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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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

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

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. extracellular vesicular exosome Source: Ensembl
  3. immunological synapse Source: Ensembl
  4. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9D7X3.
PaxDbiQ9D7X3.
PRIDEiQ9D7X3.

PTM databases

PhosphoSiteiQ9D7X3.

Expressioni

Gene expression databases

BgeeiQ9D7X3.
ExpressionAtlasiQ9D7X3. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
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

        10         20         30         40         50
MSSSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVVPRVYVG NASVAQDITQ
60 70 80 90 100
LQKLGITHVL NAAEGRSFMH VNTSASFYED SGITYLGIKA NDTQEFNLSA
110 120 130 140 150
YFERATDFID QALAHKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA
160 170 180
LSTVRQNREI GPNDGFLAQL CQLNDRLAKE GKVKL
Length:185
Mass (Da):20,472
Last modified:June 1, 2001 - v1
Checksum:i62E519E41BE575D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118853.
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

Bgeei Q9D7X3.
ExpressionAtlasi Q9D7X3. baseline and differential.
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: October 29, 2014
This is version 107 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