Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Histone H3

 H3_YEAST                Reviewed;         136 AA.
P61830; D6VQ11; E9PAG1; P02303; P13996; Q6B1U3; Q6Q7G9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Histone H3;
Name=HHT1; OrderedLocusNames=YBR010W; ORFNames=YBR0201;
and
Name=HHT2; Synonyms=SIN2; OrderedLocusNames=YNL031C; ORFNames=N2749;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6355483; DOI=10.1016/S0022-2836(83)80164-8;
Smith M.M., Andresson O.S.;
"DNA sequences of yeast H3 and H4 histone genes from two non-allelic
gene sets encode identical H3 and H4 proteins.";
J. Mol. Biol. 169:663-690(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT1).
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2).
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
GENOME REANNOTATION (HHT1 AND HHT2).
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHT1 AND HHT2).
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
PROTEIN SEQUENCE OF 2-136.
PubMed=7035169; DOI=10.1111/j.1432-1033.1982.tb05815.x;
Brandt W.F., von Holt C.;
"The primary structure of yeast histone H3.";
Eur. J. Biochem. 121:501-510(1982).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
STRAIN=ATCC 204508 / S288c, M13, M14, M22, M32, M34, M5, M8, and
YPS163;
PubMed=15059259; DOI=10.1186/gb-2004-5-4-r26;
Fay J.C., McCullough H.L., Sniegowski P.D., Eisen M.B.;
"Population genetic variation in gene expression is associated with
phenotypic variation in Saccharomyces cerevisiae.";
Genome Biol. 5:R26.1-R26.14(2004).
[8]
PROTEIN SEQUENCE OF 2-16.
PubMed=782914; DOI=10.1016/0014-5793(76)80153-6;
Brandt W.F., von Holt C.;
"The occurrence of histone H3 and H4 in yeast.";
FEBS Lett. 65:386-390(1976).
[9]
PROTEIN SEQUENCE OF 28-41, AND ACETYLATION AT LYS-37.
PubMed=17189264; DOI=10.1074/jbc.M607909200;
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
"Identification of histone H3 lysine 36 acetylation as a highly
conserved histone modification.";
J. Biol. Chem. 282:7632-7640(2007).
[10]
PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, AND MUTAGENESIS OF
ARG-53; LYS-57; LYS-80 AND THR-119.
PubMed=16260619; DOI=10.1128/MCB.25.22.10060-10070.2005;
Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A.,
Cottee R.J., Boeke J.D.;
"Insights into the role of histone H3 and histone H4 core modifiable
residues in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 25:10060-10070(2005).
[11]
IDENTIFICATION IN THE UAF COMPLEX.
PubMed=9391047; DOI=10.1073/pnas.94.25.13458;
Keener J., Dodd J.A., Lalo D., Nomura M.;
"Histones H3 and H4 are components of upstream activation factor
required for the high-level transcription of yeast rDNA by RNA
polymerase I.";
Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997).
[12]
ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
PubMed=9606197; DOI=10.1093/emboj/17.11.3155;
Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y.;
"Essential and redundant functions of histone acetylation revealed by
mutation of target lysines and loss of the Gcn5p acetyltransferase.";
EMBO J. 17:3155-3167(1998).
[13]
ACETYLATION AT LYS-15.
PubMed=10082517; DOI=10.1128/MCB.19.4.2515;
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
"Esa1p is an essential histone acetyltransferase required for cell
cycle progression.";
Mol. Cell. Biol. 19:2515-2526(1999).
[14]
PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, AND
MUTAGENESIS OF SER-11.
PubMed=10975519; DOI=10.1016/S0092-8674(00)00034-9;
Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R.,
Smith M.M., Allis C.D.;
"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora
kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.";
Cell 102:279-291(2000).
[15]
ACETYLATION.
PubMed=10777603; DOI=10.1074/jbc.275.17.13007;
Waterborg J.H.;
"Steady-state levels of histone acetylation in Saccharomyces
cerevisiae.";
J. Biol. Chem. 275:13007-13011(2000).
[16]
PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, AND MUTAGENESIS OF
SER-11.
PubMed=10911986; DOI=10.1016/S1097-2765(00)80257-9;
Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D.,
Marmorstein R., Berger S.L.;
"Phosphorylation of serine 10 in histone H3 is functionally linked in
vitro and in vivo to Gcn5-mediated acetylation at lysine 14.";
Mol. Cell 5:917-926(2000).
[17]
METHYLATION AT LYS-5.
PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
Aasland R., Stewart A.F.;
"The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue
and methylates histone 3 lysine 4.";
EMBO J. 20:7137-7148(2001).
[18]
METHYLATION AT LYS-5.
PubMed=11751634; DOI=10.1101/gad.940201;
Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K.,
Dent S.Y.R., Winston F., Allis C.D.;
"Histone H3 lysine 4 methylation is mediated by Set1 and required for
cell growth and rDNA silencing in Saccharomyces cerevisiae.";
Genes Dev. 15:3286-3295(2001).
[19]
ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
PubMed=11545749; DOI=10.1016/S1097-2765(01)00301-X;
Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
"Highly specific antibodies determine histone acetylation site usage
in yeast heterochromatin and euchromatin.";
Mol. Cell 8:473-479(2001).
[20]
METHYLATION AT LYS-80, AND MUTAGENESIS OF LYS-80.
PubMed=12080090; DOI=10.1101/gad.1001502;
Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y.,
Struhl K.;
"Lysine methylation within the globular domain of histone H3 by Dot1
is important for telomeric silencing and Sir protein association.";
Genes Dev. 16:1518-1527(2002).
[21]
METHYLATION AT LYS-80.
PubMed=12097318; DOI=10.1074/jbc.C200366200;
Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
"Disruptor of telomeric silencing-1 is a chromatin-specific histone H3
methyltransferase.";
J. Biol. Chem. 277:30421-30424(2002).
[22]
METHYLATION AT LYS-37.
PubMed=11839797; DOI=10.1128/MCB.22.5.1298-1306.2002;
Strahl B.D., Grant P.A., Briggs S.D., Sun Z.-W., Bone J.R.,
Caldwell J.A., Mollah S., Cook R.G., Shabanowitz J., Hunt D.F.,
Allis C.D.;
"Set2 is a nucleosomal histone H3-selective methyltransferase that
mediates transcriptional repression.";
Mol. Cell. Biol. 22:1298-1306(2002).
[23]
METHYLATION AT LYS-5; LYS-37 AND LYS-80.
PubMed=12152067; DOI=10.1038/nature00970;
Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J.,
Hunt D.F., Allis C.D., Strahl B.D.;
"Gene silencing: trans-histone regulatory pathway in chromatin.";
Nature 418:498-498(2002).
[24]
METHYLATION AT LYS-5.
PubMed=12353038; DOI=10.1038/nature01080;
Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J.,
Bernstein B.E., Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.;
"Active genes are tri-methylated at K4 of histone H3.";
Nature 419:407-411(2002).
[25]
METHYLATION AT LYS-5.
PubMed=11752412; DOI=10.1073/pnas.221596698;
Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.;
"A trithorax-group complex purified from Saccharomyces cerevisiae is
required for methylation of histone H3.";
Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002).
[26]
METHYLATION AT LYS-37.
PubMed=12629047; DOI=10.1101/gad.1055503;
Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H.,
Strahl B.D.;
"Phosphorylation of RNA polymerase II CTD regulates H3 methylation in
yeast.";
Genes Dev. 17:654-663(2003).
[27]
METHYLATION AT LYS-37.
PubMed=12773564; DOI=10.1128/MCB.23.12.4207-4218.2003;
Krogan N.J., Kim M., Tong A., Golshani A., Cagney G., Canadien V.,
Richards D.P., Beattie B.K., Emili A., Boone C., Shilatifard A.,
Buratowski S., Greenblatt J.;
"Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is
linked to transcriptional elongation by RNA polymerase II.";
Mol. Cell. Biol. 23:4207-4218(2003).
[28]
METHYLATION AT LYS-37.
PubMed=12917322; DOI=10.1128/MCB.23.17.5972-5978.2003;
Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M.,
Sternglanz R.;
"Set2-catalyzed methylation of histone H3 represses basal expression
of GAL4 in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 23:5972-5978(2003).
[29]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[30]
METHYLATION AT LYS-80.
PubMed=12574507; DOI=10.1073/pnas.0437846100;
Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.;
"Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast
and mammalian cells: a potential mechanism for position-effect
variegation.";
Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003).
[31]
METHYLATION AT LYS-5, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12845608; DOI=10.1002/yea.995;
Boa S., Coert C., Patterton H.-G.;
"Saccharomyces cerevisiae Set1p is a methyltransferase specific for
lysine 4 of histone H3 and is required for efficient gene
expression.";
Yeast 20:827-835(2003).
[32]
PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
PubMed=15719021; DOI=10.1038/sj.emboj.7600577;
Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.;
"Histone H3 phosphorylation can promote TBP recruitment through
distinct promoter-specific mechanisms.";
EMBO J. 24:997-1008(2005).
[33]
METHYLATION AT LYS-80.
PubMed=15632126; DOI=10.1074/jbc.M414453200;
Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.;
"The DNA damage checkpoint response requires histone H2B
ubiquitination by Rad6-Bre1 and H3 methylation by Dot1.";
J. Biol. Chem. 280:9879-9886(2005).
[34]
ACETYLATION AT LYS-57, AND MUTAGENESIS OF LYS-57.
PubMed=15888442; DOI=10.1074/jbc.C500181200;
Ozdemir A., Spicuglia S., Lasonder E., Vermeulen M., Campsteijn C.,
Stunnenberg H.G., Logie C.;
"Characterization of lysine 56 of histone H3 as an acetylation site in
Saccharomyces cerevisiae.";
J. Biol. Chem. 280:25949-25952(2005).
[35]
METHYLATION AT LYS-5.
PubMed=16185711; DOI=10.1016/j.jmb.2005.08.059;
Dehe P.-M., Pamblanco M., Luciano P., Lebrun R., Moinier D.,
Sendra R., Verreault A., Tordera V., Geli V.;
"Histone H3 lysine 4 mono-methylation does not require ubiquitination
of histone H2B.";
J. Mol. Biol. 353:477-484(2005).
[36]
METHYLATION AT LYS-5.
PubMed=15949446; DOI=10.1016/j.molcel.2005.05.009;
Morillon A., Karabetsou N., Nair A., Mellor J.;
"Dynamic lysine methylation on histone H3 defines the regulatory phase
of gene transcription.";
Mol. Cell 18:723-734(2005).
[37]
METHYLATION AT LYS-5.
PubMed=16168379; DOI=10.1016/j.molcel.2005.07.024;
Schneider J., Wood A., Lee J.-S., Schuster R., Dueker J., Maguire C.,
Swanson S.K., Florens L., Washburn M.P., Shilatifard A.;
"Molecular regulation of histone H3 trimethylation by COMPASS and the
regulation of gene expression.";
Mol. Cell 19:849-856(2005).
[38]
METHYLATION AT LYS-37.
PubMed=15798214; DOI=10.1128/MCB.25.8.3305-3316.2005;
Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L.,
Strahl B.D.;
"A novel domain in Set2 mediates RNA polymerase II interaction and
couples histone H3 K36 methylation with transcript elongation.";
Mol. Cell. Biol. 25:3305-3316(2005).
[39]
ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16015338; DOI=10.1038/nature03714;
Masumoto H., Hawke D., Kobayashi R., Verreault A.;
"A role for cell-cycle-regulated histone H3 lysine 56 acetylation in
the DNA damage response.";
Nature 436:294-298(2005).
[40]
METHYLATION AT LYS-5, AND ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
PubMed=16122352; DOI=10.1371/journal.pbio.0030328;
Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L.,
Friedman N., Rando O.J.;
"Single-nucleosome mapping of histone modifications in S.
cerevisiae.";
PLoS Biol. 3:1-17(2005).
[41]
ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57
AND LYS-65, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24;
LYS-28; LYS-37 AND LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17194708; DOI=10.1074/jbc.M607900200;
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
"Organismal differences in post-translational modifications in
histones H3 and H4.";
J. Biol. Chem. 282:7641-7655(2007).
[42]
ACETYLATION AT LYS-57, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17320445; DOI=10.1016/j.molcel.2007.02.006;
Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L.,
Freitas M.A., Denu J.M., Kaufman P.D.;
"Histone H3-K56 acetylation is catalyzed by histone chaperone-
dependent complexes.";
Mol. Cell 25:703-712(2007).
[43]
ACETYLATION AT LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-38 AND
LYS-57, PROPIONYLATION AT LYS-24 AND LYS-57, BUTYRYLATION AT LYS-15
AND LYS-28, AND METHYLATION AT LYS-37 AND LYS-38.
PubMed=19113941; DOI=10.1021/pr8005155;
Zhang K., Chen Y., Zhang Z., Zhao Y.;
"Identification and verification of lysine propionylation and
butyrylation in yeast core histones using PTMap software.";
J. Proteome Res. 8:900-906(2009).
[44]
MALONYLATION AT LYS-57, AND SUCCINYLATION AT LYS-80.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[45]
BUTYRYLATION AT LYS-15; LYS-19 AND LYS-24.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[46]
ACETYLATION AT LYS-10, AND CROTONYLATION AT LYS-10.
PubMed=27089029; DOI=10.1038/nchembio.2065;
Andrews F.H., Shinsky S.A., Shanle E.K., Bridgers J.B., Gest A.,
Tsun I.K., Krajewski K., Shi X., Strahl B.D., Kutateladze T.G.;
"The Taf14 YEATS domain is a reader of histone crotonylation.";
Nat. Chem. Biol. 12:396-398(2016).
[47]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H3 IN NUCLEOSOME COMPLEX.
PubMed=11566884; DOI=10.1093/emboj/20.18.5207;
White C.L., Suto R.K., Luger K.;
"Structure of the yeast nucleosome core particle reveals fundamental
changes in internucleosome interactions.";
EMBO J. 20:5207-5218(2001).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. Component of the UAF (upstream activation
factor) complex which interacts with the upstream element of the
RNA polymerase I promoter and forms a stable preinitiation
complex. Together with SPT15/TBP, UAF seems to stimulate basal
transcription to a fully activated level.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA. Histone H3 is a component of the UAF
(upstream activation factor) complex, which consists of UAF30,
RRN5, RRN9, RRN10, and histones H3 and H4.
{ECO:0000269|PubMed:9391047}.
-!- INTERACTION:
P32447:ASF1; NbExp=4; IntAct=EBI-8098, EBI-3003;
P35817:BDF1; NbExp=2; IntAct=EBI-8098, EBI-3493;
Q06205:FPR4; NbExp=5; IntAct=EBI-8098, EBI-6956;
P02309:HHF2; NbExp=9; IntAct=EBI-8098, EBI-8113;
P53096:HOS2; NbExp=2; IntAct=EBI-8098, EBI-8475;
Q04636:POB3; NbExp=2; IntAct=EBI-8098, EBI-27863;
P40161:RTT106; NbExp=6; IntAct=EBI-8098, EBI-29119;
P46995:SET2; NbExp=2; IntAct=EBI-8098, EBI-16985;
P36124:SET3; NbExp=2; IntAct=EBI-8098, EBI-16993;
P38890:SET5; NbExp=2; IntAct=EBI-8098, EBI-24263;
P32597:STH1; NbExp=4; IntAct=EBI-8098, EBI-18410;
Q08465:YNG1; NbExp=5; IntAct=EBI-8098, EBI-31890;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Phosphorylated by IPL1 to form H3S10ph in a cell cycle-
dependent manner during mitosis and meiosis. H3S10ph is also
formed by SNF1, promotes subsequent H3K14ac formation by GCN5, and
is required for transcriptional activation through TBP recruitment
to the promoters. Dephosphorylation is performed by GLC7.
{ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:10975519,
ECO:0000269|PubMed:15719021}.
-!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
H3K4me1/2/3. H3K4me activates gene expression by regulating
transcription elongation and plays a role in telomere length
maintenance. H3K4me enrichment correlates with transcription
levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment
at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1.
Methylated by SET2 to form H3K36me. H3K36me represses gene
expression. Methylated by DOT1 to form H3K79me. H3K79me is
required for association of SIR proteins with telomeric regions
and for telomeric silencing. The COMPASS-mediated formation of
H3K4me2/3 and the DOT1-mediated formation of H3K79me require
H2BK123ub1. {ECO:0000269|PubMed:11742990,
ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412,
ECO:0000269|PubMed:11839797, ECO:0000269|PubMed:12080090,
ECO:0000269|PubMed:12097318, ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12574507,
ECO:0000269|PubMed:12629047, ECO:0000269|PubMed:12773564,
ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:12917322,
ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:15798214,
ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711,
ECO:0000269|PubMed:17194708}.
-!- PTM: Acetylation of histone H3 leads to transcriptional
activation. H3K14ac formation by GCN5, a component of the SAGA
complex, is promoted by H3S10ph. Further acetylated by GCN5 to
form H3K9ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac. H3K14ac can
also be formed by ESA1, a component of the NuA4 histone
acetyltransferase (HAT) complex. H3K56ac formation occurs
predominantly in newly synthesized H3 molecules during G1, S and
G2/M of the cell cycle and may be involved in DNA repair.
{ECO:0000269|PubMed:10082517, ECO:0000269|PubMed:10777603,
ECO:0000269|PubMed:10911986, ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:15888442,
ECO:0000269|PubMed:16015338, ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:16260619, ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:17320445,
ECO:0000269|PubMed:9606197}.
-!- PTM: Crotonylation (Kcr) marks active promoters and enhancers and
confers resistance to transcriptional repressors.
{ECO:0000269|PubMed:27089029}.
-!- MISCELLANEOUS: Present with 213000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-!- CAUTION: To ensure consistency between histone entries, we follow
the 'Brno' nomenclature for histone modifications, with positions
referring to those used in the literature for the 'closest' model
organism. Due to slight variations in histone sequences between
organisms and to the presence of initiator methionine in
UniProtKB/Swiss-Prot sequences, the actual positions of modified
amino acids in the sequence generally differ. In this entry the
following conventions are used: H3K4me1/2/3 = mono-, di- and
trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 =
monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac =
acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac =
acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac =
acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated
Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and
trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac =
acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated
Lys-80. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X00724; CAA25310.1; -; Genomic_DNA.
EMBL; X00725; CAA25312.1; -; Genomic_DNA.
EMBL; Z35879; CAA84948.1; -; Genomic_DNA.
EMBL; Z71306; CAA95893.1; -; Genomic_DNA.
EMBL; Z71307; CAA95894.1; -; Genomic_DNA.
EMBL; AY558343; AAS56669.1; -; Genomic_DNA.
EMBL; AY692987; AAT93006.1; -; Genomic_DNA.
EMBL; AY554000; AAS64341.1; -; Genomic_DNA.
EMBL; AY554001; AAS64342.1; -; Genomic_DNA.
EMBL; AY554002; AAS64343.1; -; Genomic_DNA.
EMBL; AY554003; AAS64344.1; -; Genomic_DNA.
EMBL; AY554004; AAS64345.1; -; Genomic_DNA.
EMBL; AY554005; AAS64346.1; -; Genomic_DNA.
EMBL; AY554006; AAS64347.1; -; Genomic_DNA.
EMBL; AY554007; AAS64348.1; -; Genomic_DNA.
EMBL; AY554008; AAS64349.1; -; Genomic_DNA.
EMBL; BK006936; DAA07131.1; -; Genomic_DNA.
EMBL; BK006947; DAA10514.1; -; Genomic_DNA.
PIR; S45265; HSBY3.
RefSeq; NP_009564.1; NM_001178358.1.
RefSeq; NP_014367.1; NM_001182870.1.
PDB; 1ID3; X-ray; 3.10 A; A/E=2-136.
PDB; 1M1D; X-ray; 2.20 A; B/D=2-21.
PDB; 1PEG; X-ray; 2.59 A; P/Q=2-16.
PDB; 1PU9; X-ray; 2.30 A; B=6-24.
PDB; 1PUA; X-ray; 2.30 A; B=6-24.
PDB; 1QSN; X-ray; 2.20 A; B=10-20.
PDB; 2CNX; X-ray; 2.10 A; P=2-6.
PDB; 2H2G; X-ray; 1.63 A; B=114-124.
PDB; 2IDC; X-ray; 2.20 A; A=119-135.
PDB; 2JMJ; NMR; -; P=2-10.
PDB; 2RNW; NMR; -; B=2-16.
PDB; 2RNX; NMR; -; B=32-43.
PDB; 2RSN; NMR; -; B=2-18.
PDB; 3MP1; X-ray; 2.60 A; P=2-6.
PDB; 3MP6; X-ray; 1.48 A; P=2-5.
PDB; 3Q33; X-ray; 2.80 A; D=2-15.
PDB; 4JJN; X-ray; 3.09 A; A/E=2-136.
PDB; 4KUD; X-ray; 3.20 A; A/E=1-136.
PDB; 4PSX; X-ray; 2.51 A; P/Y=2-16.
PDB; 5D7E; X-ray; 1.90 A; C=6-12.
PDB; 5IOK; X-ray; 2.22 A; C=6-12.
PDBsum; 1ID3; -.
PDBsum; 1M1D; -.
PDBsum; 1PEG; -.
PDBsum; 1PU9; -.
PDBsum; 1PUA; -.
PDBsum; 1QSN; -.
PDBsum; 2CNX; -.
PDBsum; 2H2G; -.
PDBsum; 2IDC; -.
PDBsum; 2JMJ; -.
PDBsum; 2RNW; -.
PDBsum; 2RNX; -.
PDBsum; 2RSN; -.
PDBsum; 3MP1; -.
PDBsum; 3MP6; -.
PDBsum; 3Q33; -.
PDBsum; 4JJN; -.
PDBsum; 4KUD; -.
PDBsum; 4PSX; -.
PDBsum; 5D7E; -.
PDBsum; 5IOK; -.
ProteinModelPortal; P61830; -.
SMR; P61830; -.
BioGrid; 32711; 811.
BioGrid; 35796; 684.
DIP; DIP-417N; -.
IntAct; P61830; 152.
MINT; MINT-702778; -.
STRING; 4932.YNL031C; -.
iPTMnet; P61830; -.
MaxQB; P61830; -.
PRIDE; P61830; -.
EnsemblFungi; YBR010W; YBR010W; YBR010W.
EnsemblFungi; YNL031C; YNL031C; YNL031C.
GeneID; 852295; -.
GeneID; 855700; -.
KEGG; sce:YBR010W; -.
KEGG; sce:YNL031C; -.
SGD; S000000214; HHT1.
SGD; S000004976; HHT2.
GeneTree; ENSGT00760000118967; -.
InParanoid; P61830; -.
KO; K11253; -.
OMA; KRIEPEY; -.
OrthoDB; EOG092C5B6S; -.
BioCyc; YEAST:G3O-28997-MONOMER; -.
BioCyc; YEAST:G3O-33068-MONOMER; -.
Reactome; R-SCE-1266695; Interleukin-7 signaling.
Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
Reactome; R-SCE-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-SCE-3214815; HDACs deacetylate histones.
Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
Reactome; R-SCE-3214842; HDMs demethylate histones.
Reactome; R-SCE-3214847; HATs acetylate histones.
Reactome; R-SCE-3214858; RMTs methylate histone arginines.
Reactome; R-SCE-3247509; Chromatin modifying enzymes.
Reactome; R-SCE-427359; SIRT1 negatively regulates rRNA Expression.
Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-SCE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
EvolutionaryTrace; P61830; -.
PRO; PR:P61830; -.
Proteomes; UP000002311; Chromosome II.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0043505; C:CENP-A containing nucleosome; IDA:SGD.
GO; GO:0000788; C:nuclear nucleosome; TAS:SGD.
GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
GO; GO:0003677; F:DNA binding; TAS:SGD.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
GO; GO:0070911; P:global genome nucleotide-excision repair; IMP:SGD.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0009303; P:rRNA transcription; IMP:SGD.
GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:SGD.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Methylation; Nucleosome core;
Nucleus; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7035169,
ECO:0000269|PubMed:782914}.
CHAIN 2 136 Histone H3.
/FTId=PRO_0000221370.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11742990,
ECO:0000269|PubMed:11751634,
ECO:0000269|PubMed:11752412,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12353038,
ECO:0000269|PubMed:12845608,
ECO:0000269|PubMed:15949446,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:16168379,
ECO:0000269|PubMed:16185711,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11742990,
ECO:0000269|PubMed:11751634,
ECO:0000269|PubMed:11752412,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12353038,
ECO:0000269|PubMed:12845608,
ECO:0000269|PubMed:15949446,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:16168379,
ECO:0000269|PubMed:16185711,
ECO:0000269|PubMed:17194708}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:11742990,
ECO:0000269|PubMed:11751634,
ECO:0000269|PubMed:11752412,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12353038,
ECO:0000269|PubMed:12845608,
ECO:0000269|PubMed:15949446,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:16168379,
ECO:0000269|PubMed:16185711,
ECO:0000269|PubMed:17194708}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:27089029,
ECO:0000269|PubMed:9606197}.
MOD_RES 10 10 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:27089029}.
MOD_RES 10 10 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:10911986,
ECO:0000269|PubMed:10975519,
ECO:0000269|PubMed:15719021}.
MOD_RES 15 15 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:10082517,
ECO:0000269|PubMed:10911986,
ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:15719021,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941,
ECO:0000269|PubMed:9606197}.
MOD_RES 15 15 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:19113941,
ECO:0000269|PubMed:27105113}.
MOD_RES 19 19 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:16122352,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941,
ECO:0000269|PubMed:9606197}.
MOD_RES 19 19 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 19 19 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941}.
MOD_RES 24 24 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 24 24 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 24 24 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:19113941}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11545749,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941}.
MOD_RES 28 28 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:19113941}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:11839797,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12629047,
ECO:0000269|PubMed:12773564,
ECO:0000269|PubMed:12917322,
ECO:0000269|PubMed:15798214,
ECO:0000269|PubMed:17194708}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:11839797,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12629047,
ECO:0000269|PubMed:12773564,
ECO:0000269|PubMed:12917322,
ECO:0000269|PubMed:15798214,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941}.
MOD_RES 37 37 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17189264,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:11839797,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12629047,
ECO:0000269|PubMed:12773564,
ECO:0000269|PubMed:12917322,
ECO:0000269|PubMed:15798214,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:19113941}.
MOD_RES 38 38 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:19113941}.
MOD_RES 38 38 N6-methyllysine; alternate.
{ECO:0000269|PubMed:19113941}.
MOD_RES 57 57 N6-acetyllysine.
{ECO:0000269|PubMed:15888442,
ECO:0000269|PubMed:16015338,
ECO:0000269|PubMed:16260619,
ECO:0000269|PubMed:17194708,
ECO:0000269|PubMed:17320445,
ECO:0000269|PubMed:19113941}.
MOD_RES 57 57 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 57 57 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:19113941}.
MOD_RES 65 65 N6-acetyllysine.
{ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:12080090,
ECO:0000269|PubMed:12097318,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12574507,
ECO:0000269|PubMed:15632126,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12080090,
ECO:0000269|PubMed:12097318,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12574507,
ECO:0000269|PubMed:15632126,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000269|PubMed:12080090,
ECO:0000269|PubMed:12097318,
ECO:0000269|PubMed:12152067,
ECO:0000269|PubMed:12574507,
ECO:0000269|PubMed:15632126,
ECO:0000269|PubMed:17194708}.
MOD_RES 80 80 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MUTAGEN 11 11 S->A: Impairs histone H3 phosphorylation
and reduces transcription of some GCN5
regulated genes.
{ECO:0000269|PubMed:10911986,
ECO:0000269|PubMed:10975519}.
MUTAGEN 53 53 R->A,K,Q: Lethal.
{ECO:0000269|PubMed:16260619}.
MUTAGEN 57 57 K->A,Q,R: Increases sensitivity to
genotoxic agents inducing DNA breaks
during replication.
{ECO:0000269|PubMed:15888442,
ECO:0000269|PubMed:16015338,
ECO:0000269|PubMed:16260619}.
MUTAGEN 80 80 K->A,P,Q: Compromises telomeric
silencing. {ECO:0000269|PubMed:12080090,
ECO:0000269|PubMed:16260619}.
MUTAGEN 119 119 T->A,E: Lethal.
{ECO:0000269|PubMed:16260619}.
CONFLICT 124 124 D -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
STRAND 6 8 {ECO:0000244|PDB:2RSN}.
STRAND 11 13 {ECO:0000244|PDB:2RNW}.
HELIX 46 55 {ECO:0000244|PDB:4JJN}.
HELIX 66 77 {ECO:0000244|PDB:4JJN}.
HELIX 87 114 {ECO:0000244|PDB:4JJN}.
STRAND 118 120 {ECO:0000244|PDB:4JJN}.
HELIX 124 131 {ECO:0000244|PDB:2IDC}.
SEQUENCE 136 AA; 15356 MW; A6115FEB480AC67A CRC64;
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY LVSLFEDTNL AAIHAKRVTI
QKKDIKLARR LRGERS


Related products :

Catalog number Product name Quantity
28-858 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
28-920 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP18 is a component of the histone 0.05 mg
28-857 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
25-522 UTX is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It demethylates trimethylated and dimethylated but not monomethylate 0.05 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
29-186 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.1 mg
25-583 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.05 mg
27-131 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.05 mg
27-775 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.1 mg
25-113 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complex 0.05 mg
bs-0931P Peptides: Histone H1b(Histone H1.4) Protein Length:12-25 amino acids. 200ug lyophilized
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 0.5mg
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 100ug
E0356h ELISA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
E0356h ELISA kit H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
U0356h CLIA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
303-35199 Anti_phospho Histone H3 (P_Ser10), monoclonal antibody Binds to Histone H3 phosphorylated at serine 10. 100 ul
30-333 DOT1L is a histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. 0.05 mg
ANTY021260 Polyclonal Antibodies: Histone H2A.X (Ab-139) ; Specificity: Histone H2A.X (Ab-139) ; Application: IHC 100ug
31-007 Histone H3, along with histone H4, plays a central role in nucleosome formation. 0.1 mg
ANTY021137 Polyclonal Antibodies: Histone H3.1 (Ab-10) ; Specificity: Histone H3.1 (Ab-10) ; Application: IHC 100ug
3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur