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Q9HGX4 (H2A_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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.

Subcellular location

Nucleus. Chromosome.

Domain

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

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 By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the histone H2A family.

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-9; H2AK7ac = acetylated Lys-13; H2AS128ph = phosphorylated Ser-136.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 139138Histone H2A
PRO_0000055196

Regions

Motif136 – 1372[ST]-Q motif

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue91N6-acetyllysine By similarity
Modified residue131N6-acetyllysine By similarity
Modified residue1101N5-methylglutamine By similarity
Modified residue1361Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HGX4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB870B8978DD9CF7

FASTA13914,734
        10         20         30         40         50         60 
MSGKGKAGKS GGKAGSETKS MSRSSKAGLQ FPVGRVHRLL KKGNYAQRVG AGAPVYMAAV 

        70         80         90        100        110        120 
LEYLAAEILE LAGNAARDNK KQRIVPRHLQ LAIRNDEELH KLLGNVVISQ GGVVPHIAPE 

       130 
LLPSKSSKGK KDEGVSQEL 

« Hide

References

[1]"Efficient isolation of genes differentially expressed on cellulose by suppression subtractive hybridization in Agaricus bisporus."
Morales-Almora P., Thurston C.F.
Mycol. Res. 107:401-407(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: D649.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293758 mRNA. Translation: CAC03460.1.

3D structure databases

ProteinModelPortalQ9HGX4.
SMRQ9HGX4. Positions 18-128.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9HGX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAHLPKTES.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH2A_AGABI
AccessionPrimary (citable) accession number: Q9HGX4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 58 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families