CPLM-005601

Genbank Nucleotide ID

Protein Synonyms/Alias

H2a.x; H2ax; Hist5-2ax

Mus musculus (Mouse)

Position	Peptide	Type	References
6	**MSGRGKTGGKARA	acetylation	[1, 2, 3]
10	GRGKTGGKARAKAKS	acetylation	[1, 2, 3]
96	RNDEELNKLLGGVTI	ubiquitination	[4]
119	IQAVLLPKKSSATVG	acetylation	[2]
119	IQAVLLPKKSSATVG	ubiquitination	[5]
120	QAVLLPKKSSATVGP	ubiquitination	[4, 5]
128	SSATVGPKAPAVGKK	acetylation	[2]
128	SSATVGPKAPAVGKK	ubiquitination	[5]
134	PKAPAVGKKASQASQ	acetylation	[2]

[1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[4] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
[5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional Description

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C- terminal phosphorylation.

MOTIF 140 141 [ST]-Q motif.
MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 37 37 N6-acetyllysine; by CREBBP and EP300.
MOD_RES 140 140 Phosphoserine; by ATM, ATR and PRKDC.
MOD_RES 143 143 Phosphotyrosine; by WSTF.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; Cell cycle; Chromosome; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Meiosis; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000781; C:chromosome, telomeric region; IEA:Compara.
GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
GO:0001673; C:male germ cell nucleus; IDA:MGI.
GO:0000790; C:nuclear chromatin; IDA:MGI.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO:0005657; C:replication fork; IDA:MGI.
GO:0001741; C:XY body; IDA:MGI.
GO:0003684; F:damaged DNA binding; IDA:MGI.
GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
GO:0007126; P:meiosis; IEA:UniProtKB-KW.
GO:0006334; P:nucleosome assembly; IEA:InterPro.
GO:0007283; P:spermatogenesis; IMP:MGI.

IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR002119; Histone_H2A.

PS00046; HISTONE_H2A

PR00620; HISTONEH2A.