P08844 · H2A_EMENI

Function

function

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-9; H2AS128ph = phosphorylated Ser-129.

Features

Showing features for site.

1132102030405060708090100110120130
TypeIDPosition(s)Description
Site120Not ubiquitinated

GO annotations

AspectTerm
Cellular Componentnucleosome
Cellular Componentnucleus
Molecular Functionnucleosomal DNA binding
Molecular Functionprotein heterodimerization activity
Molecular Functionstructural constituent of chromatin
Biological ProcessDNA repair
Biological Processheterochromatin formation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Histone H2A

Gene names

    • Name
      htaA
    • Synonyms
      hta1
    • ORF names
      AN3468

Organism names

Accessions

  • Primary accession
    P08844
  • Secondary accessions
    • C8VH97
    • Q5B7L2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00000553222-132Histone H2A
Modified residue5N6-acetyllysine
Modified residue9N6-acetyllysine
Modified residue106N5-methylglutamine
Modified residue129Phosphoserine

Post-translational modification

Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases mec1/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).
Acetylated by esa1 to form H2AK4ac and H2AK7ac.

Keywords

Interaction

Subunit

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

Structure

Family & Domains

Features

Showing features for compositional bias, region, motif.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues
Region1-24Disordered
Motif129-130[ST]-Q motif

Domain

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Sequence similarities

Belongs to the histone H2A family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    132
  • Mass (Da)
    13,979
  • Last updated
    2007-01-23 v2
  • Checksum
    538FACEA096EAE00
MTGGKSGGKASGSKNAQSRSSKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQNLLPKKTPKAGKGSQEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-22Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M18258
EMBL· GenBank· DDBJ
AAA33309.1
EMBL· GenBank· DDBJ
Genomic DNA
AACD01000058
EMBL· GenBank· DDBJ
EAA63008.1
EMBL· GenBank· DDBJ
Genomic DNA
BN001306
EMBL· GenBank· DDBJ
CBF82646.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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