CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003639
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A type 1 
Protein Synonyms/Alias
 H2A.1; Histone H2A/p 
Gene Name
 HIST1H2AG; HIST1H2AI; HIST1H2AK; HIST1H2AL; HIST1H2AM 
Gene Synonyms/Alias
 H2AFP; H2AFC; H2AFD; H2AFI; H2AFN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKQGGKARAacetylation[1, 2, 3, 4, 5, 6]
37RVHRLLRKGNYAERVubiquitination[7]
75GNAARDNKKTRIIPRmethylation[8]
76NAARDNKKTRIIPRHmethylation[8]
96RNDEELNKLLGKVTIacetylation[9, 10]
96RNDEELNKLLGKVTIubiquitination[11, 12]
100ELNKLLGKVTIAQGGmethylation[8]
100ELNKLLGKVTIAQGGubiquitination[12]
120QAVLLPKKTESHHKAubiquitination[12]
Reference
 [1] Patterns of histone acetylation.
 Thorne AW, Kmiciek D, Mitchelson K, Sautiere P, Crane-Robinson C.
 Eur J Biochem. 1990 Nov 13;193(3):701-13. [PMID: 2249688]
 [2] 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]
 [3] 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]
 [4] Tip60 acetylates six lysines of a specific class in core histones in vitro.
 Kimura A, Horikoshi M.
 Genes Cells. 1998 Dec;3(12):789-800. [PMID: 10096020]
 [5] 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]
 [6] Epigenetic control of T-helper-cell differentiation.
 Wilson CB, Rowell E, Sekimata M.
 Nat Rev Immunol. 2009 Feb;9(2):91-105. [PMID: 19151746]
 [7] 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]
 [8] Identification of novel histone post-translational modifications by peptide mass fingerprinting.
 Zhang L, Eugeni EE, Parthun MR, Freitas MA.
 Chromosoma. 2003 Aug;112(2):77-86. [PMID: 12937907]
 [9] 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]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] 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]
 [12] 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
 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 (By similarity).
 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 ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 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.