UniProt Accession

 H33_MOUSE; P84244; P06351; P33155; Q3TW79; Q3U6D6; Q569U8; Q5HZY8; Q6TXQ5; Q8VDJ2; Q9D0H3; Q9V3W4 

Genbank Protein ID

 X13605; Z85979; X91866; AK002928; AK011431; AK037900; AK088075; AK135839; AK150467; AK150468; AK150591; AK150928; AK151274; AK151336; AK151451; AK151634; AK151658; AK151661; AK151869; AK152293; AK152453; AK152455; AK152623; AK152911; AK153034; AK153189; AK153239; AK153294; AK153371; AK153530; AK159615; AK159807; AK159850; AK160677; AK161675; AK162040; AK163244; AK167828; AK167879; AK168197; AK168698; AK169042; AK169226; BC002268; BC012687; BC021768; BC037730; BC083353; BC088835; BC092043; BC092300; BC106177; AY383567 

Genbank Nucleotide ID

 CAA31940.1; CAB06625.1; BAB22464.1; BAB27616.1; BAC29895.1; BAC40130.1; BAE22687.1; BAE29584.1; BAE29585.1; BAE29685.1; BAE29966.1; BAE30261.1; BAE30314.1; BAE30411.1; BAE30566.1; BAE30586.1; BAE30589.1; BAE30757.1; BAE31102.1; BAE31231.1; BAE31233.1; BAE31366.1; BAE31590.1; BAE31666.1; BAE31789.1; BAE31831.1; BAE31877.1; BAE31939.1; BAE32069.1; BAE35232.1; BAE35387.1; BAE35427.1; BAE35953.1; BAE36524.1; BAE36694.1; BAE37253.1; BAE39850.1; BAE39892.1; BAE40157.1; BAE40542.1; BAE40831.1; BAE40995.1; AAH02268.1; AAH12687.1; AAH21768.1; AAH37730.1; AAH83353.1; AAH88835.1; AAH92043.1; AAH92300.1; AAI06178.1; AAQ96274.1 

Protein Name

 Histone H3.3 

Protein Synonyms/Alias

  

Gene Name

 H3f3a; H3f3b 

Gene Synonyms/Alias

 H3.3a; H3.3b 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
5	***MARTKQTARKST	acetylation	[1]
5	***MARTKQTARKST	methylation	[2]
10	RTKQTARKSTGGKAP	acetylation	[3, 4, 5]
10	RTKQTARKSTGGKAP	methylation	[2]
15	ARKSTGGKAPRKQLA	acetylation	[1, 4, 5, 6, 7]
19	TGGKAPRKQLATKAA	acetylation	[1, 4, 5, 6, 8]
19	TGGKAPRKQLATKAA	methylation	[2]
24	PRKQLATKAARKSAP	acetylation	[1, 4, 5, 6, 7, 8]
24	PRKQLATKAARKSAP	methylation	[2]
28	LATKAARKSAPSTGG	acetylation	[1, 4, 5]
28	LATKAARKSAPSTGG	methylation	[2]
37	APSTGGVKKPHRYRP	acetylation	[4, 5, 9]
37	APSTGGVKKPHRYRP	methylation	[2]
57	REIRRYQKSTELLIR	acetylation	[7]
80	REIAQDFKTDLRFQS	acetylation	[7]
80	REIAQDFKTDLRFQS	methylation	[2]
123	KRVTIMPKDIQLARR	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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [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] 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

 Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.
 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 32 32 Phosphoserine (By similarity).
 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; TAS:Reactome.
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 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.