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 02-JUN-2021, entry version 180. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 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 SMR; P61830; -. DR BioGRID; 32711; 838. DR BioGRID; 35796; 699. 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.YNL031C; -. 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 eggNOG; KOG1745; Eukaryota. DR GeneTree; ENSGT01020000230443; -. DR HOGENOM; CLU_078295_4_0_1; -. DR InParanoid; P61830; -. DR OMA; CTMARTK; -. DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-SCE-3214815; HDACs deacetylate 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-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; TAS:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; TAS:SGD. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0006333; P:chromatin assembly or disassembly; TAS:SGD. DR GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD. 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 //