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Q9C5S1

- MKP1_ARATH

UniProt

Q9C5S1 - MKP1_ARATH

Protein

Protein-tyrosine-phosphatase MKP1

Gene

MKP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Protein-tyrosine-phosphatase that acts as a negative regulator of MPK6 and MPK3 signaling by dephosphorylating and repressing MPK6 and MPK3. Modulates defense response by repressing salicylic acid (SA) production, camalexin biosynthesis and SNC1-mediated responses. Acts as a negative regulator of MPK6-mediated pathogen-associated molecular pattern (PAMP) responses, including MPK6 and MPK3 activation, accumulation of extracellular reactive oxygen species and inhibition of seedling growth. Involved in UV-B stress tolerance. May be involved in salt and genotoxic stress responses.7 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei235 – 2351Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: TAIR
    2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    3. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. defense response Source: UniProtKB-KW
    2. inactivation of MAPK activity Source: GOC
    3. protein dephosphorylation Source: RefGenome
    4. response to salt stress Source: TAIR
    5. response to UV-B Source: TAIR
    6. response to UV-C Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Plant defense, Stress response

    Enzyme and pathway databases

    BioCyciARA:AT3G55270-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-tyrosine-phosphatase MKP1 (EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 1
    Short name:
    AtMKP1
    Gene namesi
    Name:MKP1
    Ordered Locus Names:At3g55270
    ORF Names:T26I12.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G55270.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth conditions in Wassilewskija (Ws) ecotype (PubMed:11274055), but Columbia (Col) ecotype show growth defects, elevated levels of salicylic acid (SA) and constitutive defense responses (PubMed:19789277).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi235 – 2351C → S: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 784784Protein-tyrosine-phosphatase MKP1PRO_0000417330Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641Phosphothreonine1 Publication
    Modified residuei109 – 1091Phosphothreonine1 Publication
    Modified residuei558 – 5581Phosphoserine1 Publication
    Modified residuei572 – 5721Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on threonine and serine residues by MPK6.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9C5S1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9C5S1.
    GenevestigatoriQ9C5S1.

    Interactioni

    Subunit structurei

    Interacts with MPK6. May interact with MPK3 and MPK4.3 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C5S1.
    SMRiQ9C5S1. Positions 157-287, 324-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 290142Tyrosine-protein phosphataseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni235 – 2417Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi477 – 56286Ser-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    OMAiKVADHIY.
    PhylomeDBiQ9C5S1.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR029006. ADF-H/Gelsolin-like_dom.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9C5S1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVGREDAMGN DEAPPGSKKM FWRSASWSAS RTASQVPEGD EQSLNIPCAI    50
    SSGPSRRCPA APLTPRSHHN SKARACLPPL QPLAISRRSL DEWPKAGSDD 100
    VGEWPHPPTP SGNKTGERLK LDLSSTQQRV TDKSSGLAKR EKIAFFDKEC 150
    SKVADHIYVG GDAVAKDKSI LKNNGITHIL NCVGFICPEY FKSDFCYRSL 200
    WLQDSPSEDI TSILYDVFDY FEDVREQSGR IFVHCCQGVS RSTSLVIAYL 250
    MWREGQSFDD AFQYVKSARG IADPNMGFAC QLLQCQKRVH AFPLSPTSLL 300
    RMYKMSPHSP YDPLHLVPKL LNDPCPGSLD SRGAFIIQLP SAIYIWVGRQ 350
    CETIMEKDAK AAVCQIARYE KVEAPIMVVR EGDEPVYYWD AFASILPMIG 400
    GSVIKVQPGD RKVDAYNLDF EIFQKAIEGG FVPTLASSNN EHETHLPARE 450
    NSWSSLKCKF ASRFDKGFRY VSKTPLSRVY SDSMMIVHSS GSPSSTTSSS 500
    STASPPFLSP DSVCSTNSGN SLKSFSQSSG RSSLRPSIPP SLTLPKFSSL 550
    SLLPSQTSPK ESRGVNTFLQ PSPNRKASPS LAERRGSLKG SLKLPGLADS 600
    NRGTPAFTLH PDDSNDIVFN LEGIRNGDLY PPSDCKGTSV DSDLPEKEII 650
    SLISCSKSDR HKSGGDTDSS GQPLACRWPS MEMITKLSRA YLDSESVIAI 700
    PLPSDAVGET GSRNLYIWIG KSFSLDNNCS LVDSNKAADT VENVDWVQIG 750
    ESILCQMDLP KDTPIKIVRE SEDQTELLAL LSAL 784
    Length:784
    Mass (Da):85,964
    Last modified:June 1, 2001 - v1
    Checksum:iDF14442F304BD1ED
    GO

    Sequence cautioni

    The sequence CAB75761.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti712 – 7121S → N in AAK96700. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF312745 mRNA. Translation: AAK29382.1.
    AL132954 Genomic DNA. Translation: CAB75761.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79361.1.
    AY054509 mRNA. Translation: AAK96700.1.
    PIRiT47666.
    RefSeqiNP_567018.4. NM_115385.7.
    UniGeneiAt.21664.

    Genome annotation databases

    EnsemblPlantsiAT3G55270.1; AT3G55270.1; AT3G55270.
    GeneIDi824693.
    KEGGiath:AT3G55270.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF312745 mRNA. Translation: AAK29382.1 .
    AL132954 Genomic DNA. Translation: CAB75761.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79361.1 .
    AY054509 mRNA. Translation: AAK96700.1 .
    PIRi T47666.
    RefSeqi NP_567018.4. NM_115385.7.
    UniGenei At.21664.

    3D structure databases

    ProteinModelPortali Q9C5S1.
    SMRi Q9C5S1. Positions 157-287, 324-416.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9C5S1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G55270.1 ; AT3G55270.1 ; AT3G55270 .
    GeneIDi 824693.
    KEGGi ath:AT3G55270.

    Organism-specific databases

    TAIRi AT3G55270.

    Phylogenomic databases

    OMAi KVADHIY.
    PhylomeDBi Q9C5S1.

    Enzyme and pathway databases

    BioCyci ARA:AT3G55270-MONOMER.

    Gene expression databases

    ArrayExpressi Q9C5S1.
    Genevestigatori Q9C5S1.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR029006. ADF-H/Gelsolin-like_dom.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis."
      Ulm R., Revenkova E., di Sansebastiano G.P., Bechtold N., Paszkowski J.
      Genes Dev. 15:699-709(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(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. "Distinct regulation of salinity and genotoxic stress responses by Arabidopsis MAP kinase phosphatase 1."
      Ulm R., Ichimura K., Mizoguchi T., Peck S.C., Zhu T., Wang X., Shinozaki K., Paszkowski J.
      EMBO J. 21:6483-6493(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MPK6, MUTAGENESIS OF CYS-235.
    6. "The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent gene expression in Arabidopsis."
      Kalbina I., Strid A.
      Plant Cell Environ. 29:1783-1793(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    8. "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis."
      Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., Hirt H., Buchala A., Metraux J.P., Peck S.C., Ulm R.
      Plant Cell 21:2884-2897(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MPK6, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
      Strain: cv. Columbia.
    9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Arabidopsis MAP kinase phosphatase 1 is phosphorylated and activated by its substrate AtMPK6."
      Park H.C., Song E.H., Nguyen X.C., Lee K., Kim K.E., Kim H.S., Lee S.M., Kim S.H., Bae D.W., Yun D.J., Chung W.S.
      Plant Cell Rep. 30:1523-1531(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MPK6, PHOSPHORYLATION AT THR-64; THR-109; SER-558 AND SER-572.
    11. "Arabidopsis MAP Kinase Phosphatase 1 (AtMKP1) negatively regulates MPK6-mediated PAMP responses and resistance against bacteria."
      Anderson J.C., Bartels S., Gonzalez Besteiro M.A., Shahollari B., Ulm R., Peck S.C.
      Plant J. 67:258-268(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: cv. Wassilewskija.
    12. "Arabidopsis MAP kinase phosphatase 1 and its target MAP kinases 3 and 6 antagonistically determine UV-B stress tolerance, independent of the UVR8 photoreceptor pathway."
      Besteiro M.A., Bartels S., Albert A., Ulm R.
      Plant J. 68:727-737(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMKP1_ARATH
    AccessioniPrimary (citable) accession number: Q9C5S1
    Secondary accession number(s): Q940K2, Q9M3C4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2012
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The observed mkp1 phenotype in Col ecotype is largely due to the Col-specific TIR-NB-LRR receptor-like protein SNC1, which is absent in Ws ecotype.1 Publication

    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