UniProt Accession

 H2B1J_HUMAN; P06899; B2R4J4; O60816 

Genbank Protein ID

 X00088; AF531293; AK311849; AL021807; CH471081 

Genbank Nucleotide ID

 CAA24950.1; AAN06693.1; BAG34791.1; CAA16949.1; EAX03080.1 

Protein Name

 Histone H2B type 1-J 

Protein Synonyms/Alias

 Histone H2B.1; Histone H2B.r; H2B/r 

Gene Name

 HIST1H2BJ 

Gene Synonyms/Alias

 H2BFR 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MPEPAKSAPAPKK	acetylation	[1]
6	**MPEPAKSAPAPKK	ubiquitination	[2]
13	KSAPAPKKGSKKAVT	acetylation	[1, 3]
16	PAPKKGSKKAVTKAQ	acetylation	[1, 3]
21	GSKKAVTKAQKKDGK	acetylation	[1, 3]
35	KKRKRSRKESYSIYV	ubiquitination	[2, 4, 5]
44	SYSIYVYKVLKQVHP	ubiquitination	[2, 4, 5, 6]
47	IYVYKVLKQVHPDTG	methylation	[7]
47	IYVYKVLKQVHPDTG	ubiquitination	[2]
58	PDTGISSKAMGIMNS	methylation	[7]
109	LLPGELAKHAVSEGT	methylation	[7]
109	LLPGELAKHAVSEGT	ubiquitination	[2]
117	HAVSEGTKAVTKYTS	ubiquitination	[2]
121	EGTKAVTKYTSAK**	ubiquitination	[2, 8]

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] 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]
 [3] Analysis of dynamic changes in post-translational modifications of human histones during cell cycle by mass spectrometry.
 Bonenfant D, Towbin H, Coulot M, Schindler P, Mueller DR, van Oostrum J.
 Mol Cell Proteomics. 2007 Nov;6(11):1917-32. [PMID: 17644761]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

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

Keyword

 3D-structure; Acetylation; Antibiotic; Antimicrobial; 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: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.