UniProt Accession

 H2AY_RAT; Q02874; O09140; Q63325 

Genbank Protein ID

 M99065; M99066; U79139; BC089093 

Genbank Nucleotide ID

 AAA41561.2; AAA41560.1; AAB38330.1; AAH89093.1 

Protein Name

 Core histone macro-H2A.1 

Protein Synonyms/Alias

 Histone macroH2A1; mH2A1; H2A.y; H2A/y 

Gene Name

 H2afy 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
116	IHPELLAKKRGSKGK	ubiquitination	[1]
117	HPELLAKKRGSKGKL	ubiquitination	[1]
123	KKRGSKGKLEAIITP	acetylation	[2]
123	KKRGSKGKLEAIITP	ubiquitination	[1]
134	IITPPPAKKAKSPSQ	acetylation	[2]
143	AKSPSQKKPVAKKTG	acetylation	[2]
147	SQKKPVAKKTGGKKG	acetylation	[2]

Reference

 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP- ribose, and may be involved in ADP-ribose-mediated chromatin modulation. 

Sequence Annotation

 DOMAIN 2 117 Histone H2A.
 DOMAIN 183 369 Macro.
 MOD_RES 18 18 N6-methyllysine (By similarity).
 MOD_RES 129 129 Phosphothreonine (By similarity).
 MOD_RES 169 169 Phosphoserine (By similarity).
 MOD_RES 172 172 Phosphoserine (By similarity).
 CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Alternative splicing; Chromatin regulator; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 371 AA 

Protein Sequence

Gene Ontology

 GO:0001740; C:Barr body; IEA:Compara.
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0000786; C:nucleosome; IDA:RGD.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007549; P:dosage compensation; IEA:Compara.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 

Interpro

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

Pfam

 PF00125; Histone
 PF01661; Macro 

SMART

 SM00506; A1pp
 SM00414; H2A 

PROSITE

 PS51154; MACRO 

PRINTS

 PR00620; HISTONEH2A.