CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012734
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone H2B type 2-E 
Protein Synonyms/Alias
 Histone H2B-GL105; Histone H2B.q; H2B/q 
Gene Name
 HIST2H2BE 
Gene Synonyms/Alias
 H2BFQ 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MPEPAKSAPAPKKacetylation[1, 2]
12AKSAPAPKKGSKKAVacetylation[2]
12AKSAPAPKKGSKKAVglycation[3]
13KSAPAPKKGSKKAVTacetylation[1, 2]
13KSAPAPKKGSKKAVTglycation[3]
16PAPKKGSKKAVTKAQacetylation[1, 2]
16PAPKKGSKKAVTKAQglycation[3]
17APKKGSKKAVTKAQKacetylation[2]
21GSKKAVTKAQKKDGKacetylation[1, 2]
24KAVTKAQKKDGKKRKacetylation[2]
35KKRKRSRKESYSIYVglycation[3]
47IYVYKVLKQVHPDTGmethylation[4]
47IYVYKVLKQVHPDTGubiquitination[5]
58PDTGISSKAMGIMNSmethylation[4]
58PDTGISSKAMGIMNSubiquitination[5]
86SRLAHYNKRSTITSRubiquitination[5]
109LLPGELAKHAVSEGTglycation[3]
109LLPGELAKHAVSEGTmethylation[4]
109LLPGELAKHAVSEGTubiquitination[5]
117HAVSEGTKAVTKYTSglycation[3]
117HAVSEGTKAVTKYTSubiquitination[5]
121EGTKAVTKYTSSK**ubiquitination[5]
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] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [3] Glycation and oxidation of histones H2B and H1: in vitro study and characterization by mass spectrometry.
 Guedes S, Vitorino R, Domingues MR, Amado F, Domingues P.
 Anal Bioanal Chem. 2011 Apr;399(10):3529-39. [PMID: 21274518]
 [4] 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]
 [5] 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
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
 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
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM 60
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT 120
KYTSSK 126 
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.