CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001947
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H3 
Protein Synonyms/Alias
  
Gene Name
 His3; His3:CG31613; His3:CG33803; His3:CG33806; His3:CG33809; His3:CG33812; His3:CG33815; His3:CG33818; His3:CG33821; His3:CG33824; His3:CG33827; His3:CG33830; His3:CG33833; His3:CG33836; His3:CG33839; His3:CG33842; His3:CG33845; His3:CG33848; His3:CG33851; His3:CG33854; His3:CG33857; His3:CG33860; His3:CG33863; His3:CG33866 
Gene Synonyms/Alias
 CG31613; CG33803; CG33806; CG33809; CG33812; CG33815; CG33818; CG33821; CG33824; CG33827; CG33830; CG33833; CG33836; CG33839; CG33842; CG33845; CG33848; CG33851; CG33854; CG33857; CG33860; CG33863; CG33866 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
10RTKQTARKSTGGKAPacetylation[1]
15ARKSTGGKAPRKQLAacetylation[1, 2]
19TGGKAPRKQLATKAAacetylation[1, 3]
24PRKQLATKAARKSAPacetylation[2]
28LATKAARKSAPATGGacetylation[4, 5]
37APATGGVKKPHRYRPacetylation[5]
38PATGGVKKPHRYRPGacetylation[5]
57REIRRYQKSTELLIRsuccinylation[6]
80REIAQDFKTDLRFQSacetylation[5]
80REIAQDFKTDLRFQSsuccinylation[6]
123KRVTIMPKDIQLARRacetylation[5]
Reference
 [1] Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP.
 Crump NT, Hazzalin CA, Bowers EM, Alani RM, Cole PA, Mahadevan LC.
 Proc Natl Acad Sci U S A. 2011 May 10;108(19):7814-9. [PMID: 21518915]
 [2] Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4.
 Sobel RE, Cook RG, Perry CA, Annunziato AT, Allis CD.
 Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1237-41. [PMID: 7862667]
 [3] A combination of different mass spectroscopic techniques for the analysis of dynamic changes of histone modifications.
 Bonaldi T, Imhof A, Regula JT.
 Proteomics. 2004 May;4(5):1382-96. [PMID: 15188406]
 [4] CBP-mediated acetylation of histone H3 lysine 27 antagonizes Drosophila Polycomb silencing.
 Tie F, Banerjee R, Stratton CA, Prasad-Sinha J, Stepanik V, Zlobin A, Diaz MO, Scacheri PC, Harte PJ.
 Development. 2009 Sep;136(18):3131-41. [PMID: 19700617]
 [5] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702]
 [6] 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
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
 REGION 6 11 Su(var)205 chromodomain-binding.
 MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
 MOD_RES 5 5 N6-methyllysine; alternate.
 MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
 MOD_RES 10 10 N6-methyllysine; alternate.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 15 15 N6,N6-dimethyllysine; alternate.
 MOD_RES 15 15 N6-acetyllysine; alternate.
 MOD_RES 15 15 N6-methyllysine; alternate.
 MOD_RES 19 19 N6-acetyllysine.
 MOD_RES 24 24 N6-acetyllysine.
 MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
 MOD_RES 28 28 N6-methyllysine; alternate.
 MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
 MOD_RES 37 37 N6-methyllysine; alternate.
 MOD_RES 38 38 N6,N6-dimethyllysine; alternate.
 MOD_RES 38 38 N6-methyllysine; alternate.
 MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
 MOD_RES 80 80 N6-methyllysine; alternate.  
Keyword
 3D-structure; Acetylation; Chromosome; Complete proteome; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 136 AA 
Protein Sequence
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 60
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI 120
MPKDIQLARR IRGERA 136 
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.
 IPR000164; Histone_H3. 
Pfam
 PF00125; Histone 
SMART
 SM00428; H3 
PROSITE
 PS00322; HISTONE_H3_1
 PS00959; HISTONE_H3_2 
PRINTS
 PR00622; HISTONEH3.