ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5QNW6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name H2B2F_HUMAN
Primary accession number Q5QNW6
Secondary accession number A8K0U9
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 42)
Name and origin of the protein
Protein name Histone H2B type 2-F
Synonyms None
Gene name
Name: HIST2H2BF
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION AT SER-15.
DOI=10.1016/S0092-8674(03)00355-6; PubMed=12757711 [NCBI, ExPASy, EBI, Israel, Japan]
Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
"Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase.";
Cell 113:507-517(2003).
[5]
UBIQUITINATION AT LYS-121.
DOI=10.1016/j.molcel.2005.09.025; PubMed=16307923 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[6]
ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
DOI=10.1007/s11010-005-8285-1; PubMed=16283522 [NCBI, ExPASy, EBI, Israel, Japan]
Golebiowski F., Kasprzak K.S.;
"Inhibition of core histones acetylation by carcinogenic nickel(II).";
Mol. Cell. Biochem. 279:133-139(2005).
[7]
UBIQUITINATION AT LYS-121.
DOI=10.1016/j.cell.2006.04.029; PubMed=16713563 [NCBI, ExPASy, EBI, Israel, Japan]
Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D.;
"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II.";
Cell 125:703-717(2006).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-109, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1074/mcp.M500288-MCP200; PubMed=16319397 [NCBI, ExPASy, EBI, Israel, Japan]
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.;
"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry.";
Mol. Cell. Proteomics 5:541-552(2006).
Comments
  • FUNCTION: 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.
  • SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Monoubiquitination of Lys-121 by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II.
  • PTM: Phosphorylated on Ser-15 by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.
  • SIMILARITY: Belongs to the histone H2B family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK289664; BAF82353.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591493; CAI12558.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110793; AAI10794.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00329665; -.
RefSeq NP_001019770.1; -.
UniGene Hs.632451
3D structure databases
SMR Q5QNW6; 4-125, 5-126.
ModBase Q5QNW6.
PTM databases
PhosphoSite Q5QNW6; -.
Organism-specific databases
GeneCards GC01M148048; -.
HGNC HGNC:24700; HIST2H2BF.
GenAtlas HIST2H2BF.
HPA CAB007814; -.
Gene expression databases
CleanEx HS_HIST2H2BF; -.
GermOnline ENSG00000203814; Homo sapiens.
Ontologies
GO
GO:0000786; Cellular component: nucleosome (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006334; Biological process: nucleosome assembly (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR009072; Histone-fold.
IPR007125; Histone_core_D.
IPR000558; Histone_H2B.
Graphical view of domain structure.
Gene3D G3DSA:1.10.20.10; Histone-fold; 1.
PANTHER PTHR23428; Histone_H2B; 1.
Pfam PF00125; Histone; 1.
Pfam graphical view of domain structure.
PRINTS PR00621; HISTONEH2B.
ProDom PD000497; Histone_H2B; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00427; H2B; 1.
SMART graphical view of domain structure.
PROSITE PS00357; HISTONE_H2B; 1.
Proteomic databases
PRIDE Q5QNW6; -.
Genome annotation databases
Ensembl ENSG00000203814; Homo sapiens. [Contig view]
GeneID 440689; -.
KEGG hsa:440689; -.
Phylogenomic databases
HOGENOM Q5QNW6; -.
HOVERGEN Q5QNW6; -.
OMA Q5QNW6; YTSSNIF.
Other
NextBio 109448; -.
ProtoNet Q5QNW6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Chromosomal protein; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   126  125     Histone H2B type 2-F. PRO_0000244826
MOD_RES   6     6        N6-acetyllysine. 
MOD_RES   12    12        N6-acetyllysine. 
MOD_RES   13    13        N6-acetyllysine. 
MOD_RES   15    15        Phosphoserine; by STK4. 
MOD_RES   16    16        N6-acetyllysine. 
MOD_RES   17    17        N6-acetyllysine. 
MOD_RES   21    21        N6-acetyllysine. 
MOD_RES   24    24        N6-acetyllysine. 
MOD_RES   47    47        N6-methylated lysine (By similarity). 
MOD_RES   58    58        N6-methylated lysine (By similarity). 
MOD_RES   109   109        N6-acetyllysine; alternate. 
MOD_RES   109   109        N6-methylated lysine; alternate (By similarity). 
CROSSLNK   121   121        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
Sequence information
Length: 126 AA [This is the length of the unprocessed precursor] Molecular weight: 13920 Da [This is the MW of the unprocessed precursor] CRC64: E951DF3D7E97C106 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM 

        70         80         90        100        110        120 
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT 


KYTSSK 

Q5QNW6 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!