UniProt Accession

 H2B2_YEAST; P02294; D6VQ00 

Genbank Protein ID

 V01308; Z26494; Z35763; AY693063; BK006936 

Genbank Nucleotide ID

 CAA24615.1; CAA81268.1; CAA84817.1; AAT93082.1; DAA07120.1 

Protein Name

 Histone H2B.2 

Protein Synonyms/Alias

  

Gene Name

 HTB2 

Gene Synonyms/Alias

 H2B2; YBL002W; YBL0104 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
7	*MSSAAEKKPASKAP	acetylation	[1]
8	MSSAAEKKPASKAPA	acetylation	[1]
22	AEKKPAAKKTSTSVD	acetylation	[1]
22	AEKKPAAKKTSTSVD	butyrylation	[2]
23	EKKPAAKKTSTSVDG	acetylation	[1]
38	KKRSKVRKETYSSYI	methylation	[3]
38	KKRSKVRKETYSSYI	succinylation	[4]
50	SYIYKVLKQTHPDTG	succinylation	[4]
112	ILPGELAKHAVSEGT	ubiquitination	[5]
124	EGTRAVTKYSSSTQA	ubiquitination	[5, 6, 7, 8, 9, 10, 11]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software.
 Zhang K, Chen Y, Zhang Z, Zhao Y.
 J Proteome Res. 2009 Feb;8(2):900-6. [PMID: 19113941]
 [3] Identification of lysine 37 of histone H2B as a novel site of methylation.
 Gardner KE, Zhou L, Parra MA, Chen X, Strahl BD.
 PLoS One. 2011 Jan 13;6(1):e16244. [PMID: 21249157]
 [4] 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]
 [5] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [6] A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
 Hitchcock AL, Auld K, Gygi SP, Silver PA.
 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12735-40. [PMID: 14557538]
 [7] Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.
 Henry KW, Wyce A, Lo WS, Duggan LJ, Emre NC, Kao CF, Pillus L, Shilatifard A, Osley MA, Berger SL.
 Genes Dev. 2003 Nov 1;17(21):2648-63. [PMID: 14563679]
 [8] Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis.
 Yamashita K, Shinohara M, Shinohara A.
 Proc Natl Acad Sci U S A. 2004 Aug 3;101(31):11380-5. [PMID: 15280549]
 [9] Polyubiquitylation of histone H2B.
 Geng F, Tansey WP.
 Mol Biol Cell. 2008 Sep;19(9):3616-24. [PMID: 18562693]
 [10] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [11] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269] 

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 7 7 N6-acetyllysine; alternate.
 MOD_RES 8 8 N6-acetyllysine; alternate.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 12 12 N6-acetyllysine.
 MOD_RES 17 17 N6-acetyllysine; alternate.
 CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 131 AA 

Protein Sequence

Gene Ontology

 GO:0000788; C:nuclear nucleosome; TAS:SGD.
 GO:0031298; C:replication fork protection complex; IDA:SGD.
 GO:0003677; F:DNA binding; TAS:SGD.
 GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 

Interpro

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

Pfam

 PF00125; Histone 

SMART

 SM00427; H2B 

PROSITE

 PS00357; HISTONE_H2B 

PRINTS

 PR00621; HISTONEH2B.