CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H4 
Protein Synonyms/Alias
 H4.1 
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
6**MSGRGKGGKGLGKacetylation[1, 2, 3]
9SGRGKGGKGLGKGGAacetylation[1, 2, 3]
13KGGKGLGKGGAKRHRacetylation[1, 2, 3]
17GLGKGGAKRHRKVLRacetylation[1, 2, 3, 4, 5]
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] Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4.
 Couppez M, Martin-Ponthieu A, Sautière P.
 J Biol Chem. 1987 Feb 25;262(6):2854-60. [PMID: 3818624]
 [3] Modification of histones during spermiogenesis in trout: a molecular mechanism for altering histone binding to DNA.
 Sung MT, Dixon GH.
 Proc Natl Acad Sci U S A. 1970 Nov;67(3):1616-23. [PMID: 5274484]
 [4] Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine.
 DeLange RJ, Fambrough DM, Smith EL, Bonner J.
 J Biol Chem. 1969 Jan 25;244(2):319-34. [PMID: 5773298]
 [5] Structural analysis of the glycine-rich, arginine-rich histone. 3. Sequence of the amino-terminal half of the molecule containing the modified lysine residues and the total sequence.
 Ogawa Y, Quagliarotti G, Jordan J, Taylor CW, Starbuck WC, Busch H.
 J Biol Chem. 1969 Aug 25;244(16):4387-92. [PMID: 5817359
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
 DNA_BIND 17 21
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine (By similarity).
 MOD_RES 4 4 Asymmetric dimethylarginine; by PRMT1;
 MOD_RES 4 4 Citrulline; alternate (By similarity).
 MOD_RES 4 4 Omega-N-methylarginine; by PRMT1;
 MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5 and
 MOD_RES 6 6 N6-acetyllysine; alternate (By
 MOD_RES 6 6 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 9 9 N6-acetyllysine; alternate (By
 MOD_RES 9 9 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 13 13 N6-acetyllysine; alternate (By
 MOD_RES 13 13 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 17 17 N6-acetyllysine; alternate.
 MOD_RES 17 17 N6-crotonyl-L-lysine; alternate (By
 MOD_RES 21 21 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 21 21 N6,N6-dimethyllysine; alternate.
 MOD_RES 21 21 N6-methyllysine; alternate.
 MOD_RES 32 32 N6-acetyllysine (By similarity).
 MOD_RES 48 48 Phosphoserine; by PAK2 (By similarity).
 MOD_RES 52 52 Phosphotyrosine (By similarity).
 MOD_RES 89 89 Phosphotyrosine (By similarity).
 MOD_RES 92 92 N6-acetyllysine; alternate (By
 CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Chromosome; Citrullination; Complete proteome; Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 103 AA 
Protein Sequence
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK 60
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG 103 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0045653; P:negative regulation of megakaryocyte differentiation; IEA:Compara.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 
Interpro
 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR001951; Histone_H4.
 IPR019809; Histone_H4_CS. 
Pfam
 PF00125; Histone 
SMART
 SM00417; H4 
PROSITE
 PS00047; HISTONE_H4 
PRINTS
 PR00623; HISTONEH4.