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A3LXE7 (H2A2_PICST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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 attributes

Sequence length131 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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-5; H2AK7ac = acetylated Lys-7; H2AK126su = sumoylated Lys-126; H2AS128ph = phosphorylated Ser-128.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
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 – 131130Histone H2A.2
PRO_0000297741

Regions

Motif128 – 1292[ST]-Q motif

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue51N6-acetyllysine By similarity
Modified residue71N6-acetyllysine By similarity
Modified residue1051N5-methylglutamine By similarity
Modified residue1281Phosphoserine By similarity
Cross-link126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
A3LXE7 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: C513C4FA8B6AD108

FASTA13113,915
        10         20         30         40         50         60 
MSGGKGKAGS SEKASTSRSA KAGLTFPVGR VHRLLRKGNY AQRVGSGAPV YLTSVLEYLA 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKSRII PRHLQLAIRN DEELNKLLGH VTIAQGGVLP NIHQSLLPAK 

       130 
KAKPGKASQE L 

« Hide

References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000500 Genomic DNA. Translation: ABN67443.1.
RefSeqXP_001385472.1. XM_001385435.1.

3D structure databases

ProteinModelPortalA3LXE7.
SMRA3LXE7. Positions 13-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4924.PICST_73490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4840027.
KEGGpic:PICST_73490.

Phylogenomic databases

HOGENOMHOG000234652.
KOK11251.
OMAVPARENI.

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 nameH2A2_PICST
AccessionPrimary (citable) accession number: A3LXE7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: April 3, 2007
Last modified: February 19, 2014
This is version 47 of the entry and version 1 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