CPLM-013808

Genbank Nucleotide ID

Histone H2B type 2-F

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MPDPAKSAPAPKK	acetylation	[1]
13	KSAPAPKKGSKKAVT	acetylation	[1, 2, 3]
16	PAPKKGSKKAVTKVQ	acetylation	[1, 2, 3]
17	APKKGSKKAVTKVQK	acetylation	[2, 3, 4]
21	GSKKAVTKVQKKDGK	acetylation	[1, 2, 3, 4]
24	KAVTKVQKKDGKKRK	acetylation	[3]
35	KKRKRSRKESYSVYV	succinylation	[5]
117	HAVSEGTKAVTKYTS	malonylation	[5]
117	HAVSEGTKAVTKYTS	succinylation	[5]
121	EGTKAVTKYTSSK**	succinylation	[5]

[1] 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]
[2] 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]
[3] 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]
[4] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[5] 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.

MOD_RES 2 2 N-acetylproline (By similarity).
MOD_RES 6 6 N6-acetyllysine; alternate.
MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
MOD_RES 12 12 N6-acetyllysine; alternate (By
MOD_RES 12 12 N6-crotonyl-L-lysine; alternate.
MOD_RES 13 13 N6-acetyllysine; alternate.
MOD_RES 13 13 N6-crotonyl-L-lysine; alternate.
MOD_RES 15 15 Phosphoserine; by STK4/MST1.
MOD_RES 16 16 N6-acetyllysine; alternate.
MOD_RES 16 16 N6-crotonyl-L-lysine; alternate.
MOD_RES 17 17 N6-acetyllysine; alternate.
MOD_RES 17 17 N6-crotonyl-L-lysine; alternate.
MOD_RES 21 21 N6-acetyllysine; alternate.
MOD_RES 21 21 N6-crotonyl-L-lysine; alternate.
MOD_RES 24 24 N6-acetyllysine; alternate (By
MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
MOD_RES 35 35 N6-crotonyl-L-lysine; alternate.
MOD_RES 37 37 Phosphoserine; by AMPK (By similarity).
MOD_RES 43 43 Phosphotyrosine (By similarity).
MOD_RES 47 47 N6-methyllysine (By similarity).
MOD_RES 58 58 N6,N6-dimethyllysine (By similarity).
MOD_RES 109 109 N6-methyllysine (By similarity).
MOD_RES 113 113 Phosphoserine; alternate (By similarity).
CARBOHYD 113 113 O-linked (GlcNAc...); alternate (By
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; Alternative splicing; Chromosome; Complete proteome; DNA-binding; Glycoprotein; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0006334; P:nucleosome assembly; IEA:InterPro.

IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR000558; Histone_H2B.

PS00357; HISTONE_H2B

PR00621; HISTONEH2B.