H2B_DROME
ID H2B_DROME Reviewed; 123 AA.
AC P02283; Q4ABE1; Q9W5U7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Histone H2B;
GN Name=His2B;
GN and
GN Name=His2B:CG17949; ORFNames=CG17949;
GN and
GN Name=His2B:CG33868; ORFNames=CG33868;
GN and
GN Name=His2B:CG33870; ORFNames=CG33870;
GN and
GN Name=His2B:CG33872; ORFNames=CG33872;
GN and
GN Name=His2B:CG33874; ORFNames=CG33874;
GN and
GN Name=His2B:CG33876; ORFNames=CG33876;
GN and
GN Name=His2B:CG33878; ORFNames=CG33878;
GN and
GN Name=His2B:CG33880; ORFNames=CG33880;
GN and
GN Name=His2B:CG33882; ORFNames=CG33882;
GN and
GN Name=His2B:CG33884; ORFNames=CG33884;
GN and
GN Name=His2B:CG33886; ORFNames=CG33886;
GN and
GN Name=His2B:CG33888; ORFNames=CG33888;
GN and
GN Name=His2B:CG33890; ORFNames=CG33890;
GN and
GN Name=His2B:CG33892; ORFNames=CG33892;
GN and
GN Name=His2B:CG33894; ORFNames=CG33894;
GN and
GN Name=His2B:CG33896; ORFNames=CG33896;
GN and
GN Name=His2B:CG33898; ORFNames=CG33898;
GN and
GN Name=His2B:CG33900; ORFNames=CG33900;
GN and
GN Name=His2B:CG33902; ORFNames=CG33902;
GN and
GN Name=His2B:CG33904; ORFNames=CG33904;
GN and
GN Name=His2B:CG33906; ORFNames=CG33906;
GN and
GN Name=His2B:CG33908; ORFNames=CG33908;
GN and
GN Name=His2B:CG33910; ORFNames=CG33910;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP PROTEIN SEQUENCE (HIS2B).
RX PubMed=117830; DOI=10.1021/bi00592a025;
RA Elgin S.C.R., Schilling J., Hood L.E.;
RT "Sequence of histone 2B of Drosophila melanogaster.";
RL Biochemistry 18:5679-5685(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2B).
RC STRAIN=AK-194;
RX PubMed=2536150; DOI=10.1093/nar/17.1.225;
RA Matsuo Y., Yamazaki T.;
RT "tRNA derived insertion element in histone gene repeating unit of
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 17:225-238(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS2B:CG17949).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118 (HIS2B).
RA Goldberg M.L.;
RL Thesis (1979), University of Stanford, United States.
RN [6]
RP METHYLATION AT PRO-2.
RX PubMed=3127388; DOI=10.1016/s0021-9258(18)68837-4;
RA Desrosiers R., Tanguay R.M.;
RT "Methylation of Drosophila histones at proline, lysine, and arginine
RT residues during heat shock.";
RL J. Biol. Chem. 263:4686-4692(1988).
RN [7]
RP RETRACTED PAPER.
RX PubMed=15143281; DOI=10.1126/science.1095001;
RA Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.;
RT "TAF1 activates transcription by phosphorylation of serine 33 in histone
RT H2B.";
RL Science 304:1010-1014(2004).
RN [8]
RP RETRACTION NOTICE OF PUBMED:15143281.
RX PubMed=24876484; DOI=10.1126/science.344.6187.981-a;
RA McNutt M.;
RL Science 344:981-981(2014).
RN [9]
RP PROBABLE UBIQUITINATION.
RX PubMed=15691768; DOI=10.1016/j.devcel.2004.11.020;
RA Bray S., Musisi H., Bienz M.;
RT "Bre1 is required for Notch signaling and histone modification.";
RL Dev. Cell 8:279-286(2005).
RN [10]
RP GLYCOSYLATION.
RX PubMed=22121020; DOI=10.1038/nature10656;
RA Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
RA Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H.,
RA Roeder R.G., Brown M., Kato S.;
RT "GlcNAcylation of histone H2B facilitates its monoubiquitination.";
RL Nature 480:557-560(2011).
RN [11]
RP SUCCINYLATION AT LYS-44; LYS-114 AND LYS-118.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- INTERACTION:
CC P02283; O15265: ATXN7; Xeno; NbExp=2; IntAct=EBI-188137, EBI-708350;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Monoubiquitination of Lys-118 by Bre1 gives a specific tag for
CC epigenetic transcriptional activation and is also prerequisite for
CC histone H3 'Lys-4' and 'Lys-79' methylation.
CC {ECO:0000305|PubMed:3127388}.
CC -!- PTM: Methylation at Pro-2 increases upon heat shock.
CC {ECO:0000269|PubMed:3127388}.
CC -!- PTM: GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-118.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC -!- CAUTION: Was reported to be phosphorylated at Ser-34. However, the
CC paper was retracted because some data, results and conclusions in the
CC paper are not reliable. {ECO:0000305|PubMed:15143281,
CC ECO:0000305|PubMed:24876484}.
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DR EMBL; X14215; CAA32432.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11124.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66483.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66487.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66492.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66496.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66501.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66506.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66511.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66521.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66531.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66576.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66571.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66566.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66561.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66556.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66551.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66546.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66541.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66536.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66479.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66581.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66526.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66516.1; -; Genomic_DNA.
DR PIR; S10095; HSFF22.
DR RefSeq; NP_001027283.1; NM_001032112.2.
DR RefSeq; NP_001027287.1; NM_001032116.2.
DR RefSeq; NP_001027291.1; NM_001032120.2.
DR RefSeq; NP_001027296.1; NM_001032125.2.
DR RefSeq; NP_001027300.1; NM_001032129.2.
DR RefSeq; NP_001027305.1; NM_001032134.2.
DR RefSeq; NP_001027310.1; NM_001032139.2.
DR RefSeq; NP_001027315.1; NM_001032144.2.
DR RefSeq; NP_001027320.1; NM_001032149.2.
DR RefSeq; NP_001027325.1; NM_001032154.2.
DR RefSeq; NP_001027330.1; NM_001032159.2.
DR RefSeq; NP_001027335.1; NM_001032164.2.
DR RefSeq; NP_001027340.1; NM_001032169.2.
DR RefSeq; NP_001027345.1; NM_001032174.2.
DR RefSeq; NP_001027350.1; NM_001032179.2.
DR RefSeq; NP_001027355.1; NM_001032184.2.
DR RefSeq; NP_001027360.1; NM_001032189.2.
DR RefSeq; NP_001027365.1; NM_001032194.2.
DR RefSeq; NP_001027370.1; NM_001032199.2.
DR RefSeq; NP_001027375.1; NM_001032204.2.
DR RefSeq; NP_001027380.1; NM_001032209.2.
DR RefSeq; NP_001027385.1; NM_001032214.2.
DR RefSeq; NP_724342.1; NM_165381.4.
DR PDB; 2NQB; X-ray; 2.30 A; D/H=2-123.
DR PDB; 2PYO; X-ray; 2.43 A; D/H=2-123.
DR PDB; 4QLC; X-ray; 3.50 A; D/H=2-123.
DR PDB; 4X23; X-ray; 3.50 A; D/H/N/R=33-122.
DR PDB; 5CVE; X-ray; 1.50 A; D/E=3-10.
DR PDB; 5WCU; X-ray; 5.53 A; D/H/N/R=29-122.
DR PDB; 6DZT; EM; 2.99 A; D/H=2-123.
DR PDB; 6PWE; EM; 3.95 A; D/H=1-123.
DR PDB; 6PWF; EM; 4.07 A; D/H=1-123.
DR PDB; 7PJ1; NMR; -; B=2-123.
DR PDBsum; 2NQB; -.
DR PDBsum; 2PYO; -.
DR PDBsum; 4QLC; -.
DR PDBsum; 4X23; -.
DR PDBsum; 5CVE; -.
DR PDBsum; 5WCU; -.
DR PDBsum; 6DZT; -.
DR PDBsum; 6PWE; -.
DR PDBsum; 6PWF; -.
DR PDBsum; 7PJ1; -.
DR AlphaFoldDB; P02283; -.
DR SMR; P02283; -.
DR BioGRID; 533862; 1.
DR BioGRID; 77520; 27.
DR DIP; DIP-22804N; -.
DR IntAct; P02283; 8.
DR MINT; P02283; -.
DR STRING; 7227.FBpp0085281; -.
DR GlyGen; P02283; 1 site.
DR iPTMnet; P02283; -.
DR PaxDb; P02283; -.
DR PRIDE; P02283; -.
DR ABCD; P02283; 1 sequenced antibody.
DR EnsemblMetazoa; FBtr0085927; FBpp0085281; FBgn0061209.
DR EnsemblMetazoa; FBtr0091872; FBpp0091113; FBgn0053868.
DR EnsemblMetazoa; FBtr0091874; FBpp0091115; FBgn0053870.
DR EnsemblMetazoa; FBtr0091876; FBpp0091117; FBgn0053872.
DR EnsemblMetazoa; FBtr0091878; FBpp0091119; FBgn0053874.
DR EnsemblMetazoa; FBtr0091880; FBpp0091121; FBgn0053876.
DR EnsemblMetazoa; FBtr0091882; FBpp0091123; FBgn0053878.
DR EnsemblMetazoa; FBtr0091884; FBpp0091125; FBgn0053880.
DR EnsemblMetazoa; FBtr0091886; FBpp0091127; FBgn0053882.
DR EnsemblMetazoa; FBtr0091888; FBpp0091129; FBgn0053884.
DR EnsemblMetazoa; FBtr0091890; FBpp0091131; FBgn0053886.
DR EnsemblMetazoa; FBtr0091892; FBpp0091133; FBgn0053888.
DR EnsemblMetazoa; FBtr0091894; FBpp0091135; FBgn0053890.
DR EnsemblMetazoa; FBtr0091896; FBpp0091137; FBgn0053892.
DR EnsemblMetazoa; FBtr0091898; FBpp0091139; FBgn0053894.
DR EnsemblMetazoa; FBtr0091900; FBpp0091141; FBgn0053896.
DR EnsemblMetazoa; FBtr0091902; FBpp0091143; FBgn0053898.
DR EnsemblMetazoa; FBtr0091904; FBpp0091145; FBgn0053900.
DR EnsemblMetazoa; FBtr0091906; FBpp0091147; FBgn0053902.
DR EnsemblMetazoa; FBtr0091908; FBpp0091149; FBgn0053904.
DR EnsemblMetazoa; FBtr0091910; FBpp0091151; FBgn0053906.
DR EnsemblMetazoa; FBtr0091912; FBpp0091153; FBgn0053908.
DR EnsemblMetazoa; FBtr0091914; FBpp0091155; FBgn0053910.
DR GeneID; 326273; -.
DR GeneID; 3771809; -.
DR GeneID; 3771891; -.
DR GeneID; 3771957; -.
DR GeneID; 3772013; -.
DR GeneID; 3772058; -.
DR GeneID; 3772081; -.
DR GeneID; 3772083; -.
DR GeneID; 3772094; -.
DR GeneID; 3772099; -.
DR GeneID; 3772104; -.
DR GeneID; 3772166; -.
DR GeneID; 3772203; -.
DR GeneID; 3772248; -.
DR GeneID; 3772264; -.
DR GeneID; 3772265; -.
DR GeneID; 3772271; -.
DR GeneID; 3772276; -.
DR GeneID; 3772299; -.
DR GeneID; 3772336; -.
DR GeneID; 3772496; -.
DR GeneID; 3772502; -.
DR GeneID; 3772575; -.
DR KEGG; dme:Dmel_CG17949; -.
DR KEGG; dme:Dmel_CG33868; -.
DR KEGG; dme:Dmel_CG33870; -.
DR KEGG; dme:Dmel_CG33872; -.
DR KEGG; dme:Dmel_CG33874; -.
DR KEGG; dme:Dmel_CG33876; -.
DR KEGG; dme:Dmel_CG33878; -.
DR KEGG; dme:Dmel_CG33880; -.
DR KEGG; dme:Dmel_CG33882; -.
DR KEGG; dme:Dmel_CG33884; -.
DR KEGG; dme:Dmel_CG33886; -.
DR KEGG; dme:Dmel_CG33888; -.
DR KEGG; dme:Dmel_CG33890; -.
DR KEGG; dme:Dmel_CG33892; -.
DR KEGG; dme:Dmel_CG33894; -.
DR KEGG; dme:Dmel_CG33896; -.
DR KEGG; dme:Dmel_CG33898; -.
DR KEGG; dme:Dmel_CG33900; -.
DR KEGG; dme:Dmel_CG33902; -.
DR KEGG; dme:Dmel_CG33904; -.
DR KEGG; dme:Dmel_CG33906; -.
DR KEGG; dme:Dmel_CG33908; -.
DR KEGG; dme:Dmel_CG33910; -.
DR UCSC; CG17949-RA; d. melanogaster.
DR CTD; 326273; -.
DR CTD; 3771809; -.
DR CTD; 3771891; -.
DR CTD; 3771957; -.
DR CTD; 3772013; -.
DR CTD; 3772058; -.
DR CTD; 3772081; -.
DR CTD; 3772083; -.
DR CTD; 3772094; -.
DR CTD; 3772099; -.
DR CTD; 3772104; -.
DR CTD; 3772166; -.
DR CTD; 3772203; -.
DR CTD; 3772248; -.
DR CTD; 3772264; -.
DR CTD; 3772265; -.
DR CTD; 3772271; -.
DR CTD; 3772276; -.
DR CTD; 3772299; -.
DR CTD; 3772336; -.
DR CTD; 3772496; -.
DR CTD; 3772502; -.
DR CTD; 3772575; -.
DR FlyBase; FBgn0001198; His2B.
DR FlyBase; FBgn0061209; His2B:CG17949.
DR FlyBase; FBgn0053868; His2B:CG33868.
DR FlyBase; FBgn0053870; His2B:CG33870.
DR FlyBase; FBgn0053872; His2B:CG33872.
DR FlyBase; FBgn0053874; His2B:CG33874.
DR FlyBase; FBgn0053876; His2B:CG33876.
DR FlyBase; FBgn0053878; His2B:CG33878.
DR FlyBase; FBgn0053880; His2B:CG33880.
DR FlyBase; FBgn0053882; His2B:CG33882.
DR FlyBase; FBgn0053884; His2B:CG33884.
DR FlyBase; FBgn0053886; His2B:CG33886.
DR FlyBase; FBgn0053888; His2B:CG33888.
DR FlyBase; FBgn0053890; His2B:CG33890.
DR FlyBase; FBgn0053892; His2B:CG33892.
DR FlyBase; FBgn0053894; His2B:CG33894.
DR FlyBase; FBgn0053896; His2B:CG33896.
DR FlyBase; FBgn0053898; His2B:CG33898.
DR FlyBase; FBgn0053900; His2B:CG33900.
DR FlyBase; FBgn0053902; His2B:CG33902.
DR FlyBase; FBgn0053904; His2B:CG33904.
DR FlyBase; FBgn0053906; His2B:CG33906.
DR FlyBase; FBgn0053908; His2B:CG33908.
DR FlyBase; FBgn0053910; His2B:CG33910.
DR VEuPathDB; VectorBase:FBgn0053868; -.
DR VEuPathDB; VectorBase:FBgn0053870; -.
DR VEuPathDB; VectorBase:FBgn0053872; -.
DR VEuPathDB; VectorBase:FBgn0053874; -.
DR VEuPathDB; VectorBase:FBgn0053876; -.
DR VEuPathDB; VectorBase:FBgn0053878; -.
DR VEuPathDB; VectorBase:FBgn0053880; -.
DR VEuPathDB; VectorBase:FBgn0053882; -.
DR VEuPathDB; VectorBase:FBgn0053884; -.
DR VEuPathDB; VectorBase:FBgn0053886; -.
DR VEuPathDB; VectorBase:FBgn0053888; -.
DR VEuPathDB; VectorBase:FBgn0053890; -.
DR VEuPathDB; VectorBase:FBgn0053892; -.
DR VEuPathDB; VectorBase:FBgn0053894; -.
DR VEuPathDB; VectorBase:FBgn0053896; -.
DR VEuPathDB; VectorBase:FBgn0053898; -.
DR VEuPathDB; VectorBase:FBgn0053900; -.
DR VEuPathDB; VectorBase:FBgn0053902; -.
DR VEuPathDB; VectorBase:FBgn0053904; -.
DR VEuPathDB; VectorBase:FBgn0053906; -.
DR VEuPathDB; VectorBase:FBgn0053908; -.
DR VEuPathDB; VectorBase:FBgn0053910; -.
DR VEuPathDB; VectorBase:FBgn0061209; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_0_1; -.
DR InParanoid; P02283; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P02283; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-3214847; HATs acetylate histones.
DR Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; P02283; -.
DR EvolutionaryTrace; P02283; -.
DR PRO; PR:P02283; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0053868; Expressed in midgut and 11 other tissues.
DR Genevisible; P02283; DM.
DR GO; GO:0000786; C:nucleosome; TAS:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; ISS:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR DisProt; DP01250; -.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
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 3D-structure; Chromosome; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..123
FT /note="Histone H2B"
FT /id="PRO_0000071861"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-methylproline; partial"
FT /evidence="ECO:0000269|PubMed:3127388"
FT MOD_RES 44
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 114
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 118
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="R -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7PJ1"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7PJ1"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 54..81
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6DZT"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:2NQB"
SQ SEQUENCE 123 AA; 13696 MW; 0774D25F34003062 CRC64;
MPPKTSGKAA KKAGKAQKNI TKTDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM
NSFVNDIFER IAAEASRLAH YNKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT
SSK
