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Protein

Segment polarity protein dishevelled homolog DVL-1

Gene

Dvl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. frizzled binding Source: MGI
  3. identical protein binding Source: MGI
  4. protein kinase binding Source: MGI

GO - Biological processi

  1. axon extension Source: MGI
  2. axon guidance Source: MGI
  3. axonogenesis Source: MGI
  4. canonical Wnt signaling pathway Source: MGI
  5. cochlea morphogenesis Source: MGI
  6. collateral sprouting Source: MGI
  7. convergent extension involved in neural plate elongation Source: MGI
  8. convergent extension involved in organogenesis Source: MGI
  9. cytoplasmic microtubule organization Source: MGI
  10. dendrite morphogenesis Source: MGI
  11. intracellular signal transduction Source: InterPro
  12. negative regulation of protein binding Source: MGI
  13. negative regulation of protein kinase activity Source: MGI
  14. negative regulation of protein phosphorylation Source: MGI
  15. neural tube development Source: Ensembl
  16. neuromuscular junction development Source: MGI
  17. neurotransmitter secretion Source: MGI
  18. planar cell polarity pathway involved in neural tube closure Source: MGI
  19. positive regulation of canonical Wnt signaling pathway Source: BHF-UCL
  20. positive regulation of neuron projection development Source: MGI
  21. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  22. positive regulation of protein phosphorylation Source: MGI
  23. positive regulation of transcription, DNA-templated Source: MGI
  24. positive regulation of Wnt signaling pathway Source: MGI
  25. prepulse inhibition Source: MGI
  26. protein localization to microtubule Source: MGI
  27. protein localization to nucleus Source: MGI
  28. receptor clustering Source: MGI
  29. regulation of neurotransmitter levels Source: MGI
  30. regulation of protein phosphorylation Source: MGI
  31. skeletal muscle acetylcholine-gated channel clustering Source: MGI
  32. social behavior Source: MGI
  33. synapse organization Source: MGI
  34. transcription from RNA polymerase II promoter Source: MGI
  35. Wnt signaling pathway Source: BHF-UCL
  36. Wnt signaling pathway, planar cell polarity pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_207044. TCF dependent signaling in response to WNT.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_225118. WNT mediated activation of DVL.
REACT_227429. degradation of DVL.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-1
Short name:
Dishevelled-1
Alternative name(s):
DSH homolog 1
Gene namesi
Name:Dvl1
Synonyms:Dvl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:94941. Dvl1.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytosol 1 Publication. Cytoplasmic vesicle 1 Publication
Note: Localizes at the cell membrane upon interaction with frizzled family members.

GO - Cellular componenti

  1. axon Source: MGI
  2. clathrin-coated vesicle Source: MGI
  3. cytoplasmic membrane-bounded vesicle Source: MGI
  4. cytoplasmic vesicle Source: MGI
  5. cytosol Source: GO_Central
  6. dendrite Source: Ensembl
  7. growth cone Source: Ensembl
  8. lateral plasma membrane Source: Ensembl
  9. membrane Source: BHF-UCL
  10. microtubule Source: Ensembl
  11. microtubule cytoskeleton Source: MGI
  12. neuronal cell body Source: Ensembl
  13. synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display abnormalities in social behavior and sensorimotor gating.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171Y → D: Loss of oligomerization. 1 Publication
Mutagenesisi438 – 4381K → M: Strongly reduces activity in Wnt signaling. Abolishes location at the cell membrane. 2 Publications
Mutagenesisi449 – 4491D → I: Reduces activity in Wnt signaling; when associated with I-452. 1 Publication
Mutagenesisi452 – 4521D → I: Reduces activity in Wnt signaling; when associated with I-449. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695Segment polarity protein dishevelled homolog DVL-1PRO_0000145743Add
BLAST

Post-translational modificationi

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.By similarity1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP51141.
PRIDEiP51141.

PTM databases

PhosphoSiteiP51141.

Expressioni

Tissue specificityi

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 stagei

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.

Gene expression databases

BgeeiP51141.
CleanExiMM_DVL1.
ExpressionAtlasiP51141. baseline and differential.
GenevestigatoriP51141.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dact1Q8R4A34EBI-1538407,EBI-3870250
fzd7-bQ8AVJ93EBI-1538407,EBI-3870271From a different organism.
Tfdp1Q086393EBI-1538407,EBI-1216575
Tmem88Q9D0N82EBI-1538407,EBI-6136970
Vangl1Q80Z962EBI-1538407,EBI-1750708
Vangl2Q91ZD42EBI-1538407,EBI-1750744

Protein-protein interaction databases

BioGridi199342. 18 interactions.
IntActiP51141. 19 interactions.
MINTiMINT-261881.

Structurei

Secondary structure

1
695
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi17 – 237Combined sources
Beta strandi25 – 273Combined sources
Helixi30 – 356Combined sources
Helixi42 – 443Combined sources
Beta strandi48 – 536Combined sources
Turni54 – 563Combined sources
Beta strandi57 – 626Combined sources
Beta strandi76 – 805Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi279 – 2835Combined sources
Beta strandi286 – 2883Combined sources
Helixi289 – 2924Combined sources
Helixi297 – 2993Combined sources
Beta strandi301 – 3044Combined sources
Turni310 – 3123Combined sources
Helixi318 – 3269Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi411 – 4133Combined sources
Helixi415 – 4239Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi439 – 4435Combined sources
Helixi446 – 45712Combined sources
Helixi464 – 47613Combined sources
Turni477 – 4793Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi491 – 4933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSHNMR-A395-499[»]
1MC7NMR-A251-345[»]
2KAWNMR-A248-337[»]
3PZ8X-ray2.87A/B/C/D/E/F/G/H3-104[»]
ProteinModelPortaliP51141.
SMRiP51141. Positions 3-84, 248-337, 406-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585DIXPROSITE-ProRule annotationAdd
BLAST
Domaini251 – 32373PDZPROSITE-ProRule annotationAdd
BLAST
Domaini425 – 49975DEPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi390 – 3934Poly-Ser

Domaini

The DIX domain promotes homooligomerization.
The DEP domain mediates interaction with the cell membrane.

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.
InParanoidiP51141.
KOiK02353.
OMAiYPRYGMS.
OrthoDBiEOG7BP82N.
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.
IPR008340. DVL-1.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF5. PTHR10878:SF5. 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.
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]

Sequencei

Sequence statusi: Complete.

P51141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK
60 70 80 90 100
SMDQDFGVVK EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT
110 120 130 140 150
DLPPPLERTG GIGDSRPPSF HPNVASSRDG MDNETGTESM VSHRRERARR
160 170 180 190 200
RNRDEAARTN GHPRGDRRRD LGLPPDSAST VLSSELESSS FIDSDEEDNT
210 220 230 240 250
SRLSSSTEQS TSSRLVRKHK CRRRKQRLRQ TDRASSFSSI TDSTMSLNII
260 270 280 290 300
TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM
310 320 330 340 350
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP
360 370 380 390 400
RADPVRPIDP AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG
410 420 430 440 450
APQLEEAPLT VKSDMSAIVR VMQLPDSGLE IRDRMWLKIT IANAVIGADV
460 470 480 490 500
VDWLYTHVEG FKERREARKY ASSMLKHGFL RHTVNKITFS EQCYYVFGDL
510 520 530 540 550
CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY QYPGPPPCFP
560 570 580 590 600
PAYQDPGFSC GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG
610 620 630 640 650
SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA
660 670 680 690
YAVVGGPPGG PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM
Length:695
Mass (Da):75,359
Last modified:July 27, 2011 - v2
Checksum:iFA21ACAC48FF71E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1255HPNVA → Q in AAA74049 (PubMed:9132266).Curated
Sequence conflicti121 – 1211H → Q in AAA74049 (PubMed:9132266).Curated
Sequence conflicti211 – 2111T → N in AAA74049 (PubMed:9132266).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19045.1.
RefSeqiNP_001289271.1. NM_001302342.1.
NP_034221.3. NM_010091.4.
UniGeneiMm.3400.

Genome annotation databases

EnsembliENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
GeneIDi13542.
KEGGimmu:13542.
UCSCiuc008wfc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19045.1.
RefSeqiNP_001289271.1. NM_001302342.1.
NP_034221.3. NM_010091.4.
UniGeneiMm.3400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FSHNMR-A395-499[»]
1MC7NMR-A251-345[»]
2KAWNMR-A248-337[»]
3PZ8X-ray2.87A/B/C/D/E/F/G/H3-104[»]
ProteinModelPortaliP51141.
SMRiP51141. Positions 3-84, 248-337, 406-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199342. 18 interactions.
IntActiP51141. 19 interactions.
MINTiMINT-261881.

PTM databases

PhosphoSiteiP51141.

Proteomic databases

MaxQBiP51141.
PRIDEiP51141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030948; ENSMUSP00000030948; ENSMUSG00000029071.
ENSMUST00000168552; ENSMUSP00000133137; ENSMUSG00000029071.
GeneIDi13542.
KEGGimmu:13542.
UCSCiuc008wfc.1. mouse.

Organism-specific databases

CTDi1855.
MGIiMGI:94941. Dvl1.

Phylogenomic databases

eggNOGiNOG322275.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiP51141.
KOiK02353.
OMAiYPRYGMS.
OrthoDBiEOG7BP82N.
TreeFamiTF318198.

Enzyme and pathway databases

ReactomeiREACT_207044. TCF dependent signaling in response to WNT.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_225118. WNT mediated activation of DVL.
REACT_227429. degradation of DVL.

Miscellaneous databases

ChiTaRSiDvl1. mouse.
EvolutionaryTraceiP51141.
NextBioi284142.
PROiP51141.
SOURCEiSearch...

Gene expression databases

BgeeiP51141.
CleanExiMM_DVL1.
ExpressionAtlasiP51141. baseline and differential.
GenevestigatoriP51141.

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.
IPR008340. DVL-1.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF5. PTHR10878:SF5. 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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiDVL1_MOUSE
AccessioniPrimary (citable) accession number: P51141
Secondary accession number(s): Q3U2D3, Q60868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.