| UniProt ID | HOG1_YEAST | |
|---|---|---|
| UniProt AC | P32485 | |
| Protein Name | Mitogen-activated protein kinase HOG1 | |
| Gene Name | HOG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 435 | |
| 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 via the stress response element (STRE) in promoters of target genes. Upon osmotic shock, associates with the SKO1-SSN6-TUP1 complex, phosphorylates SKO1, and converts it into an activator that subsequently recruits Swi/Snf and SAGA complexes. Activates the SMP1 transcription factor and the RCK2 kinase, both also involved in the regulation of the expression of a subset of osmotic stress-related genes. Phosphorylation of HSL1 by HOG1 leads to a G2 arrest essential for cell survival at high osmolarity. Mediates also cell-cycle arrest in G1 phase by the dual targeting of SIC1. Regulates MFA2 ARE-mediated translation in response to carbon source. Targets RDP3 histone deacetylase to osmoresponsive promoters to induce gene expression on stress. Plays an essential role in maintaining water homeostasis, arsenite detoxification, copper-resistance, hydrogen peroxide response, adaptation to citric acid stress, and repression of the mating pathway activity. Required for the Golgi apparatus localization of MNN1.. | |
| Protein Sequence | MTTNEEFIRTQIFGTVFEITNRYNDLNPVGMGAFGLVCSATDTLTSQPVAIKKIMKPFSTAVLAKRTYRELKLLKHLRHENLICLQDIFLSPLEDIYFVTELQGTDLHRLLQTRPLEKQFVQYFLYQILRGLKYVHSAGVIHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMIEGKPLFPGKDHVHQFSIITDLLGSPPKDVINTICSENTLKFVTSLPHRDPIPFSERFKTVEPDAVDLLEKMLVFDPKKRITAADALAHPYSAPYHDPTDEPVADAKFDWHFNDADLPVDTWRVMMYSEILDFHKIGGSDGQIDISATFDDQVAAATAAAAQAQAQAQAQVQLNMAAHSHNGAGTTGNDHSDIAGGNKVSDHVAANDTITDYGNQAIQYANEFQQ | |
| 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 | Acetylation | ------MTTNEEFIR ------CCCHHHHHH | 38.03 | 22814378 | |
| 146 | Ubiquitination | GVIHRDLKPSNILIN CCCCCCCCHHHEEEC | 51.17 | 23749301 | |
| 174 | Phosphorylation | RIQDPQMTGYVSTRY ECCCCCCCCCEEEEE | 21.80 | 22369663 | |
| 176 | Phosphorylation | QDPQMTGYVSTRYYR CCCCCCCCEEEEEEE | 5.09 | 22369663 | |
| 178 | Phosphorylation | PQMTGYVSTRYYRAP CCCCCCEEEEEEECC | 9.93 | 22890988 | |
| 179 | Phosphorylation | QMTGYVSTRYYRAPE CCCCCEEEEEEECCE | 16.79 | 22890988 | |
| 269 | Acetylation | IPFSERFKTVEPDAV CCHHHHCCCCCCCHH | 58.86 | 24489116 | |
| 288 | Acetylation | KMLVFDPKKRITAAD HHCCCCHHHCCCHHH | 57.43 | 24489116 | |
| 288 | Succinylation | KMLVFDPKKRITAAD HHCCCCHHHCCCHHH | 57.43 | 23954790 | |
| 418 | Phosphorylation | DHVAANDTITDYGNQ CCEECCCCCCHHHHH | 26.11 | 27017623 |
| 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_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 174 | T | Phosphorylation |
| 7523111 |
* 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_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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 TYR-176; SER-178 ANDTHR-179, AND MASS SPECTROMETRY. | |
| "Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vitalfor Hog1 biological activity."; Bell M., Engelberg D.; J. Biol. Chem. 278:14603-14606(2003). Cited for: PHOSPHORYLATION AT THR-174 AND TYR-176, AND MUTAGENESIS OF THR-174 ANDTYR-176. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND TYR-176, ANDMASS SPECTROMETRY. | |
