Q74ZL4 (H2A1_ASHGO) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 64. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]|
|Taxonomic identifier||284811 [NCBI]|
|Taxonomic lineage||Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium ›|
|Sequence length||131 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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.
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.
The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
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 by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint By similarity.
Sumoylation on Lys-126 may lead to transcriptional repression By similarity.
Acetylated by ESA1 to form H2AK4ac and H2AK7ac By similarity.
In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated Probable.
Belongs to the histone H2A family.
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-4; H2AK7ac = acetylated Lys-7; H2AS128ph = phosphorylated Ser-128.
The sequence AAS54674.1 differs from that shown. Reason: Erroneous initiation.
|Biological process||DNA damage|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWnucleosome assembly
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 – 131||130||Histone H2A.1||PRO_0000055205|
|Motif||128 – 129||2||[ST]-Q motif|
|Site||119||1||Not ubiquitinated Probable|
Amino acid modifications
|Modified residue||2||1||N-acetylserine By similarity|
|Modified residue||4||1||N6-acetyllysine By similarity|
|Modified residue||7||1||N6-acetyllysine By similarity|
|Modified residue||128||1||Phosphoserine By similarity|
|Cross-link||126||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|||"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."|
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
|AE016820 Genomic DNA. Translation: AAS54674.1. Different initiation.|
|RefSeq||NP_986850.1. NM_211912.1. |
3D structure databases
|SMR||Q74ZL4. Positions 16-125. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||18.104.22.168. 1 hit. |
|InterPro||IPR009072. Histone-fold. |
|Pfam||PF00125. Histone. 1 hit. |
|PRINTS||PR00620. HISTONEH2A. |
|SMART||SM00414. H2A. 1 hit. |
|SUPFAM||SSF47113. Histone-fold. 1 hit. |
|PROSITE||PS00046. HISTONE_H2A. 1 hit. |
|Accession||Primary (citable) accession number: Q74ZL4|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Fungal Protein Annotation Program|
Index of protein domains and families