Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone H3  

UniProtKB / Swiss-Prot ID :  H3_YEAST

Gene Name (Synonyms) : 
HHT1 YBR010W YBR0201
HHT2, SIN2 YNL031C N2749  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Nucleus. Chromosome. 

Protein 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. 

Protein Sequence MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHCCCCCHHHCCCHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
5N6,N6,N6-trimethyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6,N6-dimethyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
5N6-methyllysine; alternate.MARTKQTAR
CCCCCCCCC
39.85UniProtKB
Link-
10N6-acetyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
10N6-methyllysine; alternate.QTARKSTGG
CCCCCCCCC
50.32UniProtKB
Link-
11PhosphoserineTARKSTGGK
CCCCCCCCC
27.08PhosphoELM
Link-
11Phosphoserine.TARKSTGGK
CCCCCCCCC
27.08UniProtKB
Link-
15N6,N6-dimethyllysine; alternate.STGGKAPRK
CCCCCCCCC
57.47UniProtKB
Link-
15N6-acetyllysine; alternate.STGGKAPRK
CCCCCCCCC
57.47UniProtKB
Link-
19N6-acetyllysine; alternate.KAPRKQLAS
CCCCCCCCC
48.91UniProtKB
Link-
19N6-methyllysine; alternate.KAPRKQLAS
CCCCCCCCC
48.91UniProtKB
Link-
24N6-acetyllysine; alternate.QLASKAARK
CCCCCCCCC
40.22UniProtKB
Link-
24N6-methyllysine; alternate.QLASKAARK
CCCCCCCCC
40.22UniProtKB
Link-
28N6,N6,N6-trimethyllysine; alternate.KAARKSAPS
CCCCCCCCC
46.36UniProtKB
Link-
28N6,N6-dimethyllysine; alternate.KAARKSAPS
CCCCCCCCC
46.36UniProtKB
Link-
28N6-acetyllysine; alternate.KAARKSAPS
CCCCCCCCC
46.36UniProtKB
Link-
28N6-methyllysine; alternate.KAARKSAPS
CCCCCCCCC
46.36UniProtKB
Link-
37N6,N6,N6-trimethyllysine; alternate.TGGVKKPHR
CCCCCCCCC
64.95UniProtKB
Link
37N6,N6-dimethyllysine; alternate.TGGVKKPHR
CCCCCCCCC
64.95UniProtKB
Link
37N6-acetyllysine; alternate.TGGVKKPHR
CCCCCCCCC
64.95UniProtKB
Link
37N6-methyllysine; alternate.TGGVKKPHR
CCCCCCCCC
64.95UniProtKB
Link
57N6-acetyllysine.RRFQKSTEL
HHHHCCCCC
57.54UniProtKB
Link
65N6-acetyllysine.LLIRKLPFQ
CHHHCCCHH
54.22UniProtKB
Link
80N6,N6,N6-trimethyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link
80N6,N6-dimethyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link
80N6-methyllysine; alternate.AQDFKTDLR
HHHCCCCCC
49.79UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Insights into the role of histone H3 and histone H4 core modifiableresidues in Saccharomyces cerevisiae.";
Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A.,Cottee R.J., Boeke J.D.;
Mol. Cell. Biol. 25:10060-10070(2005).
Cited for: PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, AND MUTAGENESIS OFARG-53; LYS-57; LYS-80 AND THR-119.
"Essential and redundant functions of histone acetylation revealed bymutation of target lysines and loss of the Gcn5p acetyltransferase.";
Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y.;
EMBO J. 17:3155-3167(1998).
Cited for: ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
"Esa1p is an essential histone acetyltransferase required for cellcycle progression.";
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
Mol. Cell. Biol. 19:2515-2526(1999).
Cited for: ACETYLATION AT LYS-15.
"Phosphorylation of serine 10 in histone H3 is functionally linked invitro and in vivo to Gcn5-mediated acetylation at lysine 14.";
Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D.,Marmorstein R., Berger S.L.;
Mol. Cell 5:917-926(2000).
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, AND MUTAGENESIS OFSER-11.
"Highly specific antibodies determine histone acetylation site usagein yeast heterochromatin and euchromatin.";
Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
Mol. Cell 8:473-479(2001).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
"Histone H3 phosphorylation can promote TBP recruitment throughdistinct promoter-specific mechanisms.";
Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.;
EMBO J. 24:997-1008(2005).
Cited for: PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
"Characterization of lysine 56 of histone H3 as an acetylation site inSaccharomyces cerevisiae.";
Ozdemir A., Spicuglia S., Lasonder E., Vermeulen M., Campsteijn C.,Stunnenberg H.G., Logie C.;
J. Biol. Chem. 280:25949-25952(2005).
Cited for: ACETYLATION AT LYS-57, AND MUTAGENESIS OF LYS-57.
"A role for cell-cycle-regulated histone H3 lysine 56 acetylation inthe DNA damage response.";
Masumoto H., Hawke D., Kobayashi R., Verreault A.;
Nature 436:294-298(2005).
Cited for: MASS SPECTROMETRY, ACETYLATION AT LYS-57, AND MUTAGENESIS OF LYS-57.
"Single-nucleosome mapping of histone modifications in S.cerevisiae.";
Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L.,Friedman N., Rando O.J.;
PLoS Biol. 3:1-17(2005).
Cited for: METHYLATION AT LYS-5, AND ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
"Organismal differences in post-translational modifications inhistones H3 and H4.";
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.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: MASS SPECTROMETRY, ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57 AND LYS-65, AND METHYLATION AT LYS-5; LYS-10;LYS-15; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80.
"Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.";
Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L.,Freitas M.A., Denu J.M., Kaufman P.D.;
Mol. Cell 25:703-712(2007).
Cited for: MASS SPECTROMETRY, AND ACETYLATION AT LYS-57.
"Identification of histone H3 lysine 36 acetylation as a highlyconserved histone modification.";
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.;
J. Biol. Chem. 282:7632-7640(2007).
Cited for: PROTEIN SEQUENCE OF 28-41, AND ACETYLATION AT LYS-37.
Methylation
ReferencePubMed
"The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologueand methylates histone 3 lysine 4.";
Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,Aasland R., Stewart A.F.;
EMBO J. 20:7137-7148(2001).
Cited for: METHYLATION AT LYS-5.
"Histone H3 lysine 4 methylation is mediated by Set1 and required forcell growth and rDNA silencing in Saccharomyces cerevisiae.";
Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K.,Dent S.Y.R., Winston F., Allis C.D.;
Genes Dev. 15:3286-3295(2001).
Cited for: METHYLATION AT LYS-5.
"Lysine methylation within the globular domain of histone H3 by Dot1is important for telomeric silencing and Sir protein association.";
Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y.,Struhl K.;
Genes Dev. 16:1518-1527(2002).
Cited for: METHYLATION AT LYS-80, AND MUTAGENESIS OF LYS-80.
"Disruptor of telomeric silencing-1 is a chromatin-specific histone H3methyltransferase.";
Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.;
J. Biol. Chem. 277:30421-30424(2002).
Cited for: METHYLATION AT LYS-80.
"Set2 is a nucleosomal histone H3-selective methyltransferase thatmediates transcriptional repression.";
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.;
Mol. Cell. Biol. 22:1298-1306(2002).
Cited for: METHYLATION AT LYS-37.
"Gene silencing: trans-histone regulatory pathway in chromatin.";
Briggs S.D., Xiao T., Sun Z.-W., Caldwell J.A., Shabanowitz J.,Hunt D.F., Allis C.D., Strahl B.D.;
Nature 418:498-498(2002).
Cited for: METHYLATION AT LYS-5; LYS-37 AND LYS-80.
"Active genes are tri-methylated at K4 of histone H3.";
Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J.,Bernstein B.E., Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.;
Nature 419:407-411(2002).
Cited for: METHYLATION AT LYS-5.
"A trithorax-group complex purified from Saccharomyces cerevisiae isrequired for methylation of histone H3.";
Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.;
Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002).
Cited for: METHYLATION AT LYS-5.
"Phosphorylation of RNA polymerase II CTD regulates H3 methylation inyeast.";
Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H.,Strahl B.D.;
Genes Dev. 17:654-663(2003).
Cited for: METHYLATION AT LYS-37.
"Methylation of histone H3 by Set2 in Saccharomyces cerevisiae islinked to transcriptional elongation by RNA polymerase II.";
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.;
Mol. Cell. Biol. 23:4207-4218(2003).
Cited for: METHYLATION AT LYS-37.
"Set2-catalyzed methylation of histone H3 represses basal expressionof GAL4 in Saccharomyces cerevisiae.";
Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M.,Sternglanz R.;
Mol. Cell. Biol. 23:5972-5978(2003).
Cited for: METHYLATION AT LYS-37.
"Lysine-79 of histone H3 is hypomethylated at silenced loci in yeastand mammalian cells: a potential mechanism for position-effectvariegation.";
Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.;
Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003).
Cited for: METHYLATION AT LYS-80.
"Saccharomyces cerevisiae Set1p is a methyltransferase specific forlysine 4 of histone H3 and is required for efficient geneexpression.";
Boa S., Coert C., Patterton H.-G.;
Yeast 20:827-835(2003).
Cited for: MASS SPECTROMETRY, AND METHYLATION AT LYS-5.
"The DNA damage checkpoint response requires histone H2Bubiquitination by Rad6-Bre1 and H3 methylation by Dot1.";
Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.;
J. Biol. Chem. 280:9879-9886(2005).
Cited for: METHYLATION AT LYS-80.
"Histone H3 lysine 4 mono-methylation does not require ubiquitinationof histone H2B.";
Dehe P.-M., Pamblanco M., Luciano P., Lebrun R., Moinier D.,Sendra R., Verreault A., Tordera V., Geli V.;
J. Mol. Biol. 353:477-484(2005).
Cited for: METHYLATION AT LYS-5.
"Dynamic lysine methylation on histone H3 defines the regulatory phaseof gene transcription.";
Morillon A., Karabetsou N., Nair A., Mellor J.;
Mol. Cell 18:723-734(2005).
Cited for: METHYLATION AT LYS-5.
"Molecular regulation of histone H3 trimethylation by COMPASS and theregulation of gene expression.";
Schneider J., Wood A., Lee J.-S., Schuster R., Dueker J., Maguire C.,Swanson S.K., Florens L., Washburn M.P., Shilatifard A.;
Mol. Cell 19:849-856(2005).
Cited for: METHYLATION AT LYS-5.
"A novel domain in Set2 mediates RNA polymerase II interaction andcouples histone H3 K36 methylation with transcript elongation.";
Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L.,Strahl B.D.;
Mol. Cell. Biol. 25:3305-3316(2005).
Cited for: METHYLATION AT LYS-37.
"Single-nucleosome mapping of histone modifications in S.cerevisiae.";
Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L.,Friedman N., Rando O.J.;
PLoS Biol. 3:1-17(2005).
Cited for: METHYLATION AT LYS-5, AND ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
"Organismal differences in post-translational modifications inhistones H3 and H4.";
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.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: MASS SPECTROMETRY, ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57 AND LYS-65, AND METHYLATION AT LYS-5; LYS-10;LYS-15; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80.
Phosphorylation
ReferencePubMed
"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurorakinase and Glc7/PP1 phosphatase in budding yeast and nematodes.";
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.;
Cell 102:279-291(2000).
Cited for: PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, ANDMUTAGENESIS OF SER-11.
"Phosphorylation of serine 10 in histone H3 is functionally linked invitro and in vivo to Gcn5-mediated acetylation at lysine 14.";
Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D.,Marmorstein R., Berger S.L.;
Mol. Cell 5:917-926(2000).
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, AND MUTAGENESIS OFSER-11.
"Histone H3 phosphorylation can promote TBP recruitment throughdistinct promoter-specific mechanisms.";
Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.;
EMBO J. 24:997-1008(2005).
Cited for: PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures