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Q60838

- DVL2_MOUSE

UniProt

Q60838 - DVL2_MOUSE

Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

Dvl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes.3 Publications

    GO - Molecular functioni

    1. frizzled binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. protein domain specific binding Source: MGI
    5. protein self-association Source: UniProtKB
    6. signal transducer activity Source: InterPro

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: MGI
    2. canonical Wnt signaling pathway involved in regulation of cell proliferation Source: Ensembl
    3. cell migration in hindbrain Source: RefGenome
    4. cellular protein localization Source: MGI
    5. cochlea morphogenesis Source: MGI
    6. convergent extension involved in neural plate elongation Source: MGI
    7. convergent extension involved in organogenesis Source: MGI
    8. heart development Source: MGI
    9. heart morphogenesis Source: MGI
    10. intracellular signal transduction Source: InterPro
    11. neural tube closure Source: MGI
    12. outflow tract morphogenesis Source: BHF-UCL
    13. planar cell polarity pathway involved in neural tube closure Source: MGI
    14. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    15. positive regulation of JUN kinase activity Source: BHF-UCL
    16. positive regulation of protein tyrosine kinase activity Source: MGI
    17. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    18. positive regulation of transcription, DNA-templated Source: RefGenome
    19. regulation of JNK cascade Source: RefGenome
    20. segmentation Source: BHF-UCL
    21. segment specification Source: MGI
    22. transcription from RNA polymerase II promoter Source: Ensembl
    23. Wnt signaling pathway Source: BHF-UCL
    24. Wnt signaling pathway, planar cell polarity pathway Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_196537. Signaling by Hippo.
    REACT_203973. Asymmetric localization of PCP proteins.
    REACT_214043. PCP/CE pathway.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_222404. WNT5A-dependent internalization of FZD4.
    REACT_225118. WNT mediated activation of DVL.
    REACT_227429. degradation of DVL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Segment polarity protein dishevelled homolog DVL-2
    Short name:
    Dishevelled-2
    Alternative name(s):
    DSH homolog 2
    Gene namesi
    Name:Dvl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:106613. Dvl2.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytosol. Cytoplasmic vesicle
    Note: Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta.

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cell cortex Source: MGI
    3. clathrin-coated vesicle Source: MGI
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic vesicle Source: MGI
    6. cytoskeleton Source: BHF-UCL
    7. cytosol Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151K → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
    Mutagenesisi17 – 171I → A: Reduces oligomerization. Abolishes interaction with DIXDC1. Reduces activation of Wnt signaling. 1 Publication
    Mutagenesisi27 – 271Y → D: Loss of oligomerization. Abolishes interaction with DIXDC1. Abolishes activation of Wnt signaling. 1 Publication
    Mutagenesisi56 – 561F → H: Reduces oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication
    Mutagenesisi61 – 611D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
    Mutagenesisi63 – 631D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
    Mutagenesisi64 – 641F → A: Reduces oligomerization. Reduces activation of Wnt signaling.
    Mutagenesisi65 – 651G → D: Loss of oligomerization. Abolishes activation of Wnt signaling. 1 Publication
    Mutagenesisi66 – 661V → D: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
    Mutagenesisi68 – 681K → A: Loss of oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication
    Mutagenesisi84 – 841R → A: Strongly reduced interaction with DIXDC1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736Segment polarity protein dishevelled homolog DVL-2PRO_0000145747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CSNK1D.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ60838.
    PRIDEiQ60838.

    PTM databases

    PhosphoSiteiQ60838.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ60838.
    BgeeiQ60838.
    CleanExiMM_DVL2.
    GenevestigatoriQ60838.

    Interactioni

    Subunit structurei

    Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 By similarity. Can form large oligomers (via DIX domain). Interacts (via DIX domain) with DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the AP-2 complex. Interacts with FAM105B/otulin.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-641940,EBI-641940
    CSNK1DP487302EBI-641940,EBI-751621From a different organism.
    CSNK1EP496743EBI-641940,EBI-749343From a different organism.
    Dact1Q8R4A33EBI-641940,EBI-3870250
    DIXDC1Q155Q34EBI-641940,EBI-1104700From a different organism.
    Dvl3Q610623EBI-641940,EBI-1538450
    PLK1P5335012EBI-641940,EBI-476768From a different organism.
    Vangl1Q80Z964EBI-641940,EBI-1750708
    Vangl2Q91ZD44EBI-641940,EBI-1750744

    Protein-protein interaction databases

    BioGridi199343. 18 interactions.
    DIPiDIP-29399N.
    IntActiQ60838. 23 interactions.
    MINTiMINT-1591968.

    Structurei

    Secondary structure

    1
    736
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi423 – 4319
    Beta strandi435 – 4373
    Beta strandi440 – 4423
    Beta strandi449 – 4546
    Helixi455 – 46410
    Helixi472 – 48514
    Beta strandi486 – 4938
    Beta strandi499 – 5057

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ML6X-ray3.50A/B/C/D/E/F417-510[»]
    ProteinModelPortaliQ60838.
    SMRiQ60838. Positions 13-90, 263-353, 421-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 9383DIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 33973PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 50775DEPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 126Poly-Gly
    Compositional biasi112 – 12211Poly-ProAdd
    BLAST
    Compositional biasi235 – 2406Poly-Arg
    Compositional biasi686 – 6916Poly-Pro

    Domaini

    The DIX domain mediates homooligomerization.1 Publication

    Sequence similaritiesi

    Belongs to the DSH family.Curated
    Contains 1 DEP domain.PROSITE-ProRule annotation
    Contains 1 DIX domain.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG322275.
    GeneTreeiENSGT00390000013552.
    HOGENOMiHOG000017084.
    HOVERGENiHBG005542.
    InParanoidiQ7TN14.
    KOiK02353.
    OMAiFHLAMGN.
    OrthoDBiEOG7BP82N.
    TreeFamiTF318198.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR000591. DEP_dom.
    IPR008341. Dishevelled_2.
    IPR024580. Dishevelled_C-dom.
    IPR008339. Dishevelled_fam.
    IPR003351. Dishevelled_protein_dom.
    IPR001158. DIX.
    IPR015506. Dsh/Dvl-rel.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10878. PTHR10878. 1 hit.
    PTHR10878:SF8. PTHR10878:SF8. 1 hit.
    PfamiPF00610. DEP. 1 hit.
    PF02377. Dishevelled. 1 hit.
    PF00778. DIX. 1 hit.
    PF12316. Dsh_C. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    PRINTSiPR01760. DISHEVELLED.
    PR01762. DISHEVELLED2.
    SMARTiSM00021. DAX. 1 hit.
    SM00049. DEP. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50186. DEP. 1 hit.
    PS50841. DIX. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60838-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGSSAGGGG VGETKVIYHL DEEETPYLVK IPVPAERITL GDFKSVLQRP    50
    AGAKYFFKSM DQDFGVVKEE ISDDNARLPC FNGRVVSWLV SSDTPQPEVA 100
    PPAHESRTEL VPPPPPLPPL PPERTSGIGD SRPPSFHPNV SSSHENLEPE 150
    TETESVVSLR RDRPRRRDSS EHGAGGHRPG GPSRLERHLA GYESSSTLMT 200
    SELESTSLGD SDEDDTMSRF SSSTEQSSAS RLLKRHRRRR KQRPPRMERT 250
    SSFSSVTDST MSLNIITVTL NMEKYNFLGI SIVGQSNERG DGGIYIGSIM 300
    KGGAVAADGR IEPGDMLLQV NDMNFENMSN DDAVRVLRDI VHKPGPIVLT 350
    VAKCWDPSPQ AYFTLPRNEP IQPIDPAAWV SHSAALTGAF PAYPGSSSMS 400
    TITSGSSLPD GCEGRGLSVH MDMASVTKAM AAPESGLEVR DRMWLKITIP 450
    NAFLGSDVVD WLYHHVEGFP ERREARKYAS GLLKAGLIRH TVNKITFSEQ 500
    CYYVFGDLSG GCESYLVNLS LNDNDGSSGA SDQDTLAPLP GATPWPLLPT 550
    FSYQYPAPHP YSPQPPPYHE LSSYTYGGGS ASSQHSEGSR SSGSTRSDGG 600
    AGRTGRPEER APESKSGSGS ESELSSRGGS LRRGGEPGGT GDGGPPPSRG 650
    STGAPPNLRA LPGLHPYGAP SGMALPYNPM MVVMMPPPPP PVSTAVQPPG 700
    APPVRDLGSV PPELTASRQS FHMAMGNPSE FFVDVM 736
    Length:736
    Mass (Da):78,861
    Last modified:July 27, 2011 - v2
    Checksum:i928A527143BBBBB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti356 – 3561D → G in AAC52827. (PubMed:8887313)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24160 mRNA. Translation: AAC52827.1.
    AK146822 mRNA. Translation: BAE27460.1.
    AK159895 mRNA. Translation: BAE35461.1.
    AK168376 mRNA. Translation: BAE40307.1.
    AL596185 Genomic DNA. Translation: CAI35165.1.
    CH466596 Genomic DNA. Translation: EDL12520.1.
    BC053050 mRNA. Translation: AAH53050.1.
    CCDSiCCDS24930.1.
    RefSeqiNP_031914.3. NM_007888.3.
    UniGeneiMm.5114.

    Genome annotation databases

    EnsembliENSMUST00000019362; ENSMUSP00000019362; ENSMUSG00000020888.
    ENSMUST00000102575; ENSMUSP00000099635; ENSMUSG00000020888.
    GeneIDi13543.
    KEGGimmu:13543.
    UCSCiuc007jtm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24160 mRNA. Translation: AAC52827.1 .
    AK146822 mRNA. Translation: BAE27460.1 .
    AK159895 mRNA. Translation: BAE35461.1 .
    AK168376 mRNA. Translation: BAE40307.1 .
    AL596185 Genomic DNA. Translation: CAI35165.1 .
    CH466596 Genomic DNA. Translation: EDL12520.1 .
    BC053050 mRNA. Translation: AAH53050.1 .
    CCDSi CCDS24930.1.
    RefSeqi NP_031914.3. NM_007888.3.
    UniGenei Mm.5114.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ML6 X-ray 3.50 A/B/C/D/E/F 417-510 [» ]
    ProteinModelPortali Q60838.
    SMRi Q60838. Positions 13-90, 263-353, 421-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199343. 18 interactions.
    DIPi DIP-29399N.
    IntActi Q60838. 23 interactions.
    MINTi MINT-1591968.

    PTM databases

    PhosphoSitei Q60838.

    Proteomic databases

    PaxDbi Q60838.
    PRIDEi Q60838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019362 ; ENSMUSP00000019362 ; ENSMUSG00000020888 .
    ENSMUST00000102575 ; ENSMUSP00000099635 ; ENSMUSG00000020888 .
    GeneIDi 13543.
    KEGGi mmu:13543.
    UCSCi uc007jtm.1. mouse.

    Organism-specific databases

    CTDi 1856.
    MGIi MGI:106613. Dvl2.

    Phylogenomic databases

    eggNOGi NOG322275.
    GeneTreei ENSGT00390000013552.
    HOGENOMi HOG000017084.
    HOVERGENi HBG005542.
    InParanoidi Q7TN14.
    KOi K02353.
    OMAi FHLAMGN.
    OrthoDBi EOG7BP82N.
    TreeFami TF318198.

    Enzyme and pathway databases

    Reactomei REACT_196537. Signaling by Hippo.
    REACT_203973. Asymmetric localization of PCP proteins.
    REACT_214043. PCP/CE pathway.
    REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_222404. WNT5A-dependent internalization of FZD4.
    REACT_225118. WNT mediated activation of DVL.
    REACT_227429. degradation of DVL.

    Miscellaneous databases

    ChiTaRSi DVL2. mouse.
    NextBioi 284146.
    PROi Q60838.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60838.
    Bgeei Q60838.
    CleanExi MM_DVL2.
    Genevestigatori Q60838.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR000591. DEP_dom.
    IPR008341. Dishevelled_2.
    IPR024580. Dishevelled_C-dom.
    IPR008339. Dishevelled_fam.
    IPR003351. Dishevelled_protein_dom.
    IPR001158. DIX.
    IPR015506. Dsh/Dvl-rel.
    IPR001478. PDZ.
    IPR029071. Ubiquitin-rel_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10878. PTHR10878. 1 hit.
    PTHR10878:SF8. PTHR10878:SF8. 1 hit.
    Pfami PF00610. DEP. 1 hit.
    PF02377. Dishevelled. 1 hit.
    PF00778. DIX. 1 hit.
    PF12316. Dsh_C. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PRINTSi PR01760. DISHEVELLED.
    PR01762. DISHEVELLED2.
    SMARTi SM00021. DAX. 1 hit.
    SM00049. DEP. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50186. DEP. 1 hit.
    PS50841. DIX. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation of dishevelled structure and function between flies and mice: isolation and characterization of Dvl2."
      Klingensmith J., Yang Y., Axelrod J.D., Beier D.R., Perrimon N., Sussman D.J.
      Mech. Dev. 58:15-26(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    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: Amnion and Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Strain: C57BL/6.
    6. "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
      Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
      J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DIXDC1 AND RAC.
    7. "Independent mutations in mouse Vangl2 that cause neural tube defects in looptail mice impair interaction with members of the Dishevelled family."
      Torban E., Wang H.-J., Groulx N., Gros P.
      J. Biol. Chem. 279:52703-52713(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VANGL1 AND VANGL2.
    8. "Association of Dishevelled with the clathrin AP-2 adaptor is required for Frizzled endocytosis and planar cell polarity signaling."
      Yu A., Rual J.F., Tamai K., Harada Y., Vidal M., He X., Kirchhausen T.
      Dev. Cell 12:129-141(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE AP-2 COMPLEX.
    9. "Molecular basis of Wnt activation via the DIX-domain protein Ccd1."
      Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C., Wang Z.X., Wu J.W.
      J. Biol. Chem. 286:8597-8608(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DIXDC1, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-15; ILE-17; TYR-27; PHE-56; ASP-61; ASP-63; GLY-65; VAL-66 AND LYS-68, DOMAIN.
    10. Cited for: INTERACTION WITH FAM105B.
    11. "Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling."
      Yu A., Xing Y., Harrison S.C., Kirchhausen T.
      Structure 18:1311-1320(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 417-510 IN COMPLEX WITH AP2M1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiDVL2_MOUSE
    AccessioniPrimary (citable) accession number: Q60838
    Secondary accession number(s): Q7TN14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3