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Q5A1D3

- ERK1_CANAL

UniProt

Q5A1D3 - ERK1_CANAL

Protein

Extracellular signal-regulated kinase 1

Gene

CEK1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001ATPPROSITE-ProRule annotation
    Active sitei195 – 1951Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi77 – 859ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: CGD
    3. protein binding Source: IntAct
    4. protein kinase activity Source: CGD

    GO - Biological processi

    1. cellular response to drug Source: CGD
    2. cellular response to heat Source: CGD
    3. cellular response to oxidative stress Source: CGD
    4. cellular response to reactive oxygen species Source: CGD
    5. cellular response to starvation Source: CGD
    6. filamentous growth Source: CGD
    7. filamentous growth of a population of unicellular organisms Source: CGD
    8. filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
    9. filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
    10. fungal-type cell wall biogenesis Source: CGD
    11. fungal-type cell wall organization Source: CGD
    12. MAPK cascade Source: CGD
    13. mitotic nuclear division Source: UniProtKB-KW
    14. parasexual conjugation with cellular fusion Source: CGD
    15. pathogenesis Source: CGD
    16. positive regulation of filamentous growth of a population of unicellular organisms Source: CGD
    17. positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
    18. positive regulation of filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
    19. protein phosphorylation Source: CGD
    20. regulation of single-species biofilm formation on inanimate substrate Source: CGD
    21. retrograde transport, endosome to Golgi Source: CGD
    22. signal transduction Source: CGD
    23. single-species biofilm formation on inanimate substrate Source: CGD
    24. stress-activated protein kinase signaling cascade Source: CGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular signal-regulated kinase 1 (EC:2.7.11.24)
    Short name:
    ERK1
    Alternative name(s):
    MAP kinase 1
    Short name:
    MAPK 1
    Gene namesi
    Name:CEK1
    Synonyms:ERK1
    ORF Names:CaO19.10404, CaO19.2886
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0005224. CEK1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Extracellular signal-regulated kinase 1PRO_0000186325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei231 – 2311PhosphothreonineBy similarity
    Modified residuei233 – 2331PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-231 and Tyr-233, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ5A1D3.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STE5P329172EBI-8783371,EBI-18373From a different organism.

    Protein-protein interaction databases

    BioGridi1225883. 5 interactions.
    IntActiQ5A1D3. 2 interactions.
    STRINGi5476.CAL0005224.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini71 – 376306Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi231 – 2333TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 5349Ala/Gln-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    KOiK04371.
    OrthoDBiEOG7K3TWD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5A1D3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQQQQ QAAAAAAAAN    50
    AAATTSSSSP RQVSFNVSDH YQILEIVGEG AYGIVCSAIH KPSQQKVAIK 100
    KIEPFERSML CLRTLRELKL LKHFNHENII SILAIQRPIN YESFNEIYLI 150
    QELMETDLHR VIRTQNLSDD HIQYFIYQTL RALKAMHSAN VLHRDLKPSN 200
    LLLNSNCDLK ICDFGLARSI ASQEDNYGFM TEYVATRWYR APEIMLTFQE 250
    YTTAIDVWSV GCILAEMLSG RPLFPGRDYH NQLWLIMEVL GTPNMEDYYN 300
    IKSKRAREYI RSLPFCKKIP FSELFANTNN NTSTSTSNTG GRTNINPLAL 350
    DLLEKLLIFN PAKRITVEDA LKHPYLQLYH DPNDEPISDK IPEDFFDFDK 400
    MKDQLTIEDL KKLLYEEIMK PL 422
    Length:422
    Mass (Da):48,623
    Last modified:October 19, 2011 - v2
    Checksum:i471BE4423FDAAAD5
    GO

    Sequence cautioni

    The sequence EAK96519.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAK96578.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 354Missing in strain: ATCC 60193 / S-24; in allele 237 B.
    Natural varianti33 – 331Q → QA in strain: R-2617; in allele 249 D.
    Natural varianti34 – 352QQ → AQAQA in strain: R-2805; in allele 255 A.
    Natural varianti34 – 341Q → A in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E.
    Natural varianti38 – 436Missing in strain: ATCC 36232; in allele 225 A.
    Natural varianti38 – 414Missing in strain: R-2621; in allele 237 A.
    Natural varianti41 – 411Q → QQ in strain: R-2621; in allele 249 B.
    Natural varianti41 – 411Missing in strain: R-2540; in allele 243 A.
    Natural varianti52 – 521A → T in strain: R-2617; in allele 246 D.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000084 Genomic DNA. Translation: EAK96519.1. Different initiation.
    AACQ01000083 Genomic DNA. Translation: EAK96578.1. Different initiation.
    U95784 Genomic DNA. Translation: AAB88588.1.
    U95785 Genomic DNA. Translation: AAB88589.1.
    U95786 Genomic DNA. Translation: AAB88590.1.
    U95787 Genomic DNA. Translation: AAB88591.1.
    U95788 Genomic DNA. Translation: AAB88592.1.
    U95789 Genomic DNA. Translation: AAB88593.1.
    U95790 Genomic DNA. Translation: AAB88594.1.
    U95791 Genomic DNA. Translation: AAB88595.1.
    U95792 Genomic DNA. Translation: AAB88596.1.
    U95793 Genomic DNA. Translation: AAB88597.1.
    U95794 Genomic DNA. Translation: AAB88598.1.
    U95795 Genomic DNA. Translation: AAB88599.1.
    U95796 Genomic DNA. Translation: AAB88600.1.
    U95797 Genomic DNA. Translation: AAB88601.1.
    U95798 Genomic DNA. Translation: AAB88602.1.
    RefSeqiXP_715542.1. XM_710449.1.
    XP_715598.1. XM_710505.1.

    Genome annotation databases

    GeneIDi3642743.
    3642789.
    KEGGical:CaO19.10404.
    cal:CaO19.2886.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000084 Genomic DNA. Translation: EAK96519.1 . Different initiation.
    AACQ01000083 Genomic DNA. Translation: EAK96578.1 . Different initiation.
    U95784 Genomic DNA. Translation: AAB88588.1 .
    U95785 Genomic DNA. Translation: AAB88589.1 .
    U95786 Genomic DNA. Translation: AAB88590.1 .
    U95787 Genomic DNA. Translation: AAB88591.1 .
    U95788 Genomic DNA. Translation: AAB88592.1 .
    U95789 Genomic DNA. Translation: AAB88593.1 .
    U95790 Genomic DNA. Translation: AAB88594.1 .
    U95791 Genomic DNA. Translation: AAB88595.1 .
    U95792 Genomic DNA. Translation: AAB88596.1 .
    U95793 Genomic DNA. Translation: AAB88597.1 .
    U95794 Genomic DNA. Translation: AAB88598.1 .
    U95795 Genomic DNA. Translation: AAB88599.1 .
    U95796 Genomic DNA. Translation: AAB88600.1 .
    U95797 Genomic DNA. Translation: AAB88601.1 .
    U95798 Genomic DNA. Translation: AAB88602.1 .
    RefSeqi XP_715542.1. XM_710449.1.
    XP_715598.1. XM_710505.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1225883. 5 interactions.
    IntActi Q5A1D3. 2 interactions.
    STRINGi 5476.CAL0005224.

    Proteomic databases

    PRIDEi Q5A1D3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3642743.
    3642789.
    KEGGi cal:CaO19.10404.
    cal:CaO19.2886.

    Organism-specific databases

    CGDi CAL0005224. CEK1.

    Phylogenomic databases

    eggNOGi COG0515.
    KOi K04371.
    OrthoDBi EOG7K3TWD.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    2. "Sequence analysis of a compound coding-region microsatellite in Candida albicans resolves homoplasies and provides a high-resolution tool for genotyping."
      Metzgar D., Field D., Haubrich R., Wills C.
      FEMS Immunol. Med. Microbiol. 20:103-109(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
      Strain: ATCC 36232, ATCC 60193 / S-24, R-2436, R-2535, R-2540, R-2607, R-2617, R-2621, R-2624, R-2777 and R-2805.

    Entry informationi

    Entry nameiERK1_CANAL
    AccessioniPrimary (citable) accession number: Q5A1D3
    Secondary accession number(s): O13435
    , P28869, P87079, P87080, P87081, P87082, P87083, P87084, P87085, P87086, P87322, Q6LC13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3