UniProt Accession

 H32_MOUSE; P84228; A3KMN6; P02295; P02297; P16105; P17269; P17320; Q60582; Q78E59; Q8CGN9 

Genbank Protein ID

 X01685; M32459; M32461; X16148; M33989; X80328; U62669; U62671; U62674; U62675; AY158941; AY158947; AY158948; AY158949; AY158950; AY158951; AY158954; AY158955; AK010121; AK020421; AL590388; AL590388; BC015270; BC094041; BC101954; BC101955; BC101956; BC103549; BC120800; BC120802; BC132488; BC132490; Z30939 

Genbank Nucleotide ID

 CAA25840.1; AAA37810.1; AAA37812.1; CAA34274.1; AAA37764.1; CAA56577.1; AAB04760.1; AAB04764.1; AAB04771.1; AAB04772.1; AAO06251.1; AAO06257.1; AAO06258.1; AAO06259.1; AAO06260.1; AAO06261.1; AAO06264.1; AAO06265.1; BAB26714.1; BAB32097.1; CAI25840.1; CAI25844.1; AAH15270.1; AAH94041.1; AAI01955.1; AAI01956.1; AAI01957.1; AAI03550.1; AAI20801.1; AAI20803.1; AAI32489.1; AAI32491.1; CAA83209.1 

Protein Name

 Histone H3.2 

Protein Synonyms/Alias

  

Gene Name

 Hist1h3b; Hist1h3c; Hist1h3d; Hist1h3e; Hist1h3f; Hist2h3b; Hist2h3c1; Hist2h3c2 

Gene Synonyms/Alias

 H3-53; H3.2; H3b; H3-143; H3-B; H3-F; H3.2-221; H3f; H3.2-616; H3.2-615; Hist2h3ca1; H3.2-614; Hist2h3ca2 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
5	***MARTKQTARKST	acetylation	[1, 2]
5	***MARTKQTARKST	crotonylation	[3]
10	RTKQTARKSTGGKAP	acetylation	[1, 2, 4, 5, 6]
10	RTKQTARKSTGGKAP	crotonylation	[3]
10	RTKQTARKSTGGKAP	methylation	[6]
15	ARKSTGGKAPRKQLA	acetylation	[1, 2, 5, 6, 7, 8]
15	ARKSTGGKAPRKQLA	methylation	[6]
19	TGGKAPRKQLATKAA	acetylation	[1, 2, 5, 6, 7, 8]
19	TGGKAPRKQLATKAA	crotonylation	[3]
24	PRKQLATKAARKSAP	acetylation	[1, 2, 6, 7, 8]
24	PRKQLATKAARKSAP	crotonylation	[3]
28	LATKAARKSAPATGG	acetylation	[1, 2, 6]
28	LATKAARKSAPATGG	crotonylation	[3]
28	LATKAARKSAPATGG	methylation	[6]
37	APATGGVKKPHRYRP	acetylation	[1]
37	APATGGVKKPHRYRP	methylation	[6]
57	REIRRYQKSTELLIR	crotonylation	[3]
57	REIRRYQKSTELLIR	succinylation	[9]
80	REIAQDFKTDLRFQS	methylation	[6]
80	REIAQDFKTDLRFQS	succinylation	[9]
116	NLCAIHAKRVTIMPK	acetylation	[6]
116	NLCAIHAKRVTIMPK	butyrylation	[6]
123	KRVTIMPKDIQLARR	acetylation	[6]
123	KRVTIMPKDIQLARR	crotonylation	[6]

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] Quantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36.
 Jung HR, Pasini D, Helin K, Jensen ON.
 Mol Cell Proteomics. 2010 May;9(5):838-50. [PMID: 20150217]
 [3] Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.
 Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, Lu Z, Ye Z, Zhu Q, Wysocka J, Ye Y, Khochbin S, Ren B, Zhao Y.
 Cell. 2011 Sep 16;146(6):1016-28. [PMID: 21925322]
 [4] Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes.
 Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S.
 Mol Cell Biol. 2004 Nov;24(21):9630-45. [PMID: 15485929]
 [5] 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]
 [6] Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain.
 Tweedie-Cullen RY, Brunner AM, Grossmann J, Mohanna S, Sichau D, Nanni P, Panse C, Mansuy IM.
 PLoS One. 2012;7(5):e36980. [PMID: 22693562]
 [7] Crosstalk between CARM1 methylation and CBP acetylation on histone H3.
 Daujat S, Bauer UM, Shah V, Turner B, Berger S, Kouzarides T.
 Curr Biol. 2002 Dec 23;12(24):2090-7. [PMID: 12498683]
 [8] Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry.
 Cocklin RR, Wang M.
 J Protein Chem. 2003 May;22(4):327-34. [PMID: 13678296]
 [9] Lysine succinylation and lysine malonylation in histones.
 Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, Boeke JD, Zhao Y.
 Mol Cell Proteomics. 2012 May;11(5):100-7. [PMID: 22389435] 

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.
 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 (By similarity).
 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.
 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 (By
 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 (Probable).  

Keyword

 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; ISS:BHF-UCL.
 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; ISS:BHF-UCL. 

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.