| UniProt ID | SHO1_YEAST | |
|---|---|---|
| UniProt AC | P40073 | |
| Protein Name | High osmolarity signaling protein SHO1 | |
| Gene Name | SHO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 367 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein. Bud. Bud neck. Cell projection. Localizes at the tip of the mating projection during conjugation. |
|
| Protein Description | Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway.. | |
| Protein Sequence | MSISSKIRPTPRKPSRMATDHSFKMKKFYADPFAISSISLAIVSWVIAIGGSISSASTNESFPRFTWWGIVYQFLIICSLMLFYCFDLVDHYRIFITTSIAVAFVYNTNSATNLVYADGPKKAAASAGVILLSIINLIWILYYGGDNASPTNRWIDSFSIKGIRPSPLENSLHRARRRGNRNTTPYQNNVYNDAIRDSGYATQFDGYPQQQPSHTNYVSSTALAGFENTQPNTSEAVNLHLNTLQQRINSASNAKETNDNSNNQTNTNIGNTFDTDFSNGNTETTMGDTLGLYSDIGDDNFIYKAKALYPYDADDDDAYEISFEQNEILQVSDIEGRWWKARRANGETGIIPSNYVQLIDGPEEMHR | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSISSKIRP ------CCCCCCCCC | 31.04 | 28152593 | |
| 4 | Phosphorylation | ----MSISSKIRPTP ----CCCCCCCCCCC | 20.48 | 15665377 | |
| 5 | Phosphorylation | ---MSISSKIRPTPR ---CCCCCCCCCCCC | 30.36 | 28152593 | |
| 10 | Phosphorylation | ISSKIRPTPRKPSRM CCCCCCCCCCCCCCC | 26.36 | 15665377 | |
| 59 | N-linked_Glycosylation | SISSASTNESFPRFT CCCCCCCCCCCCCHH | 40.18 | - | |
| 161 | Acetylation | WIDSFSIKGIRPSPL EEECEEECCCCCCCC | 47.27 | 24489116 | |
| 166 | Phosphorylation | SIKGIRPSPLENSLH EECCCCCCCCHHHHH | 32.06 | 17363249 | |
| 183 | Phosphorylation | RRRGNRNTTPYQNNV HHHCCCCCCCCCCCC | 26.38 | 24909858 | |
| 184 | Phosphorylation | RRGNRNTTPYQNNVY HHCCCCCCCCCCCCC | 24.45 | 25533186 | |
| 186 | Phosphorylation | GNRNTTPYQNNVYND CCCCCCCCCCCCCCH | 23.06 | 30377154 | |
| 250 | Phosphorylation | TLQQRINSASNAKET HHHHHHHHHHCCCCC | 30.61 | 27214570 |
| 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 SHO1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SHO1_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 SHO1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A systems-biology analysis of feedback inhibition in the Sho1osmotic-stress-response pathway."; Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H.,Elston T.C., Dohlman H.G.; Curr. Biol. 17:659-667(2007). Cited for: PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, AND SUBUNIT. | |
| "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-184, AND MASSSPECTROMETRY. | |
