| UniProt ID | HOG1_SCHPO | |
|---|---|---|
| UniProt AC | Q09892 | |
| Protein Name | Mitogen-activated protein kinase sty1 | |
| Gene Name | sty1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 349 | |
| Subcellular Localization | Cytoplasm. Nucleus. Predominantly cytoplasmic in unstressed cells but rapidly concentrates within the nucleus in response to hyperosmotic conditions and phosphorylation. | |
| Protein Description | Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes. Involved in osmoregulation and stress response pathways leading to an efficient start of sexual differentiation. Supports translation initiation and facilitates adaptation to environmental stress in part through reducing eIF2-alpha phosphorylation. Links the cell-cycle G2/M control with changes in the extracellular environment that affect cell physiology. Phosphorylates atf1 and mkp1. In conjunction with hal4, has a role in the cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+). Involved in resistance to arsenite, methylglyoxal and hydrogen peroxide. Involved in induction of thermotolerance in mRNA export, as well as in vacuolar fission.. | |
| Protein Sequence | MAEFIRTQIFGTCFEITTRYSDLQPIGMGAFGLVCSAKDQLTGMNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPFEDIYFVTELLGTDLHRLLTSRPLETQFIQYFLYQILRGLKFVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYNVEVDIWSAGCIFAEMIEGKPLFPGRDHVNQFSIITELLGTPPMEVIETICSKNTLRFVQSLPQKEKVPFAEKFKNADPDAIDLLEKMLVFDPRKRISAADALAHNYLAPYHDPTDEPVADEVFDWSFQDNDLPVETWKVMMYSEVLSFHNMDNELQS | |
| 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 |
|---|---|---|---|---|---|
| 171 | Phosphorylation | RIQDPQMTGYVSTRY ECCCCCCCCCEEEEE | 21.80 | 28889911 | |
| 173 | Phosphorylation | QDPQMTGYVSTRYYR CCCCCCCCEEEEEEE | 5.09 | 28889911 | |
| 175 | Phosphorylation | PQMTGYVSTRYYRAP CCCCCCEEEEEEECC | 9.93 | 28889911 | |
| 176 | Phosphorylation | QMTGYVSTRYYRAPE CCCCCEEEEEEECCE | 16.79 | 28889911 |
| 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 HOG1_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HOG1_SCHPO !! | ||||||
* 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 HOG1_SCHPO !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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