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P51141 (DVL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Segment polarity protein dishevelled homolog DVL-1

Short name=Dishevelled-1
Alternative name(s):
DSH homolog 1
Gene names
Name:Dvl1
Synonyms:Dvl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Ref.8 Ref.11 Ref.15 Ref.17

Subunit structure

Interacts with CXXC4 By similarity. Interacts (via PDZ domain) with TMEM88 By similarity. Interacts with BRD7 and INVS. Interacts through its PDZ domain with the C-terminal regions of VANGL1, VANGL2 and CCDC88C/DAPLE. Interacts (via PDZ domain) with NXN. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 By similarity. Interacts with CYLD. Interacts (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same binding site. Interacts (via DEP domain) with MUSK; the interaction is direct and mediates the formation a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytosol. Cytoplasmic vesicle. Note: Localizes at the cell membrane upon interaction with frizzled family members. Ref.11

Tissue specificity

High levels are seen in the brain, testis and kidney, lower levels in the ovary, breast, muscle, liver and small intestine, and very low levels are seen in the spleen and thymus. A moderate level expression is seen in the heart.

Developmental stage

Is expressed throughout the embryonic central nervous system from presomite stages and in neuron-rich areas of the brain throughout postnatal development, as well as in many other tissues.

Domain

The DIX domain promotes homooligomerization. Ref.11 Ref.18

The DEP domain mediates interaction with the cell membrane. Ref.11 Ref.18

Post-translational modification

Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination By similarity. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. Ref.14

Disruption phenotype

Mice display abnormalities in social behavior and sensorimotor gating. Ref.7

Sequence similarities

Belongs to the DSH family.

Contains 1 DEP domain.

Contains 1 DIX domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
   Molecular functionDevelopmental protein
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Non-traceable author statement PubMed 8856345. Source: BHF-UCL

Wnt signaling pathway, planar cell polarity pathway

Inferred from direct assay PubMed 14966280. Source: MGI

axon extension

Inferred from direct assay PubMed 18716223. Source: MGI

axon guidance

Inferred from direct assay PubMed 18716223. Source: MGI

axonogenesis

Inferred from direct assay PubMed 14734535. Source: MGI

canonical Wnt signaling pathway

Inferred from direct assay PubMed 14648878PubMed 14966280. Source: MGI

cochlea morphogenesis

Inferred from genetic interaction PubMed 16116426. Source: MGI

collateral sprouting

Inferred from direct assay PubMed 18716223. Source: MGI

convergent extension involved in neural plate elongation

Inferred from genetic interaction PubMed 16571627. Source: MGI

convergent extension involved in organogenesis

Inferred from mutant phenotype PubMed 16116426. Source: MGI

cytoplasmic microtubule organization

Inferred from direct assay PubMed 14648878. Source: MGI

dendrite morphogenesis

Inferred from mutant phenotype PubMed 15608632. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from genetic interaction PubMed 9271238. Source: MGI

neural tube development

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from genetic interaction Ref.8. Source: MGI

neurotransmitter secretion

Inferred from genetic interaction PubMed 16818724. Source: MGI

planar cell polarity pathway involved in neural tube closure

Inferred from genetic interaction PubMed 16571627. Source: MGI

positive regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 11742004. Source: BHF-UCL

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 15548427. Source: MGI

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from Biological aspect of Ancestor. Source: RefGenome

prepulse inhibition

Inferred from mutant phenotype Ref.7. Source: MGI

protein localization to microtubule

Inferred from genetic interaction PubMed 18716223. Source: MGI

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

receptor clustering

Inferred from genetic interaction Ref.8. Source: MGI

regulation of neurotransmitter levels

Inferred from mutant phenotype PubMed 16818724. Source: MGI

regulation of protein phosphorylation

Inferred from genetic interaction PubMed 14734535. Source: MGI

skeletal muscle acetylcholine-gated channel clustering

Inferred from mutant phenotype PubMed 19020093. Source: MGI

social behavior

Inferred from mutant phenotype PubMed 14960015Ref.7. Source: MGI

synapse organization

Inferred from mutant phenotype PubMed 16818724. Source: MGI

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 14734535. Source: MGI

cell cortex

Inferred from Biological aspect of Ancestor. Source: RefGenome

clathrin-coated vesicle

Inferred from direct assay PubMed 17005174. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 11113207. Source: MGI

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

growth cone

Inferred from Biological aspect of Ancestor. Source: RefGenome

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Non-traceable author statement PubMed 8856345. Source: BHF-UCL

microtubule

Inferred from Biological aspect of Ancestor. Source: RefGenome

microtubule cytoskeleton

Inferred from direct assay PubMed 14734535. Source: MGI

neuronal cell body

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from direct assay PubMed 16818724. Source: MGI

   Molecular_functionRac GTPase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

frizzled binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695Segment polarity protein dishevelled homolog DVL-1
PRO_0000145743

Regions

Domain1 – 8585DIX
Domain251 – 32373PDZ
Domain425 – 49975DEP
Compositional bias390 – 3934Poly-Ser

Experimental info

Mutagenesis171Y → D: Loss of oligomerization. Ref.18
Mutagenesis4381K → M: Strongly reduces activity in Wnt signaling. Abolishes location at the cell membrane. Ref.11 Ref.15
Mutagenesis4491D → I: Reduces activity in Wnt signaling; when associated with I-452. Ref.15
Mutagenesis4521D → I: Reduces activity in Wnt signaling; when associated with I-449. Ref.15
Sequence conflict121 – 1255HPNVA → Q in AAA74049. Ref.2
Sequence conflict1211H → Q in AAA74049. Ref.2
Sequence conflict2111T → N in AAA74049. Ref.2

Secondary structure

............................................................ 695
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51141 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: FA21ACAC48FF71E0

FASTA69575,359
        10         20         30         40         50         60 
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK 

        70         80         90        100        110        120 
EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF 

       130        140        150        160        170        180 
HPNVASSRDG MDNETGTESM VSHRRERARR RNRDEAARTN GHPRGDRRRD LGLPPDSAST 

       190        200        210        220        230        240 
VLSSELESSS FIDSDEEDNT SRLSSSTEQS TSSRLVRKHK CRRRKQRLRQ TDRASSFSSI 

       250        260        270        280        290        300 
TDSTMSLNII TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM 

       310        320        330        340        350        360 
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP RADPVRPIDP 

       370        380        390        400        410        420 
AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG APQLEEAPLT VKSDMSAIVR 

       430        440        450        460        470        480 
VMQLPDSGLE IRDRMWLKIT IANAVIGADV VDWLYTHVEG FKERREARKY ASSMLKHGFL 

       490        500        510        520        530        540 
RHTVNKITFS EQCYYVFGDL CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY 

       550        560        570        580        590        600 
QYPGPPPCFP PAYQDPGFSC GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG 

       610        620        630        640        650        660 
SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA YAVVGGPPGG 

       670        680        690 
PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a mouse homolog of the Drosophila segment polarity gene dishevelled."
Sussman D.J., Klingensmith J., Salinas P., Adams P.S., Nusse R., Perrimon N.
Dev. Biol. 166:73-86(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"Organization and promoter analysis of the mouse dishevelled-1 gene."
Lijam N., Sussman D.J.
Genome Res. 5:116-124(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Embryo.
[7]"Social interaction and sensorimotor gating abnormalities in mice lacking Dvl1."
Lijam N., Paylor R., McDonald M.P., Crawley J.N., Deng C.-X., Herrup K., Stevens K.E., Maccaferri G., McBain C.J., Sussman D.J., Wynshaw-Boris A.
Cell 90:895-905(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Regulation of AChR clustering by Dishevelled interacting with MuSK and PAK1."
Luo Z.G., Wang Q., Zhou J.Z., Wang J., Luo Z., Liu M., He X., Wynshaw-Boris A., Xiong W.C., Lu B., Mei L.
Neuron 35:489-505(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEUROMUSCULAR JUNCTION DEVELOPMENT, INTERACTION WITH MUSK AND PAK1.
[9]"BP75, bromodomain-containing M(r) 75,000 protein, binds dishevelled-1 and enhances Wnt signaling by inactivating glycogen synthase kinase-3 beta."
Kim S., Lee J., Park J., Chung J.
Cancer Res. 63:4792-4795(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRD7.
[10]"Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth."
Lu W., Yamamoto V., Ortega B., Baltimore D.
Cell 119:97-108(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYK.
[11]"Characterization of function of three domains in dishevelled-1: DEP domain is responsible for membrane translocation of dishevelled-1."
Pan W.J., Pang S.Z., Huang T., Guo H.Y., Wu D., Li L.
Cell Res. 14:324-330(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZD7, MUTAGENESIS OF LYS-438, DOMAIN.
[12]"Independent mutations in mouse Vangl2 that cause neural tube defects in looptail mice impair interaction with members of the Dishevelled family."
Torban E., Wang H.-J., Groulx N., Gros P.
J. Biol. Chem. 279:52703-52713(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VANGL1 AND VANGL2.
[13]"The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled."
Funato Y., Michiue T., Asashima M., Miki H.
Nat. Cell Biol. 8:501-508(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NXN.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CYLD.
[15]"Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway."
Wong H.C., Mao J., Nguyen J.T., Srinivas S., Zhang W., Liu B., Li L., Wu D., Zheng J.
Nat. Struct. Biol. 7:1178-1184(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 395-495, FUNCTION, MUTAGENESIS OF LYS-438; ASP-449 AND ASP-452.
[16]"Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled."
Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M., Shi D.L., Zheng J.
Mol. Cell 12:1251-1260(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 251-345, INTERACTION WITH DACT1 AND FZD7.
[17]"Sulindac inhibits canonical Wnt signaling by blocking the PDZ domain of the protein Dishevelled."
Lee H.J., Wang N.X., Shi D.L., Zheng J.J.
Angew. Chem. Int. Ed. 48:6448-6452(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 248-337 IN COMPLEX WITH SULINDAC, INTERACTION WITH DACT1, FUNCTION.
[18]"Molecular basis of Wnt activation via the DIX-domain protein Ccd1."
Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C., Wang Z.X., Wu J.W.
J. Biol. Chem. 286:8597-8608(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 4-104, MUTAGENESIS OF TYR-17, DOMAIN, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10115 mRNA. Translation: AAA82175.1.
U28138 Genomic DNA. Translation: AAA74049.1.
AK155349 mRNA. Translation: BAE33208.1.
AL670236 Genomic DNA. Translation: CAM18392.1.
CH466594 Genomic DNA. Translation: EDL15045.1.
BC138848 mRNA. Translation: AAI38849.1.
BC138849 mRNA. Translation: AAI38850.1.
RefSeqNP_034221.3. NM_010091.3.
UniGeneMm.3400.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSHNMR-A395-495[»]
1MC7NMR-A251-345[»]
2KAWNMR-A248-337[»]
3PZ8X-ray2.87A/B/C/D/E/F/G/H4-104[»]
ProteinModelPortalP51141.
SMRP51141. Positions 3-84, 248-337, 406-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199342. 18 interactions.
IntActP51141. 17 interactions.
MINTMINT-261881.

PTM databases

PhosphoSiteP51141.

Proteomic databases

PRIDEP51141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
GeneID13542.
KEGGmmu:13542.
UCSCuc008wfc.1. mouse.

Organism-specific databases

CTD1855.
MGIMGI:94941. Dvl1.

Phylogenomic databases

eggNOGNOG322275.
GeneTreeENSGT00390000013552.
HOGENOMHOG000017084.
HOVERGENHBG005542.
InParanoidQ3U2D3.
KOK02353.
OMASESDHTA.
OrthoDBEOG7BP82N.
TreeFamTF318198.

Gene expression databases

ArrayExpressP51141.
BgeeP51141.
CleanExMM_DVL1.
GenevestigatorP51141.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProIPR000591. DEP_dom.
IPR008340. Dishevelled_1.
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:SF5. PTHR10878:SF5. 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.
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

EvolutionaryTraceP51141.
NextBio284142.
PROP51141.
SOURCESearch...

Entry information

Entry nameDVL1_MOUSE
AccessionPrimary (citable) accession number: P51141
Secondary accession number(s): Q3U2D3, Q60868
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
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

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot