H3_YEAST
ID H3_YEAST Reviewed; 136 AA.
AC P61830; D6VQ11; E9PAG1; P02303; P13996; Q6B1U3; Q6Q7G9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Histone H3;
GN Name=HHT1; OrderedLocusNames=YBR010W; ORFNames=YBR0201;
GN and
GN Name=HHT2; Synonyms=SIN2; OrderedLocusNames=YNL031C; ORFNames=N2749;
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=6355483; DOI=10.1016/s0022-2836(83)80164-8;
RA Smith M.M., Andresson O.S.;
RT "DNA sequences of yeast H3 and H4 histone genes from two non-allelic gene
RT sets encode identical H3 and H4 proteins.";
RL J. Mol. Biol. 169:663-690(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION (HHT1 AND HHT2).
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] (HHT1 AND HHT2).
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 2-136.
RX PubMed=7035169; DOI=10.1111/j.1432-1033.1982.tb05815.x;
RA Brandt W.F., von Holt C.;
RT "The primary structure of yeast histone H3.";
RL Eur. J. Biochem. 121:501-510(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
RC STRAIN=ATCC 204508 / S288c, M13, M14, M22, M32, M34, M5, M8, and YPS163;
RX PubMed=15059259; DOI=10.1186/gb-2004-5-4-r26;
RA Fay J.C., McCullough H.L., Sniegowski P.D., Eisen M.B.;
RT "Population genetic variation in gene expression is associated with
RT phenotypic variation in Saccharomyces cerevisiae.";
RL Genome Biol. 5:R26.1-R26.14(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-16.
RX PubMed=782914; DOI=10.1016/0014-5793(76)80153-6;
RA Brandt W.F., von Holt C.;
RT "The occurrence of histone H3 and H4 in yeast.";
RL FEBS Lett. 65:386-390(1976).
RN [9]
RP PROTEIN SEQUENCE OF 28-41, AND ACETYLATION AT LYS-37.
RX PubMed=17189264; DOI=10.1074/jbc.m607909200;
RA Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J.,
RA Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT "Identification of histone H3 lysine 36 acetylation as a highly conserved
RT histone modification.";
RL J. Biol. Chem. 282:7632-7640(2007).
RN [10]
RP PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, AND MUTAGENESIS OF
RP ARG-53; LYS-57; LYS-80 AND THR-119.
RX PubMed=16260619; DOI=10.1128/mcb.25.22.10060-10070.2005;
RA Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A., Cottee R.J.,
RA Boeke J.D.;
RT "Insights into the role of histone H3 and histone H4 core modifiable
RT residues in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 25:10060-10070(2005).
RN [11]
RP IDENTIFICATION IN THE UAF COMPLEX.
RX PubMed=9391047; DOI=10.1073/pnas.94.25.13458;
RA Keener J., Dodd J.A., Lalo D., Nomura M.;
RT "Histones H3 and H4 are components of upstream activation factor required
RT for the high-level transcription of yeast rDNA by RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997).
RN [12]
RP ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
RX PubMed=9606197; DOI=10.1093/emboj/17.11.3155;
RA Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y.;
RT "Essential and redundant functions of histone acetylation revealed by
RT mutation of target lysines and loss of the Gcn5p acetyltransferase.";
RL EMBO J. 17:3155-3167(1998).
RN [13]
RP ACETYLATION AT LYS-15.
RX PubMed=10082517; DOI=10.1128/mcb.19.4.2515;
RA Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
RT "Esa1p is an essential histone acetyltransferase required for cell cycle
RT progression.";
RL Mol. Cell. Biol. 19:2515-2526(1999).
RN [14]
RP PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, AND
RP MUTAGENESIS OF SER-11.
RX PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9;
RA Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
RA Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M.,
RA Allis C.D.;
RT "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase
RT and Glc7/PP1 phosphatase in budding yeast and nematodes.";
RL Cell 102:279-291(2000).
RN [15]
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 [16]
RP PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, AND MUTAGENESIS OF
RP SER-11.
RX PubMed=10911986; DOI=10.1016/s1097-2765(00)80257-9;
RA Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D.,
RA Marmorstein R., Berger S.L.;
RT "Phosphorylation of serine 10 in histone H3 is functionally linked in vitro
RT and in vivo to Gcn5-mediated acetylation at lysine 14.";
RL Mol. Cell 5:917-926(2000).
RN [17]
RP METHYLATION AT LYS-5.
RX PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
RA Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
RA Aasland R., Stewart A.F.;
RT "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and
RT methylates histone 3 lysine 4.";
RL EMBO J. 20:7137-7148(2001).
RN [18]
RP METHYLATION AT LYS-5.
RX PubMed=11751634; DOI=10.1101/gad.940201;
RA Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R.,
RA Winston F., Allis C.D.;
RT "Histone H3 lysine 4 methylation is mediated by Set1 and required for cell
RT growth and rDNA silencing in Saccharomyces cerevisiae.";
RL Genes Dev. 15:3286-3295(2001).
RN [19]
RP ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
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 [20]
RP METHYLATION AT LYS-80, AND MUTAGENESIS OF LYS-80.
RX PubMed=12080090; DOI=10.1101/gad.1001502;
RA Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y.,
RA Struhl K.;
RT "Lysine methylation within the globular domain of histone H3 by Dot1 is
RT important for telomeric silencing and Sir protein association.";
RL Genes Dev. 16:1518-1527(2002).
RN [21]
RP METHYLATION AT LYS-80.
RX PubMed=12097318; DOI=10.1074/jbc.c200366200;
RA Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
RT "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
RT methyltransferase.";
RL J. Biol. Chem. 277:30421-30424(2002).
RN [22]
RP METHYLATION AT LYS-37.
RX PubMed=11839797; DOI=10.1128/mcb.22.5.1298-1306.2002;
RA Strahl B.D., Grant P.A., Briggs S.D., Sun Z.-W., Bone J.R., Caldwell J.A.,
RA Mollah S., Cook R.G., Shabanowitz J., Hunt D.F., Allis C.D.;
RT "Set2 is a nucleosomal histone H3-selective methyltransferase that mediates
RT transcriptional repression.";
RL Mol. Cell. Biol. 22:1298-1306(2002).
RN [23]
RP METHYLATION AT LYS-5; LYS-37 AND LYS-80.
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 [24]
RP METHYLATION AT LYS-5.
RX PubMed=12353038; DOI=10.1038/nature01080;
RA Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J., Bernstein B.E.,
RA Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.;
RT "Active genes are tri-methylated at K4 of histone H3.";
RL Nature 419:407-411(2002).
RN [25]
RP METHYLATION AT LYS-5.
RX PubMed=11752412; DOI=10.1073/pnas.221596698;
RA Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.;
RT "A trithorax-group complex purified from Saccharomyces cerevisiae is
RT required for methylation of histone H3.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002).
RN [26]
RP METHYLATION AT LYS-37.
RX PubMed=12629047; DOI=10.1101/gad.1055503;
RA Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H.,
RA Strahl B.D.;
RT "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in
RT yeast.";
RL Genes Dev. 17:654-663(2003).
RN [27]
RP METHYLATION AT LYS-37.
RX PubMed=12773564; DOI=10.1128/mcb.23.12.4207-4218.2003;
RA Krogan N.J., Kim M., Tong A., Golshani A., Cagney G., Canadien V.,
RA Richards D.P., Beattie B.K., Emili A., Boone C., Shilatifard A.,
RA Buratowski S., Greenblatt J.;
RT "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to
RT transcriptional elongation by RNA polymerase II.";
RL Mol. Cell. Biol. 23:4207-4218(2003).
RN [28]
RP METHYLATION AT LYS-37.
RX PubMed=12917322; DOI=10.1128/mcb.23.17.5972-5978.2003;
RA Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M.,
RA Sternglanz R.;
RT "Set2-catalyzed methylation of histone H3 represses basal expression of
RT GAL4 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:5972-5978(2003).
RN [29]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [30]
RP METHYLATION AT LYS-80.
RX PubMed=12574507; DOI=10.1073/pnas.0437846100;
RA Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.;
RT "Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and
RT mammalian cells: a potential mechanism for position-effect variegation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003).
RN [31]
RP METHYLATION AT LYS-5, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12845608; DOI=10.1002/yea.995;
RA Boa S., Coert C., Patterton H.-G.;
RT "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine
RT 4 of histone H3 and is required for efficient gene expression.";
RL Yeast 20:827-835(2003).
RN [32]
RP PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
RX PubMed=15719021; DOI=10.1038/sj.emboj.7600577;
RA Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.;
RT "Histone H3 phosphorylation can promote TBP recruitment through distinct
RT promoter-specific mechanisms.";
RL EMBO J. 24:997-1008(2005).
RN [33]
RP METHYLATION AT LYS-80.
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 [34]
RP ACETYLATION AT LYS-57, AND MUTAGENESIS OF LYS-57.
RX PubMed=15888442; DOI=10.1074/jbc.c500181200;
RA Ozdemir A., Spicuglia S., Lasonder E., Vermeulen M., Campsteijn C.,
RA Stunnenberg H.G., Logie C.;
RT "Characterization of lysine 56 of histone H3 as an acetylation site in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:25949-25952(2005).
RN [35]
RP METHYLATION AT LYS-5.
RX PubMed=16185711; DOI=10.1016/j.jmb.2005.08.059;
RA Dehe P.-M., Pamblanco M., Luciano P., Lebrun R., Moinier D., Sendra R.,
RA Verreault A., Tordera V., Geli V.;
RT "Histone H3 lysine 4 mono-methylation does not require ubiquitination of
RT histone H2B.";
RL J. Mol. Biol. 353:477-484(2005).
RN [36]
RP METHYLATION AT LYS-5.
RX PubMed=15949446; DOI=10.1016/j.molcel.2005.05.009;
RA Morillon A., Karabetsou N., Nair A., Mellor J.;
RT "Dynamic lysine methylation on histone H3 defines the regulatory phase of
RT gene transcription.";
RL Mol. Cell 18:723-734(2005).
RN [37]
RP METHYLATION AT LYS-5.
RX PubMed=16168379; DOI=10.1016/j.molcel.2005.07.024;
RA Schneider J., Wood A., Lee J.-S., Schuster R., Dueker J., Maguire C.,
RA Swanson S.K., Florens L., Washburn M.P., Shilatifard A.;
RT "Molecular regulation of histone H3 trimethylation by COMPASS and the
RT regulation of gene expression.";
RL Mol. Cell 19:849-856(2005).
RN [38]
RP METHYLATION AT LYS-37.
RX PubMed=15798214; DOI=10.1128/mcb.25.8.3305-3316.2005;
RA Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L.,
RA Strahl B.D.;
RT "A novel domain in Set2 mediates RNA polymerase II interaction and couples
RT histone H3 K36 methylation with transcript elongation.";
RL Mol. Cell. Biol. 25:3305-3316(2005).
RN [39]
RP ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16015338; DOI=10.1038/nature03714;
RA Masumoto H., Hawke D., Kobayashi R., Verreault A.;
RT "A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the
RT DNA damage response.";
RL Nature 436:294-298(2005).
RN [40]
RP METHYLATION AT LYS-5, AND ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
RX PubMed=16122352; DOI=10.1371/journal.pbio.0030328;
RA Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L., Friedman N.,
RA Rando O.J.;
RT "Single-nucleosome mapping of histone modifications in S. cerevisiae.";
RL PLoS Biol. 3:1-17(2005).
RN [41]
RP ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND
RP LYS-65, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
RP LYS-37 AND LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17194708; DOI=10.1074/jbc.m607900200;
RA Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT "Organismal differences in post-translational modifications in histones H3
RT and H4.";
RL J. Biol. Chem. 282:7641-7655(2007).
RN [42]
RP ACETYLATION AT LYS-57, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17320445; DOI=10.1016/j.molcel.2007.02.006;
RA Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A.,
RA Denu J.M., Kaufman P.D.;
RT "Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent
RT complexes.";
RL Mol. Cell 25:703-712(2007).
RN [43]
RP ACETYLATION AT LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-38 AND LYS-57,
RP PROPIONYLATION AT LYS-24 AND LYS-57, BUTYRYLATION AT LYS-15 AND LYS-28, AND
RP METHYLATION AT LYS-37 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 [44]
RP MALONYLATION AT LYS-57, AND SUCCINYLATION AT LYS-80.
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 [45]
RP BUTYRYLATION AT LYS-15; LYS-19 AND LYS-24.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [46]
RP ACETYLATION AT LYS-10, AND CROTONYLATION AT LYS-10.
RX PubMed=27089029; DOI=10.1038/nchembio.2065;
RA Andrews F.H., Shinsky S.A., Shanle E.K., Bridgers J.B., Gest A., Tsun I.K.,
RA Krajewski K., Shi X., Strahl B.D., Kutateladze T.G.;
RT "The Taf14 YEATS domain is a reader of histone crotonylation.";
RL Nat. Chem. Biol. 12:396-398(2016).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H3 IN NUCLEOSOME COMPLEX.
RX PubMed=11566884; DOI=10.1093/emboj/20.18.5207;
RA White C.L., Suto R.K., Luger K.;
RT "Structure of the yeast nucleosome core particle reveals fundamental
RT changes in internucleosome interactions.";
RL EMBO J. 20:5207-5218(2001).
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. Component of the UAF (upstream
CC activation factor) complex which interacts with the upstream element of
CC the RNA polymerase I promoter and forms a stable preinitiation complex.
CC Together with SPT15/TBP, UAF seems to stimulate basal transcription to
CC a fully activated level.
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. Histone H3 is a component of the UAF (upstream activation factor)
CC complex, which consists of UAF30, RRN5, RRN9, RRN10, and histones H3
CC and H4. {ECO:0000269|PubMed:9391047}.
CC -!- INTERACTION:
CC P61830; P32447: ASF1; NbExp=4; IntAct=EBI-8098, EBI-3003;
CC P61830; P35817: BDF1; NbExp=2; IntAct=EBI-8098, EBI-3493;
CC P61830; Q06205: FPR4; NbExp=6; IntAct=EBI-8098, EBI-6956;
CC P61830; P02309: HHF2; NbExp=9; IntAct=EBI-8098, EBI-8113;
CC P61830; P53096: HOS2; NbExp=2; IntAct=EBI-8098, EBI-8475;
CC P61830; Q04636: POB3; NbExp=2; IntAct=EBI-8098, EBI-27863;
CC P61830; P40161: RTT106; NbExp=6; IntAct=EBI-8098, EBI-29119;
CC P61830; P46995: SET2; NbExp=2; IntAct=EBI-8098, EBI-16985;
CC P61830; P36124: SET3; NbExp=2; IntAct=EBI-8098, EBI-16993;
CC P61830; P38890: SET5; NbExp=2; IntAct=EBI-8098, EBI-24263;
CC P61830; P32597: STH1; NbExp=4; IntAct=EBI-8098, EBI-18410;
CC P61830; Q08465: YNG1; NbExp=5; IntAct=EBI-8098, EBI-31890;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Phosphorylated by IPL1 to form H3S10ph in a cell cycle-dependent
CC manner during mitosis and meiosis. H3S10ph is also formed by SNF1,
CC promotes subsequent H3K14ac formation by GCN5, and is required for
CC transcriptional activation through TBP recruitment to the promoters.
CC Dephosphorylation is performed by GLC7. {ECO:0000269|PubMed:10911986,
CC ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:15719021}.
CC -!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
CC H3K4me1/2/3. H3K4me activates gene expression by regulating
CC transcription elongation and plays a role in telomere length
CC maintenance. H3K4me enrichment correlates with transcription levels,
CC and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end
CC of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to
CC form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to
CC form H3K79me. H3K79me is required for association of SIR proteins with
CC telomeric regions and for telomeric silencing. The COMPASS-mediated
CC formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me
CC require H2BK123ub1. {ECO:0000269|PubMed:11742990,
CC ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412,
CC ECO:0000269|PubMed:11839797, ECO:0000269|PubMed:12080090,
CC ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
CC ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12574507,
CC ECO:0000269|PubMed:12629047, ECO:0000269|PubMed:12773564,
CC ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:12917322,
CC ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:15798214,
CC ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352,
CC ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711,
CC ECO:0000269|PubMed:17194708}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC H3K14ac formation by GCN5, a component of the SAGA complex, is promoted
CC by H3S10ph. Further acetylated by GCN5 to form H3K9ac, H3K18ac,
CC H3K23ac, H3K27ac and H3K36ac. H3K14ac can also be formed by ESA1, a
CC component of the NuA4 histone acetyltransferase (HAT) complex. H3K56ac
CC formation occurs predominantly in newly synthesized H3 molecules during
CC G1, S and G2/M of the cell cycle and may be involved in DNA repair.
CC {ECO:0000269|PubMed:10082517, ECO:0000269|PubMed:10777603,
CC ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:11545749,
CC ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:15888442,
CC ECO:0000269|PubMed:16015338, ECO:0000269|PubMed:16122352,
CC ECO:0000269|PubMed:16260619, ECO:0000269|PubMed:17189264,
CC ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:17320445,
CC ECO:0000269|PubMed:9606197}.
CC -!- PTM: Crotonylation (Kcr) marks active promoters and enhancers and
CC confers resistance to transcriptional repressors.
CC {ECO:0000269|PubMed:27089029}.
CC -!- MISCELLANEOUS: Present with 213000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histone H3 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: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1
CC = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
CC acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated
CC Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24;
CC H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28;
CC H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac =
CC acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37;
CC H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3
CC = mono-, di- and trimethylated Lys-80. {ECO:0000305}.
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DR EMBL; X00724; CAA25310.1; -; Genomic_DNA.
DR EMBL; X00725; CAA25312.1; -; Genomic_DNA.
DR EMBL; Z35879; CAA84948.1; -; Genomic_DNA.
DR EMBL; Z71306; CAA95893.1; -; Genomic_DNA.
DR EMBL; Z71307; CAA95894.1; -; Genomic_DNA.
DR EMBL; AY558343; AAS56669.1; -; Genomic_DNA.
DR EMBL; AY692987; AAT93006.1; -; Genomic_DNA.
DR EMBL; AY554000; AAS64341.1; -; Genomic_DNA.
DR EMBL; AY554001; AAS64342.1; -; Genomic_DNA.
DR EMBL; AY554002; AAS64343.1; -; Genomic_DNA.
DR EMBL; AY554003; AAS64344.1; -; Genomic_DNA.
DR EMBL; AY554004; AAS64345.1; -; Genomic_DNA.
DR EMBL; AY554005; AAS64346.1; -; Genomic_DNA.
DR EMBL; AY554006; AAS64347.1; -; Genomic_DNA.
DR EMBL; AY554007; AAS64348.1; -; Genomic_DNA.
DR EMBL; AY554008; AAS64349.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07131.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10514.1; -; Genomic_DNA.
DR PIR; S45265; HSBY3.
DR RefSeq; NP_009564.1; NM_001178358.1.
DR RefSeq; NP_014367.1; NM_001182870.1.
DR PDB; 1ID3; X-ray; 3.10 A; A/E=2-136.
DR PDB; 1M1D; X-ray; 2.20 A; B/D=2-21.
DR PDB; 1PEG; X-ray; 2.59 A; P/Q=2-16.
DR PDB; 1PU9; X-ray; 2.30 A; B=6-24.
DR PDB; 1PUA; X-ray; 2.30 A; B=6-24.
DR PDB; 1QSN; X-ray; 2.20 A; B=10-20.
DR PDB; 2CNX; X-ray; 2.10 A; P=2-6.
DR PDB; 2H2G; X-ray; 1.63 A; B=114-124.
DR PDB; 2IDC; X-ray; 2.20 A; A=119-135.
DR PDB; 2JMJ; NMR; -; P=2-10.
DR PDB; 2RNW; NMR; -; B=2-16.
DR PDB; 2RNX; NMR; -; B=32-43.
DR PDB; 2RSN; NMR; -; B=2-18.
DR PDB; 3MP1; X-ray; 2.60 A; P=2-6.
DR PDB; 3MP6; X-ray; 1.48 A; P=2-5.
DR PDB; 3Q33; X-ray; 2.80 A; D=2-15.
DR PDB; 4JJN; X-ray; 3.09 A; A/E=2-136.
DR PDB; 4KUD; X-ray; 3.20 A; A/E=1-136.
DR PDB; 4PSX; X-ray; 2.51 A; P/Y=2-16.
DR PDB; 5D7E; X-ray; 1.90 A; C=6-12.
DR PDB; 5IOK; X-ray; 2.22 A; C=6-12.
DR PDB; 5ZBA; X-ray; 3.50 A; C=1-136.
DR PDB; 5ZBB; X-ray; 3.60 A; C=1-136.
DR PDB; 6GEJ; EM; 3.60 A; A/B=1-136.
DR PDB; 6GEN; EM; 3.60 A; A/B=1-136.
DR PDB; 6J2P; X-ray; 2.85 A; E/F/G/H=2-8.
DR PDB; 6KMJ; X-ray; 1.40 A; C=7-22.
DR PDB; 7F4A; X-ray; 2.00 A; B=6-14.
DR PDB; 7F4E; X-ray; 1.78 A; C=6-15.
DR PDB; 7K7G; EM; 4.20 A; A/E=1-136.
DR PDBsum; 1ID3; -.
DR PDBsum; 1M1D; -.
DR PDBsum; 1PEG; -.
DR PDBsum; 1PU9; -.
DR PDBsum; 1PUA; -.
DR PDBsum; 1QSN; -.
DR PDBsum; 2CNX; -.
DR PDBsum; 2H2G; -.
DR PDBsum; 2IDC; -.
DR PDBsum; 2JMJ; -.
DR PDBsum; 2RNW; -.
DR PDBsum; 2RNX; -.
DR PDBsum; 2RSN; -.
DR PDBsum; 3MP1; -.
DR PDBsum; 3MP6; -.
DR PDBsum; 3Q33; -.
DR PDBsum; 4JJN; -.
DR PDBsum; 4KUD; -.
DR PDBsum; 4PSX; -.
DR PDBsum; 5D7E; -.
DR PDBsum; 5IOK; -.
DR PDBsum; 5ZBA; -.
DR PDBsum; 5ZBB; -.
DR PDBsum; 6GEJ; -.
DR PDBsum; 6GEN; -.
DR PDBsum; 6J2P; -.
DR PDBsum; 6KMJ; -.
DR PDBsum; 7F4A; -.
DR PDBsum; 7F4E; -.
DR PDBsum; 7K7G; -.
DR AlphaFoldDB; P61830; -.
DR SMR; P61830; -.
DR BioGRID; 32711; 862.
DR BioGRID; 35796; 703.
DR ComplexPortal; CPX-1101; RNA polymerase I upstream activating factor complex.
DR ComplexPortal; CPX-1610; Nucleosome, variant HTA2-HTB2.
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 ComplexPortal; CPX-1614; Nucleosome, variant HTZ1-HTB2.
DR ComplexPortal; CPX-2566; Nucleosome, variant HTA1-HTB2.
DR DIP; DIP-417N; -.
DR IntAct; P61830; 153.
DR MINT; P61830; -.
DR STRING; 4932.YBR010W; -.
DR CarbonylDB; P61830; -.
DR iPTMnet; P61830; -.
DR MaxQB; P61830; -.
DR PaxDb; P61830; -.
DR PRIDE; P61830; -.
DR EnsemblFungi; YBR010W_mRNA; YBR010W; YBR010W.
DR EnsemblFungi; YNL031C_mRNA; YNL031C; YNL031C.
DR GeneID; 852295; -.
DR GeneID; 855700; -.
DR KEGG; sce:YBR010W; -.
DR KEGG; sce:YNL031C; -.
DR SGD; S000000214; HHT1.
DR SGD; S000004976; HHT2.
DR VEuPathDB; FungiDB:YBR010W; -.
DR VEuPathDB; FungiDB:YNL031C; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01040000240398; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P61830; -.
DR OMA; HIVMART; -.
DR BioCyc; YEAST:G3O-28997-MON; -.
DR Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
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-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 SABIO-RK; P61830; -.
DR EvolutionaryTrace; P61830; -.
DR PRO; PR:P61830; -.
DR Proteomes; UP000002311; Chromosome II.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P61830; protein.
DR GO; GO:0043505; C:CENP-A containing nucleosome; IDA:SGD.
DR GO; GO:0000786; C:nucleosome; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; TAS: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; TAS:SGD.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0009303; P:rRNA transcription; IMP:SGD.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:SGD.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID50143; -.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing;
KW DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7035169,
FT ECO:0000269|PubMed:782914"
FT CHAIN 2..136
FT /note="Histone H3"
FT /id="PRO_0000221370"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11742990,
FT ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038,
FT ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446,
FT ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379,
FT ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11742990,
FT ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038,
FT ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446,
FT ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379,
FT ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11742990,
FT ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038,
FT ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446,
FT ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379,
FT ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11545749,
FT ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:27089029, ECO:0000269|PubMed:9606197"
FT MOD_RES 10
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27089029"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10911986,
FT ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:15719021"
FT MOD_RES 15
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:10082517,
FT ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:11545749,
FT ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:16122352,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:19113941,
FT ECO:0000269|PubMed:9606197"
FT MOD_RES 15
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941,
FT ECO:0000269|PubMed:27105113"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11545749,
FT ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:19113941, ECO:0000269|PubMed:9606197"
FT MOD_RES 19
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11545749,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:19113941"
FT MOD_RES 24
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 24
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11545749,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:19113941"
FT MOD_RES 28
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11839797,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12629047,
FT ECO:0000269|PubMed:12773564, ECO:0000269|PubMed:12917322,
FT ECO:0000269|PubMed:15798214, ECO:0000269|PubMed:17194708"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11839797,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12629047,
FT ECO:0000269|PubMed:12773564, ECO:0000269|PubMed:12917322,
FT ECO:0000269|PubMed:15798214, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:19113941"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17189264,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:19113941"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11839797,
FT ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12629047,
FT ECO:0000269|PubMed:12773564, ECO:0000269|PubMed:12917322,
FT ECO:0000269|PubMed:15798214, ECO:0000269|PubMed:17194708,
FT ECO:0000269|PubMed:19113941"
FT MOD_RES 38
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 38
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15888442,
FT ECO:0000269|PubMed:16015338, ECO:0000269|PubMed:16260619,
FT ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:17320445,
FT ECO:0000269|PubMed:19113941"
FT MOD_RES 57
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 57
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12080090,
FT ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
FT ECO:0000269|PubMed:12574507, ECO:0000269|PubMed:15632126,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12080090,
FT ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
FT ECO:0000269|PubMed:12574507, ECO:0000269|PubMed:15632126,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12080090,
FT ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
FT ECO:0000269|PubMed:12574507, ECO:0000269|PubMed:15632126,
FT ECO:0000269|PubMed:17194708"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MUTAGEN 11
FT /note="S->A: Impairs histone H3 phosphorylation and reduces
FT transcription of some GCN5 regulated genes."
FT /evidence="ECO:0000269|PubMed:10911986,
FT ECO:0000269|PubMed:10975519"
FT MUTAGEN 53
FT /note="R->A,K,Q: Lethal."
FT /evidence="ECO:0000269|PubMed:16260619"
FT MUTAGEN 57
FT /note="K->A,Q,R: Increases sensitivity to genotoxic agents
FT inducing DNA breaks during replication."
FT /evidence="ECO:0000269|PubMed:15888442,
FT ECO:0000269|PubMed:16015338, ECO:0000269|PubMed:16260619"
FT MUTAGEN 80
FT /note="K->A,P,Q: Compromises telomeric silencing."
FT /evidence="ECO:0000269|PubMed:12080090,
FT ECO:0000269|PubMed:16260619"
FT MUTAGEN 119
FT /note="T->A,E: Lethal."
FT /evidence="ECO:0000269|PubMed:16260619"
FT CONFLICT 124
FT /note="D -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2RSN"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:4JJN"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:4JJN"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:4JJN"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4JJN"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2IDC"
SQ SEQUENCE 136 AA; 15356 MW; A6115FEB480AC67A CRC64;
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY LVSLFEDTNL AAIHAKRVTI
QKKDIKLARR LRGERS
