H2B1_YEAST
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 03-AUG-2022, entry version 217.
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}.
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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 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 AlphaFoldDB; P02293; -.
DR SMR; P02293; -.
DR BioGRID; 32276; 435.
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; P02293; -.
DR PRIDE; P02293; -.
DR EnsemblFungi; YDR224C_mRNA; YDR224C; YDR224C.
DR GeneID; 851810; -.
DR KEGG; sce:YDR224C; -.
DR SGD; S000002632; HTB1.
DR VEuPathDB; FungiDB:YDR224C; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244943; -.
DR HOGENOM; CLU_075666_1_3_1; -.
DR InParanoid; P02293; -.
DR OMA; DIFDRMA; -.
DR BioCyc; YEAST:G3O-29804-MON; -.
DR Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
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; IC: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:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0006301; P:postreplication repair; IGI:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID50196; -.
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; 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 double-
FT strand brakes formation during meiosis and histone H3-K79
FT 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
