Q9C5S1 (MKP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7 Ref.8 Ref.9 Ref.10
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with MPK6. May interact with MPK3 and MPK4. Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm › cytosol Ref.7.
Post-translational modification	Phosphorylated on threonine and serine residues by MPK6. Ref.8
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.7). Ref.1 Ref.7
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.7).
Sequence similarities	Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence CAB75761.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Plant defense Stress response
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC response to UV-B Inferred from mutant phenotype Ref.10. Source: TAIR response to UV-C Inferred from mutant phenotype Ref.1. Source: TAIR response to salt stress Inferred from mutant phenotype Ref.5. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from direct assay Ref.10. Source: TAIR protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 784	784	Protein-tyrosine-phosphatase MKP1		PRO_0000417330
Regions
	Domain	149 – 290	142	Tyrosine-protein phosphatase
	Region	235 – 241	7	Substrate binding By similarity
	Compositional bias	477 – 562	86	Ser-rich
Sites
	Active site	235	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	64	1	Phosphothreonine Ref.8
	Modified residue	109	1	Phosphothreonine Ref.8
	Modified residue	558	1	Phosphoserine Ref.8
	Modified residue	572	1	Phosphoserine Ref.8
Experimental info
	Mutagenesis	235	1	C → S: Loss of activity. Ref.5
	Sequence conflict	712	1	S → N in AAK96700. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9C5S1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: DF14442F304BD1ED	FASTA	784	85,964
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
IPI	IPI00535064.
PIR	T47666.
RefSeq	NP_567018.4. NM_115385.7.
UniGene	At.21664.
3D structure databases
HSSP	HSSP built from PDB template 1VHR based on UniProtKB P51452.
ProteinModelPortal	Q9C5S1.
SMR	Q9C5S1. Positions 157-287, 324-416.
ModBase	Search...
Proteomic databases
PRIDE	Q9C5S1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G55270.1; AT3G55270.1; AT3G55270.
GeneID	824693.
KEGG	ath:AT3G55270.
Organism-specific databases
TAIR	At3g55270.
Phylogenomic databases
OMA	MFWRSAS.
PhylomeDB	Q9C5S1.
ProtClustDB	CLSN2717377.
Gene expression databases
ArrayExpress	Q9C5S1.
Genevestigator	Q9C5S1.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MKP1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program