UniProt Accession

 H33_HUMAN; P84243; P06351; P33155; Q5VV55; Q5VV56; Q66I33; Q9V3W4 

Genbank Protein ID

 M11354; M11353; Z48950; X05855; X05856; X05857; AF218029; BX537379; AL512343; AL512343; BC001124; BC006497; BC012813; BC017558; BC029405; BC038989; BC066901; BC067757; BC081560; BC081561; BC095447; BC108701 

Genbank Nucleotide ID

 AAA52653.1; AAA52654.1; CAA88778.1; CAA29288.1; CAA29288.1; CAA29288.1; AAG17271.1; CAD97621.1; CAH73371.1; CAH73372.1; AAH01124.1; AAH06497.1; AAH12813.1; AAH17558.1; AAH29405.1; AAH38989.1; AAH81560.1; AAH81561.1; AAH95447.1; AAI08702.1 

Protein Name

 Histone H3.3 

Protein Synonyms/Alias

  

Gene Name

 H3F3A; H3F3B 

Gene Synonyms/Alias

 H3.3A; H3F3; PP781; H3.3B 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MARTKQTARKST	acetylation	[1, 2]
5	***MARTKQTARKST	methylation	[3]
10	RTKQTARKSTGGKAP	acetylation	[1, 2, 4]
10	RTKQTARKSTGGKAP	methylation	[3]
15	ARKSTGGKAPRKQLA	acetylation	[1, 2, 5, 6, 7, 8]
15	ARKSTGGKAPRKQLA	methylation	[3]
19	TGGKAPRKQLATKAA	acetylation	[1, 2, 5, 8]
19	TGGKAPRKQLATKAA	methylation	[3]
19	TGGKAPRKQLATKAA	ubiquitination	[9, 10, 11]
24	PRKQLATKAARKSAP	acetylation	[1, 2, 5, 8]
24	PRKQLATKAARKSAP	methylation	[3]
24	PRKQLATKAARKSAP	sumoylation	[12]
24	PRKQLATKAARKSAP	ubiquitination	[9, 10, 11]
28	LATKAARKSAPSTGG	acetylation	[13, 14]
28	LATKAARKSAPSTGG	methylation	[3]
28	LATKAARKSAPSTGG	ubiquitination	[11, 15]
37	APSTGGVKKPHRYRP	acetylation	[2, 13, 14]
37	APSTGGVKKPHRYRP	methylation	[3]
37	APSTGGVKKPHRYRP	ubiquitination	[11, 15, 16, 17]
38	PSTGGVKKPHRYRPG	methylation	[3]
38	PSTGGVKKPHRYRPG	ubiquitination	[17]
57	REIRRYQKSTELLIR	acetylation	[2, 4, 18]
57	REIRRYQKSTELLIR	methylation	[3]
57	REIRRYQKSTELLIR	ubiquitination	[9, 10, 11]
65	STELLIRKLPFQRLV	methylation	[3]
80	REIAQDFKTDLRFQS	acetylation	[2]
80	REIAQDFKTDLRFQS	methylation	[3]
80	REIAQDFKTDLRFQS	ubiquitination	[9, 10, 11]
123	KRVTIMPKDIQLARR	methylation	[3]
123	KRVTIMPKDIQLARR	ubiquitination	[9, 10, 11]

Reference

 [1] Patterns of histone acetylation.
 Thorne AW, Kmiciek D, Mitchelson K, Sautiere P, Crane-Robinson C.
 Eur J Biochem. 1990 Nov 13;193(3):701-13. [PMID: 2249688]
 [2] 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]
 [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] Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells.
 Tjeertes JV, Miller KM, Jackson SP.
 EMBO J. 2009 Jul 8;28(13):1878-89. [PMID: 19407812]
 [5] Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates.
 Schiltz RL, Mizzen CA, Vassilev A, Cook RG, Allis CD, Nakatani Y.
 J Biol Chem. 1999 Jan 15;274(3):1189-92. [PMID: 9880483]
 [6] Tip60 acetylates six lysines of a specific class in core histones in vitro.
 Kimura A, Horikoshi M.
 Genes Cells. 1998 Dec;3(12):789-800. [PMID: 10096020]
 [7] Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo.
 Winkler GS, Kristjuhan A, Erdjument-Bromage H, Tempst P, Svejstrup JQ.
 Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3517-22. [PMID: 11904415]
 [8] Analysis of dynamic changes in post-translational modifications of human histones during cell cycle by mass spectrometry.
 Bonenfant D, Towbin H, Coulot M, Schindler P, Mueller DR, van Oostrum J.
 Mol Cell Proteomics. 2007 Nov;6(11):1917-32. [PMID: 17644761]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [11] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [12] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [13] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [14] 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]
 [15] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [16] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [17] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [18] The type III histone deacetylase Sirt1 protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclaf1 promoter to inhibit T cell activation.
 Kong S, Kim SJ, Sandal B, Lee SM, Gao B, Zhang DD, Fang D.
 J Biol Chem. 2011 May 13;286(19):16967-75. [PMID: 21454709] 

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.
 MOD_RES 4 4 Phosphothreonine; by GSG2.
 MOD_RES 5 5 Allysine; alternate.
 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.
 MOD_RES 9 9 Citrulline; alternate.
 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.
 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.
 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.
 MOD_RES 57 57 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 57 57 N6-acetyllysine; alternate.
 MOD_RES 57 57 N6-crotonyl-L-lysine; alternate.
 MOD_RES 57 57 N6-methyllysine; by EHMT2; alternate.
 MOD_RES 58 58 Phosphoserine.
 MOD_RES 65 65 N6-methyllysine.
 MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
 MOD_RES 80 80 N6-acetyllysine; alternate.
 MOD_RES 80 80 N6-methyllysine; alternate.
 MOD_RES 81 81 Phosphothreonine.
 MOD_RES 108 108 Phosphothreonine (By similarity).
 MOD_RES 123 123 N6-methyllysine.  

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:0005576; C:extracellular region; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0009725; P:response to hormone stimulus; 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.