CPLM-015630

Genbank Nucleotide ID

Protein Synonyms/Alias

Histone H3/m; Histone H3/o

HIST2H3A; HIST2H3C; HIST2H3D

Homo sapiens (Human)

Position	Peptide	Type	References
5	***MARTKQTARKST	methylation	[1]
10	RTKQTARKSTGGKAP	methylation	[1]
15	ARKSTGGKAPRKQLA	methylation	[1]
15	ARKSTGGKAPRKQLA	succinylation	[2]
15	ARKSTGGKAPRKQLA	ubiquitination	[3]
19	TGGKAPRKQLATKAA	acetylation	[4]
19	TGGKAPRKQLATKAA	methylation	[1]
19	TGGKAPRKQLATKAA	ubiquitination	[3, 5]
24	PRKQLATKAARKSAP	acetylation	[4]
24	PRKQLATKAARKSAP	methylation	[1]
24	PRKQLATKAARKSAP	ubiquitination	[3, 5]
28	LATKAARKSAPATGG	methylation	[1]
28	LATKAARKSAPATGG	ubiquitination	[3]
37	APATGGVKKPHRYRP	methylation	[1]
37	APATGGVKKPHRYRP	ubiquitination	[3, 5]
57	REIRRYQKSTELLIR	methylation	[1]
57	REIRRYQKSTELLIR	succinylation	[2]
57	REIRRYQKSTELLIR	ubiquitination	[3, 5]
65	STELLIRKLPFQRLV	methylation	[1]
80	REIAQDFKTDLRFQS	acetylation	[6]
80	REIAQDFKTDLRFQS	methylation	[1]
80	REIAQDFKTDLRFQS	succinylation	[2]
80	REIAQDFKTDLRFQS	ubiquitination	[3, 5]
123	KRVTIMPKDIQLARR	methylation	[1]
123	KRVTIMPKDIQLARR	succinylation	[2]
123	KRVTIMPKDIQLARR	ubiquitination	[3, 5]

[1] 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]
[2] 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]
[3] 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]
[4] Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics.
Yang YY, Grammel M, Hang HC.
Bioorg Med Chem Lett. 2011 Sep 1;21(17):4976-9. [PMID: 21669532]
[5] 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]
[6] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]

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.

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 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.
MOD_RES 123 123 N6-methyllysine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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:0006334; P:nucleosome assembly; IEA:InterPro.

IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR000164; Histone_H3.

PS00322; HISTONE_H3_1
PS00959; HISTONE_H3_2