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Q9C5S1 (MKP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-tyrosine-phosphatase MKP1

EC=3.1.3.48
Alternative name(s):
Mitogen-activated protein kinase phosphatase 1
Short name=AtMKP1
Gene names
Name:MKP1
Ordered Locus Names:At3g55270
ORF Names:T26I12.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with MPK6. May interact with MPK3 and MPK4. Ref.5 Ref.8 Ref.10

Subcellular location

Cytoplasmcytosol Ref.8.

Post-translational modification

Phosphorylated on threonine and serine residues by MPK6. Ref.10

Disruption phenotype

No visible phenotype under normal growth conditions in Wassilewskija (Ws) ecotype (Ref.1), but Columbia (Col) ecotype show growth defects, elevated levels of salicylic acid (SA) and constitutive defense responses (Ref.8). Ref.1 Ref.8

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 (Ref.8).

Sequence similarities

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784Protein-tyrosine-phosphatase MKP1
PRO_0000417330

Regions

Domain149 – 290142Tyrosine-protein phosphatase
Region235 – 2417Substrate binding By similarity
Compositional bias477 – 56286Ser-rich

Sites

Active site2351Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue641Phosphothreonine Ref.10
Modified residue1091Phosphothreonine Ref.10
Modified residue5581Phosphoserine Ref.10
Modified residue5721Phosphoserine Ref.10

Experimental info

Mutagenesis2351C → S: Loss of activity. Ref.5
Sequence conflict7121S → N in AAK96700. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9C5S1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: DF14442F304BD1ED

FASTA78485,964
        10         20         30         40         50         60 
MVGREDAMGN DEAPPGSKKM FWRSASWSAS RTASQVPEGD EQSLNIPCAI SSGPSRRCPA 

        70         80         90        100        110        120 
APLTPRSHHN SKARACLPPL QPLAISRRSL DEWPKAGSDD VGEWPHPPTP SGNKTGERLK 

       130        140        150        160        170        180 
LDLSSTQQRV TDKSSGLAKR EKIAFFDKEC SKVADHIYVG GDAVAKDKSI LKNNGITHIL 

       190        200        210        220        230        240 
NCVGFICPEY FKSDFCYRSL WLQDSPSEDI TSILYDVFDY FEDVREQSGR IFVHCCQGVS 

       250        260        270        280        290        300 
RSTSLVIAYL MWREGQSFDD AFQYVKSARG IADPNMGFAC QLLQCQKRVH AFPLSPTSLL 

       310        320        330        340        350        360 
RMYKMSPHSP YDPLHLVPKL LNDPCPGSLD SRGAFIIQLP SAIYIWVGRQ CETIMEKDAK 

       370        380        390        400        410        420 
AAVCQIARYE KVEAPIMVVR EGDEPVYYWD AFASILPMIG GSVIKVQPGD RKVDAYNLDF 

       430        440        450        460        470        480 
EIFQKAIEGG FVPTLASSNN EHETHLPARE NSWSSLKCKF ASRFDKGFRY VSKTPLSRVY 

       490        500        510        520        530        540 
SDSMMIVHSS GSPSSTTSSS STASPPFLSP DSVCSTNSGN SLKSFSQSSG RSSLRPSIPP 

       550        560        570        580        590        600 
SLTLPKFSSL SLLPSQTSPK ESRGVNTFLQ PSPNRKASPS LAERRGSLKG SLKLPGLADS 

       610        620        630        640        650        660 
NRGTPAFTLH PDDSNDIVFN LEGIRNGDLY PPSDCKGTSV DSDLPEKEII SLISCSKSDR 

       670        680        690        700        710        720 
HKSGGDTDSS GQPLACRWPS MEMITKLSRA YLDSESVIAI PLPSDAVGET GSRNLYIWIG 

       730        740        750        760        770        780 
KSFSLDNNCS LVDSNKAADT VENVDWVQIG ESILCQMDLP KDTPIKIVRE SEDQTELLAL 


LSAL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312745 mRNA. Translation: AAK29382.1.
AL132954 Genomic DNA. Translation: CAB75761.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79361.1.
AY054509 mRNA. Translation: AAK96700.1.
PIRT47666.
RefSeqNP_567018.4. NM_115385.7.
UniGeneAt.21664.

3D structure databases

ProteinModelPortalQ9C5S1.
SMRQ9C5S1. Positions 157-287, 324-416.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9C5S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55270.1; AT3G55270.1; AT3G55270.
GeneID824693.
KEGGath:AT3G55270.

Organism-specific databases

TAIRAT3G55270.

Phylogenomic databases

OMAKVADHIY.
PhylomeDBQ9C5S1.

Enzyme and pathway databases

BioCycARA:AT3G55270-MONOMER.

Gene expression databases

ArrayExpressQ9C5S1.
GenevestigatorQ9C5S1.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR029006. 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]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMKP1_ARATH
AccessionPrimary (citable) accession number: Q9C5S1
Secondary accession number(s): Q940K2, Q9M3C4
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names