P08018 · PBS2_YEAST
- ProteinMAP kinase kinase PBS2
- GenePBS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment (PubMed:10970855, PubMed:15256499, PubMed:7681220).
Activates the MAP kinase HOG1 by concomitant phosphorylation at 'Thr-174' and 'Tyr-176' (PubMed:38270553, PubMed:7681220).
Activates the MAP kinase HOG1 by concomitant phosphorylation at 'Thr-174' and 'Tyr-176' (PubMed:38270553, PubMed:7681220).
Miscellaneous
Present with 2160 molecules/cell in log phase SD medium.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cellular bud neck | |
Cellular Component | cellular bud tip | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic stress granule | |
Cellular Component | NatB complex | |
Molecular Function | ATP binding | |
Molecular Function | MAP kinase kinase activity | |
Molecular Function | MAP-kinase scaffold activity | |
Molecular Function | peptide alpha-N-acetyltransferase activity | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein tyrosine kinase activity | |
Biological Process | actin filament organization | |
Biological Process | cellular hyperosmotic response | |
Biological Process | hyperosmotic response | |
Biological Process | MAPK cascade | |
Biological Process | osmosensory signaling pathway | |
Biological Process | osmosensory signaling pathway via Sho1 osmosensor | |
Biological Process | p38MAPK cascade | |
Biological Process | protein import into nucleus | |
Biological Process | protein phosphorylation | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMAP kinase kinase PBS2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP08018
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Leads to sensitivity to osmotic stress (induced by NaCl, KCl, and sorbitol), actinomycin D (transcription inhibitor), galactose, sirolimus (rapamycin), UV irradiation, and methyl methanesulfonate (MMS).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 96 | In PBS2-13; loss of SH3-domain interaction. | ||||
Sequence: P → S | ||||||
Mutagenesis | 389 | Loss of activity. | ||||
Sequence: K → M | ||||||
Mutagenesis | 514 | Loss of phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 518 | Loss of phosphorylation. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086483 | 1-668 | MAP kinase kinase PBS2 | |||
Sequence: MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHYNNINADLHARVKAFQEQRALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSKSTLKNVLDNQETQNITDVNINIDTTKITATTIGVNTGLPATDITPSVSNTASATHKAQLLNPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSGGGGLFANFSKYVDIKSGSLNFAGKLSLSSKGIDFSNGSSSRITLDELEFLDELGHGNYGNVSKVLHKPTNVIMATKEVRLELDEAKFRQILMELEVLHKCNSPYIVDFYGAFFIEGAVYMCMEYMDGGSLDKIYDESSEIGGIDEPQLAFIANAVIHGLKELKEQHNIIHRDVKPTNILCSANQGTVKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSLNPDRATYTVQSDIWSLGLSILEMALGRYPYPPETYDNIFSQLSAIVDGPPPRLPSDKFSSDAQDFVSLCLQKIPERRPTYAALTEHPWLVKYRNQDVHMSEYITERLERRNKILRERGENGLSKNVPALHMGGL | ||||||
Modified residue | 68 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 269 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 514 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 518 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with NBP2, PTC1, SHO1 and STE11.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08018 | NBP2 Q12163 | 3 | EBI-12972, EBI-34713 | |
BINARY | P08018 | SHO1 P40073 | 8 | EBI-12972, EBI-18140 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-43 | Disordered | ||||
Sequence: MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHY | ||||||
Compositional bias | 11-43 | Polar residues | ||||
Sequence: HEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHY | ||||||
Region | 61-120 | Disordered | ||||
Sequence: RALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSK | ||||||
Compositional bias | 64-89 | Polar residues | ||||
Sequence: KRSASVGSNQSEQDKGSSQSPKHIQQ | ||||||
Compositional bias | 104-120 | Polar residues | ||||
Sequence: SKVSQRMSSQVVQASSK | ||||||
Region | 181-313 | Disordered | ||||
Sequence: NPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSG | ||||||
Compositional bias | 234-313 | Polar residues | ||||
Sequence: MPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSG | ||||||
Domain | 360-623 | Protein kinase | ||||
Sequence: LEFLDELGHGNYGNVSKVLHKPTNVIMATKEVRLELDEAKFRQILMELEVLHKCNSPYIVDFYGAFFIEGAVYMCMEYMDGGSLDKIYDESSEIGGIDEPQLAFIANAVIHGLKELKEQHNIIHRDVKPTNILCSANQGTVKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSLNPDRATYTVQSDIWSLGLSILEMALGRYPYPPETYDNIFSQLSAIVDGPPPRLPSDKFSSDAQDFVSLCLQKIPERRPTYAALTEHPWL |
Domain
Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1.
Sequence similarities
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)72,720
- Last updated2011-09-21 v4
- Checksum9BC3435BDAFE8019
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-43 | Polar residues | ||||
Sequence: HEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHY | ||||||
Compositional bias | 64-89 | Polar residues | ||||
Sequence: KRSASVGSNQSEQDKGSSQSPKHIQQ | ||||||
Compositional bias | 104-120 | Polar residues | ||||
Sequence: SKVSQRMSSQVVQASSK | ||||||
Sequence conflict | 222-223 | in Ref. 4 and 5; CAA89423 | ||||
Sequence: GL → AV | ||||||
Compositional bias | 234-313 | Polar residues | ||||
Sequence: MPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J02946 EMBL· GenBank· DDBJ | AAA16819.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
U12237 EMBL· GenBank· DDBJ | AAA20392.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49403 EMBL· GenBank· DDBJ | CAA89423.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006943 EMBL· GenBank· DDBJ | DAA08673.2 EMBL· GenBank· DDBJ | Genomic DNA |