P50527 · STE20_SCHPO
- ProteinSerine/threonine-protein kinase shk1/pak1
- Geneshk1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids658 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
MAP4K component of the MAPK pathway required for the mating pheromone response. Phosphorylates histone H2B to form H2BS10ph (By similarity).
Phosphorylates tea1. Required for skb1-dependent mitotic inhibitory function. Regulates microtubule dynamics and cell polarity
Phosphorylates tea1. Required for skb1-dependent mitotic inhibitory function. Regulates microtubule dynamics and cell polarity
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase shk1/pak1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP50527
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at cell ends, septum forming regions and at the mitotic spindle.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086651 | 1-658 | Serine/threonine-protein kinase shk1/pak1 | |||
Sequence: MERGTLQPRKKAPNGYGITPIVAHKTGEPVRYEVEDDLRKLKPSRTAPKPPAINTNLAEDTFSGFPLSQSRTTVSRVSLGSRQHSSSSIRKLQTNVSDVRSYDERNQKKSAFENFVSSMSSFLTGGGSSPTSSYGSGSASPRKSTVISSPFDPKHVTHVGFNYDTGEFTGMPTEWQALLKVSGITKSEQVQHPQAVLDAMAFYSQSKKYLEEGAKPPFPRESTEKPLLSVSALSSSSHLQPTSATSSSSRLYPSRPAPTPPASSSSSPLLSSQTVKTTTSNASRQPSPLVSSKSTDNIIRSHSPVLLTPQTLSTSETKHIRPNNSTPYQRRAETSTKPKAVATPQKVEAPSAPRLQKRAPRQQSNDSAVLAKLQSICNPKNPTLLYRNFVKIGQGASGDVYSARQVGTNLSVAIKKMNINQQPKKEFIVNEILVMKSHHHKNIVNFIDTFFYKSELWMVMEYMRGGSLTEVVTNNTLSEGQIAAICKETLEGLQHLHENGIVHRDIKSDNILLSLQGDIKLTDFGFCAQIDSNMTKRTTMVGTPYWMAPEVVTRKEYGFKVDVWSLGIMAIEMVEGEPPYLNENPLRALYLIATIGTPKISRPELLSSVFHDFLSKSLTVNPKQRPSSGELLRHPFLKQAVPVSSLIPLIKSIHHSGK | ||||||
Modified residue | 301 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 303 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated on serine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms an activated complex with GTP-bound ras-like cdc42. Interacts with skb1 and the SH3 domain of skb5 via its amino-terminal regulatory domain. Skb1, cdc42 and shk1 are able to form a ternary complex in vivo. Interacts with rga8 and may interact with byr2.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MERGTLQPRKKAPNGYGITPI | ||||||
Region | 39-104 | Disordered | ||||
Sequence: RKLKPSRTAPKPPAINTNLAEDTFSGFPLSQSRTTVSRVSLGSRQHSSSSIRKLQTNVSDVRSYDE | ||||||
Compositional bias | 56-96 | Polar residues | ||||
Sequence: NLAEDTFSGFPLSQSRTTVSRVSLGSRQHSSSSIRKLQTNV | ||||||
Region | 126-147 | Disordered | ||||
Sequence: GGSSPTSSYGSGSASPRKSTVI | ||||||
Domain | 147-160 | CRIB | ||||
Sequence: ISSPFDPKHVTHVG | ||||||
Region | 213-365 | Disordered | ||||
Sequence: GAKPPFPRESTEKPLLSVSALSSSSHLQPTSATSSSSRLYPSRPAPTPPASSSSSPLLSSQTVKTTTSNASRQPSPLVSSKSTDNIIRSHSPVLLTPQTLSTSETKHIRPNNSTPYQRRAETSTKPKAVATPQKVEAPSAPRLQKRAPRQQSN | ||||||
Compositional bias | 227-253 | Polar residues | ||||
Sequence: LLSVSALSSSSHLQPTSATSSSSRLYP | ||||||
Compositional bias | 264-341 | Polar residues | ||||
Sequence: SSSSPLLSSQTVKTTTSNASRQPSPLVSSKSTDNIIRSHSPVLLTPQTLSTSETKHIRPNNSTPYQRRAETSTKPKAV | ||||||
Domain | 386-637 | Protein kinase | ||||
Sequence: YRNFVKIGQGASGDVYSARQVGTNLSVAIKKMNINQQPKKEFIVNEILVMKSHHHKNIVNFIDTFFYKSELWMVMEYMRGGSLTEVVTNNTLSEGQIAAICKETLEGLQHLHENGIVHRDIKSDNILLSLQGDIKLTDFGFCAQIDSNMTKRTTMVGTPYWMAPEVVTRKEYGFKVDVWSLGIMAIEMVEGEPPYLNENPLRALYLIATIGTPKISRPELLSSVFHDFLSKSLTVNPKQRPSSGELLRHPFL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length658
- Mass (Da)72,358
- Last updated2000-05-30 v2
- Checksum69D72E5C925021E5
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 56-96 | Polar residues | ||||
Sequence: NLAEDTFSGFPLSQSRTTVSRVSLGSRQHSSSSIRKLQTNV | ||||||
Compositional bias | 227-253 | Polar residues | ||||
Sequence: LLSVSALSSSSHLQPTSATSSSSRLYP | ||||||
Compositional bias | 264-341 | Polar residues | ||||
Sequence: SSSSPLLSSQTVKTTTSNASRQPSPLVSSKSTDNIIRSHSPVLLTPQTLSTSETKHIRPNNSTPYQRRAETSTKPKAV | ||||||
Sequence conflict | 492-495 | in Ref. 1; AAC49125 | ||||
Sequence: GLQH → LYSD | ||||||
Sequence conflict | 537 | in Ref. 1; AAC49125 | ||||
Sequence: R → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22371 EMBL· GenBank· DDBJ | AAC49125.1 EMBL· GenBank· DDBJ | mRNA | ||
L41552 EMBL· GenBank· DDBJ | AAB52609.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CU329671 EMBL· GenBank· DDBJ | CAA22347.1 EMBL· GenBank· DDBJ | Genomic DNA |