P16892 · FUS3_YEAST
- ProteinMitogen-activated protein kinase FUS3
- GeneFUS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.
Miscellaneous
Present with 8480 molecules/cell in log phase SD medium.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Activated by tyrosine and threonine phosphorylation after pheromone treatment.
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase FUS3
- EC number
- Short namesMAP kinase FUS3
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP16892
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186326 | 1-353 | Mitogen-activated protein kinase FUS3 | |||
Sequence: MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYLQTYHDPNDEPEGEPIPPSFFEFDHYKEALTTKDLKKLIWNEIFS | ||||||
Modified residue | 180 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 182 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Cross-link | 345 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
In the nucleus, FUS3 forms a complex with DIG1, DIG2 and STE12. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. During its activation and phosphorylation, FUS3 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with STE7 and STE5.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P16892 | BCK2 P33306 | 2 | EBI-7193, EBI-3480 | |
BINARY | P16892 | FUS3 P16892 | 2 | EBI-7193, EBI-7193 | |
XENO | P16892 | Kpol_1061p54 A7TJH8 | 2 | EBI-7193, EBI-8783719 | |
BINARY | P16892 | KSS1 P14681 | 2 | EBI-7193, EBI-9945 | |
BINARY | P16892 | STE11 P23561 | 6 | EBI-7193, EBI-18259 | |
BINARY | P16892 | STE5 P32917 | 11 | EBI-7193, EBI-18373 | |
BINARY | P16892 | STE7 P06784 | 15 | EBI-7193, EBI-18389 | |
BINARY | P16892 | TIM12 P32830 | 2 | EBI-7193, EBI-11303 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-309 | Protein kinase | ||||
Sequence: FQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYL | ||||||
Motif | 180-182 | TXY | ||||
Sequence: TEY |
Domain
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similarities
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length353
- Mass (Da)40,772
- Last updated1993-10-01 v2
- Checksum5117980D20A1E7E2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 334 | in Ref. 1; AAA34613 | ||||
Sequence: Y → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M31132 EMBL· GenBank· DDBJ | AAA34613.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X69572 EMBL· GenBank· DDBJ | CAA49292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X68577 EMBL· GenBank· DDBJ | CAA48569.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35777 EMBL· GenBank· DDBJ | CAA84835.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY693096 EMBL· GenBank· DDBJ | AAT93115.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006936 EMBL· GenBank· DDBJ | DAA07104.1 EMBL· GenBank· DDBJ | Genomic DNA |