UniProt Accession

 H31_MOUSE; P68433; P02295; P02296; P16106; Q05A97; Q3B7Z8; Q3B7Z9; Q5T009 

Genbank Protein ID

 X01684; M32460; M32462; X16496; U62670; U62672; AY158944; AY158945; AY158946; AY158952; Y12290; AK006742; AK018952; AK155722; AL590388; AL589651; AL589651; BC107285; BC107287; BC115816; BC116383; BC125355; BC125357 

Genbank Nucleotide ID

 CAA25839.1; AAA37811.1; AAA37813.1; CAA34512.1; AAB04763.1; AAB04765.1; AAO06254.1; AAO06255.1; AAO06256.1; AAO06262.1; CAA72968.1; BAB24722.1; BAB31493.1; BAE33402.1; CAI25837.1; CAI24113.1; CAI24105.1; AAI07286.1; AAI07288.1; AAI15817.1; AAI16384.1; AAI25356.1; AAI25358.1 

Protein Name

 Histone H3.1 

Protein Synonyms/Alias

  

Gene Name

 Hist1h3a; Hist1h3g; Hist1h3h; Hist1h3i 

Gene Synonyms/Alias

 H3a; H3.1-221; H3g; H3.1-291; H3h; H3.1-I; H3i 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
5	***MARTKQTARKST	acetylation	[1]
10	RTKQTARKSTGGKAP	acetylation	[1, 2, 3, 4]
15	ARKSTGGKAPRKQLA	acetylation	[1, 2, 3, 4, 5]
19	TGGKAPRKQLATKAA	acetylation	[1, 2, 3, 4]
24	PRKQLATKAARKSAP	acetylation	[1, 2, 3, 5]
28	LATKAARKSAPATGG	acetylation	[1, 6, 7, 8]
28	LATKAARKSAPATGG	succinylation	[8]
37	APATGGVKKPHRYRP	acetylation	[7]
38	PATGGVKKPHRYRPG	acetylation	[7]

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] Histone h3 modifications in rat hepatic stellate cells by ethanol.
 Kim JS, Shukla SD.
 Alcohol Alcohol. 2005 Sep-Oct;40(5):367-72. [PMID: 15939707]
 [3] Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain.
 Tweedie-Cullen RY, Reck JM, Mansuy IM.
 J Proteome Res. 2009 Nov;8(11):4966-82. [PMID: 19737024]
 [4] 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]
 [5] Mass spectrometric characterization of human histone H3: a bird's eye view.
 Thomas CE, Kelleher NL, Mizzen CA.
 J Proteome Res. 2006 Feb;5(2):240-7. [PMID: 16457588]
 [6] Quantitative proteomic analysis of post-translational modifications of human histones.
 Beck HC, Nielsen EC, Matthiesen R, Jensen LH, Sehested M, Finn P, Grauslund M, Hansen AM, Jensen ON.
 Mol Cell Proteomics. 2006 Jul;5(7):1314-25. [PMID: 16627869]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

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;
 MOD_RES 3 3 Phosphoarginine; alternate (Probable).
 MOD_RES 4 4 Phosphothreonine; by GSG2.
 MOD_RES 5 5 Allysine; alternate (By similarity).
 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-crotonyl-L-lysine; alternate.
 MOD_RES 5 5 N6-methyllysine; alternate.
 MOD_RES 7 7 Phosphothreonine; by PKC (By similarity).
 MOD_RES 9 9 Citrulline; alternate (Probable).
 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.
 MOD_RES 10 10 N6-crotonyl-L-lysine; alternate.
 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 (Probable).
 MOD_RES 19 19 N6-acetyllysine; alternate.
 MOD_RES 19 19 N6-crotonyl-L-lysine; alternate.
 MOD_RES 19 19 N6-methyllysine; alternate.
 MOD_RES 24 24 N6-acetyllysine; alternate.
 MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
 MOD_RES 24 24 N6-methyllysine; alternate.
 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-crotonyl-L-lysine; alternate.
 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
 MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
 MOD_RES 37 37 N6-acetyllysine; alternate.
 MOD_RES 37 37 N6-methyllysine; alternate.
 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.
 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.
 MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
 MOD_RES 80 80 N6-acetyllysine; alternate (By
 MOD_RES 80 80 N6-methyllysine; alternate.
 MOD_RES 81 81 Phosphothreonine (By similarity).
 MOD_RES 108 108 Phosphothreonine (By similarity).
 MOD_RES 123 123 N6-methyllysine.
 MOD_RES 129 129 Phosphoarginine (Probable).
 MOD_RES 130 130 Phosphoarginine (Probable).
 MOD_RES 132 132 Phosphoarginine (Potential).  

Keyword

 3D-structure; Acetylation; Chromosome; Citrullination; Complete proteome; Direct protein sequencing; 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; IEA:UniProtKB-KW.
 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.