Q64522 (H2A2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2A type 2-B

Alternative name(s):
H2a-613A

Gene names

Name:

Hist2h2ab

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
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.
Post-translational modification	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 By similarity. 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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. Ref.2 Ref.3 Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1 By similarity. The chromatin-associated form is phosphorylated on Thr-121 during mitosis By similarity. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
Sequence similarities	Belongs to the histone H2A family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 – 130	129	Histone H2A type 2-B		PRO_0000227506
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 Probable
	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) Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q64522 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: ECE2F541F53F5FD7	FASTA	130	14,013
	10 20 30 40 50 60 MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT 70 80 90 100 110 120 AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK 130 TESHKPGKNK

References

[1]	"Characterization of the 55-kb mouse histone gene cluster on chromosome 3." Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F. Genome Res. 6:702-714(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[2]	"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation." de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N. Dev. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-120.
[3]	"Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation." Fang J., Chen T., Chadwick B., Li E., Zhang Y. J. Biol. Chem. 279:52812-52815(2004) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-120.
[4]	"Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells." Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A. Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62673 Genomic DNA. Translation: AAB04767.1.
IPI	IPI00623951.
RefSeq	NP_835585.3. NM_178213.3.
UniGene	Mm.435460.
3D structure databases
ProteinModelPortal	Q64522.
SMR	Q64522. Positions 14-119.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64522. 1 interaction.
STRING	10090.ENSMUSP00000072858.
PTM databases
PhosphoSite	Q64522.
Proteomic databases
PaxDb	Q64522.
PRIDE	Q64522.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000073115; ENSMUSP00000072858; ENSMUSG00000063689.
GeneID	621893.
KEGG	mmu:621893.
UCSC	uc008qmh.1. mouse.
Organism-specific databases
CTD	317772.
MGI	MGI:2448314. Hist2h2ab.
Phylogenomic databases
eggNOG	COG5262.
GeneTree	ENSGT00690000101783.
HOGENOM	HOG000234652.
HOVERGEN	HBG009342.
InParanoid	Q64522.
KO	K11251.
OMA	LAIHNDE.
OrthoDB	EOG4TXBTD.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse). REACT_75800. Meiotic Synapsis (mouse).
Gene expression databases
Bgee	Q64522.
CleanEx	MM_HIST2H2AB.
Genevestigator	Q64522.
GermOnline	ENSMUSG00000063689. Mus musculus.
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...
Other
NextBio	416006.
SOURCE	Search...

Entry information

Entry name

H2A2B_MOUSE

Accession

Primary (citable) accession number: Q64522

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program