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Protein

Dual specificity protein phosphatase 3

Gene

Dusp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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: MGI
  2. phosphoprotein phosphatase activity Source: MGI
  3. protein kinase binding Source: MGI
  4. protein tyrosine/serine/threonine phosphatase activity Source: MGI
  5. protein tyrosine phosphatase activity Source: MGI

GO - Biological processi

  1. inactivation of MAPK activity Source: MGI
  2. in utero embryonic development Source: Ensembl
  3. negative regulation of ERK1 and ERK2 cascade Source: MGI
  4. negative regulation of JNK cascade Source: MGI
  5. negative regulation of MAPK cascade Source: MGI
  6. negative regulation of T cell activation Source: MGI
  7. negative regulation of T cell receptor signaling pathway Source: MGI
  8. peptidyl-tyrosine dephosphorylation Source: MGI
  9. positive regulation of mitotic cell cycle Source: MGI
  10. 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. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. immunological synapse Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
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.
CCDSiCCDS25482.1.
RefSeqiNP_082483.1. NM_028207.3.
UniGeneiMm.196295.
Mm.491149.

3D structure databases

ProteinModelPortaliQ9D7X3.
SMRiQ9D7X3. Positions 7-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9D7X3.

Proteomic databases

MaxQBiQ9D7X3.
PaxDbiQ9D7X3.
PRIDEiQ9D7X3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1845.
MGIiMGI:1919599. Dusp3.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233767.
HOVERGENiHBG001524.
InParanoidiQ9D7X3.
KOiK17614.
TreeFamiTF105128.

Enzyme and pathway databases

ReactomeiREACT_210064. ERKs are inactivated.

Miscellaneous databases

NextBioi336089.
PROiQ9D7X3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7X3.
ExpressionAtlasiQ9D7X3. baseline and differential.
GenevestigatoriQ9D7X3.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 110 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.