Full text data of HIST2H2BE
HIST2H2BE
(H2BFQ)
[Confidence: low (only semi-automatic identification from reviews)]
Histone H2B type 2-E (Histone H2B-GL105; Histone H2B.q; H2B/q)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H2B type 2-E (Histone H2B-GL105; Histone H2B.q; H2B/q)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q16778
ID H2B2E_HUMAN Reviewed; 126 AA.
AC Q16778; A3KMC7; A8K110; Q4KMY1; Q5QNX0; Q9UE88;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Histone H2B type 2-E;
DE AltName: Full=Histone H2B-GL105;
DE AltName: Full=Histone H2B.q;
DE Short=H2B/q;
GN Name=HIST2H2BE; Synonyms=H2BFQ;
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].
RC TISSUE=Lymphocyte;
RX PubMed=1469070; DOI=10.1002/jcb.240500406;
RA Collart D., Romain P.L., Huebner K., Pockwinse S., Pilapil S.,
RA Cannizzaro L.A., Lian J.B., Croce C.M., Stein J.L., Stein G.S.;
RT "A human histone H2B.1 variant gene, located on chromosome 1, utilizes
RT alternative 3' end processing.";
RL J. Cell. Biochem. 50:374-385(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [8]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=11859126;
RA Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.;
RT "Endotoxin-neutralizing antimicrobial proteins of the human
RT placenta.";
RL J. Immunol. 168:2356-2364(2002).
RN [9]
RP PROTEIN SEQUENCE OF 2-13.
RX PubMed=8620898; DOI=10.1111/j.1432-1033.1996.0086n.x;
RA Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A.,
RA Liden S., Joernvall H., Boman H.G.;
RT "Biochemical and antibacterial analysis of human wound and blister
RT fluid.";
RL Eur. J. Biochem. 237:86-92(1996).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=12860195; DOI=10.1016/S0196-9781(03)00114-1;
RA Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H.,
RA Agerberth B.;
RT "Antimicrobial peptides in the first line defence of human colon
RT mucosa.";
RL Peptides 24:523-530(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=15019208; DOI=10.1016/j.peptides.2003.07.028;
RA Howell S.J., Wilk D., Yadav S.P., Bevins C.L.;
RT "Antimicrobial polypeptides of the human colonic epithelium.";
RL Peptides 24:1763-1770(2003).
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-126.
RC TISSUE=Liver;
RX PubMed=1993178; DOI=10.1021/bi00220a024;
RA Collart D., Ramsey-Ewing A., Bortell R., Lian J., Stein J., Stein G.;
RT "Isolation and characterization of a cDNA from a human histone H2B
RT gene which is reciprocally expressed in relation to replication-
RT dependent H2B histone genes during HL60 cell differentiation.";
RL Biochemistry 30:1610-1617(1991).
RN [14]
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 [15]
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 [16]
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 [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16457587; DOI=10.1021/pr050268v;
RA Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.;
RT "Gene-specific characterization of human histone H2B by electron
RT capture dissociation.";
RL J. Proteome Res. 5:233-239(2006).
RN [19]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND
RP LYS-35.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [20]
RP UBIQUITINATION AT LYS-35.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin
RT ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79
RT methylation.";
RL Mol. Cell 43:132-144(2011).
RN [21]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP49.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
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 -!- FUNCTION: Has broad antibacterial activity. May contribute to the
CC formation of the functional antimicrobial barrier of the colonic
CC epithelium, and to the bactericidal activity of amniotic fluid.
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 at Lys-35 (H2BK34Ub) by the MSL1/MSL2
CC dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79'
CC (H3K79me) methylation and transcription activation at specific
CC gene loci, such as HOXA9 and MEIS1 loci. Similarly,
CC monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex
CC gives a specific tag for epigenetic transcriptional activation and
CC is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer
CC to stimulate elongation by RNA polymerase II. H2BK120Ub also acts
CC as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set
CC of exons.
CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to
CC stress promotes transcription (By similarity). Phosphorylated on
CC Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates
CC apoptotic chromatin condensation. Also phosphorylated on Ser-15 in
CC response to DNA double strand breaks (DSBs), and in correlation
CC with somatic hypermutation and immunoglobulin class-switch
CC recombination.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-
CC 121. It fluctuates in response to extracellular glucose, and
CC associates with transcribed genes (By similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H2B family.
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DR EMBL; X57985; CAA41051.1; -; Genomic_DNA.
DR EMBL; AY131979; AAN59961.1; -; Genomic_DNA.
DR EMBL; CR541895; CAG46693.1; -; mRNA.
DR EMBL; AK289725; BAF82414.1; -; mRNA.
DR EMBL; AL591493; CAI12568.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53605.1; -; Genomic_DNA.
DR EMBL; BC005827; AAH05827.1; -; mRNA.
DR EMBL; BC069193; AAH69193.1; -; mRNA.
DR EMBL; BC096121; AAH96121.1; -; mRNA.
DR EMBL; BC098112; AAH98112.1; -; mRNA.
DR EMBL; BC098289; AAH98289.1; -; mRNA.
DR EMBL; BC107084; AAI07085.1; -; mRNA.
DR EMBL; BC107085; AAI07086.1; -; mRNA.
DR EMBL; M60756; AAA63192.1; -; mRNA.
DR PIR; I37467; I37467.
DR PIR; S65409; S65409.
DR RefSeq; NP_003519.1; NM_003528.2.
DR UniGene; Hs.2178; -.
DR ProteinModelPortal; Q16778; -.
DR SMR; Q16778; 5-126.
DR DIP; DIP-39324N; -.
DR IntAct; Q16778; 12.
DR MINT; MINT-1461208; -.
DR STRING; 9606.ENSP00000358151; -.
DR PhosphoSite; Q16778; -.
DR DMDM; 7387736; -.
DR PaxDb; Q16778; -.
DR PRIDE; Q16778; -.
DR DNASU; 8349; -.
DR Ensembl; ENST00000369155; ENSP00000358151; ENSG00000184678.
DR Ensembl; ENST00000583061; ENSP00000464485; ENSG00000264719.
DR GeneID; 8349; -.
DR KEGG; hsa:8349; -.
DR UCSC; uc001etc.3; human.
DR CTD; 8349; -.
DR GeneCards; GC01M149856; -.
DR H-InvDB; HIX0029389; -.
DR HGNC; HGNC:4760; HIST2H2BE.
DR MIM; 601831; gene.
DR neXtProt; NX_Q16778; -.
DR PharmGKB; PA29135; -.
DR eggNOG; NOG315146; -.
DR HOGENOM; HOG000231213; -.
DR HOVERGEN; HBG007774; -.
DR InParanoid; Q16778; -.
DR KO; K11252; -.
DR OMA; TMAANDI; -.
DR OrthoDB; EOG72VH8J; -.
DR PhylomeDB; Q16778; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR ChiTaRS; HIST2H2BE; human.
DR GeneWiki; HIST2H2BE; -.
DR GenomeRNAi; 8349; -.
DR NextBio; 31268; -.
DR PRO; PR:Q16778; -.
DR Bgee; Q16778; -.
DR CleanEx; HS_HIST2H2BE; -.
DR Genevestigator; Q16778; -.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Histone H2B type 2-E.
FT /FTId=PRO_0000071835.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT MOD_RES 6 6 N6-acetyllysine; alternate.
FT MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 12 12 N6-acetyllysine; alternate.
FT MOD_RES 12 12 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 13 13 N6-acetyllysine; alternate.
FT MOD_RES 13 13 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 15 15 Phosphoserine; by STK4/MST1.
FT MOD_RES 16 16 N6-acetyllysine; alternate.
FT MOD_RES 16 16 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 17 17 N6-acetyllysine; alternate.
FT MOD_RES 17 17 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 21 21 N6-acetyllysine; alternate.
FT MOD_RES 21 21 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 35 35 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 37 37 Phosphoserine; by AMPK (By similarity).
FT MOD_RES 47 47 N6-methyllysine.
FT MOD_RES 58 58 N6,N6-dimethyllysine.
FT MOD_RES 80 80 Dimethylated arginine (By similarity).
FT MOD_RES 86 86 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 86 86 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 87 87 Omega-N-methylarginine (By similarity).
FT MOD_RES 93 93 Omega-N-methylarginine (By similarity).
FT MOD_RES 109 109 N6-methyllysine.
FT MOD_RES 116 116 Phosphothreonine (By similarity).
FT MOD_RES 117 117 N6-methylated lysine (By similarity).
FT CARBOHYD 113 113 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 5 5 A -> S (in Ref. 7; AAH98112/AAH98289).
SQ SEQUENCE 126 AA; 13920 MW; 0410A881ABBE6647 CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
//
ID H2B2E_HUMAN Reviewed; 126 AA.
AC Q16778; A3KMC7; A8K110; Q4KMY1; Q5QNX0; Q9UE88;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Histone H2B type 2-E;
DE AltName: Full=Histone H2B-GL105;
DE AltName: Full=Histone H2B.q;
DE Short=H2B/q;
GN Name=HIST2H2BE; Synonyms=H2BFQ;
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].
RC TISSUE=Lymphocyte;
RX PubMed=1469070; DOI=10.1002/jcb.240500406;
RA Collart D., Romain P.L., Huebner K., Pockwinse S., Pilapil S.,
RA Cannizzaro L.A., Lian J.B., Croce C.M., Stein J.L., Stein G.S.;
RT "A human histone H2B.1 variant gene, located on chromosome 1, utilizes
RT alternative 3' end processing.";
RL J. Cell. Biochem. 50:374-385(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [8]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=11859126;
RA Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.;
RT "Endotoxin-neutralizing antimicrobial proteins of the human
RT placenta.";
RL J. Immunol. 168:2356-2364(2002).
RN [9]
RP PROTEIN SEQUENCE OF 2-13.
RX PubMed=8620898; DOI=10.1111/j.1432-1033.1996.0086n.x;
RA Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A.,
RA Liden S., Joernvall H., Boman H.G.;
RT "Biochemical and antibacterial analysis of human wound and blister
RT fluid.";
RL Eur. J. Biochem. 237:86-92(1996).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=12860195; DOI=10.1016/S0196-9781(03)00114-1;
RA Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H.,
RA Agerberth B.;
RT "Antimicrobial peptides in the first line defence of human colon
RT mucosa.";
RL Peptides 24:523-530(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=15019208; DOI=10.1016/j.peptides.2003.07.028;
RA Howell S.J., Wilk D., Yadav S.P., Bevins C.L.;
RT "Antimicrobial polypeptides of the human colonic epithelium.";
RL Peptides 24:1763-1770(2003).
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-126.
RC TISSUE=Liver;
RX PubMed=1993178; DOI=10.1021/bi00220a024;
RA Collart D., Ramsey-Ewing A., Bortell R., Lian J., Stein J., Stein G.;
RT "Isolation and characterization of a cDNA from a human histone H2B
RT gene which is reciprocally expressed in relation to replication-
RT dependent H2B histone genes during HL60 cell differentiation.";
RL Biochemistry 30:1610-1617(1991).
RN [14]
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 [15]
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 [16]
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 [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16457587; DOI=10.1021/pr050268v;
RA Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.;
RT "Gene-specific characterization of human histone H2B by electron
RT capture dissociation.";
RL J. Proteome Res. 5:233-239(2006).
RN [19]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND
RP LYS-35.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [20]
RP UBIQUITINATION AT LYS-35.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin
RT ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79
RT methylation.";
RL Mol. Cell 43:132-144(2011).
RN [21]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP49.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
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 -!- FUNCTION: Has broad antibacterial activity. May contribute to the
CC formation of the functional antimicrobial barrier of the colonic
CC epithelium, and to the bactericidal activity of amniotic fluid.
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 at Lys-35 (H2BK34Ub) by the MSL1/MSL2
CC dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79'
CC (H3K79me) methylation and transcription activation at specific
CC gene loci, such as HOXA9 and MEIS1 loci. Similarly,
CC monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex
CC gives a specific tag for epigenetic transcriptional activation and
CC is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer
CC to stimulate elongation by RNA polymerase II. H2BK120Ub also acts
CC as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set
CC of exons.
CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to
CC stress promotes transcription (By similarity). Phosphorylated on
CC Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates
CC apoptotic chromatin condensation. Also phosphorylated on Ser-15 in
CC response to DNA double strand breaks (DSBs), and in correlation
CC with somatic hypermutation and immunoglobulin class-switch
CC recombination.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-
CC 121. It fluctuates in response to extracellular glucose, and
CC associates with transcribed genes (By similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H2B family.
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DR EMBL; X57985; CAA41051.1; -; Genomic_DNA.
DR EMBL; AY131979; AAN59961.1; -; Genomic_DNA.
DR EMBL; CR541895; CAG46693.1; -; mRNA.
DR EMBL; AK289725; BAF82414.1; -; mRNA.
DR EMBL; AL591493; CAI12568.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53605.1; -; Genomic_DNA.
DR EMBL; BC005827; AAH05827.1; -; mRNA.
DR EMBL; BC069193; AAH69193.1; -; mRNA.
DR EMBL; BC096121; AAH96121.1; -; mRNA.
DR EMBL; BC098112; AAH98112.1; -; mRNA.
DR EMBL; BC098289; AAH98289.1; -; mRNA.
DR EMBL; BC107084; AAI07085.1; -; mRNA.
DR EMBL; BC107085; AAI07086.1; -; mRNA.
DR EMBL; M60756; AAA63192.1; -; mRNA.
DR PIR; I37467; I37467.
DR PIR; S65409; S65409.
DR RefSeq; NP_003519.1; NM_003528.2.
DR UniGene; Hs.2178; -.
DR ProteinModelPortal; Q16778; -.
DR SMR; Q16778; 5-126.
DR DIP; DIP-39324N; -.
DR IntAct; Q16778; 12.
DR MINT; MINT-1461208; -.
DR STRING; 9606.ENSP00000358151; -.
DR PhosphoSite; Q16778; -.
DR DMDM; 7387736; -.
DR PaxDb; Q16778; -.
DR PRIDE; Q16778; -.
DR DNASU; 8349; -.
DR Ensembl; ENST00000369155; ENSP00000358151; ENSG00000184678.
DR Ensembl; ENST00000583061; ENSP00000464485; ENSG00000264719.
DR GeneID; 8349; -.
DR KEGG; hsa:8349; -.
DR UCSC; uc001etc.3; human.
DR CTD; 8349; -.
DR GeneCards; GC01M149856; -.
DR H-InvDB; HIX0029389; -.
DR HGNC; HGNC:4760; HIST2H2BE.
DR MIM; 601831; gene.
DR neXtProt; NX_Q16778; -.
DR PharmGKB; PA29135; -.
DR eggNOG; NOG315146; -.
DR HOGENOM; HOG000231213; -.
DR HOVERGEN; HBG007774; -.
DR InParanoid; Q16778; -.
DR KO; K11252; -.
DR OMA; TMAANDI; -.
DR OrthoDB; EOG72VH8J; -.
DR PhylomeDB; Q16778; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR ChiTaRS; HIST2H2BE; human.
DR GeneWiki; HIST2H2BE; -.
DR GenomeRNAi; 8349; -.
DR NextBio; 31268; -.
DR PRO; PR:Q16778; -.
DR Bgee; Q16778; -.
DR CleanEx; HS_HIST2H2BE; -.
DR Genevestigator; Q16778; -.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Histone H2B type 2-E.
FT /FTId=PRO_0000071835.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT MOD_RES 6 6 N6-acetyllysine; alternate.
FT MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 12 12 N6-acetyllysine; alternate.
FT MOD_RES 12 12 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 13 13 N6-acetyllysine; alternate.
FT MOD_RES 13 13 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 15 15 Phosphoserine; by STK4/MST1.
FT MOD_RES 16 16 N6-acetyllysine; alternate.
FT MOD_RES 16 16 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 17 17 N6-acetyllysine; alternate.
FT MOD_RES 17 17 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 21 21 N6-acetyllysine; alternate.
FT MOD_RES 21 21 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 35 35 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 37 37 Phosphoserine; by AMPK (By similarity).
FT MOD_RES 47 47 N6-methyllysine.
FT MOD_RES 58 58 N6,N6-dimethyllysine.
FT MOD_RES 80 80 Dimethylated arginine (By similarity).
FT MOD_RES 86 86 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 86 86 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 87 87 Omega-N-methylarginine (By similarity).
FT MOD_RES 93 93 Omega-N-methylarginine (By similarity).
FT MOD_RES 109 109 N6-methyllysine.
FT MOD_RES 116 116 Phosphothreonine (By similarity).
FT MOD_RES 117 117 N6-methylated lysine (By similarity).
FT CARBOHYD 113 113 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 5 5 A -> S (in Ref. 7; AAH98112/AAH98289).
SQ SEQUENCE 126 AA; 13920 MW; 0410A881ABBE6647 CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
//
MIM
601831
*RECORD*
*FIELD* NO
601831
*FIELD* TI
*601831 HISTONE GENE CLUSTER 2, H2B HISTONE FAMILY, MEMBER E; HIST2H2BE
;;HISTONE GENE CLUSTER 2, H2BE;;
read moreHIST2 CLUSTER, H2BE;;
H2B HISTONE FAMILY, MEMBER Q; H2BFQ;;
H2B/Q;;
H2B.1
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
CLONING
Collart et al. (1992) cloned a histone H2B gene, which they termed
H2B.1, from a human genomic DNA library. The H2B.1 protein contains 126
amino acids. Collart et al. (1992) reported that the 3-prime
untranslated region of H2B.1 contains the conserved histone 3-prime
stem-loop motif commonly found in cell cycle-dependent histones, as well
as a polyadenylation signal typical of constitutively expressed
histones. Alternative splicing of the 3-prime untranslated region of
H2B.1 produces both a 500-nucleotide cell cycle-dependent mRNA and a
2,300-nucleotide constitutively expressed mRNA.
GENE STRUCTURE
Collart et al. (1992) determined that the H2B.1 gene is intronless. It
is is paired with a functional H2A histone gene (HIST2H2AC; 602797), and
the 2 genes are separated by a bidirectionally transcribed intergenic
promoter region of 329 nucleotides containing consensus TATA and CCAAT
boxes and an OTF-1 element.
MAPPING
Collart et al. (1992) mapped the H2B.1 gene to human chromosome 1q21-q23
using a somatic cell hybrid panel and in situ hybridization.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 1q21, which they called histone gene
cluster-2 (HIST2), contains 6 histone genes, including HIST2H2BE. The
cluster also contains 4 H2B pseudogenes, designated HIST2H2BA through
HIST2H2BD.
GENE FUNCTION
See HIST1H2BA (601831) for functional information on H2B histones.
*FIELD* RF
1. Collart, D.; Romain, P. L.; Huebner, K.; Pockwinse, S.; Pilapil,
S.; Cannizzaro, L. A.; Lian, J. B.; Croce, C. M.; Stein, J. L.; Stein,
G. S.: A human histone H2B.1 variant gene, located on chromosome
1, utilizes alternative 3-prime end processing. J. Cell. Biochem. 50:
374-385, 1992.
2. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 1/28/2013
Ada Hamosh - updated: 4/16/2012
Ada Hamosh - updated: 2/7/2012
Ada Hamosh - updated: 4/18/2006
Ada Hamosh - updated: 12/10/2004
Ada Hamosh - updated: 6/9/2004
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Jennifer P. Macke: 5/28/1997
*FIELD* ED
mgross: 01/29/2013
mgross: 1/29/2013
mgross: 1/28/2013
alopez: 4/16/2012
alopez: 2/9/2012
terry: 2/7/2012
mgross: 4/7/2011
mgross: 5/26/2010
alopez: 3/25/2008
alopez: 4/25/2006
terry: 4/18/2006
alopez: 12/14/2004
terry: 12/10/2004
alopez: 6/9/2004
terry: 6/9/2004
tkritzer: 3/31/2003
alopez: 7/14/1998
alopez: 7/9/1998
alopez: 7/8/1998
alopez: 7/16/1997
*RECORD*
*FIELD* NO
601831
*FIELD* TI
*601831 HISTONE GENE CLUSTER 2, H2B HISTONE FAMILY, MEMBER E; HIST2H2BE
;;HISTONE GENE CLUSTER 2, H2BE;;
read moreHIST2 CLUSTER, H2BE;;
H2B HISTONE FAMILY, MEMBER Q; H2BFQ;;
H2B/Q;;
H2B.1
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
CLONING
Collart et al. (1992) cloned a histone H2B gene, which they termed
H2B.1, from a human genomic DNA library. The H2B.1 protein contains 126
amino acids. Collart et al. (1992) reported that the 3-prime
untranslated region of H2B.1 contains the conserved histone 3-prime
stem-loop motif commonly found in cell cycle-dependent histones, as well
as a polyadenylation signal typical of constitutively expressed
histones. Alternative splicing of the 3-prime untranslated region of
H2B.1 produces both a 500-nucleotide cell cycle-dependent mRNA and a
2,300-nucleotide constitutively expressed mRNA.
GENE STRUCTURE
Collart et al. (1992) determined that the H2B.1 gene is intronless. It
is is paired with a functional H2A histone gene (HIST2H2AC; 602797), and
the 2 genes are separated by a bidirectionally transcribed intergenic
promoter region of 329 nucleotides containing consensus TATA and CCAAT
boxes and an OTF-1 element.
MAPPING
Collart et al. (1992) mapped the H2B.1 gene to human chromosome 1q21-q23
using a somatic cell hybrid panel and in situ hybridization.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 1q21, which they called histone gene
cluster-2 (HIST2), contains 6 histone genes, including HIST2H2BE. The
cluster also contains 4 H2B pseudogenes, designated HIST2H2BA through
HIST2H2BD.
GENE FUNCTION
See HIST1H2BA (601831) for functional information on H2B histones.
*FIELD* RF
1. Collart, D.; Romain, P. L.; Huebner, K.; Pockwinse, S.; Pilapil,
S.; Cannizzaro, L. A.; Lian, J. B.; Croce, C. M.; Stein, J. L.; Stein,
G. S.: A human histone H2B.1 variant gene, located on chromosome
1, utilizes alternative 3-prime end processing. J. Cell. Biochem. 50:
374-385, 1992.
2. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 1/28/2013
Ada Hamosh - updated: 4/16/2012
Ada Hamosh - updated: 2/7/2012
Ada Hamosh - updated: 4/18/2006
Ada Hamosh - updated: 12/10/2004
Ada Hamosh - updated: 6/9/2004
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Jennifer P. Macke: 5/28/1997
*FIELD* ED
mgross: 01/29/2013
mgross: 1/29/2013
mgross: 1/28/2013
alopez: 4/16/2012
alopez: 2/9/2012
terry: 2/7/2012
mgross: 4/7/2011
mgross: 5/26/2010
alopez: 3/25/2008
alopez: 4/25/2006
terry: 4/18/2006
alopez: 12/14/2004
terry: 12/10/2004
alopez: 6/9/2004
terry: 6/9/2004
tkritzer: 3/31/2003
alopez: 7/14/1998
alopez: 7/9/1998
alopez: 7/8/1998
alopez: 7/16/1997