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Q39021

- MPK1_ARATH

UniProt

Q39021 - MPK1_ARATH

Protein

Mitogen-activated protein kinase 1

Gene

MPK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by threonine and tyrosine phosphorylation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei61 – 611ATPPROSITE-ProRule annotation
    Active sitei158 – 1581Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 469ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. auxin-activated signaling pathway Source: TAIR

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G10210-MONOMER.
    ARA:GQT-430-MONOMER.
    BRENDAi2.7.11.24. 399.
    ReactomeiREACT_190855. CREB phosphorylation through the activation of Ras.
    REACT_190946. KSRP destabilizes mRNA.
    REACT_202229. ERK1 activation.
    REACT_208246. ERKs are inactivated.
    REACT_209747. ERK2 activation.
    REACT_216613. Signalling to ERK5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 1 (EC:2.7.11.24)
    Short name:
    AtMPK1
    Short name:
    MAP kinase 1
    Gene namesi
    Name:MPK1
    Ordered Locus Names:At1g10210
    ORF Names:F14N23.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G10210.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Mitogen-activated protein kinase 1PRO_0000186310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911PhosphothreonineBy similarity
    Modified residuei193 – 1931PhosphotyrosineBy similarity
    Modified residuei196 – 1961PhosphothreonineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-191 and Tyr-193, which activates the enzyme By similarity. Autophosphorylated on threonine and tyrosine residues Probable. Phosphorylated on Ser residue.By similarity1 PublicationCurated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ39021.
    PRIDEiQ39021.

    Expressioni

    Tissue specificityi

    Highest levels in the stem. Present in the leaf, root and flower, but not in seeds.1 Publication

    Gene expression databases

    ArrayExpressiQ39021.
    GenevestigatoriQ39021.

    Interactioni

    Subunit structurei

    Interacts with MKK3.1 Publication

    Protein-protein interaction databases

    BioGridi22799. 3 interactions.
    IntActiQ39021. 3 interactions.
    STRINGi3702.AT1G10210.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ39021.
    SMRiQ39021. Positions 25-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 319288Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi191 – 1933TXY

    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.
    HOGENOMiHOG000233024.
    InParanoidiQ39021.
    KOiK04371.
    OMAiQGLSNDH.
    PhylomeDBiQ39021.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    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.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q39021-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATLVDPPNG IRNEGKHYFS MWQTLFEIDT KYMPIKPIGR GAYGVVCSSV    50
    NSDTNEKVAI KKIHNVYENR IDALRTLREL KLLRHLRHEN VIALKDVMMP 100
    IHKMSFKDVY LVYELMDTDL HQIIKSSQVL SNDHCQYFLF QLLRGLKYIH 150
    SANILHRDLK PGNLLVNANC DLKICDFGLA RASNTKGQFM TEYVVTRWYR 200
    APELLLCCDN YGTSIDVWSV GCIFAELLGR KPIFQGTECL NQLKLIVNIL 250
    GSQREEDLEF IDNPKAKRYI RSLPYSPGMS LSRLYPGAHV LAIDLLQKML 300
    VFDPSKRISV SEALQHPYMA PLYDPNANPP AQVPIDLDVD EDLREEMIRE 350
    MMWNEMLHYH PQASTLNTEL 370
    Length:370
    Mass (Da):42,644
    Last modified:June 6, 2002 - v2
    Checksum:iF2962D7881C87A1B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291V → R in BAA03535. (PubMed:8130795)Curated
    Sequence conflicti250 – 2501L → I in BAA03535. (PubMed:8130795)Curated
    Sequence conflicti262 – 2621D → V in BAA03535. (PubMed:8130795)Curated
    Sequence conflicti287 – 2871G → C in BAA03535. (PubMed:8130795)Curated
    Sequence conflicti310 – 3101V → A in BAA03535. (PubMed:8130795)Curated
    Sequence conflicti352 – 3521M → I in BAA03535. (PubMed:8130795)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14713 mRNA. Translation: BAA03535.1.
    AC005489 Genomic DNA. Translation: AAD32871.1.
    CP002684 Genomic DNA. Translation: AEE28553.1.
    CP002684 Genomic DNA. Translation: AEE28554.1.
    AY059937 mRNA. Translation: AAL24419.1.
    BT000062 mRNA. Translation: AAN15381.1.
    PIRiF86236.
    RefSeqiNP_001031017.1. NM_001035940.1.
    NP_172492.1. NM_100895.2.
    UniGeneiAt.261.

    Genome annotation databases

    EnsemblPlantsiAT1G10210.1; AT1G10210.1; AT1G10210.
    AT1G10210.2; AT1G10210.2; AT1G10210.
    GeneIDi837559.
    KEGGiath:AT1G10210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14713 mRNA. Translation: BAA03535.1 .
    AC005489 Genomic DNA. Translation: AAD32871.1 .
    CP002684 Genomic DNA. Translation: AEE28553.1 .
    CP002684 Genomic DNA. Translation: AEE28554.1 .
    AY059937 mRNA. Translation: AAL24419.1 .
    BT000062 mRNA. Translation: AAN15381.1 .
    PIRi F86236.
    RefSeqi NP_001031017.1. NM_001035940.1.
    NP_172492.1. NM_100895.2.
    UniGenei At.261.

    3D structure databases

    ProteinModelPortali Q39021.
    SMRi Q39021. Positions 25-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 22799. 3 interactions.
    IntActi Q39021. 3 interactions.
    STRINGi 3702.AT1G10210.1-P.

    Proteomic databases

    PaxDbi Q39021.
    PRIDEi Q39021.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G10210.1 ; AT1G10210.1 ; AT1G10210 .
    AT1G10210.2 ; AT1G10210.2 ; AT1G10210 .
    GeneIDi 837559.
    KEGGi ath:AT1G10210.

    Organism-specific databases

    GeneFarmi 855. 89.
    TAIRi AT1G10210.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    InParanoidi Q39021.
    KOi K04371.
    OMAi QGLSNDH.
    PhylomeDBi Q39021.

    Enzyme and pathway databases

    BioCyci ARA:AT1G10210-MONOMER.
    ARA:GQT-430-MONOMER.
    BRENDAi 2.7.11.24. 399.
    Reactomei REACT_190855. CREB phosphorylation through the activation of Ras.
    REACT_190946. KSRP destabilizes mRNA.
    REACT_202229. ERK1 activation.
    REACT_208246. ERKs are inactivated.
    REACT_209747. ERK2 activation.
    REACT_216613. Signalling to ERK5.

    Gene expression databases

    ArrayExpressi Q39021.
    Genevestigatori Q39021.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of two cDNAs that encode MAP kinase homologues in Arabidopsis thaliana and analysis of the possible role of auxin in activating such kinase activities in cultured cells."
      Mizoguchi T., Gotoh Y., Nishida E., Yamaguchi-Shinozaki K., Hayashida N., Iwasaki T., Kamada H., Shinozaki K.
      Plant J. 5:111-122(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Mitogen-activated protein kinase cascades in plants: a new nomenclature."
      MAPK group
      Trends Plant Sci. 7:301-308(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    6. Cited for: GENE FAMILY.
    7. "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream of group C mitogen-activated protein kinases and participates in pathogen signaling."
      Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A., Teige M., Hirt H.
      Plant Cell 19:3266-3279(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKK3.

    Entry informationi

    Entry nameiMPK1_ARATH
    AccessioniPrimary (citable) accession number: Q39021
    Secondary accession number(s): Q9SY63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3