CPLM-003637

Genbank Nucleotide ID

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
5	***MAGGKAGKDSGK	acetylation	[1, 2]
8	MAGGKAGKDSGKAKT	acetylation	[1, 2]
12	KAGKDSGKAKTKAVS	acetylation	[1, 2]
14	GKDSGKAKTKAVSRS	acetylation	[2]
102	EELDSLIKATIAGGG	acetylation	[3, 4]
102	EELDSLIKATIAGGG	succinylation	[4]
116	GVIPHIHKSLIGKKG	acetylation	[4]
116	GVIPHIHKSLIGKKG	ubiquitination	[5]
121	IHKSLIGKKGQQKTV	ubiquitination	[5]
122	HKSLIGKKGQQKTV*	ubiquitination	[5, 6]
126	IGKKGQQKTV*****	ubiquitination	[6]

[1] Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain.
Tweedie-Cullen RY, Reck JM, Mansuy IM.
J Proteome Res. 2009 Nov;8(11):4966-82. [PMID: 19737024]
[2] 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]
[3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[4] 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]
[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]
[6] 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]

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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Essential for early development.

REGION 2 17 Required for interaction with INCENP.
REGION 93 103 Required for interaction with INCENP.
MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 5 5 N6-acetyllysine (Probable).
MOD_RES 8 8 N6-acetyllysine (Probable).
MOD_RES 12 12 N6-acetyllysine (Probable).
MOD_RES 14 14 N6-acetyllysine (By similarity).
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; Chromosome; Complete proteome; Developmental protein; DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO:0005634; C:nucleus; IDA:MGI.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
GO:0006334; P:nucleosome assembly; IEA:InterPro.

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

PS00046; HISTONE_H2A

PR00620; HISTONEH2A.