UniProt Accession

 H31T_HUMAN; Q16695; B2R5K3; Q6FGU4 

Genbank Protein ID

 Z49861; AF531308; CR542013; AK312217; AL139288; CH471098; BC069079; BC101837; BC101839 

Genbank Nucleotide ID

 CAA90020.1; AAN39284.1; CAG46810.1; BAG35150.1; CAI23333.1; EAW69877.1; AAH69079.1; AAI01838.1; AAI01840.1 

Protein Name

 Histone H3.1t 

Protein Synonyms/Alias

 H3/t; H3t; H3/g 

Gene Name

 HIST3H3 

Gene Synonyms/Alias

 H3FT 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
19	TGGKAPRKQLATKVA	acetylation	[1, 2]
24	PRKQLATKVARKSAP	acetylation	[1, 2]
28	LATKVARKSAPATGG	methylation	[3]
37	APATGGVKKPHRYRP	ubiquitination	[4]
57	REIRRYQKSTELLIR	ubiquitination	[4, 5]
80	REIAQDFKTDLRFQS	ubiquitination	[4, 5]
123	KRVTIMPKDIQLARR	ubiquitination	[4, 5]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

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 GSG2 (By
 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-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 (By
 MOD_RES 10 10 N6,N6-dimethyllysine; alternate (By
 MOD_RES 10 10 N6-acetyllysine; alternate (By
 MOD_RES 10 10 N6-methyllysine; alternate (By
 MOD_RES 11 11 Phosphoserine; by AURKB, AURKC, RPS6KA3,
 MOD_RES 12 12 Phosphothreonine; by PKC (By similarity).
 MOD_RES 15 15 N6-acetyllysine (By similarity).
 MOD_RES 18 18 Asymmetric dimethylarginine; by CARM1;
 MOD_RES 18 18 Citrulline; alternate (By similarity).
 MOD_RES 19 19 N6-acetyllysine; alternate.
 MOD_RES 19 19 N6-methyllysine; alternate (By
 MOD_RES 24 24 N6-acetyllysine; alternate.
 MOD_RES 24 24 N6-methyllysine; alternate (By
 MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 28 28 N6,N6-dimethyllysine; alternate (By
 MOD_RES 28 28 N6-acetyllysine; alternate (By
 MOD_RES 28 28 N6-methyllysine; alternate (By
 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-methyllysine; by EHMT2; alternate (By
 MOD_RES 58 58 Phosphoserine.
 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.
 MOD_RES 108 108 Phosphothreonine (By similarity).
 MOD_RES 123 123 N6-methyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Chromosome; Citrullination; Complete proteome; DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 136 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
 GO:0000723; P:telomere maintenance; TAS:Reactome. 

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.