Q5A1D3 · ERK1_CANAL

Function

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Activated by tyrosine and threonine phosphorylation.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site76-84ATP (UniProtKB | ChEBI)
Binding site99ATP (UniProtKB | ChEBI)
Active site194Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionMAP kinase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processcell division
Biological Processcellular response to starvation
Biological Processfilamentous growth
Biological Processfilamentous growth of a population of unicellular organisms in response to biotic stimulus
Biological Processfilamentous growth of a population of unicellular organisms in response to starvation
Biological Processfungal-type cell wall biogenesis
Biological Processfungal-type cell wall organization
Biological Processintracellular signal transduction
Biological Processparasexual reproduction with cellular fusion
Biological Processpheromone-dependent signal transduction involved in conjugation with cellular fusion
Biological Processpositive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus
Biological Processpositive regulation of filamentous growth of a population of unicellular organisms in response to starvation
Biological Processprotein phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Extracellular signal-regulated kinase 1
  • EC number
  • Short names
    ERK1
  • Alternative names
    • MAP kinase 1 (MAPK 1)

Gene names

    • Name
      CEK1
    • Synonyms
      ERK1
    • ORF names
      CaO19.10404, CaO19.2886
    • Ordered locus names
      CAALFM_C406480CA

Organism names

  • Taxonomic identifier
  • Strains
    • SC5314 / ATCC MYA-2876
    • ATCC 36232
    • ATCC 60193 / S-24
    • R-2436
    • R-2535
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    Q5A1D3
  • Secondary accessions
    • A0A1D8PMK1
    • O13435
    • P28869
    • P87079
    • P87080

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant32-35in strain: ATCC 60193 / S-24; in allele 237 B
Natural variant33in strain: R-2617; in allele 249 D
Natural variant34in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E
Natural variant34-35in strain: R-2805; in allele 255 A
Natural variant38-41in strain: R-2621; in allele 237 A
Natural variant38-43in strain: ATCC 36232; in allele 225 A
Natural variant41in strain: R-2621; in allele 249 B
Natural variant41in strain: R-2540; in allele 243 A
Natural variant52in strain: R-2617; in allele 246 D

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.

Go to variant viewer

Miscellaneous

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001863251-421Extracellular signal-regulated kinase 1
Modified residue230Phosphothreonine
Modified residue232Phosphotyrosine

Post-translational modification

Dually phosphorylated on Thr-230 and Tyr-232, which activates the enzyme.

Keywords

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q5A1D3STE5 P329172EBI-8783371, EBI-18373

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain70-375Protein kinase
Motif230-232TXY

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    421
  • Mass (Da)
    48,536
  • Last updated
    2017-03-15 v3
  • Checksum
    EC070EC9E6501B52
MNIDQHHQLQQQHQQQMLQQQAQAQAQAQAQAQQQQQQQQQAAAAAAAANAAATTSSSPRQVSFNVSDHYQILEIVGEGAYGIVCSAIHKPSQQKVAIKKIEPFERSMLCLRTLRELKLLKHFNHENIISILAIQRPINYESFNEIYLIQELMETDLHRVIRTQNLSDDHIQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNSNCDLKICDFGLARSIASQEDNYGFMTEYVATRWYRAPEIMLTFQEYTTAIDVWSVGCILAEMLSGRPLFPGRDYHNQLWLIMEVLGTPNMEDYYNIKSKRAREYIRSLPFCKKIPFSELFANTNNNTSTSTSNTGGRTNINPLALDLLEKLLIFNPAKRITVEDALKHPYLQLYHDPNDEPISDKIPEDFFDFDKMKDQLTIEDLKKLLYEEIMKPL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp