CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005115
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A type 1 
Protein Synonyms/Alias
  
Gene Name
 Hist1h2ab; Hist1h2ac; Hist1h2ad; Hist1h2ae; Hist1h2ag; Hist1h2ai; Hist1h2an; Hist1h2ao 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKQGGKARAacetylation[1, 2, 3, 4, 5, 6]
10GRGKQGGKARAKAKTacetylation[2, 3, 4, 5, 6]
37RVHRLLRKGNYSERVcrotonylation[7]
96RNDEELNKLLGRVTIacetylation[3, 4, 5, 8, 9]
96RNDEELNKLLGRVTIphosphoglycerylation[10]
96RNDEELNKLLGRVTIsuccinylation[5]
96RNDEELNKLLGRVTIubiquitination[11]
119IQAVLLPKKTESHHKcrotonylation[7]
Reference
 [1] Acetylation of trout testis histones in vivo. Site of the modification in histone IIb 1 .
 Peter E, Candido M, Dixon GH.
 J Biol Chem. 1972 Jun 25;247(12):3868-73. [PMID: 5033394]
 [2] Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain.
 Tweedie-Cullen RY, Reck JM, Mansuy IM.
 J Proteome Res. 2009 Nov;8(11):4966-82. [PMID: 19737024]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] 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]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [7] Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.
 Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, Lu Z, Ye Z, Zhu Q, Wysocka J, Ye Y, Khochbin S, Ren B, Zhao Y.
 Cell. 2011 Sep 16;146(6):1016-28. [PMID: 21925322]
 [8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [9] 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]
 [10] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [11] 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
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; alternate (By similarity).
 MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5;
 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 (By
 MOD_RES 121 121 Phosphothreonine (By similarity).
 MOD_RES 126 126 N6-crotonyl-L-lysine (By similarity).
 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 SERVGAGAPV YLAAVLEYLT 60
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR 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.