Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9DBB1

- DUS6_MOUSE

UniProt

Q9DBB1 - DUS6_MOUSE

Protein

Dual specificity protein phosphatase 6

Gene

Dusp6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Inactivates MAP kinases. Has a specificity for the ERK family By similarity.By similarity

    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 sitei293 – 2931Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell differentiation Source: Ensembl
    2. dorsal/ventral pattern formation Source: RefGenome
    3. negative regulation of ERK1 and ERK2 cascade Source: RefGenome
    4. negative regulation of protein phosphorylation Source: MGI
    5. positive regulation of apoptotic process Source: RefGenome
    6. protein dephosphorylation Source: MGI
    7. regulation of endodermal cell fate specification Source: RefGenome
    8. regulation of fibroblast growth factor receptor signaling pathway Source: RefGenome
    9. regulation of heart growth Source: MGI
    10. response to drug Source: Ensembl
    11. response to growth factor Source: Ensembl
    12. response to nitrosative stress Source: Ensembl
    13. response to organic cyclic compound Source: Ensembl

    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 6 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Mitogen-activated protein kinase phosphatase 3
    Short name:
    MAP kinase phosphatase 3
    Short name:
    MKP-3
    Gene namesi
    Name:Dusp6
    Synonyms:Mkp3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1914853. Dusp6.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381Dual specificity protein phosphatase 6PRO_0000094805Add
    BLAST

    Proteomic databases

    PaxDbiQ9DBB1.
    PRIDEiQ9DBB1.

    PTM databases

    PhosphoSiteiQ9DBB1.

    Expressioni

    Gene expression databases

    BgeeiQ9DBB1.
    CleanExiMM_DUSP6.
    GenevestigatoriQ9DBB1.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mapk1P630852EBI-7812384,EBI-397697

    Protein-protein interaction databases

    BioGridi212304. 1 interaction.
    IntActiQ9DBB1. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBB1.
    SMRiQ9DBB1. Positions 1-154, 205-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 148119RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini206 – 381176Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00750000117282.
    HOVERGENiHBG007347.
    InParanoidiQ9DBB1.
    KOiK04459.
    OMAiSEWNENT.
    OrthoDBiEOG793B7W.
    PhylomeDBiQ9DBB1.
    TreeFamiTF105122.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSiPR01764. MAPKPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBB1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIDTLRPVPF ASEMAICKTV SWLNEQLELG NERLLLMDCR PQELYESSHI    50
    ESAINVAIPG IMLRRLQKGN LPVRALFTRC EDRDRFTRRC GTDTVVLYDE 100
    NSSDWNENTG GESVLGLLLK KLKDEGCRAF YLEGGFSKFQ AEFALHCETN 150
    LDGSCSSSSP PLPVLGLGGL RISSDSSSDI ESDLDRDPNS ATDSDGSPLS 200
    NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT PNLPNLFENA 250
    GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS 300
    VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS 350
    SPCDNRVPTP QLYFTTPSNQ NVYQVDSLQS T 381
    Length:381
    Mass (Da):42,408
    Last modified:June 1, 2001 - v1
    Checksum:i7EA1FB154F4AD2DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221W → G in BAB26093. (PubMed:16141072)Curated
    Sequence conflicti34 – 341L → F in BAB26093. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005062 mRNA. Translation: BAB23786.1.
    AK009131 mRNA. Translation: BAB26093.1.
    AK088468 mRNA. Translation: BAC40372.1.
    AK088665 mRNA. Translation: BAC40489.1.
    AK159146 mRNA. Translation: BAE34853.1.
    AK159502 mRNA. Translation: BAE35135.1.
    AK159900 mRNA. Translation: BAE35465.1.
    BC003869 mRNA. Translation: AAH03869.1.
    CCDSiCCDS24147.1.
    RefSeqiNP_080544.1. NM_026268.3.
    UniGeneiMm.1791.

    Genome annotation databases

    EnsembliENSMUST00000020118; ENSMUSP00000020118; ENSMUSG00000019960.
    GeneIDi67603.
    KEGGimmu:67603.
    UCSCiuc007gxk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005062 mRNA. Translation: BAB23786.1 .
    AK009131 mRNA. Translation: BAB26093.1 .
    AK088468 mRNA. Translation: BAC40372.1 .
    AK088665 mRNA. Translation: BAC40489.1 .
    AK159146 mRNA. Translation: BAE34853.1 .
    AK159502 mRNA. Translation: BAE35135.1 .
    AK159900 mRNA. Translation: BAE35465.1 .
    BC003869 mRNA. Translation: AAH03869.1 .
    CCDSi CCDS24147.1.
    RefSeqi NP_080544.1. NM_026268.3.
    UniGenei Mm.1791.

    3D structure databases

    ProteinModelPortali Q9DBB1.
    SMRi Q9DBB1. Positions 1-154, 205-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212304. 1 interaction.
    IntActi Q9DBB1. 1 interaction.

    PTM databases

    PhosphoSitei Q9DBB1.

    Proteomic databases

    PaxDbi Q9DBB1.
    PRIDEi Q9DBB1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020118 ; ENSMUSP00000020118 ; ENSMUSG00000019960 .
    GeneIDi 67603.
    KEGGi mmu:67603.
    UCSCi uc007gxk.2. mouse.

    Organism-specific databases

    CTDi 1848.
    MGIi MGI:1914853. Dusp6.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00750000117282.
    HOVERGENi HBG007347.
    InParanoidi Q9DBB1.
    KOi K04459.
    OMAi SEWNENT.
    OrthoDBi EOG793B7W.
    PhylomeDBi Q9DBB1.
    TreeFami TF105122.

    Enzyme and pathway databases

    Reactomei REACT_210064. ERKs are inactivated.

    Miscellaneous databases

    ChiTaRSi DUSP6. mouse.
    NextBioi 325017.
    PROi Q9DBB1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DBB1.
    CleanExi MM_DUSP6.
    Genevestigatori Q9DBB1.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR008343. MKP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR001763. Rhodanese-like_dom.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
    PRINTSi PR01764. MAPKPHPHTASE.
    SMARTi SM00195. DSPc. 1 hit.
    SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 and NOD.
      Tissue: Liver, Thymus and Tongue.
    2. "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].

    Entry informationi

    Entry nameiDUS6_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBB1
    Secondary accession number(s): Q542I5, Q9D7L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 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, 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