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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

Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical 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.3 Publications

GO - Molecular functioni

  • frizzled binding Source: UniProtKB
  • protein binding, bridging Source: ParkinsonsUK-UCL
  • protein domain specific binding Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: UniProtKB
  • Rac GTPase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • 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 GTPase activity Source: ParkinsonsUK-UCL
  • 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
  • protein oligomerization Source: ParkinsonsUK-UCL
  • 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

ReactomeiR-MMU-201688. WNT mediated activation of DVL.
R-MMU-2028269. Signaling by Hippo.
R-MMU-4086400. PCP/CE pathway.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641258. Degradation of DVL.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.

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
Proteomesi
  • UP000000589 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
  • lateral plasma membrane Source: MGI
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15K → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication1
Mutagenesisi17I → A: Reduces oligomerization. Abolishes interaction with DIXDC1. Reduces activation of Wnt signaling. 1 Publication1
Mutagenesisi27Y → D: Loss of oligomerization. Abolishes interaction with DIXDC1. Abolishes activation of Wnt signaling. 1 Publication1
Mutagenesisi56F → H: Reduces oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication1
Mutagenesisi61D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication1
Mutagenesisi63D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication1
Mutagenesisi64F → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1
Mutagenesisi65G → D: Loss of oligomerization. Abolishes activation of Wnt signaling. 1 Publication1
Mutagenesisi66V → D: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication1
Mutagenesisi68K → A: Loss of oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication1
Mutagenesisi84R → A: Strongly reduced interaction with DIXDC1. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001457471 – 736Segment polarity protein dishevelled homolog DVL-2Add BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37Omega-N-methylarginineBy similarity1
Modified residuei59PhosphoserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei211PhosphoserineCombined sources1
Modified residuei231Omega-N-methylarginineBy similarity1
Modified residuei289Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei289Symmetric dimethylarginine; alternateBy similarity1
Modified residuei364PhosphothreonineBy similarity1
Modified residuei632Symmetric dimethylarginineBy similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei718Dimethylated arginine; alternateBy similarity1
Modified residuei718Omega-N-methylarginine; alternateBy similarity1
Modified residuei720PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by CSNK1D (By similarity). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ60838.
MaxQBiQ60838.
PaxDbiQ60838.
PRIDEiQ60838.

PTM databases

iPTMnetiQ60838.
PhosphoSitePlusiQ60838.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSMUSG00000020888.
CleanExiMM_DVL2.
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. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (By similarity).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
WWOXQ9NZC72EBI-641940,EBI-4320739From a different organism.

GO - Molecular functioni

  • frizzled binding Source: UniProtKB
  • protein binding, bridging Source: ParkinsonsUK-UCL
  • protein domain specific binding Source: MGI
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein self-association Source: UniProtKB
  • Rac GTPase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi199343. 19 interactors.
DIPiDIP-29399N.
IntActiQ60838. 25 interactors.
MINTiMINT-1591968.
STRINGi10090.ENSMUSP00000019362.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi423 – 431Combined sources9
Beta strandi435 – 437Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi449 – 454Combined sources6
Helixi455 – 464Combined sources10
Helixi472 – 485Combined sources14
Beta strandi486 – 493Combined sources8
Beta strandi499 – 505Combined sources7
Beta strandi534 – 547Combined sources14
Beta strandi553 – 567Combined sources15
Beta strandi573 – 578Combined sources6
Turni602 – 604Combined sources3
Beta strandi605 – 614Combined sources10
Beta strandi620 – 628Combined sources9
Beta strandi633 – 648Combined sources16
Helixi649 – 651Combined sources3
Beta strandi653 – 661Combined sources9
Beta strandi663 – 675Combined sources13
Beta strandi689 – 697Combined sources9
Beta strandi704 – 710Combined sources7
Beta strandi712 – 714Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ML6X-ray3.50A/B/C/D/E/F417-510[»]
ProteinModelPortaliQ60838.
SMRiQ60838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 93DIXPROSITE-ProRule annotationAdd BLAST83
Domaini267 – 339PDZPROSITE-ProRule annotationAdd BLAST73
Domaini433 – 507DEPPROSITE-ProRule annotationAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 12Poly-Gly6
Compositional biasi112 – 122Poly-ProAdd BLAST11
Compositional biasi235 – 240Poly-Arg6
Compositional biasi686 – 691Poly-Pro6

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

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ60838.
KOiK02353.
OMAiSFHLAMG.
OrthoDBiEOG091G041O.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. 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)DescriptionActionsGraphical viewLength
Sequence conflicti356D → G in AAC52827 (PubMed:8887313).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ML6X-ray3.50A/B/C/D/E/F417-510[»]
ProteinModelPortaliQ60838.
SMRiQ60838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199343. 19 interactors.
DIPiDIP-29399N.
IntActiQ60838. 25 interactors.
MINTiMINT-1591968.
STRINGi10090.ENSMUSP00000019362.

PTM databases

iPTMnetiQ60838.
PhosphoSitePlusiQ60838.

Proteomic databases

EPDiQ60838.
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

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiQ60838.
KOiK02353.
OMAiSFHLAMG.
OrthoDBiEOG091G041O.
TreeFamiTF318198.

Enzyme and pathway databases

ReactomeiR-MMU-201688. WNT mediated activation of DVL.
R-MMU-2028269. Signaling by Hippo.
R-MMU-4086400. PCP/CE pathway.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641258. Degradation of DVL.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

ChiTaRSiDvl2. mouse.
PROiQ60838.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020888.
CleanExiMM_DVL2.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 153 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

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 one 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.