DVL2_HUMAN
ID DVL2_HUMAN Reviewed; 736 AA.
AC O14641; D3DTN3; Q53XM0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-2;
DE Short=Dishevelled-2;
DE AltName: Full=DSH homolog 2;
GN Name=DVL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9192851; DOI=10.1006/geno.1997.4713;
RA Semenov M.V., Snyder M.;
RT "Human dishevelled genes constitute a DHR-containing multigene family.";
RL Genomics 42:302-310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH ARRB1.
RX PubMed=11742073; DOI=10.1073/pnas.211572798;
RA Chen W., Hu L.A., Semenov M.V., Yanagawa S., Kikuchi A., Lefkowitz R.J.,
RA Miller W.E.;
RT "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity
RT through interaction with phosphorylated dishevelled proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14889-14894(2001).
RN [6]
RP INTERACTION WITH DIXDC1 AND RAC.
RX PubMed=15262978; DOI=10.1074/jbc.m404598200;
RA Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase
RT activation by Axin and dishevelled through distinct mechanisms.";
RL J. Biol. Chem. 279:39366-39373(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION BY CSNK1D/CK1.
RX PubMed=21422228; DOI=10.1083/jcb.201011111;
RA Greer Y.E., Rubin J.S.;
RT "Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a-
RT dependent neurite outgrowth.";
RL J. Cell Biol. 192:993-1004(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP INTERACTION WITH DACT1.
RX PubMed=22610794; DOI=10.1002/humu.22121;
RA Shi Y., Ding Y., Lei Y.P., Yang X.Y., Xie G.M., Wen J., Cai C.Q., Li H.,
RA Chen Y., Zhang T., Wu B.L., Jin L., Chen Y.G., Wang H.Y.;
RT "Identification of novel rare mutations of DACT1 in human neural tube
RT defects.";
RL Hum. Mutat. 33:1450-1455(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP INTERACTION WITH FAM105B.
RX PubMed=23708998; DOI=10.1038/nature12296;
RA Rivkin E., Almeida S.M., Ceccarelli D.F., Juang Y.C., Maclean T.A.,
RA Srikumar T., Huang H., Dunham W.H., Fukumura R., Xie G., Gondo Y.,
RA Raught B., Gingras A.C., Sicheri F., Cordes S.P.;
RT "The linear ubiquitin-specific deubiquitinase gumby regulates
RT angiogenesis.";
RL Nature 498:318-324(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH DCDC2.
RX PubMed=25557784; DOI=10.1016/j.ajhg.2014.12.002;
RA Schueler M., Braun D.A., Chandrasekar G., Gee H.Y., Klasson T.D.,
RA Halbritter J., Bieder A., Porath J.D., Airik R., Zhou W., LoTurco J.J.,
RA Che A., Otto E.A., Boeckenhauer D., Sebire N.J., Honzik T., Harris P.C.,
RA Koon S.J., Gunay-Aygun M., Saunier S., Zerres K., Bruechle N.O.,
RA Drenth J.P., Pelletier L., Tapia-Paez I., Lifton R.P., Giles R.H., Kere J.,
RA Hildebrandt F.;
RT "DCDC2 mutations cause a renal-hepatic ciliopathy by disrupting Wnt
RT signaling.";
RL Am. J. Hum. Genet. 96:81-92(2015).
RN [16]
RP INTERACTION WITH FOXK1 AND FOXK2, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP AND MUTAGENESIS OF 250-THR--SER-252; THR-250; SER-251; SER-252;
RP 254-SER--THR-257; SER-252; SER-255; THR-257; 259-SER--SER-262; SER-259;
RP THR-260; SER-262; 267-THR--THR-269; THR-267; THR-269; TYR-275; SER-281;
RP SER-286; TYR-295; SER-298 AND SER-329.
RX PubMed=25805136; DOI=10.1016/j.devcel.2015.01.031;
RA Wang W., Li X., Lee M., Jun S., Aziz K.E., Feng L., Tran M.K., Li N.,
RA McCrea P.D., Park J.I., Chen J.;
RT "FOXKs promote Wnt/beta-catenin signaling by translocating DVL into the
RT nucleus.";
RL Dev. Cell 32:707-718(2015).
RN [17]
RP INTERACTION WITH PKD1.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 264-353, AND FUNCTION.
RX PubMed=19252499; DOI=10.1038/nchembio.152;
RA Zhang Y., Appleton B.A., Wiesmann C., Lau T., Costa M., Hannoush R.N.,
RA Sidhu S.S.;
RT "Inhibition of Wnt signaling by Dishevelled PDZ peptides.";
RL Nat. Chem. Biol. 5:217-219(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 261-354.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PDZ domains of human dishevelled 2 (homologous to
RT Drosophila dsh).";
RL Submitted (FEB-2009) to the PDB data bank.
RN [20]
RP VARIANT THR-282.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Plays a role in the signal transduction pathways mediated by
CC multiple Wnt genes. Participates both in canonical and non-canonical
CC Wnt signaling by binding to the cytoplasmic C-terminus of frizzled
CC family members and transducing the Wnt signal to down-stream effectors.
CC Promotes internalization and degradation of frizzled proteins upon Wnt
CC signaling. {ECO:0000250|UniProtKB:Q60838, ECO:0000269|PubMed:19252499}.
CC -!- SUBUNIT: Interacts through its PDZ domain with the C-terminal regions
CC of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the
CC interaction is enhanced by phosphorylation of DVL1 (By similarity). Can
CC form large oligomers (via DIX domain). Interacts (via DIX domain) with
CC DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the
CC AP-2 complex (By similarity). Interacts with DACT1 and FAM105B/otulin.
CC Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and
CC FOXK2; the interaction induces DVL2 nuclear translocation
CC (PubMed:25805136). Interacts with MAPK15 (By similarity). Interacts
CC with PKD1 (via extracellular domain) (PubMed:27214281). Interacts with
CC LMBR1L (By similarity). {ECO:0000250|UniProtKB:Q60838,
CC ECO:0000269|PubMed:11742073, ECO:0000269|PubMed:15262978,
CC ECO:0000269|PubMed:22610794, ECO:0000269|PubMed:23708998,
CC ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25805136,
CC ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC O14641; P25054: APC; NbExp=2; IntAct=EBI-740850, EBI-727707;
CC O14641; O15169: AXIN1; NbExp=3; IntAct=EBI-740850, EBI-710484;
CC O14641; P28329-3: CHAT; NbExp=3; IntAct=EBI-740850, EBI-25837549;
CC O14641; Q5R2U3: CK1E; NbExp=2; IntAct=EBI-740850, EBI-9106301;
CC O14641; P49674: CSNK1E; NbExp=4; IntAct=EBI-740850, EBI-749343;
CC O14641; Q9NYF0: DACT1; NbExp=6; IntAct=EBI-740850, EBI-3951744;
CC O14641; Q155Q3: DIXDC1; NbExp=2; IntAct=EBI-740850, EBI-1104700;
CC O14641; O14641: DVL2; NbExp=4; IntAct=EBI-740850, EBI-740850;
CC O14641; P22607: FGFR3; NbExp=3; IntAct=EBI-740850, EBI-348399;
CC O14641; P01112: HRAS; NbExp=3; IntAct=EBI-740850, EBI-350145;
CC O14641; Q5S007: LRRK2; NbExp=5; IntAct=EBI-740850, EBI-5323863;
CC O14641; P53350: PLK1; NbExp=2; IntAct=EBI-740850, EBI-476768;
CC O14641; P57078: RIPK4; NbExp=4; IntAct=EBI-740850, EBI-4422308;
CC O14641; Q96CG3: TIFA; NbExp=3; IntAct=EBI-740850, EBI-740711;
CC O14641; Q08117-2: TLE5; NbExp=3; IntAct=EBI-740850, EBI-11741437;
CC O14641; P04637: TP53; NbExp=6; IntAct=EBI-740850, EBI-366083;
CC O14641; Q14134: TRIM29; NbExp=5; IntAct=EBI-740850, EBI-702370;
CC O14641; Q96RL1: UIMC1; NbExp=4; IntAct=EBI-740850, EBI-725300;
CC O14641; Q9GZV5: WWTR1; NbExp=4; IntAct=EBI-740850, EBI-747743;
CC O14641; P49910: ZNF165; NbExp=3; IntAct=EBI-740850, EBI-741694;
CC O14641; Q9Z101: Pard6a; Xeno; NbExp=6; IntAct=EBI-740850, EBI-81732;
CC O14641; A2A5Z6: Smurf2; Xeno; NbExp=8; IntAct=EBI-740850, EBI-2348309;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q60838};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q60838}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q60838}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q60838}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q60838}. Nucleus {ECO:0000269|PubMed:25805136}.
CC Note=Localizes at the cell membrane upon interaction with frizzled
CC family members and promotes their internalization. Localizes to
CC cytoplasmic puncta (By similarity). Interaction with FOXK1 and FOXK2
CC induces nuclear translocation (PubMed:25805136).
CC {ECO:0000250|UniProtKB:Q60838, ECO:0000269|PubMed:25805136}.
CC -!- DOMAIN: The DIX domain mediates homooligomerization. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CSNK1D (PubMed:21422228, PubMed:9192851). WNT3A
CC induces DVL2 phosphorylation by CSNK1E and MARK kinases
CC (PubMed:25805136). {ECO:0000269|PubMed:21422228,
CC ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:9192851}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR EMBL; AF006012; AAB65243.1; -; mRNA.
DR EMBL; BT009822; AAP88824.1; -; mRNA.
DR EMBL; CH471108; EAW90244.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90245.1; -; Genomic_DNA.
DR EMBL; BC014844; AAH14844.1; -; mRNA.
DR CCDS; CCDS11091.1; -.
DR RefSeq; NP_004413.1; NM_004422.2.
DR PDB; 2REY; X-ray; 1.55 A; A=261-355.
DR PDB; 3CBX; X-ray; 1.70 A; A/B=264-354.
DR PDB; 3CBY; X-ray; 1.50 A; A/B=264-354.
DR PDB; 3CBZ; X-ray; 1.38 A; A=264-354.
DR PDB; 3CC0; X-ray; 1.75 A; A/B/C=264-354.
DR PDB; 4WIP; X-ray; 2.69 A; A/B/C=12-106.
DR PDB; 5LNP; X-ray; 1.99 A; A/B/C/D=416-510.
DR PDB; 5SUY; X-ray; 1.88 A; A/B/C/D=416-510.
DR PDB; 5SUZ; X-ray; 1.84 A; A/B=416-509.
DR PDB; 6IW3; X-ray; 1.64 A; A=12-93.
DR PDB; 6JCK; X-ray; 3.09 A; B=12-93.
DR PDBsum; 2REY; -.
DR PDBsum; 3CBX; -.
DR PDBsum; 3CBY; -.
DR PDBsum; 3CBZ; -.
DR PDBsum; 3CC0; -.
DR PDBsum; 4WIP; -.
DR PDBsum; 5LNP; -.
DR PDBsum; 5SUY; -.
DR PDBsum; 5SUZ; -.
DR PDBsum; 6IW3; -.
DR PDBsum; 6JCK; -.
DR AlphaFoldDB; O14641; -.
DR BMRB; O14641; -.
DR SMR; O14641; -.
DR BioGRID; 108189; 419.
DR CORUM; O14641; -.
DR DIP; DIP-34433N; -.
DR IntAct; O14641; 168.
DR MINT; O14641; -.
DR STRING; 9606.ENSP00000005340; -.
DR BindingDB; O14641; -.
DR ChEMBL; CHEMBL1255125; -.
DR GlyGen; O14641; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14641; -.
DR MetOSite; O14641; -.
DR PhosphoSitePlus; O14641; -.
DR BioMuta; DVL2; -.
DR EPD; O14641; -.
DR jPOST; O14641; -.
DR MassIVE; O14641; -.
DR MaxQB; O14641; -.
DR PaxDb; O14641; -.
DR PeptideAtlas; O14641; -.
DR PRIDE; O14641; -.
DR ProteomicsDB; 48140; -.
DR Antibodypedia; 3985; 502 antibodies from 39 providers.
DR DNASU; 1856; -.
DR Ensembl; ENST00000005340.10; ENSP00000005340.4; ENSG00000004975.12.
DR GeneID; 1856; -.
DR KEGG; hsa:1856; -.
DR MANE-Select; ENST00000005340.10; ENSP00000005340.4; NM_004422.3; NP_004413.1.
DR UCSC; uc002gez.2; human.
DR CTD; 1856; -.
DR DisGeNET; 1856; -.
DR GeneCards; DVL2; -.
DR HGNC; HGNC:3086; DVL2.
DR HPA; ENSG00000004975; Low tissue specificity.
DR MIM; 602151; gene.
DR neXtProt; NX_O14641; -.
DR OpenTargets; ENSG00000004975; -.
DR PharmGKB; PA27542; -.
DR VEuPathDB; HostDB:ENSG00000004975; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR InParanoid; O14641; -.
DR OMA; PAGAKYY; -.
DR OrthoDB; 474724at2759; -.
DR PhylomeDB; O14641; -.
DR TreeFam; TF318198; -.
DR PathwayCommons; O14641; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5368598; Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; O14641; -.
DR SIGNOR; O14641; -.
DR BioGRID-ORCS; 1856; 11 hits in 1085 CRISPR screens.
DR ChiTaRS; DVL2; human.
DR EvolutionaryTrace; O14641; -.
DR GeneWiki; DVL2; -.
DR GenomeRNAi; 1856; -.
DR Pharos; O14641; Tbio.
DR PRO; PR:O14641; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O14641; protein.
DR Bgee; ENSG00000004975; Expressed in ventricular zone and 189 other tissues.
DR ExpressionAtlas; O14641; baseline and differential.
DR Genevisible; O14641; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0044340; P:canonical Wnt signaling pathway involved in regulation of cell proliferation; IDA:BHF-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISS:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007379; P:segment specification; ISS:BHF-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:BHF-UCL.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR024580; Dishevelled_C-dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR008341; DVL2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10878; PTHR10878; 1.
DR PANTHER; PTHR10878:SF8; PTHR10878:SF8; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF12316; Dsh_C; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR01760; DISHEVELLED.
DR PRINTS; PR01762; DISHEVELLED2.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..736
FT /note="Segment polarity protein dishevelled homolog DVL-2"
FT /id="PRO_0000145746"
FT DOMAIN 11..93
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 267..339
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 433..507
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 92..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..355
FT /note="Required for interaction with FOXK2"
FT /evidence="ECO:0000269|PubMed:25805136"
FT REGION 558..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 282
FT /note="I -> T (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064708"
FT MUTAGEN 250..252
FT /note="TSS->AAA: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 250
FT /note="T->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 251
FT /note="S->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 252
FT /note="S->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 254..257
FT /note="SSVT->AAVA: Almost abolishes interaction with
FT FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 254
FT /note="S->A: Reduces interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 255
FT /note="S->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 257
FT /note="T->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 259..262
FT /note="STMS->AAMA: Almost abolishes interaction with
FT FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 259
FT /note="S->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 260
FT /note="T->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 262
FT /note="S->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 267..269
FT /note="TVT->AVA: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 267
FT /note="T->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 269
FT /note="T->A: Almost abolishes interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 275
FT /note="Y->F: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 281
FT /note="S->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 286
FT /note="S->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 295
FT /note="Y->F: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 298
FT /note="S->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT MUTAGEN 329
FT /note="S->A: No effect on interaction with FOXK2."
FT /evidence="ECO:0000269|PubMed:25805136"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:6IW3"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:6IW3"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6IW3"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6IW3"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6IW3"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6IW3"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6IW3"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6JCK"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6IW3"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3CBZ"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3CBZ"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3CBZ"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3CBZ"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:3CBZ"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:3CBZ"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:3CBZ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3CBZ"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3CBZ"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:5SUZ"
FT STRAND 440..454
FT /evidence="ECO:0007829|PDB:5SUZ"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:5SUZ"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:5SUZ"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:5SUZ"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:5SUZ"
SQ SEQUENCE 736 AA; 78948 MW; 4BAD95B6C3FE531B CRC64;
MAGSSTGGGG VGETKVIYHL DEEETPYLVK IPVPAERITL GDFKSVLQRP AGAKYFFKSM
DQDFGVVKEE ISDDNARLPC FNGRVVSWLV SSDNPQPEMA PPVHEPRAEL APPAPPLPPL
PPERTSGIGD SRPPSFHPNV SSSHENLEPE TETESVVSLR RERPRRRDSS EHGAGGHRTG
GPSRLERHLA GYESSSTLMT SELESTSLGD SDEEDTMSRF SSSTEQSSAS RLLKRHRRRR
KQRPPRLERT SSFSSVTDST MSLNIITVTL NMEKYNFLGI SIVGQSNERG DGGIYIGSIM
KGGAVAADGR IEPGDMLLQV NDMNFENMSN DDAVRVLRDI VHKPGPIVLT VAKCWDPSPQ
AYFTLPRNEP IQPIDPAAWV SHSAALTGTF PAYPGSSSMS TITSGSSLPD GCEGRGLSVH
TDMASVTKAM AAPESGLEVR DRMWLKITIP NAFLGSDVVD WLYHHVEGFP ERREARKYAS
GLLKAGLIRH TVNKITFSEQ CYYVFGDLSG GCESYLVNLS LNDNDGSSGA SDQDTLAPLP
GATPWPLLPT FSYQYPAPHP YSPQPPPYHE LSSYTYGGGS ASSQHSEGSR SSGSTRSDGG
AGRTGRPEER APESKSGSGS ESEPSSRGGS LRRGGEASGT SDGGPPPSRG STGGAPNLRA
HPGLHPYGPP PGMALPYNPM MVVMMPPPPP PVPPAVQPPG APPVRDLGSV PPELTASRQS
FHMAMGNPSE FFVDVM
