CPLM-022495

Genbank Nucleotide ID

Core histone macro-H2A.2

Protein Synonyms/Alias

Histone macroH2A2; mH2A2

Homo sapiens (Human)

Position	Peptide	Type	References
12	SGKKKMSKLSRSARA	acetylation	[1]
116	IHPELLAKKRGTKGK	ubiquitination	[2, 3, 4, 5, 6]
117	HPELLAKKRGTKGKS	ubiquitination	[7]
123	KKRGTKGKSETILSP	ubiquitination	[4, 5, 6]
239	ALEKAGGKEFLETVK	ubiquitination	[5, 6]
246	KEFLETVKELRKSQG	ubiquitination	[3]
332	TAAQVTLKAISAHFD	ubiquitination	[3]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]

Functional Description

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 stable X chromosome inactivation.

DOMAIN 2 117 Histone H2A.
DOMAIN 184 370 Macro.

3D-structure; Chromatin regulator; Chromosome; Complete proteome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0001740; C:Barr body; IDA:MGI.
GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
GO:0007549; P:dosage compensation; IDA:MGI.
GO:0006334; P:nucleosome assembly; IEA:InterPro.

IPR002589; A1pp.
IPR021171; Core_histone_macro-H2A.
IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR002119; Histone_H2A.

PF00125; Histone
PF01661; Macro

PR00620; HISTONEH2A.