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Q92997

- DVL3_HUMAN

UniProt

Q92997 - DVL3_HUMAN

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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

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 heterodimerization activity Source: BHF-UCL
  5. receptor binding Source: BHF-UCL

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
Complete GO annotation...

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
Complete GO annotation...

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 – 481Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine2 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 – 3461Phosphothreonine1 Publication
Modified residuei614 – 6141Symmetric dimethylarginine; by PRMT71 Publication
Modified residuei698 – 6981Dimethylated arginine; alternate1 Publication
Modified residuei698 – 6981Omega-N-methylarginine; alternate1 Publication
Modified residuei700 – 7001Phosphoserine1 Publication

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

BgeeiQ92997.
CleanExiHS_DVL3.
ExpressionAtlasiQ92997. baseline and differential.
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. 44 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.
GeneTreeiENSGT00390000013552.
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.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008342. DVL3.
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

        10         20         30         40         50
MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD
60 70 80 90 100
DDFGVVKEEI SDDNAKLPCF NGRVVSWLVS AEGSHPDPAP FCADNPSELP
110 120 130 140 150
PPMERTGGIG DSRPPSFHPH AGGGSQENLD NDTETDSLVS AQRERPRRRD
160 170 180 190 200
GPEHATRLNG TAKGERRREP GGYDSSSTLM SSELETTSFF DSDEDDSTSR
210 220 230 240 250
FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD STMSLNIITV
260 270 280 290 300
TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL
310 320 330 340 350
QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS
360 370 380 390 400
EPIRPIDPAA WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER
410 420 430 440 450
LDDFHLSIHS DMAAIVKAMA SPESGLEVRD RMWLKITIPN AFIGSDVVDW
460 470 480 490 500
LYHNVEGFTD RREARKYASN LLKAGFIRHT VNKITFSEQC YYIFGDLCGN
510 520 530 540 550
MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY PPPPHPYNPH
560 570 580 590 600
PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG
610 620 630 640 650
SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL ASSLRSHHTH
660 670 680 690 700
PSYGPPGVPP LYGPPMLMMP PPPAAMGPPG APPGRDLASV PPELTASRQS
710
FRMAMGNPSE FFVDVM
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]
uc011bqw.2. human.

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. 44 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 ]
uc011bqw.2. human.

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.
GeneTreei ENSGT00390000013552.
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

Bgeei Q92997.
CleanExi HS_DVL3.
ExpressionAtlasi Q92997. baseline and differential.
Genevestigatori Q92997.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008342. DVL3.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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