CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012733
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A type 2-C 
Protein Synonyms/Alias
 Histone H2A-GL101; Histone H2A/q 
Gene Name
 HIST2H2AC 
Gene Synonyms/Alias
 H2AFQ 
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]
14QGGKARAKAKSRSSRacetylation[4]
96RNDEELNKLLGKVTIubiquitination[5]
100ELNKLLGKVTIAQGGubiquitination[5]
119IQAVLLPKKTESHKAubiquitination[5, 6, 7, 8, 9, 10]
120QAVLLPKKTESHKAKubiquitination[5, 6, 7, 8, 9, 10, 11]
125PKKTESHKAKSK***ubiquitination[6, 11, 12]
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] 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]
 [5] 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]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
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 (By
 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.
 MOD_RES 123 123 Phosphoserine.
 MOD_RES 125 125 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
 129 AA 
Protein Sequence
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT 60
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK 120
TESHKAKSK 129 
Gene Ontology
 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB. 
Interpro
 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR002119; Histone_H2A. 
Pfam
 PF00125; Histone 
SMART
 SM00414; H2A 
PROSITE
 PS00046; HISTONE_H2A 
PRINTS
 PR00620; HISTONEH2A.