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Q64523

- H2A2C_MOUSE

UniProt

Q64523 - H2A2C_MOUSE

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Protein

Histone H2A type 2-C

Gene
Hist2h2ac, Hist2h2ab
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine; by RPS6KA5 By similarity
Modified residuei4 – 41Citrulline; alternate By similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternate Inferred
Modified residuei6 – 61N6-acetyllysine By similarity
Modified residuei10 – 101N6-acetyllysine By 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; alternate By similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei121 – 1211Phosphothreonine; by VPRBP By similarity
Modified residuei123 – 1231Phosphoserine By similarity
Modified residuei125 – 1251N6-crotonyllysine By 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.2 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.
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.
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

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

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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: September 3, 2014
This is version 125 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

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