| UniProt ID | STE7_YEAST | |
|---|---|---|
| UniProt AC | P06784 | |
| Protein Name | Serine/threonine-protein kinase STE7 | |
| Gene Name | STE7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 515 | |
| Subcellular Localization | ||
| Protein Description | Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases.. | |
| Protein Sequence | MFQRKTLQRRNLKGLNLNLHPDVGNNGQLQEKTETHQGQSRIEGHVMSNINAIQNNSNLFLRRGIKKKLTLDAFGDDQAISKPNTVVIQQPQNEPVLVLSSLSQSPCVSSSSSLSTPCIIDAYSNNFGLSPSSTNSTPSTIQGLSNIATPVENEHSISLPPLEESLSPAAADLKDTLSGTSNGNYIQLQDLVQLGKIGAGNSGTVVKALHVPDSKIVAKKTIPVEQNNSTIINQLVRELSIVKNVKPHENIITFYGAYYNQHINNEIIILMEYSDCGSLDKILSVYKRFVQRGTVSSKKTWFNELTISKIAYGVLNGLDHLYRQYKIIHRDIKPSNVLINSKGQIKLCDFGVSKKLINSIADTFVGTSTYMSPERIQGNVYSIKGDVWSLGLMIIELVTGEFPLGGHNDTPDGILDLLQRIVNEPSPRLPKDRIYSKEMTDFVNRCCIKNERERSSIHELLHHDLIMKYVSPSKDDKFRHWCRKIKSKIKEDKRIKREALDRAKLEKKQSERSTH | |
| 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 |
|---|---|---|---|---|---|
| 149 | Phosphorylation | QGLSNIATPVENEHS HCCCCCCCCCCCCCC | 24.87 | 28889911 | |
| 204 | Phosphorylation | IGAGNSGTVVKALHV CCCCCCCCEEEEEEC | 23.19 | 27214570 | |
| 359 | Phosphorylation | VSKKLINSIADTFVG CCHHHHHHHHHHCCC | 16.50 | 8131746 | |
| 363 | Phosphorylation | LINSIADTFVGTSTY HHHHHHHHCCCCCCC | 15.93 | 8131746 | |
| 471 | Phosphorylation | DLIMKYVSPSKDDKF HHHHHHCCCCCCHHH | 21.99 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 363 | T | Phosphorylation | Kinase | STE11 | P23561 | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STE7_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 STE7_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Activation of MEK family kinases requires phosphorylation of twoconserved Ser/Thr residues."; Zheng C.-F., Guan K.-L.; EMBO J. 13:1123-1131(1994). Cited for: PHOSPHORYLATION AT SER-359 AND THR-363, AND MUTAGENESIS. | |
| "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 THR-149, AND MASSSPECTROMETRY. | |