CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009868
UniProt Accession
Genbank Protein ID
  
Genbank Nucleotide ID
  
Protein Name
 Histone H3.1 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
5***MARTKQTARKSTacetylation[1]
9ARTKQTARKSTGGKAsuccinylation[2]
10RTKQTARKSTGGKAPacetylation[1, 3, 4]
15ARKSTGGKAPRKQLAacetylation[1, 4, 5, 6]
19TGGKAPRKQLATKAAacetylation[1, 4]
24PRKQLATKAARKSAPacetylation[1, 4, 5, 6]
28LATKAARKSAPATGGacetylation[3]
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] Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.
 Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H, Kim J, Woo J, Kim JH, Choi BH, He B, Chen W, Zhang S, Cerione RA, Auwerx J, Hao Q, Lin H.
 Science. 2011 Nov 11;334(6057):806-9. [PMID: 22076378]
 [3] Complete amino-acid sequence of calf-thymus histone 3.
 DeLange RJ, Hooper JA, Smith EL.
 Proc Natl Acad Sci U S A. 1972 Apr;69(4):882-4. [PMID: 4502939]
 [4] Amino-terminal sequences and sites of in vivo acetylation of trout-testis histones 3 and IIb 2 .
 Candido EP, Dixon GH.
 Proc Natl Acad Sci U S A. 1972 Aug;69(8):2015-9. [PMID: 4506069]
 [5] Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3.
 DeLange RJ, Hooper JA, Smith EL.
 J Biol Chem. 1973 May 10;248(9):3261-74. [PMID: 4735580]
 [6] Calf thymus histone 3: sequences of the amino-and carboxyl-terminal regions and of the regions containing lysyl residues modified by acetylation and methylation.
 DeLange RJ, Smith EL, Bonner J.
 Biochem Biophys Res Commun. 1970 Aug 24;40(4):989-93. [PMID: 5531405
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 3 3 Asymmetric dimethylarginine; by PRMT6 (By
 MOD_RES 4 4 Phosphothreonine (By similarity).
 MOD_RES 5 5 Allysine; alternate (By similarity).
 MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 5 5 N6,N6-dimethyllysine; alternate (By
 MOD_RES 5 5 N6-acetyllysine; alternate (By
 MOD_RES 5 5 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 5 5 N6-methyllysine; alternate (By
 MOD_RES 7 7 Phosphothreonine; by PKC (By similarity).
 MOD_RES 9 9 Citrulline; alternate (By similarity).
 MOD_RES 9 9 Symmetric dimethylarginine; by PRMT5;
 MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
 MOD_RES 10 10 N6-acetyllysine; alternate (By
 MOD_RES 10 10 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 10 10 N6-methyllysine; alternate.
 MOD_RES 11 11 Phosphoserine; by AURKB, AURKC, RPS6KA3,
 MOD_RES 12 12 Phosphothreonine; by PKC and CHEK1 (By
 MOD_RES 15 15 N6-acetyllysine.
 MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
 MOD_RES 18 18 Citrulline; alternate (By similarity).
 MOD_RES 19 19 N6-acetyllysine; alternate (By
 MOD_RES 19 19 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 19 19 N6-methyllysine; alternate (By
 MOD_RES 24 24 N6-acetyllysine; alternate.
 MOD_RES 24 24 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 24 24 N6-methyllysine; alternate (By
 MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
 MOD_RES 28 28 N6-acetyllysine; alternate (By
 MOD_RES 28 28 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 28 28 N6-methyllysine; alternate.
 MOD_RES 29 29 Phosphoserine; by AURKB, AURKC and
 MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 37 37 N6,N6-dimethyllysine; alternate (By
 MOD_RES 37 37 N6-acetyllysine; alternate (By
 MOD_RES 37 37 N6-methyllysine; alternate (By
 MOD_RES 38 38 N6-methyllysine (By similarity).
 MOD_RES 42 42 Phosphotyrosine (By similarity).
 MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 57 57 N6-acetyllysine; alternate (By
 MOD_RES 57 57 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate (By
 MOD_RES 58 58 Phosphoserine (By similarity).
 MOD_RES 65 65 N6-methyllysine (By similarity).
 MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 80 80 N6,N6-dimethyllysine; alternate (By
 MOD_RES 80 80 N6-acetyllysine; alternate (By
 MOD_RES 80 80 N6-methyllysine; alternate (By
 MOD_RES 81 81 Phosphothreonine (By similarity).
 MOD_RES 108 108 Phosphothreonine (By similarity).
 MOD_RES 123 123 N6-methyllysine (By similarity).
 DISULFID 97 111 In monomeric form.
 DISULFID 97 97 Interchain; in polymeric form; alternate.
 DISULFID 111 111 Interchain; in polymeric form; alternate.  
Keyword
 Acetylation; Chromosome; Citrullination; Complete proteome; Direct protein sequencing; Disulfide bond; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 136 AA 
Protein Sequence
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 60
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY 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.
 GO:0060968; P:regulation of gene silencing; IEA:Compara. 
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.