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Q9D7X3 (DUS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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:
Dual specificity protein phosphatase 3

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
T-DSP11
Vaccinia H1-related phosphatase
Short name=VHR
Gene names
Name:Dusp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2 By similarity. Ref.5

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with VRK3, which seems to activate it's phosphatase activity. Ref.5

Subcellular location

Nucleus Ref.5.

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processin utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of JNK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of T cell activation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of T cell receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of mitotic cell cycle

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein dephosphorylation

Inferred from direct assay PubMed 18035061. Source: MGI

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

immunological synapse

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionMAP kinase phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 18035061. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from direct assay PubMed 11432789. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Dual specificity protein phosphatase 3
PRO_0000094796

Regions

Domain99 – 16971Tyrosine-protein phosphatase

Sites

Active site1241Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D7X3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 62E519E41BE575D5

FASTA18520,472
        10         20         30         40         50         60 
MSSSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVVPRVYVG NASVAQDITQ LQKLGITHVL 

        70         80         90        100        110        120 
NAAEGRSFMH VNTSASFYED SGITYLGIKA NDTQEFNLSA YFERATDFID QALAHKNGRV 

       130        140        150        160        170        180 
LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSTVRQNREI GPNDGFLAQL CQLNDRLAKE 


GKVKL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of novel putative dual specificity protein phosphatases T-DSP6 and T-DSP11 with low molecular masses containing a single catalytic domain but not cdc25 homology domain."
Aoyama K., Matsuda T., Aoki N.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 90-104 AND 159-176, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[5]"Negative regulation of ERK activity by VRK3-mediated activation of VHR phosphatase."
Kang T.H., Kim K.T.
Nat. Cell Biol. 8:863-869(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VRK3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF280809 mRNA. Translation: AAK69507.1.
AK008734 mRNA. Translation: BAB25864.1.
BC016269 mRNA. Translation: AAH16269.1.
CCDSCCDS25482.1.
RefSeqNP_082483.1. NM_028207.3.
UniGeneMm.196295.
Mm.491149.

3D structure databases

ProteinModelPortalQ9D7X3.
SMRQ9D7X3. Positions 7-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215327. 3 interactions.
IntActQ9D7X3. 1 interaction.
MINTMINT-4093702.

PTM databases

PhosphoSiteQ9D7X3.

Proteomic databases

MaxQBQ9D7X3.
PaxDbQ9D7X3.
PRIDEQ9D7X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003612; ENSMUSP00000003612; ENSMUSG00000003518.
ENSMUST00000107172; ENSMUSP00000102790; ENSMUSG00000003518.
GeneID72349.
KEGGmmu:72349.
UCSCuc007lqa.2. mouse.

Organism-specific databases

CTD1845.
MGIMGI:1919599. Dusp3.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00550000074474.
HOGENOMHOG000233767.
HOVERGENHBG001524.
InParanoidQ9D7X3.
KOK17614.
TreeFamTF105128.

Gene expression databases

ArrayExpressQ9D7X3.
BgeeQ9D7X3.
GenevestigatorQ9D7X3.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
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]
PRINTSPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
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...

Other

NextBio336089.
PROQ9D7X3.
SOURCESearch...

Entry information

Entry nameDUS3_MOUSE
AccessionPrimary (citable) accession number: Q9D7X3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot