UniProt ID | STE11_YEAST | |
---|---|---|
UniProt AC | P23561 | |
Protein Name | Serine/threonine-protein kinase STE11 | |
Gene Name | STE11 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 717 | |
Subcellular Localization | ||
Protein Description | Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.. | |
Protein Sequence | MEQTQTAEGTDLLIGDEKTNDLPFVQLFLEEIGCTQYLDSFIQCNLVTEEEIKYLDKDILIALGVNKIGDRLKILRKSKSFQRDKRIEQVNRLKNLMEKVSSLSTATLSMNSELIPEKHCVIFILNDGSAKKVNVNGCFNADSIKKRLIRRLPHELLATNSNGEVTKMVQDYDVFVLDYTKNVLHLLYDVELVTICHANDRVEKNRLIFVSKDQTPSDKAISTSKKLYLRTLSALSQVGPSSSNLLAQNKGISHNNAEGKLRIDNTEKDRIRQIFNQRPPSEFISTNLAGYFPHTDMKRLQKTMRESFRHSARLSIAQRRPLSAESNNIGDILLKHSNAVDMALLQGLDQTRLSSKLDTTKIPKLAHKRPEDNDAISNQLELLSVESGEEEDHDFFGEDSDIVSLPTKIATPKNWLKGACIGSGSFGSVYLGMNAHTGELMAVKQVEIKNNNIGVPTDNNKQANSDENNEQEEQQEKIEDVGAVSHPKTNQNIHRKMVDALQHEMNLLKELHHENIVTYYGASQEGGNLNIFLEYVPGGSVSSMLNNYGPFEESLITNFTRQILIGVAYLHKKNIIHRDIKGANILIDIKGCVKITDFGISKKLSPLNKKQNKRASLQGSVFWMSPEVVKQTATTAKADIWSTGCVVIEMFTGKHPFPDFSQMQAIFKIGTNTTPEIPSWATSEGKNFLRKAFELDYQYRPSALELLQHPWLDAHII | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | Phosphorylation | ----MEQTQTAEGTD ----CCCCCCCCCCC | 18.00 | 30377154 | |
101 | Phosphorylation | KNLMEKVSSLSTATL HHHHHHHHHCCHHHH | 36.31 | 28889911 | |
105 | Phosphorylation | EKVSSLSTATLSMNS HHHHHCCHHHHCCCC | 29.02 | 28889911 | |
215 | Phosphorylation | IFVSKDQTPSDKAIS EEECCCCCCCCCCCC | 34.59 | 28889911 | |
231 | Phosphorylation | SKKLYLRTLSALSQV CHHHHHHHHHHHHHH | 23.59 | 28889911 | |
233 | Phosphorylation | KLYLRTLSALSQVGP HHHHHHHHHHHHHCC | 26.93 | 30377154 | |
236 | Phosphorylation | LRTLSALSQVGPSSS HHHHHHHHHHCCCHH | 23.65 | 25371407 | |
241 | Phosphorylation | ALSQVGPSSSNLLAQ HHHHHCCCHHHHHHH | 40.23 | 20377248 | |
242 | Phosphorylation | LSQVGPSSSNLLAQN HHHHCCCHHHHHHHC | 26.78 | 24961812 | |
243 | Phosphorylation | SQVGPSSSNLLAQNK HHHCCCHHHHHHHCC | 35.52 | 21551504 | |
281 | Phosphorylation | IFNQRPPSEFISTNL HHHCCCCHHHHCCCC | 48.06 | 10837245 | |
285 | Phosphorylation | RPPSEFISTNLAGYF CCCHHHHCCCCCCCC | 19.30 | 10837245 | |
286 | Phosphorylation | PPSEFISTNLAGYFP CCHHHHCCCCCCCCC | 29.45 | 10837245 | |
315 | Phosphorylation | FRHSARLSIAQRRPL HHHHHHHHHHHHCCC | 15.43 | 28889911 | |
323 | Phosphorylation | IAQRRPLSAESNNIG HHHHCCCCCCCCCHH | 32.45 | 17330950 | |
326 | Phosphorylation | RRPLSAESNNIGDIL HCCCCCCCCCHHHHH | 34.59 | 25752575 | |
384 | Phosphorylation | SNQLELLSVESGEEE HHHHHEEEECCCCCC | 36.14 | 21440633 | |
387 | Phosphorylation | LELLSVESGEEEDHD HHEEEECCCCCCCCC | 49.72 | 27214570 | |
423 | Phosphorylation | LKGACIGSGSFGSVY CCCCEECCCCCCCEE | 16.02 | 27017623 | |
425 | Phosphorylation | GACIGSGSFGSVYLG CCEECCCCCCCEEEE | 28.29 | 27017623 | |
428 | Phosphorylation | IGSGSFGSVYLGMNA ECCCCCCCEEEEEEC | 12.94 | 27017623 | |
465 | Phosphorylation | DNNKQANSDENNEQE CCCCCCCCCCCCHHH | 49.68 | 25521595 | |
485 | Phosphorylation | IEDVGAVSHPKTNQN HHHHHHCCCCCCCCH | 33.27 | 21551504 | |
616 | Phosphorylation | KKQNKRASLQGSVFW HHHCCCHHHCCCEEE | 25.84 | 20377248 | |
620 | Phosphorylation | KRASLQGSVFWMSPE CCHHHCCCEEECCHH | 10.94 | 20377248 | |
661 | Phosphorylation | KHPFPDFSQMQAIFK CCCCCCHHHHHHHHC | 31.93 | 21440633 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STE11_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 STE11_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-323; SER-326AND SER-387, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY. |