P38623 · RCK2_YEAST
- ProteinSerine/threonine-protein kinase RCK2
- GeneRCK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids610 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.
Miscellaneous
Present with 1790 molecules/cell in log phase SD medium.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by Ser-520 phosphorylation by HOG1.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | osmosensory signaling pathway | |
Biological Process | regulation of meiotic nuclear division |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase RCK2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38623
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086604 | 1-610 | Serine/threonine-protein kinase RCK2 | |||
Sequence: MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWLNTFDCLPKEGESSQKKAGTSERRHPHKKQFQLFQRDSSLLFSPAAVAMRDAFDIGNAVKRTEEDRMGTRGGLGSLAEDEELEDSYSGAQGDEQLEQNMFQLTLDTSTILQRRKKVQENDVGPTIPISATIRE | ||||||
Modified residue | 46 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 50 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 350 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 520 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after osmotic stress.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P38623 | HOG1 P32485 | 5 | EBI-14885, EBI-8437 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-55 | Disordered | ||||
Sequence: MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKN | ||||||
Compositional bias | 7-28 | Basic and acidic residues | ||||
Sequence: LFSKKKPDQADLSQESKKPFKG | ||||||
Compositional bias | 29-55 | Polar residues | ||||
Sequence: KTRSSGTNNKDVSQITSSPKKSFQDKN | ||||||
Region | 99-127 | Disordered | ||||
Sequence: TSVPAIDVHESSEGQLSSDPLISDESLSE | ||||||
Domain | 163-478 | Protein kinase | ||||
Sequence: YKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWL | ||||||
Region | 493-506 | Calmodulin-binding | ||||
Sequence: KKAGTSERRHPHKK | ||||||
Region | 541-564 | Disordered | ||||
Sequence: EDRMGTRGGLGSLAEDEELEDSYS |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length610
- Mass (Da)68,062
- Last updated2010-10-05 v3
- Checksum00DDC674F6723E6A
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-28 | Basic and acidic residues | ||||
Sequence: LFSKKKPDQADLSQESKKPFKG | ||||||
Compositional bias | 29-55 | Polar residues | ||||
Sequence: KTRSSGTNNKDVSQITSSPKKSFQDKN | ||||||
Sequence conflict | 109 | in Ref. 1; CAA50389 and 2; AAA64421 | ||||
Sequence: S → N | ||||||
Sequence conflict | 188 | in Ref. 1; CAA50389 and 2; AAA64421 | ||||
Sequence: N → H | ||||||
Sequence conflict | 233 | in Ref. 1; CAA50389 and 2; AAA64421 | ||||
Sequence: V → A | ||||||
Sequence conflict | 328 | in Ref. 1; CAA50389 and 2; AAA64421 | ||||
Sequence: R → P | ||||||
Sequence conflict | 456 | in Ref. 1; CAA50389 and 2; AAA64421 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X71065 EMBL· GenBank· DDBJ | CAA50389.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U23464 EMBL· GenBank· DDBJ | AAA64421.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20865 EMBL· GenBank· DDBJ | AAB67392.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09562.1 EMBL· GenBank· DDBJ | Genomic DNA |