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Protein

Histone H2A type 2-C

Gene

Hist2h2ac

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_264471. NoRC negatively regulates rRNA expression.
REACT_27235. Meiotic Recombination.
REACT_287050. Meiotic synapsis.
REACT_326896. NoRC negatively regulates rRNA expression.
REACT_351456. DNA methylation.
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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2448316. Hist2h2ac.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. nucleosome Source: UniProtKB-KW
  3. nucleus Source: MGI
Complete GO annotation...

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
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

Deiminated on Arg-4 in granulocytes upon calcium entry.By similarity
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 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. 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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.By similarity3 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
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.1 Publication
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.1 Publication
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

MaxQBiQ64523.
PaxDbiQ64523.
PRIDEiQ64523.

PTM databases

PhosphoSiteiQ64523.

Expressioni

Gene expression databases

BgeeiQ64523.
CleanExiMM_HIST2H2AB.
MM_HIST2H2AC.
ExpressionAtlasiQ64523. baseline and differential.
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. 10 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.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
KOiK11251.
OMAiNSKSRSA.
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

        10         20         30         40         50
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK
110 120
VTIAQGGVLP NIQAVLLPKK TESHKAKSK
Length:129
Mass (Da):13,988
Last modified:January 22, 2007 - v3
Checksum:i358AE20D1C531724
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi235095. 10 interactions.

PTM databases

PhosphoSiteiQ64523.

Proteomic databases

MaxQBiQ64523.
PaxDbiQ64523.
PRIDEiQ64523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8338.
MGIiMGI:2448316. Hist2h2ac.

Phylogenomic databases

eggNOGiCOG5262.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
KOiK11251.
OMAiNSKSRSA.
OrthoDBiEOG7M0NTR.
PhylomeDBiQ64523.
TreeFamiTF300137.

Enzyme and pathway databases

ReactomeiREACT_264471. NoRC negatively regulates rRNA expression.
REACT_27235. Meiotic Recombination.
REACT_287050. Meiotic synapsis.
REACT_326896. NoRC negatively regulates rRNA expression.
REACT_351456. DNA methylation.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi394286.
PROiQ64523.
SOURCEiSearch...

Gene expression databases

BgeeiQ64523.
CleanExiMM_HIST2H2AB.
MM_HIST2H2AC.
ExpressionAtlasiQ64523. baseline and differential.
GenevestigatoriQ64523.

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]
ProtoNetiSearch...

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(1995) [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(2001) [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(2003) [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(2003) [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(2005) [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(2010) [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(2013) [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 6, 2006
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.