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Q9M8K7 (DUS1B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Dual specificity protein phosphatase 1B
PRO_0000415897

Regions

Domain92 – 15665Tyrosine-protein phosphatase

Sites

Active site1091Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence77 – 8610Missing in isoform 2.
VSP_042414

Experimental info

Mutagenesis1091C → S: Loss of phosphatase activity. Ref.6 Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 57D722910B79A900

FASTA16718,431
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7468282915C904E1
Show »

FASTA15717,315

References

« Hide '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. 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.
[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. 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] (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.
RefSeqNP_001189821.1. NM_001202892.1.
NP_566272.1. NM_111486.3.
NP_850522.1. NM_180191.2.
UniGeneAt.40567.

3D structure databases

ProteinModelPortalQ9M8K7.
SMRQ9M8K7. Positions 22-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G06110.2-P.

Proteomic databases

PRIDEQ9M8K7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G06110.2; AT3G06110.2; AT3G06110.
AT3G06110.3; AT3G06110.3; AT3G06110.
GeneID819784.
KEGGath:AT3G06110.

Organism-specific databases

TAIRAT3G06110.

Phylogenomic databases

HOGENOMHOG000233767.
InParanoidQ9M8K7.
OMARSKRPQV.
PhylomeDBQ9M8K7.
ProtClustDBCLSN2684327.

Enzyme and pathway databases

BioCycARA:AT3G06110-MONOMER.
ARA:GQT-438-MONOMER.

Gene expression databases

GenevestigatorQ9M8K7.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9M8K7.

Entry information

Entry nameDUS1B_ARATH
AccessionPrimary (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: February 19, 2014
This is version 77 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