A1A4R1 (H2A2C_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified July 9, 2014. Version 54. History...
Names and origin
|Protein names||Recommended name:|
Histone H2A type 2-C
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||129 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
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.
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. 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 similarity.
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 By similarity.
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 By similarity.
Belongs to the histone H2A family.
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: InterPro
Inferred from electronic annotation. Source: UniProtKB-KWnucleus
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 129||128||Histone H2A type 2-C||PRO_0000281917|
Amino acid modifications
|Modified residue||2||1||N-acetylserine By similarity|
|Modified residue||2||1||Phosphoserine; by RPS6KA5 By similarity|
|Modified residue||4||1||Citrulline; alternate By similarity|
|Modified residue||4||1||Symmetric dimethylarginine; by PRMT5; alternate By similarity|
|Modified residue||6||1||N6-acetyllysine By similarity|
|Modified residue||10||1||N6-acetyllysine By similarity|
|Modified residue||37||1||N6-crotonyllysine By similarity|
|Modified residue||105||1||N5-methylglutamine By similarity|
|Modified residue||119||1||N6-crotonyllysine By similarity|
|Modified residue||120||1||N6-crotonyllysine; alternate By similarity|
|Modified residue||121||1||Phosphothreonine; by VPRBP By similarity|
|Modified residue||123||1||Phosphoserine By similarity|
|Modified residue||125||1||N6-crotonyllysine By similarity|
|Cross-link||14||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity|
|Cross-link||16||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity|
|Cross-link||120||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity|
|BC126824 mRNA. Translation: AAI26825.1.|
|RefSeq||NP_001075189.1. NM_001081720.2. |
3D structure databases
|SMR||A1A4R1. Positions 14-119. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
Enzyme and pathway databases
|Reactome||REACT_214934. Cell Cycle. |
Family and domain databases
|Gene3D||22.214.171.124. 1 hit. |
|InterPro||IPR009072. Histone-fold. |
|Pfam||PF00125. Histone. 1 hit. |
|PRINTS||PR00620. HISTONEH2A. |
|SMART||SM00414. H2A. 1 hit. |
|SUPFAM||SSF47113. SSF47113. 1 hit. |
|PROSITE||PS00046. HISTONE_H2A. 1 hit. |
|Accession||Primary (citable) accession number: A1A4R1|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families