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Q9D7X3

- DUS3_MOUSE

UniProt

Q9D7X3 - DUS3_MOUSE

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Protein
Dual specificity protein phosphatase 3
Gene
Dusp3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. MAP kinase phosphatase activity Source: RefGenome
  2. phosphoprotein phosphatase activity Source: MGI
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC
  4. protein tyrosine/serine/threonine phosphatase activity Source: MGI

GO - Biological processi

  1. in utero embryonic development Source: Ensembl
  2. negative regulation of ERK1 and ERK2 cascade Source: RefGenome
  3. negative regulation of JNK cascade Source: RefGenome
  4. negative regulation of T cell activation Source: RefGenome
  5. negative regulation of T cell receptor signaling pathway Source: RefGenome
  6. positive regulation of mitotic cell cycle Source: RefGenome
  7. protein dephosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_210064. ERKs are inactivated.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Dusp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1919599. Dusp3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: RefGenome
  2. immunological synapse Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Dual specificity protein phosphatase 3
PRO_0000094796Add
BLAST

Proteomic databases

MaxQBiQ9D7X3.
PaxDbiQ9D7X3.
PRIDEiQ9D7X3.

PTM databases

PhosphoSiteiQ9D7X3.

Expressioni

Gene expression databases

ArrayExpressiQ9D7X3.
BgeeiQ9D7X3.
GenevestigatoriQ9D7X3.

Interactioni

Subunit structurei

Interacts with VRK3, which seems to activate it's phosphatase activity.1 Publication

Protein-protein interaction databases

BioGridi215327. 3 interactions.
IntActiQ9D7X3. 1 interaction.
MINTiMINT-4093702.

Structurei

3D structure databases

ProteinModelPortaliQ9D7X3.
SMRiQ9D7X3. Positions 7-184.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 16971Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00550000074474.
HOGENOMiHOG000233767.
HOVERGENiHBG001524.
InParanoidiQ9D7X3.
KOiK17614.
TreeFamiTF105128.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D7X3-1 [UniParc]FASTAAdd to Basket

« Hide

MSSSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVVPRVYVG NASVAQDITQ    50
LQKLGITHVL NAAEGRSFMH VNTSASFYED SGITYLGIKA NDTQEFNLSA 100
YFERATDFID QALAHKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA 150
LSTVRQNREI GPNDGFLAQL CQLNDRLAKE GKVKL 185
Length:185
Mass (Da):20,472
Last modified:June 1, 2001 - v1
Checksum:i62E519E41BE575D5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF280809 mRNA. Translation: AAK69507.1.
AK008734 mRNA. Translation: BAB25864.1.
BC016269 mRNA. Translation: AAH16269.1.
CCDSiCCDS25482.1.
RefSeqiNP_082483.1. NM_028207.3.
UniGeneiMm.196295.
Mm.491149.

Genome annotation databases

EnsembliENSMUST00000003612; ENSMUSP00000003612; ENSMUSG00000003518.
ENSMUST00000107172; ENSMUSP00000102790; ENSMUSG00000003518.
GeneIDi72349.
KEGGimmu:72349.
UCSCiuc007lqa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF280809 mRNA. Translation: AAK69507.1 .
AK008734 mRNA. Translation: BAB25864.1 .
BC016269 mRNA. Translation: AAH16269.1 .
CCDSi CCDS25482.1.
RefSeqi NP_082483.1. NM_028207.3.
UniGenei Mm.196295.
Mm.491149.

3D structure databases

ProteinModelPortali Q9D7X3.
SMRi Q9D7X3. Positions 7-184.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 215327. 3 interactions.
IntActi Q9D7X3. 1 interaction.
MINTi MINT-4093702.

PTM databases

PhosphoSitei Q9D7X3.

Proteomic databases

MaxQBi Q9D7X3.
PaxDbi Q9D7X3.
PRIDEi Q9D7X3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003612 ; ENSMUSP00000003612 ; ENSMUSG00000003518 .
ENSMUST00000107172 ; ENSMUSP00000102790 ; ENSMUSG00000003518 .
GeneIDi 72349.
KEGGi mmu:72349.
UCSCi uc007lqa.2. mouse.

Organism-specific databases

CTDi 1845.
MGIi MGI:1919599. Dusp3.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00550000074474.
HOGENOMi HOG000233767.
HOVERGENi HBG001524.
InParanoidi Q9D7X3.
KOi K17614.
TreeFami TF105128.

Enzyme and pathway databases

Reactomei REACT_210064. ERKs are inactivated.

Miscellaneous databases

NextBioi 336089.
PROi Q9D7X3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D7X3.
Bgeei Q9D7X3.
Genevestigatori Q9D7X3.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDUS3_MOUSE
AccessioniPrimary (citable) accession number: Q9D7X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi