| UniProt ID | H3_YEAST | |
|---|---|---|
| UniProt AC | P61830 | |
| Protein Name | Histone H3 | |
| Gene Name | HHT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 136 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | 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 | MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | 11742990 | |
| 5 | "N6,N6,N6-trimethyllysine" | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
| 7 | Phosphorylation | -MARTKQTARKSTGG -CCCCCHHHHHHCCC | 29.95 | 27717283 | |
| 10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 17194708 | |
| 10 | Crotonylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 27089029 | |
| 10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 17194708 | |
| 11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHHCCCCCCH | 27.08 | 10911986 | |
| 12 | Phosphorylation | KQTARKSTGGKAPRK CHHHHHHCCCCCCHH | 53.65 | 27717283 | |
| 15 | Acetylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 10911986 | |
| 15 | Butyrylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 27105113 | |
| 15 | "N6,N6-dimethyllysine" | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
| 15 | Methylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 17194708 | |
| 19 | Butyrylation | TGGKAPRKQLASKAA CCCCCCHHHHHHHHH | 48.91 | 27105113 | |
| 19 | Acetylation | TGGKAPRKQLASKAA CCCCCCHHHHHHHHH | 48.91 | 17194708 | |
| 19 | Methylation | TGGKAPRKQLASKAA CCCCCCHHHHHHHHH | 48.91 | 17194708 | |
| 24 | Methylation | PRKQLASKAARKSAP CHHHHHHHHHHHHCC | 40.22 | 17194708 | |
| 24 | Propionylation | PRKQLASKAARKSAP CHHHHHHHHHHHHCC | 40.22 | 19113941 | |
| 24 | Butyrylation | PRKQLASKAARKSAP CHHHHHHHHHHHHCC | 40.22 | 27105113 | |
| 24 | Acetylation | PRKQLASKAARKSAP CHHHHHHHHHHHHCC | 40.22 | 11545749 | |
| 28 | "N6,N6,N6-trimethyllysine" | LASKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
| 28 | Acetylation | LASKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | 11545749 | |
| 28 | Butyrylation | LASKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | 19113941 | |
| 28 | Methylation | LASKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | 17194708 | |
| 28 | Ubiquitination | LASKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | 23749301 | |
| 29 | Phosphorylation | ASKAARKSAPSTGGV HHHHHHHHCCCCCCC | 39.60 | 23749301 | |
| 32 | Phosphorylation | AARKSAPSTGGVKKP HHHHHCCCCCCCCCC | 39.13 | 23749301 | |
| 37 | Acetylation | APSTGGVKKPHRYKP CCCCCCCCCCCCCCC | 64.95 | 17189264 | |
| 37 | "N6,N6,N6-trimethyllysine" | APSTGGVKKPHRYKP CCCCCCCCCCCCCCC | 64.95 | - | |
| 37 | Methylation | APSTGGVKKPHRYKP CCCCCCCCCCCCCCC | 64.95 | 11839797 | |
| 38 | Ubiquitination | PSTGGVKKPHRYKPG CCCCCCCCCCCCCCC | 43.58 | 23749301 | |
| 38 | Acetylation | PSTGGVKKPHRYKPG CCCCCCCCCCCCCCC | 43.58 | 19113941 | |
| 38 | Methylation | PSTGGVKKPHRYKPG CCCCCCCCCCCCCCC | 43.58 | 19113941 | |
| 42 | Phosphorylation | GVKKPHRYKPGTVAL CCCCCCCCCCCCHHH | 20.64 | 21440633 | |
| 43 | Ubiquitination | VKKPHRYKPGTVALR CCCCCCCCCCCHHHH | 36.61 | 22817900 | |
| 57 | Ubiquitination | REIRRFQKSTELLIR HHHHHHHHCHHHHHH | 57.54 | 23749301 | |
| 57 | Acetylation | REIRRFQKSTELLIR HHHHHHHHCHHHHHH | 57.54 | 17320445 | |
| 57 | Propionylation | REIRRFQKSTELLIR HHHHHHHHCHHHHHH | 57.54 | 19113941 | |
| 57 | Malonylation | REIRRFQKSTELLIR HHHHHHHHCHHHHHH | 57.54 | 22389435 | |
| 58 | Phosphorylation | EIRRFQKSTELLIRK HHHHHHHCHHHHHHH | 19.14 | 21440633 | |
| 59 | Phosphorylation | IRRFQKSTELLIRKL HHHHHHCHHHHHHHC | 37.37 | 25521595 | |
| 65 | Acetylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | 17194708 | |
| 65 | Ubiquitination | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | 15699485 | |
| 80 | Methylation | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | 12574507 | |
| 80 | Acetylation | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | 24489116 | |
| 80 | Succinylation | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | 22389435 | |
| 80 | "N6,N6,N6-trimethyllysine" | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | - | |
| 80 | Ubiquitination | REIAQDFKTDLRFQS HHHHHHHHCCHHHHH | 49.79 | 23749301 | |
| 100 | Phosphorylation | LQESVEAYLVSLFED HHHHHHHHHHHHHCC | 8.30 | 28889911 | |
| 116 | Ubiquitination | NLAAIHAKRVTIQKK CHHHHHHEECEECHH | 32.99 | 17644757 | |
| 122 | Acetylation | AKRVTIQKKDIKLAR HEECEECHHHHHHHH | 48.87 | 25381059 | |
| 122 | Ubiquitination | AKRVTIQKKDIKLAR HEECEECHHHHHHHH | 48.87 | 22817900 | |
| 123 | Ubiquitination | KRVTIQKKDIKLARR EECEECHHHHHHHHH | 48.59 | 22817900 | |
| 126 | Ubiquitination | TIQKKDIKLARRLRG EECHHHHHHHHHHCC | 46.34 | 22817900 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of H3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H3_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of H3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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 | |
| Reference | PubMed |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| "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. | |
| Phosphorylation | |
| Reference | PubMed |
| "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. | |
| "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. | |
| "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. | |
