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Q92997

- DVL3_HUMAN

UniProt

Q92997 - DVL3_HUMAN

Protein

Segment polarity protein dishevelled homolog DVL-3

Gene

DVL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    May play a role in the signal transduction pathway mediated by multiple Wnt genes.

    GO - Molecular functioni

    1. beta-catenin binding Source: BHF-UCL
    2. frizzled binding Source: UniProtKB
    3. protease binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein heterodimerization activity Source: BHF-UCL
    6. receptor binding Source: BHF-UCL
    7. signal transducer activity Source: InterPro

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: BHF-UCL
    2. cochlea morphogenesis Source: RefGenome
    3. convergent extension Source: RefGenome
    4. intracellular signal transduction Source: InterPro
    5. non-canonical Wnt signaling pathway Source: BHF-UCL
    6. non-canonical Wnt signaling pathway via JNK cascade Source: BHF-UCL
    7. outflow tract septum morphogenesis Source: RefGenome
    8. planar cell polarity pathway involved in neural tube closure Source: RefGenome
    9. positive regulation of JUN kinase activity Source: BHF-UCL
    10. positive regulation of protein phosphorylation Source: BHF-UCL
    11. positive regulation of transcription, DNA-templated Source: BHF-UCL
    12. response to drug Source: Ensembl
    13. Wnt signaling pathway Source: BHF-UCL
    14. Wnt signaling pathway, planar cell polarity pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_172581. PCP/CE pathway.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200668. WNT mediated activation of DVL.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200841. degradation of DVL.
    SignaLinkiQ92997.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Segment polarity protein dishevelled homolog DVL-3
    Short name:
    Dishevelled-3
    Alternative name(s):
    DSH homolog 3
    Gene namesi
    Name:DVL3
    Synonyms:KIAA0208
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3087. DVL3.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cell cortex Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi271 – 2711R → K: Localizes to plasma membranes. 1 Publication
    Mutagenesisi342 – 3421R → K: No effect on subcellular location. 1 Publication
    Mutagenesisi614 – 6141R → K: Localizes to plasma membranes. 1 Publication

    Organism-specific databases

    PharmGKBiPA27543.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 716716Segment polarity protein dishevelled homolog DVL-3PRO_0000145749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Omega-N-methylarginine1 Publication
    Modified residuei48 – 481Phosphoserine2 Publications
    Modified residuei192 – 1921Phosphoserine3 Publications
    Modified residuei212 – 2121Omega-N-methylarginine1 Publication
    Modified residuei271 – 2711Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
    Modified residuei271 – 2711Symmetric dimethylarginine; by PRMT7; alternate1 Publication
    Modified residuei342 – 3421Omega-N-methylarginine; alternate2 Publications
    Modified residuei342 – 3421Symmetric dimethylarginine; by PRMT7; alternate2 Publications
    Modified residuei346 – 3461Phosphothreonine2 Publications
    Modified residuei614 – 6141Symmetric dimethylarginine; by PRMT71 Publication
    Modified residuei698 – 6981Dimethylated arginine; alternate1 Publication
    Modified residuei698 – 6981Omega-N-methylarginine; alternate1 Publication
    Modified residuei700 – 7001Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.1 Publication
    Phosphorylated by CSNK1D.4 Publications
    Arginine methylation may function as a switch in regulation of function in Wnt signaling.2 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92997.
    PaxDbiQ92997.
    PRIDEiQ92997.

    PTM databases

    PhosphoSiteiQ92997.

    Expressioni

    Gene expression databases

    ArrayExpressiQ92997.
    BgeeiQ92997.
    CleanExiHS_DVL3.
    GenevestigatoriQ92997.

    Organism-specific databases

    HPAiCAB046486.
    HPA049163.

    Interactioni

    Subunit structurei

    Interacts (via the PDZ domain) with the C-terminal regions of VANGL1 and VANGL2 By similarity. Interacts (via the region containing both the PDZ and DEP domains) with LRRFIP2; the DIX domain may inhibit this interaction. Interacts with CYLD, CEP164 and DAB2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CEP164Q9UPV05EBI-739789,EBI-3937015
    Dab2P980782EBI-739789,EBI-1391846From a different organism.
    DVL1O146405EBI-739789,EBI-723489
    LRRFIP2Q9Y6082EBI-739789,EBI-1023718
    LRRK2Q5S0074EBI-739789,EBI-5323863
    PRICKLE1Q96MT33EBI-739789,EBI-2348662
    PRPF3O433952EBI-739789,EBI-744322

    Protein-protein interaction databases

    BioGridi108190. 43 interactions.
    DIPiDIP-34509N.
    IntActiQ92997. 45 interactions.
    MINTiMINT-1186858.
    STRINGi9606.ENSP00000316054.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92997.
    SMRiQ92997. Positions 3-79, 247-335, 411-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8282DIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini249 – 32173PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini422 – 49675DEPPROSITE-ProRule annotationAdd
    BLAST

    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.
    HOGENOMiHOG000017084.
    HOVERGENiHBG005542.
    InParanoidiQ92997.
    KOiK02353.
    OMAiGPEHTTR.
    OrthoDBiEOG7BP82N.
    PhylomeDBiQ92997.
    TreeFamiTF318198.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR000591. DEP_dom.
    IPR008342. Dishevelled_3.
    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:SF6. PTHR10878:SF6. 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.
    PR01763. DISHEVELLED3.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92997-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD    50
    DDFGVVKEEI SDDNAKLPCF NGRVVSWLVS AEGSHPDPAP FCADNPSELP 100
    PPMERTGGIG DSRPPSFHPH AGGGSQENLD NDTETDSLVS AQRERPRRRD 150
    GPEHATRLNG TAKGERRREP GGYDSSSTLM SSELETTSFF DSDEDDSTSR 200
    FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD STMSLNIITV 250
    TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL 300
    QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS 350
    EPIRPIDPAA WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER 400
    LDDFHLSIHS DMAAIVKAMA SPESGLEVRD RMWLKITIPN AFIGSDVVDW 450
    LYHNVEGFTD RREARKYASN LLKAGFIRHT VNKITFSEQC YYIFGDLCGN 500
    MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY PPPPHPYNPH 550
    PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG 600
    SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL ASSLRSHHTH 650
    PSYGPPGVPP LYGPPMLMMP PPPAAMGPPG APPGRDLASV PPELTASRQS 700
    FRMAMGNPSE FFVDVM 716
    Length:716
    Mass (Da):78,055
    Last modified:May 30, 2000 - v2
    Checksum:iB1A55EBF9507D06E
    GO
    Isoform 2 (identifier: Q92997-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         350-367: SEPIRPIDPAAWVSHTAA → T

    Note: No experimental confirmation available.

    Show »
    Length:699
    Mass (Da):76,256
    Checksum:iAD4CB18FDB88AA63
    GO

    Sequence cautioni

    The sequence BAA13199.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → D in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti76 – 761S → Y in AAB84228. (PubMed:9344861)Curated
    Sequence conflicti102 – 1021P → S in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti151 – 1511G → W in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti182 – 1821S → R in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti218 – 2181K → N in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti222 – 2221R → W in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti230 – 2301E → D in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti233 – 2331S → C in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti236 – 2361S → T in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti239 – 2391T → S in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti242 – 2421T → A in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti303 – 3031N → K in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti431 – 4311R → C in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti450 – 4501W → C in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti465 – 4651R → P in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti472 – 4721L → V in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti543 – 5431P → R in AAB65244. (PubMed:9192851)Curated
    Sequence conflicti553 – 5542FP → LG in AAB65244. (PubMed:9192851)Curated
    Sequence conflicti629 – 6291A → T in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti633 – 6331S → I in AAB47447. (PubMed:8817329)Curated
    Sequence conflicti682 – 71635PPGRD…FVDVM → LRAATWPQCPRN in BAA13199. (PubMed:9039502)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti216 – 2161R → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036116
    Natural varianti433 – 4331W → L.1 Publication
    Corresponds to variant rs17853048 [ dbSNP | Ensembl ].
    VAR_025519

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei350 – 36718SEPIR…SHTAA → T in isoform 2. 1 PublicationVSP_053371Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49262 mRNA. Translation: AAB47447.1.
    U75651 mRNA. Translation: AAB84228.1.
    AF006013 mRNA. Translation: AAB65244.1.
    D86963 mRNA. Translation: BAA13199.2. Different initiation.
    AK304686 mRNA. Translation: BAG65457.1.
    AC131235 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78295.1.
    CH471052 Genomic DNA. Translation: EAW78296.1.
    BC032459 mRNA. Translation: AAH32459.1.
    CCDSiCCDS3253.1. [Q92997-1]
    PIRiJC5763.
    RefSeqiNP_004414.3. NM_004423.3. [Q92997-1]
    UniGeneiHs.388116.

    Genome annotation databases

    EnsembliENST00000313143; ENSP00000316054; ENSG00000161202. [Q92997-1]
    ENST00000431765; ENSP00000405885; ENSG00000161202. [Q92997-2]
    GeneIDi1857.
    KEGGihsa:1857.
    UCSCiuc003fms.3. human. [Q92997-1]

    Polymorphism databases

    DMDMi6919875.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49262 mRNA. Translation: AAB47447.1 .
    U75651 mRNA. Translation: AAB84228.1 .
    AF006013 mRNA. Translation: AAB65244.1 .
    D86963 mRNA. Translation: BAA13199.2 . Different initiation.
    AK304686 mRNA. Translation: BAG65457.1 .
    AC131235 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78295.1 .
    CH471052 Genomic DNA. Translation: EAW78296.1 .
    BC032459 mRNA. Translation: AAH32459.1 .
    CCDSi CCDS3253.1. [Q92997-1 ]
    PIRi JC5763.
    RefSeqi NP_004414.3. NM_004423.3. [Q92997-1 ]
    UniGenei Hs.388116.

    3D structure databases

    ProteinModelPortali Q92997.
    SMRi Q92997. Positions 3-79, 247-335, 411-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108190. 43 interactions.
    DIPi DIP-34509N.
    IntActi Q92997. 45 interactions.
    MINTi MINT-1186858.
    STRINGi 9606.ENSP00000316054.

    Chemistry

    ChEMBLi CHEMBL6028.

    PTM databases

    PhosphoSitei Q92997.

    Polymorphism databases

    DMDMi 6919875.

    Proteomic databases

    MaxQBi Q92997.
    PaxDbi Q92997.
    PRIDEi Q92997.

    Protocols and materials databases

    DNASUi 1857.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313143 ; ENSP00000316054 ; ENSG00000161202 . [Q92997-1 ]
    ENST00000431765 ; ENSP00000405885 ; ENSG00000161202 . [Q92997-2 ]
    GeneIDi 1857.
    KEGGi hsa:1857.
    UCSCi uc003fms.3. human. [Q92997-1 ]

    Organism-specific databases

    CTDi 1857.
    GeneCardsi GC03P183873.
    HGNCi HGNC:3087. DVL3.
    HPAi CAB046486.
    HPA049163.
    MIMi 601368. gene.
    neXtProti NX_Q92997.
    PharmGKBi PA27543.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322275.
    HOGENOMi HOG000017084.
    HOVERGENi HBG005542.
    InParanoidi Q92997.
    KOi K02353.
    OMAi GPEHTTR.
    OrthoDBi EOG7BP82N.
    PhylomeDBi Q92997.
    TreeFami TF318198.

    Enzyme and pathway databases

    Reactomei REACT_172581. PCP/CE pathway.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200668. WNT mediated activation of DVL.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200841. degradation of DVL.
    SignaLinki Q92997.

    Miscellaneous databases

    ChiTaRSi DVL3. human.
    GeneWikii DVL3.
    GenomeRNAii 1857.
    NextBioi 35477520.
    PROi Q92997.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92997.
    Bgeei Q92997.
    CleanExi HS_DVL3.
    Genevestigatori Q92997.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR000591. DEP_dom.
    IPR008342. Dishevelled_3.
    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:SF6. PTHR10878:SF6. 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.
    PR01763. DISHEVELLED3.
    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. "cDNA characterization and chromosomal mapping of two human homologues of the Drosophila dishevelled polarity gene."
      Pizzuti A., Amati F., Calabrese G., Mari A., Colosimo A., Silani V., Giardino L., Ratti A., Penso D., Calza L., Palka G., Scarlato G., Novelli G., Dallapiccola B.
      Hum. Mol. Genet. 5:953-958(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "cDNA cloning of a human dishevelled DVL-3 gene, mapping to 3q27, and expression in human breast and colon carcinomas."
      Bui T.D., Beier D.R., Jonssen M., Smith K., Dorrington S.M., Kaklamanis L., Kearney L., Regan R., Sussman D.J., Harris A.L.
      Biochem. Biophys. Res. Commun. 239:510-516(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Human dishevelled genes constitute a DHR-containing multigene family."
      Semenov M.V., Snyder M.
      Genomics 42:302-310(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Uterus.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1), VARIANT LEU-433.
      Tissue: Brain.
    9. "Regulation of the Wnt signaling pathway by disabled-2 (Dab2)."
      Howe P.H.
      EMBO J. 22:3084-3094(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2.
    10. "Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis."
      Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S., Schultz P.G.
      Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRRFIP2.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl."
      Tauriello D.V., Haegebarth A., Kuper I., Edelmann M.J., Henraat M., Canninga-van Dijk M.R., Kessler B.M., Clevers H., Maurice M.M.
      Mol. Cell 37:607-619(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION, INTERACTION WITH CYLD.
    13. "Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a-dependent neurite outgrowth."
      Greer Y.E., Rubin J.S.
      J. Cell Biol. 192:993-1004(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSNK1D/CK1.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
      Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.
      , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
      Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP164.
    16. "Delicate analysis of post-translational modifications on Dishevelled 3."
      Wu C., Wei W., Li C., Li Q., Sheng Q., Zeng R.
      J. Proteome Res. 11:3829-3837(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-192; THR-346 AND SER-700, METHYLATION AT ARG-27; ARG-212; ARG-342 AND ARG-698.
    17. "Dishevelled3 is a novel arginine methyl transferase substrate."
      Bikkavilli R.K., Avasarala S., Vanscoyk M., Sechler M., Kelley N., Malbon C.C., Winn R.A.
      Sci. Rep. 2:805-805(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-271; ARG-342 AND ARG-614, MUTAGENESIS OF ARG-271; ARG-342 AND ARG-614.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-216.

    Entry informationi

    Entry nameiDVL3_HUMAN
    AccessioniPrimary (citable) accession number: Q92997
    Secondary accession number(s): B4E3E5
    , D3DNT0, O14642, Q13531, Q8N5E9, Q92607
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3