P04912 · H2A2_YEAST
- ProteinHistone H2A.2
- GeneHTA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids132 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Present with 32100 molecules/cell in log phase SD medium.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 120 | Not ubiquitinated | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Cellular Component | replication fork protection complex | |
Molecular Function | DNA binding | |
Molecular Function | nucleosomal DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | chromatin organization | |
Biological Process | DNA repair | |
Biological Process | heterochromatin formation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H2A.2
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP04912
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 129 | Causes hypersensitivity to DNA-damage-inducing agents. | ||||
Sequence: S → A | ||||||
Mutagenesis | 129 | No effect. | ||||
Sequence: S → E or T |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000055327 | 2-132 | Histone H2A.2 | |||
Sequence: SGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKTAKASQEL | ||||||
Modified residue | 5 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 8 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 14 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 22 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 106 | N5-methylglutamine | ||||
Sequence: Q | ||||||
Modified residue | 120 | N6-malonyllysine | ||||
Sequence: K | ||||||
Cross-link | 127 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Modified residue | 129 | Phosphoserine | ||||
Sequence: S |
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 interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
N-acetylated by NAT4.
Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac.
Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239).
Sumoylated to from H2AK126su. May lead to transcriptional repression.
Keywords
- PTM
Proteomic databases
PTM databases
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. Interacts with NAP1.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 129-130 | [ST]-Q motif | ||||
Sequence: SQ |
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
- Length132
- Mass (Da)13,989
- Last updated2007-01-23 v2
- ChecksumE808C94A0363CD53
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V01305 EMBL· GenBank· DDBJ | CAA24612.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z26494 EMBL· GenBank· DDBJ | CAA81267.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35764 EMBL· GenBank· DDBJ | CAA84818.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY693115 EMBL· GenBank· DDBJ | AAT93134.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006936 EMBL· GenBank· DDBJ | DAA07119.1 EMBL· GenBank· DDBJ | Genomic DNA |