UniProt Accession

 H2B1O_HUMAN; P23527; Q3KPI7; Q8TCV6 

Genbank Protein ID

 X57138; AF531298; Z98744; BC106720 

Genbank Nucleotide ID

 CAA40416.1; AAN06698.1; CAD24078.1; AAI06721.1 

Protein Name

 Histone H2B type 1-O 

Protein Synonyms/Alias

 Histone H2B.2; Histone H2B.n; H2B/n 

Gene Name

 HIST1H2BO 

Gene Synonyms/Alias

 H2BFH; H2BFN 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MPDPAKSAPAPKK	acetylation	[1, 2, 3]
6	**MPDPAKSAPAPKK	ubiquitination	[4, 5]
12	AKSAPAPKKGSKKAV	acetylation	[2]
13	KSAPAPKKGSKKAVT	acetylation	[1, 2]
16	PAPKKGSKKAVTKAQ	acetylation	[1, 2]
21	GSKKAVTKAQKKDGK	acetylation	[1, 2]
35	KKRKRSRKESYSIYV	ubiquitination	[5]
44	SYSIYVYKVLKQVHP	ubiquitination	[5]
47	IYVYKVLKQVHPDTG	ubiquitination	[5]
109	LLPGELAKHAVSEGT	ubiquitination	[6]
117	HAVSEGTKAVTKYTS	ubiquitination	[5]
121	EGTKAVTKYTSSK**	acetylation	[3, 7, 8]
121	EGTKAVTKYTSSK**	ubiquitination	[4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17]
126	VTKYTSSK*******	ubiquitination	[17]

Reference

 [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] 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]
 [5] 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]
 [6] 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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Proteomic snapshot of the EGF-induced ubiquitin network.
 Argenzio E, Bange T, Oldrini B, Bianchi F, Peesari R, Mari S, Di Fiore PP, Mann M, Polo S.
 Mol Syst Biol. 2011 Jan 18;7:462. [PMID: 21245847]
 [13] 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]
 [14] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [15] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [16] 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]
 [17] 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] 

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 2 2 N-acetylproline; partial.
 MOD_RES 6 6 N6-acetyllysine; alternate.
 MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
 MOD_RES 12 12 N6-acetyllysine; alternate.
 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.
 MOD_RES 58 58 N6,N6-dimethyllysine.
 MOD_RES 109 109 N6-methyllysine.
 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)  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 126 AA 

Protein Sequence

Gene Ontology

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

Interpro

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

Pfam

 PF00125; Histone 

SMART

 SM00427; H2B 

PROSITE

 PS00357; HISTONE_H2B 

PRINTS

 PR00621; HISTONEH2B.