CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014907
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A type 2-A 
Protein Synonyms/Alias
 Histone H2A.2; Histone H2A/o 
Gene Name
 HIST2H2AA3; HIST2H2AA4 
Gene Synonyms/Alias
 H2AFO; HIST2H2AA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKQGGKARAacetylation[1, 2, 3]
96RNDEELNKLLGKVTIubiquitination[4, 5, 6, 7]
100ELNKLLGKVTIAQGGubiquitination[4, 5, 7]
119IQAVLLPKKTESHHKubiquitination[4, 7]
120QAVLLPKKTESHHKAubiquitination[7]
126KKTESHHKAKGK***ubiquitination[4]
128TESHHKAKGK*****ubiquitination[4]
Reference
 [1] Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase.
 Verreault A, Kaufman PD, Kobayashi R, Stillman B.
 Curr Biol. 1998 Jan 15;8(2):96-108. [PMID: 9427644]
 [2] Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates.
 Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y.
 J Biol Chem. 1999 Jan 15;274(3):1189-92. [PMID: 9880483]
 [3] Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry.
 Bonenfant D, Coulot M, Towbin H, Schindler P, van Oostrum J.
 Mol Cell Proteomics. 2006 Mar;5(3):541-52. [PMID: 16319397]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] 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
Functional Description
 Core component of nucleosome. 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. 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine; by RPS6KA5.
 MOD_RES 4 4 Citrulline.
 MOD_RES 6 6 N6-acetyllysine.
 MOD_RES 37 37 N6-crotonyl-L-lysine.
 MOD_RES 119 119 N6-crotonyl-L-lysine.
 MOD_RES 120 120 N6-crotonyl-L-lysine; alternate.
 MOD_RES 121 121 Phosphothreonine (Probable).
 MOD_RES 126 126 N6-crotonyl-L-lysine.
 CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Chromosome; Citrullination; Complete proteome; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 130 AA 
Protein Sequence
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT 60
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK 120
TESHHKAKGK 130 
Gene Ontology
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 
Interpro
 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR002119; Histone_H2A. 
Pfam
 PF00125; Histone 
SMART
 SM00414; H2A 
PROSITE
 PS00046; HISTONE_H2A 
PRINTS
 PR00620; HISTONEH2A.