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P43068

- MKC1_CANAX

UniProt

P43068 - MKC1_CANAX

Protein

Mitogen-activated protein kinase MKC1

Gene

MKC1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 sitei74 – 741ATPPROSITE-ProRule annotation
    Active sitei174 – 1741Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 429ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase MKC1 (EC:2.7.11.24)
    Short name:
    MAP kinase MKC1
    Gene namesi
    Name:MKC1
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Mitogen-activated protein kinase MKC1PRO_0000186334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111PhosphothreonineBy similarity
    Modified residuei213 – 2131PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-211 and Tyr-213, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP43068.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 339312Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi211 – 2133TXY

    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.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01773. P38MAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P43068-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQQEAPIYY GRSVNKVYNQ EFIIDSRFKI VKELGHGAYG IVCSAKYDNG    50
    SKKVPDSNNG NASSSANASF VAIKKITNIF SKNILCKRAL RELKLLQFFR 100
    GHKNITCLYD LDIIPNPMTG EFNEIYLYEE LMECDMHQII RSGQPLSDQH 150
    YQSFIYQVLC GLNFIHSADV LHRDLKPGNL LVNADCELKI CDFGLARGFS 200
    ENPDENAGFM TEYVATRWYR APEIMLSFTN YTKAIDIWSV GCILAELLGG 250
    KPLFRGKDYV DQLNQILMIL GTPPESTLQR IGSHRAQNYV RSLPITRKAS 300
    YEELFPDANP LALDLLERML TLDPRERITV RDALNHKYLE LWHDPKEEIE 350
    CQVKFDFKSF ETVDGLDEMK QLIMDEVQKF REFVRKPIEE QQRIQMQLHM 400
    QKREEQRQEE EEKELLEQQR QFPAQESMDI SQTPYNNLET NIGTPQVEDD 450
    YPRPQELDEF TFSNLESSSS MNLFQDMAKP SGEEYIKLEE ELGFGLDWCY 500
    V 501
    Length:501
    Mass (Da):58,192
    Last modified:November 1, 1995 - v1
    Checksum:i0EA9F8B6CB97AB07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76708 Genomic DNA. Translation: CAA54129.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76708 Genomic DNA. Translation: CAA54129.1 .

    3D structure databases

    ProteinModelPortali P43068.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0515.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008352. MAPK_p38.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01773. P38MAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional characterization of the MKC1 gene of Candida albicans, which encodes a mitogen-activated protein kinase homolog related to cell integrity."
      Navarro-Garcia F., Sanchez M., Pla J., Nombela C.
      Mol. Cell. Biol. 15:2197-2206(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 64385 / 1001.

    Entry informationi

    Entry nameiMKC1_CANAX
    AccessioniPrimary (citable) accession number: P43068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3