Q9M8K7 (DUS1B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 1B
Short name=AtDsPTP1B
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
MAPK phosphatase 2
Short name=AtMKP2

Gene names

Name:	DSPTP1B
Synonyms:	MKP2
Ordered Locus Names:	At3g06110
ORF Names:	F28L1.5

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	167 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a dual specificity toward Ser/Thr and Tyr-containing proteins. Prevents biotic and abiotic stress responses, including ozone, oxidative stress and pathogen attacks; represses MAPK activities during hypersensitive response to limit the spread of the HR response after infection by necrotrophic pathogen such as Botrytis cinerea. May be also involved in ABA and salt responses. Dephosphorylates MPK3 and MPK6. Ref.6 Ref.7 Ref.8
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Associates with MPK3 and MPK6. Interacts with MPK6 is promoted during HR-like responses triggered by fungal elicitors, whereas interaction with MPK3 in repressed. Ref.7 Ref.8
Subcellular location	Nucleus. Cytoplasm. Note: Upon fungal elicitation, relocalizes surrounding spherical structures that could correspond to epiplasts. Ref.6 Ref.7
Tissue specificity	Expressed in flowers, seedlings, roots, leaves, and seeds. Present in stomata and meristematic cells. Ref.7
Developmental stage	In flowers, expressed in stigmatic papillae, anthers, pollen grains and floral abscission zones. As flowers mature, progressively restricted to the abscission zones and the septum of the siliques. During seed development Mainly detected in seeds endosperm layer until the fourth day after germination. In young seedlings, confined to the cotyledons. Later observed in roots, especially in vascular organs and at branching points of lateral roots. In adult leaves, particularly localized in vascular tissues and hydathodes; mostly present in both young and senescent leaves, tissues undergoing developmental transitions. Ref.7
Induction	Accumulates in response to stress conditions caused by abscisic acid (ABA) or salt treatment. Ref.8
Disruption phenotype	Delayed wilting symptoms in response to Ralstonia solanacearum and, by contrast, acceleration of disease progression during Botrytis cinerea infection, suggesting that this phosphatase plays differential functions in biotrophic versus necrotrophic pathogen-induced responses. Prolonged MPK3 and MPK6 activation during ozone treatment. Ref.7
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Hypersensitive response elicitation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to oxidative stress Inferred from mutant phenotype Ref.7. Source: UniProtKB intracellular protein kinase cascade Inferred by curator Ref.6. Source: TAIR modulation by symbiont of host defense-related programmed cell death Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of plant-type hypersensitive response Inferred from mutant phenotype Ref.7. Source: UniProtKB peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC response to ozone Inferred from mutant phenotype Ref.6. Source: TAIR
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from direct assay Ref.6. Source: TAIR plasma membrane Inferred from direct assay PubMed 17644812. Source: TAIR
Molecular_function	MAP kinase phosphatase activity Inferred from direct assay Ref.6. Source: TAIR protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9M8K7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9M8K7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-86: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 167	167	Dual specificity protein phosphatase 1B		PRO_0000415897
Regions
	Domain	92 – 156	65	Tyrosine-protein phosphatase
Sites
	Active site	109	1	Phosphocysteine intermediate By similarity
Natural variations
	Alternative sequence	77 – 86	10	Missing in isoform 2.		VSP_042414
Experimental info
	Mutagenesis	109	1	C → S: Loss of phosphatase activity. Ref.6 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 57D722910B79A900	FASTA	167	18,431
	10 20 30 40 50 60 MEKVVDLFGV GEANSQKLLE GGKDLSEIQQ GLFIGSVAEA NNKDFLKSSN ITHVLTVAVA 70 80 90 100 110 120 LAPPYPDDFV YKVIEVVDRS ETDLTVYFDE CYSFIDQAIQ SGGGVLVHCF MGMSRSVTIV 130 140 150 160 VAYLMKKHGM GFSKAMELVR SRRHQAYPNP GFISQLQQFE KSIQGNA
	Isoform 2 [UniParc]. Checksum: 7468282915C904E1	FASTA	157	17,315
	10 20 30 40 50 60 MEKVVDLFGV GEANSQKLLE GGKDLSEIQQ GLFIGSVAEA NNKDFLKSSN ITHVLTVAVA 70 80 90 100 110 120 LAPPYPDDFV YKVIEVYFDE CYSFIDQAIQ SGGGVLVHCF MGMSRSVTIV VAYLMKKHGM 130 140 150 GFSKAMELVR SRRHQAYPNP GFISQLQQFE KSIQGNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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] (ISOFORM 1). Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative stress tolerance and inactivates the MPK3 and MPK6 MAPKs." Lee J.S., Ellis B.E. J. Biol. Chem. 282:25020-25029(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PHOSPHATASE, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-109. Strain: cv. Columbia.
[7]	"MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and functionally interacts with MPK3 and MPK6." Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M., Coca M., Pages M. Plant J. 63:1017-1030(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEFENSE RESPONSE, INTERACTION WITH MPK3 AND MPK6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: cv. Columbia.
[8]	"Regulation of MAPK signaling and cell death by MAPK phosphatase MKP2." Vilela B., Pages M., Lumbreras V. Plant Signal. Behav. 5:1497-1500(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MPK6, MUTAGENESIS OF CYS-109, INDUCTION BY STRESS CONDITIONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC018907 Genomic DNA. Translation: AAF30304.1. CP002686 Genomic DNA. Translation: AEE74344.1. CP002686 Genomic DNA. Translation: AEE74345.1. CP002686 Genomic DNA. Translation: AEE74346.1. AK117443 mRNA. Translation: BAC42108.1. BT005135 mRNA. Translation: AAO50668.1. AY085765 mRNA. Translation: AAM62982.1.
IPI	IPI00543963. IPI00547755.
RefSeq	NP_001189821.1. NM_001202892.1. NP_566272.1. NM_111486.3. NP_850522.1. NM_180191.2.
UniGene	At.40567.
3D structure databases
HSSP	HSSP built from PDB template 1M3G based on UniProtKB Q05923.
ProteinModelPortal	Q9M8K7.
SMR	Q9M8K7. Positions 22-161.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT3G06110.2-P.
Proteomic databases
PRIDE	Q9M8K7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G06110.2; AT3G06110.2; AT3G06110. AT3G06110.3; AT3G06110.3; AT3G06110.
GeneID	819784.
KEGG	ath:AT3G06110.
Organism-specific databases
TAIR	At3g06110.
Phylogenomic databases
HOGENOM	HOG000233767.
InParanoid	Q9M8K7.
OMA	SKRPQVA.
PhylomeDB	Q9M8K7.
ProtClustDB	CLSN2684327.
Gene expression databases
ArrayExpress	Q9M8K7.
Genevestigator	Q9M8K7.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DUS1B_ARATH

Accession

Primary (citable) accession number: Q9M8K7
Secondary accession number(s): Q8LDW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2012
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program