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 27-MAR-2024, entry version 217. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7XYF; EM; 4.30 A; D/H=29-123. DR PDB; 7XYG; EM; 5.40 A; D/H=1-123. DR PDB; 8UX1; EM; 2.50 A; D/H=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 PDBsum; 7XYF; -. DR PDBsum; 7XYG; -. DR PDBsum; 8UX1; -. DR AlphaFoldDB; P02283; -. DR EMDB; EMD-20506; -. DR EMDB; EMD-20507; -. DR EMDB; EMD-42685; -. DR EMDB; EMD-8938; -. DR SASBDB; 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 GlyCosmos; P02283; 1 site, No reported glycans. DR GlyGen; P02283; 1 site. DR iPTMnet; P02283; -. DR PaxDb; 7227-FBpp0085281; -. 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 AGR; FB:FBgn0001198; -. DR AGR; FB:FBgn0053868; -. DR AGR; FB:FBgn0053870; -. DR AGR; FB:FBgn0053872; -. DR AGR; FB:FBgn0053874; -. DR AGR; FB:FBgn0053876; -. DR AGR; FB:FBgn0053878; -. DR AGR; FB:FBgn0053880; -. DR AGR; FB:FBgn0053882; -. DR AGR; FB:FBgn0053884; -. DR AGR; FB:FBgn0053886; -. DR AGR; FB:FBgn0053888; -. DR AGR; FB:FBgn0053890; -. DR AGR; FB:FBgn0053892; -. DR AGR; FB:FBgn0053894; -. DR AGR; FB:FBgn0053896; -. DR AGR; FB:FBgn0053898; -. DR AGR; FB:FBgn0053900; -. DR AGR; FB:FBgn0053902; -. DR AGR; FB:FBgn0053904; -. DR AGR; FB:FBgn0053906; -. DR AGR; FB:FBgn0053908; -. DR AGR; FB:FBgn0053910; -. DR AGR; FB:FBgn0061209; -. 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; ENSGT01100000263569; -. DR HOGENOM; CLU_075666_2_0_1; -. DR InParanoid; P02283; -. DR OMA; TEMGAGE; -. DR OrthoDB; 3566571at2759; -. DR PhylomeDB; P02283; -. DR Reactome; R-DME-3214847; HATs acetylate histones. DR Reactome; R-DME-5689880; Ub-specific processing proteases. 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 SignaLink; P02283; -. DR EvolutionaryTrace; P02283; -. DR PRO; PR:P02283; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0053868; Expressed in midgut and 11 other cell types or tissues. 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 DisProt; DP01250; -. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000558; Histone_H2B. DR PANTHER; PTHR23428; HISTONE H2B; 1. DR PANTHER; PTHR23428:SF70; 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. DR Genevisible; P02283; DM. 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 //