UniProt Accession

 H2B1C_HUMAN; P62807; P02278; Q3B872; Q4VB69; Q93078; Q93080 

Genbank Protein ID

 M60750; Z80782; Z80779; Z80780; Z80783; AF531286; AF531288; AF531289; AF531290; AF531292; AL031777; AL031777; AL031777; AL353759; BC001131; BC009612; BC096120; BC096122; BC096123; BC101653; BC101655; BC101748; BC101750; BC106899 

Genbank Nucleotide ID

 AAA63189.1; CAB02544.1; CAB02541.1; CAB02542.1; CAB02545.1; AAN06686.1; AAN06688.1; AAN06689.1; AAN06690.1; AAN06692.1; CAC03411.1; CAC03417.1; CAC03420.1; CAC04130.1; AAH96120.1; AAH96122.1; AAH96123.1; AAI01654.1; AAI01656.1; AAI01749.1; AAI01751.1; AAI06900.1 

Protein Name

 Histone H2B type 1-C/E/F/G/I 

Protein Synonyms/Alias

 Histone H2B.1 A; Histone H2B.a; H2B/a; Histone H2B.g; H2B/g; Histone H2B.h; H2B/h; Histone H2B.k; H2B/k; Histone H2B.l; H2B/l 

Gene Name

 HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG; HIST1H2BI 

Gene Synonyms/Alias

 H2BFL; H2BFH; H2BFG; H2BFA; H2BFK 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MPEPAKSAPAPKK	acetylation	[1, 2, 3]
6	**MPEPAKSAPAPKK	crotonylation	[4]
6	**MPEPAKSAPAPKK	ubiquitination	[5, 6]
12	AKSAPAPKKGSKKAV	acetylation	[1, 3, 7]
12	AKSAPAPKKGSKKAV	crotonylation	[4]
13	KSAPAPKKGSKKAVT	acetylation	[1, 2, 3, 7]
13	KSAPAPKKGSKKAVT	crotonylation	[4]
16	PAPKKGSKKAVTKAQ	acetylation	[1, 2, 3, 7]
16	PAPKKGSKKAVTKAQ	crotonylation	[4]
17	APKKGSKKAVTKAQK	acetylation	[1, 3, 7]
17	APKKGSKKAVTKAQK	crotonylation	[4]
21	GSKKAVTKAQKKDGK	acetylation	[1, 2, 3, 7]
21	GSKKAVTKAQKKDGK	crotonylation	[4]
24	KAVTKAQKKDGKKRK	crotonylation	[4]
24	KAVTKAQKKDGKKRK	methylation	[8]
35	KKRKRSRKESYSVYV	crotonylation	[4]
35	KKRKRSRKESYSVYV	ubiquitination	[5]
44	SYSVYVYKVLKQVHP	methylation	[8]
44	SYSVYVYKVLKQVHP	ubiquitination	[5]
47	VYVYKVLKQVHPDTG	methylation	[3, 9]
47	VYVYKVLKQVHPDTG	ubiquitination	[5]
58	PDTGISSKAMGIMNS	methylation	[3, 9]
109	LLPGELAKHAVSEGT	methylation	[3, 9]
117	HAVSEGTKAVTKYTS	ubiquitination	[5]
121	EGTKAVTKYTSSK**	acetylation	[10]
121	EGTKAVTKYTSSK**	methylation	[11]
121	EGTKAVTKYTSSK**	ubiquitination	[5]

Reference

 [1] Patterns of histone acetylation.
 Thorne AW, Kmiciek D, Mitchelson K, Sautiere P, Crane-Robinson C.
 Eur J Biochem. 1990 Nov 13;193(3):701-13. [PMID: 2249688]
 [2] 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]
 [3] Quantitative proteomic analysis of post-translational modifications of human histones.
 Beck HC, Nielsen EC, Matthiesen R, Jensen LH, Sehested M, Finn P, Grauslund M, Hansen AM, Jensen ON.
 Mol Cell Proteomics. 2006 Jul;5(7):1314-25. [PMID: 16627869]
 [4] Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.
 Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, Lu Z, Ye Z, Zhu Q, Wysocka J, Ye Y, Khochbin S, Ren B, Zhao Y.
 Cell. 2011 Sep 16;146(6):1016-28. [PMID: 21925322]
 [5] 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]
 [6] 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]
 [7] Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry.
 Bonenfant D, Coulot M, Towbin H, Schindler P, van Oostrum J.
 Mol Cell Proteomics. 2006 Mar;5(3):541-52. [PMID: 16319397]
 [8] Identification of novel histone post-translational modifications by peptide mass fingerprinting.
 Zhang L, Eugeni EE, Parthun MR, Freitas MA.
 Chromosoma. 2003 Aug;112(2):77-86. [PMID: 12937907]
 [9] 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]
 [10] An acetylation-mono-ubiquitination switch on lysine 120 of H2B.
 Gatta R, Dolfini D, Zambelli F, Imbriano C, Pavesi G, Mantovani R.
 Epigenetics. 2011 May;6(5):630-7. [PMID: 21739721]
 [11] The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions.
 Kim J, Hake SB, Roeder RG.
 Mol Cell. 2005 Dec 9;20(5):759-70. [PMID: 16337599] 

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 (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.
 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.
 CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Polymorphism; 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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
 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.