Q5A1D3 · ERK1_CANAL
- ProteinExtracellular signal-regulated kinase 1
- GeneCEK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Cofactor
Activity regulation
Activated by tyrosine and threonine phosphorylation.
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 nameExtracellular signal-regulated kinase 1
- EC number
- Short namesERK1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionQ5A1D3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 32-35 | in strain: ATCC 60193 / S-24; in allele 237 B | ||||
Sequence: Missing | ||||||
Natural variant | 33 | in strain: R-2617; in allele 249 D | ||||
Sequence: Q → QA | ||||||
Natural variant | 34 | in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E | ||||
Sequence: Q → A | ||||||
Natural variant | 34-35 | in strain: R-2805; in allele 255 A | ||||
Sequence: QQ → AQAQA | ||||||
Natural variant | 38-41 | in strain: R-2621; in allele 237 A | ||||
Sequence: Missing | ||||||
Natural variant | 38-43 | in strain: ATCC 36232; in allele 225 A | ||||
Sequence: Missing | ||||||
Natural variant | 41 | in strain: R-2621; in allele 249 B | ||||
Sequence: Q → QQ | ||||||
Natural variant | 41 | in strain: R-2540; in allele 243 A | ||||
Sequence: Missing | ||||||
Natural variant | 52 | in strain: R-2617; in allele 246 D | ||||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
Miscellaneous
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186325 | 1-421 | Extracellular signal-regulated kinase 1 | |||
Sequence: MNIDQHHQLQQQHQQQMLQQQAQAQAQAQAQAQQQQQQQQQAAAAAAAANAAATTSSSPRQVSFNVSDHYQILEIVGEGAYGIVCSAIHKPSQQKVAIKKIEPFERSMLCLRTLRELKLLKHFNHENIISILAIQRPINYESFNEIYLIQELMETDLHRVIRTQNLSDDHIQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNSNCDLKICDFGLARSIASQEDNYGFMTEYVATRWYRAPEIMLTFQEYTTAIDVWSVGCILAEMLSGRPLFPGRDYHNQLWLIMEVLGTPNMEDYYNIKSKRAREYIRSLPFCKKIPFSELFANTNNNTSTSTSNTGGRTNINPLALDLLEKLLIFNPAKRITVEDALKHPYLQLYHDPNDEPISDKIPEDFFDFDKMKDQLTIEDLKKLLYEEIMKPL | ||||||
Modified residue | 230 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 232 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Dually phosphorylated on Thr-230 and Tyr-232, which activates the enzyme.
Keywords
- PTM
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q5A1D3 | STE5 P32917 | 2 | EBI-8783371, EBI-18373 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 70-375 | Protein kinase | ||||
Sequence: YQILEIVGEGAYGIVCSAIHKPSQQKVAIKKIEPFERSMLCLRTLRELKLLKHFNHENIISILAIQRPINYESFNEIYLIQELMETDLHRVIRTQNLSDDHIQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNSNCDLKICDFGLARSIASQEDNYGFMTEYVATRWYRAPEIMLTFQEYTTAIDVWSVGCILAEMLSGRPLFPGRDYHNQLWLIMEVLGTPNMEDYYNIKSKRAREYIRSLPFCKKIPFSELFANTNNNTSTSTSNTGGRTNINPLALDLLEKLLIFNPAKRITVEDALKHPYL | ||||||
Motif | 230-232 | 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
- Length421
- Mass (Da)48,536
- Last updated2017-03-15 v3
- ChecksumEC070EC9E6501B52
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP017626 EMBL· GenBank· DDBJ | AOW29372.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95784 EMBL· GenBank· DDBJ | AAB88588.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95785 EMBL· GenBank· DDBJ | AAB88589.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95786 EMBL· GenBank· DDBJ | AAB88590.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95787 EMBL· GenBank· DDBJ | AAB88591.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95788 EMBL· GenBank· DDBJ | AAB88592.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95789 EMBL· GenBank· DDBJ | AAB88593.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95790 EMBL· GenBank· DDBJ | AAB88594.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95791 EMBL· GenBank· DDBJ | AAB88595.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95792 EMBL· GenBank· DDBJ | AAB88596.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95793 EMBL· GenBank· DDBJ | AAB88597.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95794 EMBL· GenBank· DDBJ | AAB88598.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95795 EMBL· GenBank· DDBJ | AAB88599.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95796 EMBL· GenBank· DDBJ | AAB88600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95797 EMBL· GenBank· DDBJ | AAB88601.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95798 EMBL· GenBank· DDBJ | AAB88602.1 EMBL· GenBank· DDBJ | Genomic DNA |