A1CJ10 (H2A_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2A

Gene names

Name:	hta1
ORF Names:	ACLA_033370

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus clavatus

Protein attributes

Sequence length	133 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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-9; H2AS128ph = phosphorylated Ser-130.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 133	132	Histone H2A		PRO_0000297730
Regions
	Motif	130 – 131	2	[ST]-Q motif
Sites
	Site	120	1	Not ubiquitinated Probable
Amino acid modifications
	Modified residue	5	1	N6-acetyllysine By similarity
	Modified residue	9	1	N6-acetyllysine By similarity
	Modified residue	130	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1CJ10 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 71C5A26F88D96EAE	FASTA	133	14,092
	10 20 30 40 50 60 MTGGKSGGKA SGSKNAQSRS SKAGLAFPVG RVHRLLRKGN YAQRVGAGAP VYLAAVLEYL 70 80 90 100 110 120 AAEILELAGN AARDNKKTRI IPRHLQLAIR NDEELNKLLG HVTIAQGGVL PNIHQNLLPK 130 KTPKSGKGPS QEL

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027056 Genomic DNA. Translation: EAW09134.1.
RefSeq	XP_001270560.1. XM_001270559.1.
3D structure databases
ProteinModelPortal	A1CJ10.
SMR	A1CJ10. Positions 17-125.
ModBase	Search...
Protein-protein interaction databases
STRING	5057.CADACLAP00003871.
Proteomic databases
PRIDE	A1CJ10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00003951; CADACLAP00003871; CADACLAG00003951.
GeneID	4703215.
KEGG	act:ACLA_033370.
Phylogenomic databases
eggNOG	COG5262.
HOGENOM	HOG000234652.
KO	K11251.
OrthoDB	EOG4GQTFP.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

H2A_ASPCL

Accession

Primary (citable) accession number: A1CJ10

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program