UniProt Accession

 H2B1_YEAST; P02293; D6VSK6 

Genbank Protein ID

 J01327; U13239; Z48612; AY557724; M37743; BK006938 

Genbank Nucleotide ID

 AAA88719.1; AAC33141.1; CAA88504.1; AAS56050.1; AAA34694.2; DAA12066.1 

Protein Name

 Histone H2B.1 

Protein Synonyms/Alias

 Suppressor of Ty protein 12 

Gene Name

 HTB1 

Gene Synonyms/Alias

 H2B1; SPT12; YDR224C; YD9934.09C 

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
4	****MSAKAEKKPAS	acetylation	[1]
7	*MSAKAEKKPASKAP	acetylation	[1, 2, 3]
8	MSAKAEKKPASKAPA	acetylation	[1, 3]
12	AEKKPASKAPAEKKP	acetylation	[1, 3, 4]
17	ASKAPAEKKPAAKKT	acetylation	[1, 2, 3]
18	SKAPAEKKPAAKKTS	acetylation	[1, 2]
22	AEKKPAAKKTSTSTD	acetylation	[1, 2, 3]
23	EKKPAAKKTSTSTDG	acetylation	[1, 2, 3]
47	TYSSYIYKVLKQTHP	acetylation	[1]
47	TYSSYIYKVLKQTHP	ubiquitination	[5]
50	SYIYKVLKQTHPDTG	acetylation	[1]
50	SYIYKVLKQTHPDTG	ubiquitination	[5]
61	PDTGISQKSMSILNS	ubiquitination	[5]
83	RIATEASKLAAYNKK	acetylation	[1]
83	RIATEASKLAAYNKK	ubiquitination	[5]
89	SKLAAYNKKSTISAR	ubiquitination	[5]
112	ILPGELAKHAVSEGT	acetylation	[1]
112	ILPGELAKHAVSEGT	ubiquitination	[5]
124	EGTRAVTKYSSSTQA	acetylation	[1]
124	EGTRAVTKYSSSTQA	ubiquitination	[5, 6, 7, 8, 9]

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] Deciphering the roles of the histone H2B N-terminal domain in genome-wide transcription.
 Parra MA, Kerr D, Fahy D, Pouchnik DJ, Wyrick JJ.
 Mol Cell Biol. 2006 May;26(10):3842-52. [PMID: 16648479]
 [3] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [4] Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10.
 Ahn SH, Diaz RL, Grunstein M, Allis CD.
 Mol Cell. 2006 Oct 20;24(2):211-20. [PMID: 17052455]
 [5] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [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] 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]
 [8] A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking.
 Tagwerker C, Flick K, Cui M, Guerrero C, Dou Y, Auer B, Baldi P, Huang L, Kaiser P.
 Mol Cell Proteomics. 2006 Apr;5(4):737-48. [PMID: 16432255]
 [9] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232] 

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; IDA:SGD.
 GO:0031298; C:replication fork protection complex; IDA:SGD.
 GO:0003677; F:DNA binding; IDA:SGD.
 GO:0006333; P:chromatin assembly or disassembly; IDA:SGD.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0006301; P:postreplication repair; IGI:SGD. 

Interpro

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

Pfam

 PF00125; Histone 

SMART

 SM00427; H2B 

PROSITE

 PS00357; HISTONE_H2B 

PRINTS

 PR00621; HISTONEH2B.