CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001161
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Core histone macro-H2A.1 
Protein Synonyms/Alias
 Histone macroH2A1; mH2A1; Histone H2A.y; H2A/y; Medulloblastoma antigen MU-MB-50.205 
Gene Name
 H2AFY 
Gene Synonyms/Alias
 MACROH2A1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18TKTSRSAKAGVIFPVubiquitination[1]
116IHPELLAKKRGSKGKubiquitination[1]
117HPELLAKKRGSKGKLubiquitination[1]
123KKRGSKGKLEAIITPubiquitination[1]
167KKQGEVSKAASADSTubiquitination[1]
189GFTVLSTKSLFLGQKubiquitination[1]
Reference
 [1] 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
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.
 MOD_RES 123 123 N6,N6-dimethyllysine (Probable).
 MOD_RES 129 129 Phosphothreonine.
 MOD_RES 170 170 Phosphoserine.
 MOD_RES 173 173 Phosphoserine.
 MOD_RES 178 178 Phosphothreonine.
 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; 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 QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA 180
DGFTVLSTKS LFLGQKLQVV QADIASIDSD AVVHPTNTDF YIGGEVGNTL EKKGGKEFVE 240
AVLELRKKNG PLEVAGAAVS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD 300
KKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVSTMS SSIKTVYFVL FDSESIGIYV 360
QEMAKLDAN 369 
Gene Ontology
 GO:0001740; C:Barr body; IDA:MGI.
 GO:0000793; C:condensed chromosome; IEA:Compara.
 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007549; P:dosage compensation; IDA:MGI.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB. 
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.