ID H2B1_YEAST Reviewed; 131 AA. AC P02293; D6VSK6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 226. DE RecName: Full=Histone H2B.1; DE AltName: Full=Suppressor of Ty protein 12; GN Name=HTB1; Synonyms=H2B1, SPT12; OrderedLocusNames=YDR224C; GN ORFNames=YD9934.09C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7006833; DOI=10.1016/0092-8674(80)90556-5; RA Wallis J.W., Hereford L., Grunstein M.; RT "Histone H2B genes of yeast encode two different proteins."; RL Cell 22:799-805(1980). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7885847; DOI=10.1093/nar/23.3.507; RA Davies C.J., Hutchison C.A. III; RT "Insertion site specificity of the transposon Tn3."; RL Nucleic Acids Res. 23:507-514(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP PROTEIN SEQUENCE OF 64-89, AND PROBABLE CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=7002547; DOI=10.1111/j.1432-1033.1980.tb04841.x; RA Brandt W.F., Patterson K., von Holt C.; RT "The histones of yeast. The isolation and partial structure of the core RT histones."; RL Eur. J. Biochem. 110:67-76(1980). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-131. RX PubMed=2188095; DOI=10.1128/mcb.10.6.2687-2694.1990; RA Xu H., Johnson L., Grunstein M.; RT "Coding and noncoding sequences at the 3' end of yeast histone H2B mRNA RT confer cell cycle regulation."; RL Mol. Cell. Biol. 10:2687-2694(1990). RN [8] RP ACETYLATION. RX PubMed=10777603; DOI=10.1074/jbc.275.17.13007; RA Waterborg J.H.; RT "Steady-state levels of histone acetylation in Saccharomyces cerevisiae."; RL J. Biol. Chem. 275:13007-13011(2000). RN [9] RP UBIQUITINATION AT LYS-124, AND MUTAGENESIS OF LYS-124. RX PubMed=10642555; DOI=10.1126/science.287.5452.501; RA Robzyk K., Recht J., Osley M.A.; RT "Rad6-dependent ubiquitination of histone H2B in yeast."; RL Science 287:501-504(2000). RN [10] RP ACETYLATION AT LYS-12 AND LYS-17. RX PubMed=11545749; DOI=10.1016/s1097-2765(01)00301-x; RA Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.; RT "Highly specific antibodies determine histone acetylation site usage in RT yeast heterochromatin and euchromatin."; RL Mol. Cell 8:473-479(2001). RN [11] RP FUNCTION, AND MUTAGENESIS OF VAL-48; TYR-87 AND ASN-88. RX PubMed=11973294; DOI=10.1093/genetics/160.4.1375; RA Martini E.M.D., Keeney S., Osley M.A.; RT "A role for histone H2B during repair of UV-induced DNA damage in RT Saccharomyces cerevisiae."; RL Genetics 160:1375-1387(2002). RN [12] RP FUNCTION, AND MUTAGENESIS OF LYS-124. RX PubMed=12152067; DOI=10.1038/nature00970; RA Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J., Hunt D.F., RA Allis C.D., Strahl B.D.; RT "Gene silencing: trans-histone regulatory pathway in chromatin."; RL Nature 418:498-498(2002). RN [13] RP UBIQUITINATION, AND DEUBIQUITINATION BY UBP8. RX PubMed=14563679; DOI=10.1101/gad.1144003; RA Henry K.W., Wyce A., Lo W.-S., Duggan L.J., Emre N.C.T., Kao C.-F., RA Pillus L., Shilatifard A., Osley M.A., Berger S.L.; RT "Transcriptional activation via sequential histone H2B ubiquitylation and RT deubiquitylation, mediated by SAGA-associated Ubp8."; RL Genes Dev. 17:2648-2663(2003). RN [14] RP UBIQUITINATION AT LYS-124. RX PubMed=12535538; DOI=10.1016/s1097-2765(02)00826-2; RA Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., RA Madhani H.D.; RT "A conserved RING finger protein required for histone H2B RT monoubiquitination and cell size control."; RL Mol. Cell 11:261-266(2003). RN [15] RP UBIQUITINATION AT LYS-124. RX PubMed=12535539; DOI=10.1016/s1097-2765(02)00802-x; RA Wood A., Krogan N.J., Dover J., Schneider J., Heidt J., Boateng M.A., RA Dean K., Golshani A., Zhang Y., Greenblatt J.F., Johnston M., RA Shilatifard A.; RT "Bre1, an E3 ubiquitin ligase required for recruitment and substrate RT selection of Rad6 at a promoter."; RL Mol. Cell 11:267-274(2003). RN [16] RP ACETYLATION AT LYS-12 AND LYS-17. RX PubMed=15186774; DOI=10.1016/j.cell.2004.05.023; RA Kurdistani S.K., Tavazoie S., Grunstein M.; RT "Mapping global histone acetylation patterns to gene expression."; RL Cell 117:721-733(2004). RN [17] RP UBIQUITINATION BY UBC2, AND FUNCTION. RX PubMed=14752010; DOI=10.1101/gad.1149604; RA Kao C.-F., Hillyer C., Tsukuda T., Henry K.W., Berger S.L., Osley M.A.; RT "Rad6 plays a role in transcriptional activation through ubiquitylation of RT histone H2B."; RL Genes Dev. 18:184-195(2004). RN [18] RP UBIQUITINATION AT LYS-124, AND MUTAGENESIS OF LYS-124. RX PubMed=14660635; DOI=10.1074/jbc.c300505200; RA Dong L., Xu C.W.; RT "Carbohydrates induce mono-ubiquitination of H2B in yeast."; RL J. Biol. Chem. 279:1577-1580(2004). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15166219; DOI=10.1074/jbc.m404173200; RA Zhou W., Ryan J.J., Zhou H.; RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. RT Induction of protein sumoylation by cellular stresses."; RL J. Biol. Chem. 279:32262-32268(2004). RN [20] RP FUNCTION, UBIQUITINATION AT LYS-124 BY THE UBC2-BRE1 COMPLEX, AND RP MUTAGENESIS OF LYS-124. RX PubMed=15280549; DOI=10.1073/pnas.0400078101; RA Yamashita K., Shinohara M., Shinohara A.; RT "Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of RT double-strand breaks during meiosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11380-11385(2004). RN [21] RP PHOSPHORYLATION AT SER-11, MUTAGENESIS OF SER-11, AND FUNCTION. RX PubMed=15652479; DOI=10.1016/j.cell.2004.11.016; RA Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.; RT "Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen RT peroxide-induced apoptosis in S. cerevisiae."; RL Cell 120:25-36(2005). RN [22] RP PHOSPHORYLATION AT SER-11, AND FUNCTION. RX PubMed=15970663; DOI=10.4161/cc.4.6.1745; RA Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.; RT "H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S. RT cerevisiae."; RL Cell Cycle 4:780-783(2005). RN [23] RP FUNCTION, AND MUTAGENESIS OF LYS-124. RX PubMed=15632126; DOI=10.1074/jbc.m414453200; RA Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.; RT "The DNA damage checkpoint response requires histone H2B ubiquitination by RT Rad6-Bre1 and H3 methylation by Dot1."; RL J. Biol. Chem. 280:9879-9886(2005). RN [24] RP UBIQUITINATION BY THE UBC2-BRE1 COMPLEX, AND FUNCTION. RX PubMed=15632065; DOI=10.1128/mcb.25.2.637-651.2005; RA Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A., RA Strahl B.D.; RT "Histone H2B ubiquitylation is associated with elongating RNA polymerase RT II."; RL Mol. Cell. Biol. 25:637-651(2005). RN [25] RP DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX. RX PubMed=15657441; DOI=10.1128/mcb.25.3.1162-1172.2005; RA Ingvarsdottir K., Krogan N.J., Emre N.C.T., Wyce A., Thompson N.J., RA Emili A., Hughes T.R., Greenblatt J.F., Berger S.L.; RT "H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional RT module within the Saccharomyces cerevisiae SAGA complex."; RL Mol. Cell. Biol. 25:1162-1172(2005). RN [26] RP DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX. RX PubMed=15657442; DOI=10.1128/mcb.25.3.1173-1182.2005; RA Lee K.K., Florens L., Swanson S.K., Washburn M.P., Workman J.L.; RT "The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its RT association with the SAGA complex."; RL Mol. Cell. Biol. 25:1173-1182(2005). RN [27] RP SUMOYLATION AT LYS-7; LYS-8; LYS-17 AND LYS-18, ACETYLATION AT LYS-7; LYS-8 RP AND LYS-17, MUTAGENESIS OF 7-LYS-LYS-8 AND 17-LYS-LYS-18, FUNCTION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16598039; DOI=10.1101/gad.1404206; RA Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M., RA Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., RA Johnson E.S., Berger S.L.; RT "Histone sumoylation is a negative regulator in Saccharomyces cerevisiae RT and shows dynamic interplay with positive-acting histone modifications."; RL Genes Dev. 20:966-976(2006). RN [28] RP UBIQUITINATION AT LYS-124. RX PubMed=16432255; DOI=10.1074/mcp.m500368-mcp200; RA Tagwerker C., Flick K., Cui M., Guerrero C., Dou Y., Auer B., Baldi P., RA Huang L., Kaiser P.; RT "A tandem affinity tag for two-step purification under fully denaturing RT conditions: application in ubiquitin profiling and protein complex RT identification combined with in vivocross-linking."; RL Mol. Cell. Proteomics 5:737-748(2006). RN [29] RP ACETYLATION AT LYS-17; LYS-18; LYS-22 AND LYS-23, BUTYRYLATION AT LYS-22, RP AND METHYLATION AT LYS-23 AND LYS-38. RX PubMed=19113941; DOI=10.1021/pr8005155; RA Zhang K., Chen Y., Zhang Z., Zhao Y.; RT "Identification and verification of lysine propionylation and butyrylation RT in yeast core histones using PTMap software."; RL J. Proteome Res. 8:900-906(2009). RN [30] RP SUCCINYLATION AT LYS-35 AND LYS-47. 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). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [32] RP STRUCTURE BY NMR OF 37-131. RX PubMed=18641662; DOI=10.1038/nsmb.1465; RA Zhou Z., Feng H., Hansen D.F., Kato H., Luk E., Freedberg D.I., Kay L.E., RA Wu C., Bai Y.; RT "NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B."; RL Nat. Struct. Mol. Biol. 15:868-869(2008). 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. {ECO:0000269|PubMed:11973294, CC ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14752010, CC ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632065, CC ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:15652479, CC ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:16598039}. 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 P02293; P32597: STH1; NbExp=3; IntAct=EBI-8088, EBI-18410; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- PTM: Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form CC H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic CC transcriptional activation and is also prerequisite for H3K4me and CC H3K79me formation. H2BK123ub1 also modulates the formation of double- CC strand breaks during meiosis and is a prerequisite for DNA-damage CC checkpoint activation. Deubiquitination is performed by UBP8 in CC presence of SGF11. CC -!- PTM: Phosphorylated by STE20 to form H2BS10ph during progression CC through meiotic prophase. May be correlated with chromosome CC condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is CC a step leading to apoptosis. {ECO:0000269|PubMed:15652479, CC ECO:0000269|PubMed:15970663}. CC -!- PTM: Acetylated by GCN5, a component of the SAGA complex, to form CC H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component CC of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N- CC terminal lysines and particularly formation of H2BK11acK16ac has a CC positive effect on transcription. {ECO:0000269|PubMed:10777603, CC ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, CC ECO:0000269|PubMed:16598039}. CC -!- PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su CC or H2BK17su, occurs preferentially near the telomeres and represses CC gene transcription. {ECO:0000269|PubMed:15166219, CC ECO:0000269|PubMed:16598039}. CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}. CC -!- CAUTION: To ensure consistency between histone entries, we follow the CC 'Brno' nomenclature for histone modifications, with positions referring CC to those used in the literature for the 'closest' model organism. Due CC to slight variations in histone sequences between organisms and to the CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the CC actual positions of modified amino acids in the sequence generally CC differ. In this entry the following conventions are used: H2BK6ac = CC acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys- CC 8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; CC H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = CC sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = CC monoubiquitinated Lys-124. {ECO:0000305}. 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; J01327; AAA88719.1; -; Genomic_DNA. DR EMBL; U13239; AAC33141.1; -; Genomic_DNA. DR EMBL; Z48612; CAA88504.1; -; Genomic_DNA. DR EMBL; AY557724; AAS56050.1; -; Genomic_DNA. DR EMBL; M37743; AAA34694.2; -; mRNA. DR EMBL; BK006938; DAA12066.1; -; Genomic_DNA. DR PIR; A02621; HSBY22. DR RefSeq; NP_010510.3; NM_001180532.3. DR PDB; 2JSS; NMR; -; A=37-131. DR PDB; 4KUD; X-ray; 3.20 A; D/H=1-131. DR PDB; 4M6B; X-ray; 1.78 A; A/D=37-131. DR PDB; 4WNN; X-ray; 1.80 A; B/D/F/H=31-131. DR PDB; 5BT1; X-ray; 2.62 A; D=1-131. DR PDB; 6AE8; X-ray; 1.65 A; A/B=37-131. DR PDB; 6GEJ; EM; 3.60 A; G/H=1-131. DR PDB; 6GEN; EM; 3.60 A; G/H=1-131. DR PDB; 6QLD; EM; 4.15 A; h=36-129. DR PDB; 7DLX; X-ray; 2.40 A; A/B/C/D/E/F/G/H=37-131. DR PDB; 7K78; EM; 3.10 A; D/H=1-131. DR PDB; 7K7G; EM; 4.20 A; D/H=1-131. DR PDB; 7ON1; EM; 3.35 A; d/h=1-131. DR PDB; 7SSA; EM; 3.20 A; D/H=2-131. DR PDB; 8OW0; EM; 3.40 A; d/h=1-131. DR PDB; 8OW1; EM; 3.70 A; d/h=1-131. DR PDBsum; 2JSS; -. DR PDBsum; 4KUD; -. DR PDBsum; 4M6B; -. DR PDBsum; 4WNN; -. DR PDBsum; 5BT1; -. DR PDBsum; 6AE8; -. DR PDBsum; 6GEJ; -. DR PDBsum; 6GEN; -. DR PDBsum; 6QLD; -. DR PDBsum; 7DLX; -. DR PDBsum; 7K78; -. DR PDBsum; 7K7G; -. DR PDBsum; 7ON1; -. DR PDBsum; 7SSA; -. DR PDBsum; 8OW0; -. DR PDBsum; 8OW1; -. DR AlphaFoldDB; P02293; -. DR EMDB; EMD-12993; -. DR EMDB; EMD-17226; -. DR EMDB; EMD-17227; -. DR EMDB; EMD-22696; -. DR EMDB; EMD-22698; -. DR EMDB; EMD-25406; -. DR EMDB; EMD-4395; -. DR EMDB; EMD-4396; -. DR EMDB; EMD-4579; -. DR SMR; P02293; -. DR BioGRID; 32276; 515. DR ComplexPortal; CPX-1611; Nucleosome, variant HTA2-HTB1. DR ComplexPortal; CPX-1612; Nucleosome, variant HTA1-HTB1. DR ComplexPortal; CPX-1613; Nucleosome, variant HTZ1-HTB1. DR DIP; DIP-416N; -. DR ELM; P02293; -. DR IntAct; P02293; 241. DR MINT; P02293; -. DR STRING; 4932.YDR224C; -. DR iPTMnet; P02293; -. DR MaxQB; P02293; -. DR PaxDb; 4932-YDR224C; -. DR PeptideAtlas; P02293; -. DR EnsemblFungi; YDR224C_mRNA; YDR224C; YDR224C. DR GeneID; 851810; -. DR KEGG; sce:YDR224C; -. DR AGR; SGD:S000002632; -. DR SGD; S000002632; HTB1. DR VEuPathDB; FungiDB:YDR224C; -. DR eggNOG; KOG1744; Eukaryota. DR GeneTree; ENSGT01100000263569; -. DR HOGENOM; CLU_075666_1_3_1; -. DR InParanoid; P02293; -. DR OMA; DIFDRMA; -. DR OrthoDB; 231723at2759; -. DR BioCyc; YEAST:G3O-29804-MONOMER; -. DR BioGRID-ORCS; 851810; 4 hits in 10 CRISPR screens. DR EvolutionaryTrace; P02293; -. DR PRO; PR:P02293; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P02293; Protein. DR GO; GO:0000786; C:nucleosome; IDA:SGD. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IDA:SGD. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; IDA:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006301; P:postreplication repair; IGI:SGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR IDEAL; IID50196; -. 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305" FT CHAIN 2..131 FT /note="Histone H2B.1" FT /id="PRO_0000071938" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 7 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16598039" FT MOD_RES 8 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16598039" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15652479, FT ECO:0000269|PubMed:15970663" FT MOD_RES 12 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:11545749, FT ECO:0000269|PubMed:15186774" FT MOD_RES 17 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:11545749, FT ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, FT ECO:0000269|PubMed:19113941" FT MOD_RES 18 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 22 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 22 FT /note="N6-butyryllysine; alternate" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 23 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 23 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 35 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:22389435" FT MOD_RES 38 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:19113941" FT MOD_RES 47 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:22389435" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 8 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 17 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000305" FT CROSSLNK 18 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000305" FT CROSSLNK 124 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:10642555, FT ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, FT ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, FT ECO:0000269|PubMed:16432255" FT MUTAGEN 7..8 FT /note="KK->AA: Reduces sumoylation." FT /evidence="ECO:0000269|PubMed:16598039" FT MUTAGEN 11 FT /note="S->A: Desensitizes cells to H(2)O(2) treatment." FT /evidence="ECO:0000269|PubMed:15652479" FT MUTAGEN 11 FT /note="S->E: Induces apoptotic-like features including FT chromatin condensation." FT /evidence="ECO:0000269|PubMed:15652479" FT MUTAGEN 17..18 FT /note="KK->AA: Reduces sumoylation." FT /evidence="ECO:0000269|PubMed:16598039" FT MUTAGEN 48 FT /note="V->F: Confers UV-radiation sensitivity; when FT associated with F-87 and S-88." FT /evidence="ECO:0000269|PubMed:11973294" FT MUTAGEN 87 FT /note="Y->F: Confers UV-radiation sensitivity; when FT associated with F-48 and S-88." FT /evidence="ECO:0000269|PubMed:11973294" FT MUTAGEN 88 FT /note="N->S: Confers UV-radiation sensitivity; when FT associated with F-48 and F-87." FT /evidence="ECO:0000269|PubMed:11973294" FT MUTAGEN 124 FT /note="K->R: Impairs ubiquitin conjugation, DNA FT double-strand brakes formation during meiosis and histone FT H3-K79 methylation." FT /evidence="ECO:0000269|PubMed:10642555, FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14660635, FT ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632126" FT HELIX 42..52 FT /evidence="ECO:0007829|PDB:6AE8" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:6AE8" FT HELIX 60..87 FT /evidence="ECO:0007829|PDB:6AE8" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:6AE8" FT HELIX 95..105 FT /evidence="ECO:0007829|PDB:6AE8" FT HELIX 108..126 FT /evidence="ECO:0007829|PDB:6AE8" SQ SEQUENCE 131 AA; 14252 MW; 9F5E9CFB341DB399 CRC64; MSAKAEKKPA SKAPAEKKPA AKKTSTSTDG KKRSKARKET YSSYIYKVLK QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT AVRLILPGEL AKHAVSEGTR AVTKYSSSTQ A //