Q8NJT7 · HOG1_HORWE
- ProteinMitogen-activated protein kinase HOG1
- GeneHOG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids359 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Proline-directed serine/threonine-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.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
Cofactor
Activity regulation
Activated by tyrosine and threonine phosphorylation.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | MAP kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | stress-activated MAPK cascade |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase HOG1
- EC number
- Short namesMAP kinase HOG1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Mycosphaerellales > Teratosphaeriaceae > Hortaea
Accessions
- Primary accessionQ8NJT7
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000289693 | 1-359 | Mitogen-activated protein kinase HOG1 | |||
Sequence: MAEFVRAQIFGTTFEITSRYTDLQPVGMGAFGLVCSAKDQLTSQAVAVKKIMKPFSTPVLSKRTYRELKLLKHLRHENIICLSDIFISPLEDMYVVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIATICSENTLRFVQSLPKRERQPLKNKFKNADPQAIELLERMLVFDPRKRVKAGEALADPYLAPYHDPTDEPEAQEKFDWSFNDADLPVDTWKIMMYSEILDFHNVDANAEQAAHNNDTVAG | ||||||
Modified residue | 171 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 173 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-299 | Protein kinase | ||||
Sequence: YTDLQPVGMGAFGLVCSAKDQLTSQAVAVKKIMKPFSTPVLSKRTYRELKLLKHLRHENIICLSDIFISPLEDMYVVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVIATICSENTLRFVQSLPKRERQPLKNKFKNADPQAIELLERMLVFDPRKRVKAGEALADPYL | ||||||
Motif | 171-173 | TXY | ||||
Sequence: TGY |
Domain
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)41,083
- Last updated2002-10-01 v1
- Checksum3080AC701D691844