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Q92997 (DVL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Segment polarity protein dishevelled homolog DVL-3

Short name=Dishevelled-3
Alternative name(s):
DSH homolog 3
Gene names
Name:DVL3
Synonyms:KIAA0208
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.9 Ref.10 Ref.12 Ref.15

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. Ref.12

Phosphorylated by CSNK1D. Ref.13 Ref.16

Arginine methylation may function as a switch in regulation of function in Wnt signaling.

Sequence similarities

Belongs to the DSH family.

Contains 1 DEP domain.

Contains 1 DIX domain.

Contains 1 PDZ (DHR) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionDevelopmental protein
   PTMMethylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

Wnt signaling pathway, planar cell polarity pathway

Inferred from direct assay Ref.9. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from direct assay PubMed 17593335. Source: BHF-UCL

cochlea morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

convergent extension

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

non-canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 19137009. Source: BHF-UCL

non-canonical Wnt signaling pathway via JNK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

outflow tract septum morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

planar cell polarity pathway involved in neural tube closure

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of JUN kinase activity

Inferred from mutant phenotype PubMed 19137009. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 20137080. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10644691Ref.9PubMed 17593335. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionbeta-catenin binding

Inferred from direct assay PubMed 10644691. Source: BHF-UCL

frizzled binding

Inferred from physical interaction PubMed 19388021. Source: UniProtKB

protease binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 19137009. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 17030191. Source: BHF-UCL

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92997-1)

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.
Isoform 2 (identifier: Q92997-2)

The sequence of this isoform differs from the canonical sequence as follows:
     350-367: SEPIRPIDPAAWVSHTAA → T
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 716716Segment polarity protein dishevelled homolog DVL-3
PRO_0000145749

Regions

Domain1 – 8282DIX
Domain249 – 32173PDZ
Domain422 – 49675DEP

Amino acid modifications

Modified residue271Omega-N-methylarginine Ref.16
Modified residue481Phosphoserine Ref.14
Modified residue1921Phosphoserine Ref.11 Ref.16
Modified residue2121Omega-N-methylarginine Ref.16
Modified residue2711Asymmetric dimethylarginine; by PRMT1; alternate Ref.17
Modified residue2711Symmetric dimethylarginine; by PRMT7; alternate Ref.17
Modified residue3421Omega-N-methylarginine; alternate Ref.16 Ref.17
Modified residue3421Symmetric dimethylarginine; by PRMT7; alternate Ref.16 Ref.17
Modified residue3461Phosphothreonine Ref.16
Modified residue6141Symmetric dimethylarginine; by PRMT7 Ref.17
Modified residue6981Dimethylated arginine; alternate Ref.16
Modified residue6981Omega-N-methylarginine; alternate Ref.16
Modified residue7001Phosphoserine Ref.16

Natural variations

Alternative sequence350 – 36718SEPIR…SHTAA → T in isoform 2.
VSP_053371
Natural variant2161R → T in a breast cancer sample; somatic mutation. Ref.18
VAR_036116
Natural variant4331W → L. Ref.8
Corresponds to variant rs17853048 [ dbSNP | Ensembl ].
VAR_025519

Experimental info

Mutagenesis2711R → K: Localizes to plasma membranes. Ref.17
Mutagenesis3421R → K: No effect on subcellular location. Ref.17
Mutagenesis6141R → K: Localizes to plasma membranes. Ref.17
Sequence conflict21G → D in AAB47447. Ref.1
Sequence conflict761S → Y in AAB84228. Ref.2
Sequence conflict1021P → S in AAB47447. Ref.1
Sequence conflict1511G → W in AAB47447. Ref.1
Sequence conflict1821S → R in AAB47447. Ref.1
Sequence conflict2181K → N in AAB47447. Ref.1
Sequence conflict2221R → W in AAB47447. Ref.1
Sequence conflict2301E → D in AAB47447. Ref.1
Sequence conflict2331S → C in AAB47447. Ref.1
Sequence conflict2361S → T in AAB47447. Ref.1
Sequence conflict2391T → S in AAB47447. Ref.1
Sequence conflict2421T → A in AAB47447. Ref.1
Sequence conflict3031N → K in AAB47447. Ref.1
Sequence conflict4311R → C in AAB47447. Ref.1
Sequence conflict4501W → C in AAB47447. Ref.1
Sequence conflict4651R → P in AAB47447. Ref.1
Sequence conflict4721L → V in AAB47447. Ref.1
Sequence conflict5431P → R in AAB65244. Ref.3
Sequence conflict553 – 5542FP → LG in AAB65244. Ref.3
Sequence conflict6291A → T in AAB47447. Ref.1
Sequence conflict6331S → I in AAB47447. Ref.1
Sequence conflict682 – 71635PPGRD…FVDVM → LRAATWPQCPRN in BAA13199. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: B1A55EBF9507D06E

FASTA71678,055
        10         20         30         40         50         60 
MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD DDFGVVKEEI 

        70         80         90        100        110        120 
SDDNAKLPCF NGRVVSWLVS AEGSHPDPAP FCADNPSELP PPMERTGGIG DSRPPSFHPH 

       130        140        150        160        170        180 
AGGGSQENLD NDTETDSLVS AQRERPRRRD GPEHATRLNG TAKGERRREP GGYDSSSTLM 

       190        200        210        220        230        240 
SSELETTSFF DSDEDDSTSR FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD 

       250        260        270        280        290        300 
STMSLNIITV TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL 

       310        320        330        340        350        360 
QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS EPIRPIDPAA 

       370        380        390        400        410        420 
WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER LDDFHLSIHS DMAAIVKAMA 

       430        440        450        460        470        480 
SPESGLEVRD RMWLKITIPN AFIGSDVVDW LYHNVEGFTD RREARKYASN LLKAGFIRHT 

       490        500        510        520        530        540 
VNKITFSEQC YYIFGDLCGN MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY 

       550        560        570        580        590        600 
PPPPHPYNPH PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG 

       610        620        630        640        650        660 
SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL ASSLRSHHTH PSYGPPGVPP 

       670        680        690        700        710 
LYGPPMLMMP PPPAAMGPPG APPGRDLASV PPELTASRQS FRMAMGNPSE FFVDVM 

« Hide

Isoform 2 [UniParc].

Checksum: AD4CB18FDB88AA63
Show »

FASTA69976,256

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-216.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5763.
RefSeqNP_004414.3. NM_004423.3.
UniGeneHs.388116.

3D structure databases

ProteinModelPortalQ92997.
SMRQ92997. Positions 3-79, 247-335, 411-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108190. 37 interactions.
DIPDIP-34509N.
IntActQ92997. 45 interactions.
MINTMINT-1186858.
STRING9606.ENSP00000316054.

Chemistry

ChEMBLCHEMBL6028.

PTM databases

PhosphoSiteQ92997.

Polymorphism databases

DMDM6919875.

Proteomic databases

PaxDbQ92997.
PRIDEQ92997.

Protocols and materials databases

DNASU1857.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313143; ENSP00000316054; ENSG00000161202. [Q92997-1]
ENST00000431765; ENSP00000405885; ENSG00000161202. [Q92997-2]
GeneID1857.
KEGGhsa:1857.
UCSCuc003fms.3. human. [Q92997-1]

Organism-specific databases

CTD1857.
GeneCardsGC03P183873.
HGNCHGNC:3087. DVL3.
HPACAB046486.
HPA049163.
MIM601368. gene.
neXtProtNX_Q92997.
PharmGKBPA27543.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322275.
HOGENOMHOG000017084.
HOVERGENHBG005542.
InParanoidQ92997.
KOK02353.
OMAGPEHTTR.
OrthoDBEOG7BP82N.
PhylomeDBQ92997.
TreeFamTF318198.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ92997.

Gene expression databases

ArrayExpressQ92997.
BgeeQ92997.
CleanExHS_DVL3.
GenevestigatorQ92997.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000591. DEP_dom.
IPR008342. Dishevelled_3.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF6. PTHR10878:SF6. 1 hit.
PfamPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSPR01760. DISHEVELLED.
PR01763. DISHEVELLED3.
SMARTSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDVL3. human.
GeneWikiDVL3.
GenomeRNAi1857.
NextBio35477520.
PROQ92997.
SOURCESearch...

Entry information

Entry nameDVL3_HUMAN
AccessionPrimary (citable) accession number: Q92997
Secondary accession number(s): B4E3E5 expand/collapse secondary AC list , D3DNT0, O14642, Q13531, Q8N5E9, Q92607
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM