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Database: UniProt
Entry: P02293
LinkDB: P02293
Original site: P02293 
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   07-APR-2021, entry version 212.
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;
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;
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   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   SMR; P02293; -.
DR   BioGRID; 32276; 426.
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; ENSGT01020000230503; -.
DR   HOGENOM; CLU_075666_1_3_1; -.
DR   InParanoid; P02293; -.
DR   OMA; DIFDRMA; -.
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-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
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: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:0006333; P:chromatin assembly or disassembly; 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   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   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:0007744|PDB:6AE8"
FT   STRAND          57..59
FT                   /evidence="ECO:0007744|PDB:6AE8"
FT   HELIX           60..87
FT                   /evidence="ECO:0007744|PDB:6AE8"
FT   STRAND          91..93
FT                   /evidence="ECO:0007744|PDB:6AE8"
FT   HELIX           95..105
FT                   /evidence="ECO:0007744|PDB:6AE8"
FT   HELIX           108..126
FT                   /evidence="ECO:0007744|PDB:6AE8"
SQ   SEQUENCE   131 AA;  14252 MW;  9F5E9CFB341DB399 CRC64;
     MSAKAEKKPA SKAPAEKKPA AKKTSTSTDG KKRSKARKET YSSYIYKVLK QTHPDTGISQ
     KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT AVRLILPGEL AKHAVSEGTR
     AVTKYSSSTQ A
//
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