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Q9ZR37 (DUS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 1
Short name=AtDsPTP1
EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:DSPTP1
Ordered Locus Names:At3g23610
ORF Names:MDB19.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a dual specificity toward Ser/Thr and Tyr-containing proteins. Dephosphorylates MPK4 in vitro. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Enzyme regulation

Inhibited by sodium vanadate and sodium tungstate. NaF and spermifine repress specifically phosphoserine and phosphothreonine phosphatase activity. Ref.1

Subunit structure

Interacts with calmodulin (CaM) in a calcium Ca2+-dependent manner. Ref.4

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Tissue specificity

Expressed in roots, stems, leaves and flowers. Ref.1

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence BAB02780.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-tyrosine dephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ZR37-1)

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: Q9ZR37-2)

The sequence of this isoform differs from the canonical sequence as follows:
     191-198: VSDQFFSF → GKQVTIAQCQA
Note: Derived from EST data. No experimental confirmation available.
Isoform 3 (identifier: Q9ZR37-3)

The sequence of this isoform differs from the canonical sequence as follows:
     192-198: SDQFFSF → VVEEKTVPCKYLLHASSFFSIKQGSKLRLHNVRREDH
Note: Constructed according to the conserved gene model. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Dual specificity protein phosphatase 1
PRO_0000415896

Regions

Domain118 – 18265Tyrosine-protein phosphatase
Region26 – 4722CaM binding domain 1
Region151 – 18030CaM binding domain 2
Compositional bias8 – 1710Poly-Ser

Sites

Active site1351Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence191 – 1988VSDQFFSF → GKQVTIAQCQA in isoform 2.
VSP_042412
Alternative sequence192 – 1987SDQFFSF → VVEEKTVPCKYLLHASSFFS IKQGSKLRLHNVRREDH in isoform 3.
VSP_042413

Experimental info

Mutagenesis321I → R: Impaired CaM binding and loss of phosphatase activity. Ref.4
Mutagenesis351L → R: Impaired CaM binding. Ref.4
Mutagenesis1351C → S: Loss of phosphatase activity. Ref.1
Mutagenesis1661K → E: Impaired CaM binding. Ref.4

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: EBF1C98A177E6450

FASTA19822,017
        10         20         30         40         50         60 
MSSRDRGSPS SSSSSSSLPG IEKYNEKVKN QIQALVRVIK VARTYRDDNV PSLIEQGLYL 

        70         80         90        100        110        120 
GSVAAASNKN VLKSYNVTHI LTVASSLRPA HPDDFVYKVV RVVDKEDTNL EMYFDECVDF 

       130        140        150        160        170        180 
IDEAKRQGGS VLVHCFVGKS RSVTIVVAYL MKKHGMTLAQ ALQHVKSKRP VASPNAGFIR 

       190 
QLQDLEKSMQ VSDQFFSF

« Hide

Isoform 2 [UniParc].

Checksum: 2FA50431F9A00273
Show »

FASTA20122,187
Isoform 3 [UniParc].

Checksum: A8D74C6A929B00D5
Show »

FASTA22825,493

References

« Hide 'large scale' references
[1]"Identification of a dual-specificity protein phosphatase that inactivates a MAP kinase from Arabidopsis."
Gupta R., Huang Y., Kieber J., Luan S.
Plant J. 16:581-589(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS DUAL-SPECIFICITY PROTEIN PHOSPHATASE, MUTAGENESIS OF CYS-135, TISSUE SPECIFICITY, ENZYME REGULATION.
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(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]"Regulation of the dual specificity protein phosphatase, DsPTP1, through interactions with calmodulin."
Yoo J.H., Cheong M.S., Park C.Y., Moon B.C., Kim M.C., Kang Y.H., Park H.C., Choi M.S., Lee J.H., Jung W.Y., Yoon H.W., Chung W.S., Lim C.O., Lee S.Y., Cho M.J.
J. Biol. Chem. 279:848-858(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF ILE-32; LEU-35 AND LYS-166.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y18620 mRNA. Translation: CAA77232.1.
AB023036 Genomic DNA. Translation: BAB02780.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE76784.1.
CP002686 Genomic DNA. Translation: AEE76785.1.
CP002686 Genomic DNA. Translation: AEE76786.1.
IPIIPI00525668.
IPI00527221.
IPI00891414.
IPI00991367.
RefSeqNP_001118683.1. NM_001125211.2.
NP_001189955.1. NM_001203026.1.
NP_189003.1. NM_113265.1.
UniGeneAt.25373.

3D structure databases

HSSPHSSP built from PDB template 1MKP based on UniProtKB Q16828.
ProteinModelPortalQ9ZR37.
SMRQ9ZR37. Positions 57-187.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT3G23610.2-P.

Proteomic databases

PRIDEQ9ZR37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G23610.1; AT3G23610.1; AT3G23610.
GeneID821941.
KEGGath:AT3G23610.

Organism-specific databases

TAIRAt3g23610.

Phylogenomic databases

HOGENOMHOG000233767.
InParanoidQ9ZR37.
KOK05766.
OMALEMYFDE.
PhylomeDBQ9ZR37.
ProtClustDBCLSN2684327.

Gene expression databases

ArrayExpressQ9ZR37.
GenevestigatorQ9ZR37.

Family and domain databases

InterProIPR020417. Atypical_DUSP.
IPR000340. 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]
PRINTSPR01908. ADSPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDUS1_ARATH
AccessionPrimary (citable) accession number: Q9ZR37
Secondary accession number(s): B3H4F5, F4J449, Q9LUG6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents