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Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

Dvl2

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. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes.3 Publications

GO - Molecular functioni

  • frizzled binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein domain specific binding Source: MGI
  • protein self-association Source: UniProtKB

GO - Biological processi

  • canonical Wnt signaling pathway Source: MGI
  • canonical Wnt signaling pathway involved in regulation of cell proliferation Source: MGI
  • cellular protein localization Source: MGI
  • cochlea morphogenesis Source: MGI
  • convergent extension involved in neural plate elongation Source: MGI
  • convergent extension involved in organogenesis Source: MGI
  • heart development Source: MGI
  • heart morphogenesis Source: MGI
  • intracellular signal transduction Source: InterPro
  • neural tube closure Source: MGI
  • non-canonical Wnt signaling pathway Source: MGI
  • outflow tract morphogenesis Source: BHF-UCL
  • planar cell polarity pathway involved in neural tube closure Source: MGI
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of JUN kinase activity Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of protein tyrosine kinase activity Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • segmentation Source: BHF-UCL
  • segment specification Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • Wnt signaling pathway Source: BHF-UCL
  • 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_274512. negative regulation of TCF-dependent signaling by DVL-interacting proteins.
REACT_297888. degradation of DVL.
REACT_299462. WNT5A-dependent internalization of FZD4.
REACT_301726. Signaling by Hippo.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_333985. PCP/CE pathway.
REACT_335672. TCF dependent signaling in response to WNT.
REACT_337993. WNT mediated activation of DVL.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-2
Short name:
Dishevelled-2
Alternative name(s):
DSH homolog 2
Gene namesi
Name:Dvl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:106613. Dvl2.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • cell cortex Source: MGI
  • clathrin-coated vesicle Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: MGI
  • cytoskeleton Source: BHF-UCL
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151K → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi17 – 171I → A: Reduces oligomerization. Abolishes interaction with DIXDC1. Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi27 – 271Y → D: Loss of oligomerization. Abolishes interaction with DIXDC1. Abolishes activation of Wnt signaling. 1 Publication
Mutagenesisi56 – 561F → H: Reduces oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication
Mutagenesisi61 – 611D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi63 – 631D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi64 – 641F → A: Reduces oligomerization. Reduces activation of Wnt signaling.
Mutagenesisi65 – 651G → D: Loss of oligomerization. Abolishes activation of Wnt signaling. 1 Publication
Mutagenesisi66 – 661V → D: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication
Mutagenesisi68 – 681K → A: Loss of oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication
Mutagenesisi84 – 841R → A: Strongly reduced interaction with DIXDC1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Segment polarity protein dishevelled homolog DVL-2PRO_0000145747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Omega-N-methylarginineBy similarity
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei231 – 2311Omega-N-methylarginineBy similarity
Modified residuei289 – 2891Asymmetric dimethylarginine; alternateBy similarity
Modified residuei289 – 2891Symmetric dimethylarginine; alternateBy similarity
Modified residuei364 – 3641PhosphothreonineBy similarity
Modified residuei632 – 6321Symmetric dimethylarginineBy similarity
Modified residuei718 – 7181Dimethylated arginine; alternateBy similarity
Modified residuei718 – 7181Omega-N-methylarginine; alternateBy similarity
Modified residuei720 – 7201PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CSNK1D.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ60838.
PaxDbiQ60838.
PRIDEiQ60838.

PTM databases

PhosphoSiteiQ60838.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ60838.
CleanExiMM_DVL2.
ExpressionAtlasiQ60838. baseline and differential.
GenevisibleiQ60838. MM.

Interactioni

Subunit structurei

Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). Can form large oligomers (via DIX domain). Interacts (via DIX domain) with DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the AP-2 complex. Interacts with FAM105B/otulin. Interacts with DCDC2.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-641940,EBI-641940
CSNK1DP487302EBI-641940,EBI-751621From a different organism.
CSNK1EP496743EBI-641940,EBI-749343From a different organism.
Dact1Q8R4A33EBI-641940,EBI-3870250
DIXDC1Q155Q34EBI-641940,EBI-1104700From a different organism.
Dvl3Q610623EBI-641940,EBI-1538450
PLK1P5335012EBI-641940,EBI-476768From a different organism.
Vangl1Q80Z964EBI-641940,EBI-1750708
Vangl2Q91ZD44EBI-641940,EBI-1750744

Protein-protein interaction databases

BioGridi199343. 18 interactions.
DIPiDIP-29399N.
IntActiQ60838. 23 interactions.
MINTiMINT-1591968.
STRINGi10090.ENSMUSP00000019362.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi423 – 4319Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi449 – 4546Combined sources
Helixi455 – 46410Combined sources
Helixi472 – 48514Combined sources
Beta strandi486 – 4938Combined sources
Beta strandi499 – 5057Combined sources
Beta strandi534 – 54714Combined sources
Beta strandi553 – 56715Combined sources
Beta strandi573 – 5797Combined sources
Turni602 – 6043Combined sources
Beta strandi605 – 61410Combined sources
Beta strandi620 – 6289Combined sources
Beta strandi633 – 64816Combined sources
Helixi649 – 6513Combined sources
Beta strandi653 – 6619Combined sources
Beta strandi663 – 67513Combined sources
Beta strandi689 – 6979Combined sources
Beta strandi704 – 7107Combined sources
Beta strandi712 – 7143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML6X-ray3.50A/B/C/D/E/F417-510[»]
ProteinModelPortaliQ60838.
SMRiQ60838. Positions 13-90, 263-353, 421-582.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9383DIXPROSITE-ProRule annotationAdd
BLAST
Domaini267 – 33973PDZPROSITE-ProRule annotationAdd
BLAST
Domaini433 – 50775DEPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 126Poly-Gly
Compositional biasi112 – 12211Poly-ProAdd
BLAST
Compositional biasi235 – 2406Poly-Arg
Compositional biasi686 – 6916Poly-Pro

Domaini

The DIX domain mediates homooligomerization.1 Publication

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.
InParanoidiQ60838.
KOiK02353.
OMAiSFHLAMG.
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.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 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.
PR01762. DISHEVELLED2.
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.

Q60838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSSAGGGG VGETKVIYHL DEEETPYLVK IPVPAERITL GDFKSVLQRP
60 70 80 90 100
AGAKYFFKSM DQDFGVVKEE ISDDNARLPC FNGRVVSWLV SSDTPQPEVA
110 120 130 140 150
PPAHESRTEL VPPPPPLPPL PPERTSGIGD SRPPSFHPNV SSSHENLEPE
160 170 180 190 200
TETESVVSLR RDRPRRRDSS EHGAGGHRPG GPSRLERHLA GYESSSTLMT
210 220 230 240 250
SELESTSLGD SDEDDTMSRF SSSTEQSSAS RLLKRHRRRR KQRPPRMERT
260 270 280 290 300
SSFSSVTDST MSLNIITVTL NMEKYNFLGI SIVGQSNERG DGGIYIGSIM
310 320 330 340 350
KGGAVAADGR IEPGDMLLQV NDMNFENMSN DDAVRVLRDI VHKPGPIVLT
360 370 380 390 400
VAKCWDPSPQ AYFTLPRNEP IQPIDPAAWV SHSAALTGAF PAYPGSSSMS
410 420 430 440 450
TITSGSSLPD GCEGRGLSVH MDMASVTKAM AAPESGLEVR DRMWLKITIP
460 470 480 490 500
NAFLGSDVVD WLYHHVEGFP ERREARKYAS GLLKAGLIRH TVNKITFSEQ
510 520 530 540 550
CYYVFGDLSG GCESYLVNLS LNDNDGSSGA SDQDTLAPLP GATPWPLLPT
560 570 580 590 600
FSYQYPAPHP YSPQPPPYHE LSSYTYGGGS ASSQHSEGSR SSGSTRSDGG
610 620 630 640 650
AGRTGRPEER APESKSGSGS ESELSSRGGS LRRGGEPGGT GDGGPPPSRG
660 670 680 690 700
STGAPPNLRA LPGLHPYGAP SGMALPYNPM MVVMMPPPPP PVSTAVQPPG
710 720 730
APPVRDLGSV PPELTASRQS FHMAMGNPSE FFVDVM
Length:736
Mass (Da):78,861
Last modified:July 27, 2011 - v2
Checksum:i928A527143BBBBB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561D → G in AAC52827 (PubMed:8887313).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24160 mRNA. Translation: AAC52827.1.
AK146822 mRNA. Translation: BAE27460.1.
AK159895 mRNA. Translation: BAE35461.1.
AK168376 mRNA. Translation: BAE40307.1.
AL596185 Genomic DNA. Translation: CAI35165.1.
CH466596 Genomic DNA. Translation: EDL12520.1.
BC053050 mRNA. Translation: AAH53050.1.
CCDSiCCDS24930.1.
RefSeqiNP_031914.3. NM_007888.3.
UniGeneiMm.5114.

Genome annotation databases

EnsembliENSMUST00000019362; ENSMUSP00000019362; ENSMUSG00000020888.
ENSMUST00000102575; ENSMUSP00000099635; ENSMUSG00000020888.
ENSMUST00000190940; ENSMUSP00000140073; ENSMUSG00000020888.
GeneIDi13543.
KEGGimmu:13543.
UCSCiuc007jtm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24160 mRNA. Translation: AAC52827.1.
AK146822 mRNA. Translation: BAE27460.1.
AK159895 mRNA. Translation: BAE35461.1.
AK168376 mRNA. Translation: BAE40307.1.
AL596185 Genomic DNA. Translation: CAI35165.1.
CH466596 Genomic DNA. Translation: EDL12520.1.
BC053050 mRNA. Translation: AAH53050.1.
CCDSiCCDS24930.1.
RefSeqiNP_031914.3. NM_007888.3.
UniGeneiMm.5114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML6X-ray3.50A/B/C/D/E/F417-510[»]
ProteinModelPortaliQ60838.
SMRiQ60838. Positions 13-90, 263-353, 421-582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199343. 18 interactions.
DIPiDIP-29399N.
IntActiQ60838. 23 interactions.
MINTiMINT-1591968.
STRINGi10090.ENSMUSP00000019362.

PTM databases

PhosphoSiteiQ60838.

Proteomic databases

MaxQBiQ60838.
PaxDbiQ60838.
PRIDEiQ60838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019362; ENSMUSP00000019362; ENSMUSG00000020888.
ENSMUST00000102575; ENSMUSP00000099635; ENSMUSG00000020888.
ENSMUST00000190940; ENSMUSP00000140073; ENSMUSG00000020888.
GeneIDi13543.
KEGGimmu:13543.
UCSCiuc007jtm.1. mouse.

Organism-specific databases

CTDi1856.
MGIiMGI:106613. Dvl2.

Phylogenomic databases

eggNOGiNOG322275.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ60838.
KOiK02353.
OMAiSFHLAMG.
OrthoDBiEOG7BP82N.
TreeFamiTF318198.

Enzyme and pathway databases

ReactomeiREACT_274512. negative regulation of TCF-dependent signaling by DVL-interacting proteins.
REACT_297888. degradation of DVL.
REACT_299462. WNT5A-dependent internalization of FZD4.
REACT_301726. Signaling by Hippo.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_333985. PCP/CE pathway.
REACT_335672. TCF dependent signaling in response to WNT.
REACT_337993. WNT mediated activation of DVL.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiDvl2. mouse.
NextBioi284146.
PROiQ60838.
SOURCEiSearch...

Gene expression databases

BgeeiQ60838.
CleanExiMM_DVL2.
ExpressionAtlasiQ60838. baseline and differential.
GenevisibleiQ60838. MM.

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.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 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.
PR01762. DISHEVELLED2.
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. "Conservation of dishevelled structure and function between flies and mice: isolation and characterization of Dvl2."
    Klingensmith J., Yang Y., Axelrod J.D., Beier D.R., Perrimon N., Sussman D.J.
    Mech. Dev. 58:15-26(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "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: C57BL/6J.
    Tissue: Amnion and Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. 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].
  5. "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].
    Strain: C57BL/6.
  6. "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
    Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
    J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIXDC1 AND RAC.
  7. "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.
  8. "Association of Dishevelled with the clathrin AP-2 adaptor is required for Frizzled endocytosis and planar cell polarity signaling."
    Yu A., Rual J.F., Tamai K., Harada Y., Vidal M., He X., Kirchhausen T.
    Dev. Cell 12:129-141(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE AP-2 COMPLEX.
  9. "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: FUNCTION, INTERACTION WITH DIXDC1, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-15; ILE-17; TYR-27; PHE-56; ASP-61; ASP-63; GLY-65; VAL-66 AND LYS-68, DOMAIN.
  10. Cited for: INTERACTION WITH FAM105B.
  11. "Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling."
    Yu A., Xing Y., Harrison S.C., Kirchhausen T.
    Structure 18:1311-1320(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 417-510 IN COMPLEX WITH AP2M1, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDVL2_MOUSE
AccessioniPrimary (citable) accession number: Q60838
Secondary accession number(s): Q7TN14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 138 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.