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Q9C5S1

- MKP1_ARATH

UniProt

Q9C5S1 - MKP1_ARATH

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Protein
Protein-tyrosine-phosphatase MKP1
Gene
MKP1, At3g55270, T26I12.150
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei235 – 2351Phosphocysteine intermediate By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions in Wassilewskija (Ws) ecotype (1 Publication), but Columbia (Col) ecotype show growth defects, elevated levels of salicylic acid (SA) and constitutive defense responses (1 Publication).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 MKP1
PRO_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.

Family & Domainsi

Domains and Repeats

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

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi477 – 56286Ser-rich
Add
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti712 – 7121S → N in AAK96700. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 73 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

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