ID H2B3B_HUMAN Reviewed; 126 AA. AC Q8N257; A4FU05; Q3ZCP6; Q5TA30; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 05-OCT-2010, entry version 73. DE RecName: Full=Histone H2B type 3-B; DE AltName: Full=H2B type 12; GN Name=HIST3H2BB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3; RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.; RT "The human and mouse replication-dependent histone genes."; RL Genomics 80:487-498(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Tongue; RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13; RP LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109, RP UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY. RX PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200; RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., RA Finn P., Grauslund M., Hansen A.M., Jensen O.N.; RT "Quantitative proteomic analysis of post-translational modifications RT of human histones."; RL Mol. Cell. Proteomics 5:1314-1325(2006). RN [7] RP PHOSPHORYLATION AT SER-15. RX PubMed=12757711; DOI=10.1016/S0092-8674(03)00355-6; RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.; RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian RT sterile twenty kinase."; RL Cell 113:507-517(2003). RN [8] RP UBIQUITINATION AT LYS-121. RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025; RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., RA Tempst P., Reinberg D.; RT "Monoubiquitination of human histone H2B: the factors involved and RT their roles in HOX gene regulation."; RL Mol. Cell 20:601-611(2005). RN [9] RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21. RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1; RA Golebiowski F., Kasprzak K.S.; RT "Inhibition of core histones acetylation by carcinogenic nickel(II)."; RL Mol. Cell. Biochem. 279:133-139(2005). RN [10] RP UBIQUITINATION AT LYS-121. RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029; RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., RA Reinberg D.; RT "Histone H2B monoubiquitination functions cooperatively with FACT to RT regulate elongation by RNA polymerase II."; RL Cell 125:703-717(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12; LYS-13; LYS-16; LYS-17; RP LYS-21; LYS-24 AND LYS-109, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16319397; DOI=10.1074/mcp.M500288-MCP200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86 AND LYS-121, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and CC compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template. Histones CC thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability. DNA CC accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and CC nucleosome remodeling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Monoubiquitination of Lys-121 by the RNF20/40 complex gives a CC specific tag for epigenetic transcriptional activation and is also CC prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It CC also functions cooperatively with the FACT dimer to stimulate CC elongation by RNA polymerase II. CC -!- PTM: Phosphorylated on Ser-15 by STK4/MST1 during apoptosis; which CC facilitates apoptotic chromatin condensation. Also phosphorylated CC on Ser-15 in response to DNA double strand breaks (DSBs), and in CC correlation with somatic hypermutation and immunoglobulin class- CC switch recombination. CC -!- SIMILARITY: Belongs to the histone H2B family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY131981; AAN59962.1; -; Genomic_DNA. DR EMBL; AK091220; BAC03613.1; -; mRNA. DR EMBL; AL139288; CAI23330.1; -; Genomic_DNA. DR EMBL; CH471098; EAW69879.1; -; Genomic_DNA. DR EMBL; BC100855; AAI00856.1; -; mRNA. DR EMBL; BC100856; AAI00857.1; -; mRNA. DR EMBL; BC100857; AAI00858.2; -; mRNA. DR EMBL; BC100858; AAI00859.1; -; mRNA. DR EMBL; BC137467; AAI37468.1; -; mRNA. DR EMBL; BC137468; AAI37469.1; -; mRNA. DR IPI; IPI00166293; -. DR RefSeq; NP_778225.1; -. DR UniGene; Hs.376691; -. DR ProteinModelPortal; Q8N257; -. DR SMR; Q8N257; 5-126. DR STRING; Q8N257; -. DR PhosphoSite; Q8N257; -. DR PRIDE; Q8N257; -. DR Ensembl; ENST00000369160; ENSP00000375736; ENSG00000196890. DR GeneID; 128312; -. DR KEGG; hsa:128312; -. DR UCSC; uc001hsz.1; human. DR CTD; 128312; -. DR GeneCards; GC01P228645; -. DR H-InvDB; HIX0001671; -. DR HGNC; HGNC:20514; HIST3H2BB. DR PharmGKB; PA134875583; -. DR HOGENOM; HBG715487; -. DR HOVERGEN; HBG007774; -. DR InParanoid; Q8N257; -. DR OMA; SEGSKAM; -. DR OrthoDB; EOG9W9MP7; -. DR PhylomeDB; Q8N257; -. DR Reactome; REACT_22172; Chromosome Maintenance. DR NextBio; 82284; -. DR ArrayExpress; Q8N257; -. DR Bgee; Q8N257; -. DR CleanEx; HS_HIST3H2BB; -. DR Genevestigator; Q8N257; -. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR PANTHER; PTHR23428; Histone_H2B; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. PE 1: Evidence at protein level; KW Acetylation; Chromosome; Complete proteome; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 126 Histone H2B type 3-B. FT /FTId=PRO_0000071837. FT MOD_RES 6 6 N6-acetyllysine. FT MOD_RES 12 12 N6-acetyllysine. FT MOD_RES 13 13 N6-acetyllysine. FT MOD_RES 15 15 Phosphoserine; by STK4. FT MOD_RES 16 16 N6-acetyllysine. FT MOD_RES 17 17 N6-acetyllysine. FT MOD_RES 21 21 N6-acetyllysine. FT MOD_RES 24 24 N6-acetyllysine. FT MOD_RES 47 47 N6-methyllysine. FT MOD_RES 58 58 N6,N6-dimethyllysine. FT MOD_RES 86 86 N6-acetyllysine. FT MOD_RES 109 109 N6-acetyllysine; alternate. FT MOD_RES 109 109 N6-methyllysine; alternate. FT MOD_RES 113 113 Phosphoserine (By similarity). FT MOD_RES 121 121 N6-acetyllysine. FT CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). SQ SEQUENCE 126 AA; 13908 MW; F1E12FE400DCF25E CRC64; MPDPSKSAPA PKKGSKKAVT KAQKKDGKKR KRGRKESYSI YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIASEASR LAHYNKRSTI TSREVQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK //