CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022711
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
116IHPELLAKKRGSKGKacetylation[1]
116IHPELLAKKRGSKGKubiquitination[2]
123KKRGSKGKLEAIITPacetylation[1, 3]
123KKRGSKGKLEAIITPubiquitination[2]
189GFTVLSTKSLFLGQKubiquitination[2]
285SPVWGADKCEELLEKacetylation[1, 3]
292KCEELLEKTVKNCLAacetylation[3]
292KCEELLEKTVKNCLAubiquitination[2]
307LADDRKLKSIAFPSIubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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
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 184 370 Macro.
 MOD_RES 18 18 N6-methyllysine (By similarity).
 MOD_RES 129 129 Phosphothreonine.
 MOD_RES 170 170 Phosphoserine (By similarity).
 MOD_RES 173 173 Phosphoserine (By similarity).
 MOD_RES 178 178 Phosphothreonine (By similarity).
 CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Chromatin regulator; Chromosome; Complete proteome; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 372 AA 
Protein Sequence
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI 60
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS 120
KGKLEAIITP PPAKKAKSPS QKKPVAKKTG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT 180
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE 240
FVEAVLELRK KNGPLEVAGA AISAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL 300
ADDRKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FMLFDSESIG 360
IYVQEMAKLD AN 372 
Gene Ontology
 GO:0001740; C:Barr body; ISO:MGI.
 GO:0005813; C:centrosome; TAS:MGI.
 GO:0000793; C:condensed chromosome; IDA:MGI.
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007549; P:dosage compensation; ISO:MGI.
 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.