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Q06060

- MPK_PEA

UniProt

Q06060 - MPK_PEA

Protein

Mitogen-activated protein kinase homolog D5

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      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 sitei91 – 911ATPPROSITE-ProRule annotation
    Active sitei188 – 1881Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi68 – 769ATPPROSITE-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

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 4872.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase homolog D5 (EC:2.7.11.24)
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Mitogen-activated protein kinase homolog D5PRO_0000186319Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei220 – 2201PhosphothreonineBy similarity
    Modified residuei222 – 2221PhosphotyrosineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-220 and Tyr-222, which activates the enzyme.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ06060.

    Expressioni

    Tissue specificityi

    Leaves, roots, root apices, and dormant and growing axillary buds.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06060.
    SMRiQ06060. Positions 51-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 347286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi220 – 2223TXY

    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

    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.

    Q06060-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGGGGAPAA DAVMEDAAPQ QQEPQQQAAM GIENIPATLS HGGRFIQYNI    50
    FGNIFEVTAK YRPPIMPIGK GAYGIVCSAH NSETNEHVAV KKIANAFDNK 100
    IDAKRTLREI KLVRHMDHEN VVAIRDIVPP PQREVFNDVY IAYELMDTDL 150
    HQIIRSNQAL SEEHCQYFLY QILRGLKYIH SANVLHRDLK PSNLLLNANC 200
    DLKICDFGLA RVTSETDFMT EYVVTRWYRA PELLLNSSDY TAAIDVWSVG 250
    CIFMELMDRK PLFPGRDHVH QLRLLMELIG TPSEADLGFL NENAKRYIRQ 300
    LPLYRRQSFQ EKFPHVHPEA IDLVEKMLTF DPRQRITVEN ALAHPYLTSL 350
    HDISDEPVCT TPFSFDFEQH ALTEEQMKEL IYREALAFNP EYQQ 394
    Length:394
    Mass (Da):45,145
    Last modified:October 1, 1994 - v1
    Checksum:iE7B4758EBD8F24A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70703 mRNA. Translation: CAA50036.1.
    PIRiS33635.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70703 mRNA. Translation: CAA50036.1 .
    PIRi S33635.

    3D structure databases

    ProteinModelPortali Q06060.
    SMRi Q06060. Positions 51-394.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q06060.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 4872.

    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. "Molecular cloning and expression of a MAP kinase homologue from pea."
      Stafstrom J.P., Altschuler M., Anderson D.H.
      Plant Mol. Biol. 22:83-90(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Alaska.
      Tissue: Seedling.

    Entry informationi

    Entry nameiMPK_PEA
    AccessioniPrimary (citable) accession number: Q06060
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain whether Met-1, Met-14 or Met-30 is the initiator.Curated

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3