Q6BKW8 · H2A1_DEBHA
- ProteinHistone H2A.1
- GeneHTA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids130 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Features
Showing features for site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 119 | Not ubiquitinated | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameHistone H2A.1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Debaryomyces
Accessions
- Primary accessionQ6BKW8
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylserine | |||
Chain | PRO_0000228728 | 2-130 | Histone H2A.1 | ||
Modified residue | 5 | N6-acetyllysine | |||
Modified residue | 7 | N6-acetyllysine | |||
Modified residue | 105 | N5-methylglutamine | |||
Modified residue | 127 | Phosphoserine | |||
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
- PTM
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 region, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-22 | Disordered | |||
Motif | 127-128 | [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 statusComplete
- Length130
- Mass (Da)13,861
- Last updated2007-01-23 v3
- ChecksumE5C741FBA63A57D2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR382138 EMBL· GenBank· DDBJ | CAG89536.1 EMBL· GenBank· DDBJ | Genomic DNA |