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C4YGK0

- ERK1_CANAW

UniProt

C4YGK0 - ERK1_CANAW

Protein

Extracellular signal-regulated kinase 1

Gene

CEK1

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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 sitei95 – 951ATPPROSITE-ProRule annotation
    Active sitei190 – 1901Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi72 – 809ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW

    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:CAWG_03179
    OrganismiCandida albicans (strain WO-1) (Yeast)
    Taxonomic identifieri294748 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000001429: Chromosome 4, Supercontig 1.4

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Extracellular signal-regulated kinase 1PRO_0000413039Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei226 – 2261PhosphothreonineBy similarity
    Modified residuei228 – 2281PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-226 and Tyr-228, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliC4YGK0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 369304Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi226 – 2283TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 4945Ala/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

    HOGENOMiHOG000233024.
    OMAiAIQRPIN.
    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.

    C4YGK0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIDQHHQLQ QQHQQQMLQQ QAQAQAQAQA QAQQQQQAAA AAAAANAAAT    50
    TSSSPRQVSF NVSDHYQILE IVGEGAYGIV CSAIHKPSQQ KVAIKKIEPF 100
    ERSMLCLRTL RELKLLKHFN HENIISILAI QRPINYESFN EIYLIQELME 150
    TDLHRVIRTQ NLSDDHIQYF IYQTLRALKA MHSANVLHRD LKPSNLLLNS 200
    NCDLKICDFG LARSIASQED NYGFMTEYVA TRWYRAPEIM LTFQEYTTAI 250
    DVWSVGCILA EMLSGRPLFP GRDYHNQLWL IMEVLGTPNM EDYYNIKSKR 300
    AREYIRSLPF CKKIPFSELF ANTNNNTSTS NTGGRTNINP LALDLLEKLL 350
    IFNPAKRITV EDALKHPYLQ LYHDPNDEPI SDKIPEDFFD FDKMKDQLTI 400
    EDLKKLLYEE IMKPL 415
    Length:415
    Mass (Da):47,836
    Last modified:July 28, 2009 - v1
    Checksum:i572857CFD5B00B67
    GO

    Sequence cautioni

    The sequence AAA34343.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531S → SS in AAA34343. (PubMed:1409649)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76585 Genomic DNA. Translation: AAA34343.2. Different initiation.
    CH672349 Genomic DNA. Translation: EEQ44882.1.
    PIRiA47211.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76585 Genomic DNA. Translation: AAA34343.2 . Different initiation.
    CH672349 Genomic DNA. Translation: EEQ44882.1 .
    PIRi A47211.

    3D structure databases

    ProteinModelPortali C4YGK0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOGENOMi HOG000233024.
    OMAi AIQRPIN.
    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. "Dominant negative selection of heterologous genes: isolation of Candida albicans genes that interfere with Saccharomyces cerevisiae mating factor-induced cell cycle arrest."
      Whiteway M., Dignard D., Thomas D.Y.
      Proc. Natl. Acad. Sci. U.S.A. 89:9410-9414(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: WO-1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WO-1.

    Entry informationi

    Entry nameiERK1_CANAW
    AccessioniPrimary (citable) accession number: C4YGK0
    Secondary accession number(s): P28869
    , P87079, P87080, P87081, P87082, P87083, P87084, P87085, P87086, P87322
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 35 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3