UniProt Accession

 H31_TETTH; P69150; P15511; P92147; Q95047 

Genbank Protein ID

 M87304; M87504; M11142; M11143 

Genbank Nucleotide ID

 AAC37190.1; AAC37189.1; AAA30115.1; AAA30116.1 

Protein Name

 Histone H3 

Protein Synonyms/Alias

 H3S; Histone H3-I/H3-II; Major histone H3; H3F 

Gene Name

 HHT1; HHT2 

Gene Synonyms/Alias

 TTHERM_00570560; TTHERM_00189180 

Created Date

 July 27, 2013 

Organism

 Tetrahymena thermophila 

NCBI Taxa ID

 5911 

Lysine Modification

Position	Peptide	Type	References
5	***MARTKQTARKST	acetylation	[1]
10	RTKQTARKSTGAKAP	acetylation	[1, 2, 3]
15	ARKSTGAKAPRKQLA	acetylation	[1, 2, 3]
19	TGAKAPRKQLASKAA	acetylation	[1, 2]
24	PRKQLASKAARKSAP	acetylation	[1, 2]
37	APATGGIKKPHRFRP	acetylation	[1, 4]
57	REIRKYQKSTDLLIR	acetylation	[1]

Reference

 [1] Organismal differences in post-translational modifications in histones H3 and H4.
 Garcia BA, Hake SB, Diaz RL, Kauer M, Morris SA, Recht J, Shabanowitz J, Mishra N, Strahl BD, Allis CD, Hunt DF.
 J Biol Chem. 2007 Mar 9;282(10):7641-55. [PMID: 17194708]
 [2] Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. Evidence for functionally distinct H4 acetylation sites.
 Chicoine LG, Schulman IG, Richman R, Cook RG, Allis CD.
 J Biol Chem. 1986 Jan 25;261(3):1071-6. [PMID: 3080415]
 [3] 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]
 [4] Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.
 Morris SA, Rao B, Garcia BA, Hake SB, Diaz RL, Shabanowitz J, Hunt DF, Allis CD, Lieb JD, Strahl BD.
 J Biol Chem. 2007 Mar 9;282(10):7632-40. [PMID: 17189264] 

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. H3 is deposited into chromatin exclusively through a DNA replication-coupled pathway that can be associated with either DNA duplication or DNA repair synthesis during meiotic homologous recombination. 

Sequence Annotation

 MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
 MOD_RES 5 5 N6-acetyllysine; alternate.
 MOD_RES 5 5 N6-methyllysine; alternate.
 MOD_RES 10 10 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 10 10 N6-acetyllysine; alternate.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 15 15 N6-acetyllysine.
 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-acetyllysine; alternate.
 MOD_RES 28 28 N6-methyllysine; alternate.
 MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
 MOD_RES 37 37 N6-acetyllysine; alternate.
 MOD_RES 37 37 N6-methyllysine; alternate.
 MOD_RES 57 57 N6-acetyllysine; alternate.
 MOD_RES 57 57 N6-methyllysine; alternate.
 MOD_RES 80 80 N6-methyllysine.  

Keyword

 Acetylation; Chromosome; Direct protein sequencing; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 136 AA 

Protein Sequence

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.