CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018916
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2A type 1-C 
Protein Synonyms/Alias
 Histone H2A/l 
Gene Name
 HIST1H2AC 
Gene Synonyms/Alias
 H2AFL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKQGGKARAacetylation[1, 2, 3]
10GRGKQGGKARAKAKSacetylation[3]
10GRGKQGGKARAKAKSsuccinylation[4]
14QGGKARAKAKSRSSRacetylation[3]
16GKARAKAKSRSSRAGacetylation[3]
96RNDEELNKLLGRVTIsuccinylation[4]
96RNDEELNKLLGRVTIubiquitination[5, 6, 7]
119IQAVLLPKKTESHHKubiquitination[6]
120QAVLLPKKTESHHKAubiquitination[6]
126KKTESHHKAKGK***acetylation[3]
128TESHHKAKGK*****acetylation[3]
130SHHKAKGK*******acetylation[3]
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] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [4] Lysine succinylation and lysine malonylation in histones.
 Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, Boeke JD, Zhao Y.
 Mol Cell Proteomics. 2012 May;11(5):100-7. [PMID: 22389435]
 [5] 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]
 [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] 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 ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 60
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK 120
TESHHKAKGK 130 
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.