Beta strandi101 – 1033
    Helixi114 – 1163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F8NX-ray2.90K1-128[»]
    ProteinModelPortaliQ8CGP6.
    SMRiQ8CGP6. Positions 12-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8CGP6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    GeneTreeiENSGT00730000110388.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiQ8CGP6.
    KOiK11251.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiQ8CGP6.
    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.

    Q8CGP6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR 100
    VTIAQGGVLP NIQAVLLPKK TESHHKAK 128
    Length:128
    Mass (Da):13,950
    Last modified:January 23, 2007 - v3
    Checksum:i7184B2CC89F5BD20
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY158914 Genomic DNA. Translation: AAO06224.1.
    AL590614 Genomic DNA. Translation: CAI26126.1.
    CCDSiCCDS26304.1.
    RefSeqiNP_783590.1. NM_175659.2.
    UniGeneiMm.250564.
    Mm.262527.

    Genome annotation databases

    EnsembliENSMUST00000091742; ENSMUSP00000089336; ENSMUSG00000069302.
    GeneIDi319168.
    KEGGimmu:319168.
    UCSCiuc007psa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY158914 Genomic DNA. Translation: AAO06224.1 .
    AL590614 Genomic DNA. Translation: CAI26126.1 .
    CCDSi CCDS26304.1.
    RefSeqi NP_783590.1. NM_175659.2.
    UniGenei Mm.250564.
    Mm.262527.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F8N X-ray 2.90 K 1-128 [» ]
    ProteinModelPortali Q8CGP6.
    SMRi Q8CGP6. Positions 12-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8CGP6. 1 interaction.
    MINTi MINT-4606203.
    STRINGi 10090.ENSMUSP00000089336.

    Proteomic databases

    PaxDbi Q8CGP6.
    PRIDEi Q8CGP6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091742 ; ENSMUSP00000089336 ; ENSMUSG00000069302 .
    GeneIDi 319168.
    KEGGi mmu:319168.
    UCSCi uc007psa.1. mouse.

    Organism-specific databases

    CTDi 85235.
    MGIi MGI:2448295. Hist1h2ah.

    Phylogenomic databases

    eggNOGi COG5262.
    GeneTreei ENSGT00730000110388.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi Q8CGP6.
    KOi K11251.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi Q8CGP6.
    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_226917. HATs acetylate histones.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    EvolutionaryTracei Q8CGP6.
    NextBioi 394260.
    PROi Q8CGP6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CGP6.
    CleanExi MM_HIST1H2AH.
    Genevestigatori Q8CGP6.

    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. "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].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 nameiH2A1H_MOUSE
    AccessioniPrimary (citable) accession number: Q8CGP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3