Dvl2

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
Inferred from physical interactionⁱ
- "Direct interaction between NHERF1 and Frizzled regulates beta-catenin signaling."
  Wheeler D.S., Barrick S.R., Grubisha M.J., Brufsky A.M., Friedman P.A., Romero G.
  Oncogene 30:32-42(2011) [PubMed] [Europe PMC] [Abstract]
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- "The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization."
  Schwarz-Romond T., Fiedler M., Shibata N., Butler P.J., Kikuchi A., Higuchi Y., Bienz M.
  Nat Struct Mol Biol 14:484-492(2007) [PubMed] [Europe PMC] [Abstract]
- Ref.10
  "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.
protein domain specific binding
Source: MGI
Inferred from physical interactionⁱ
- "Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions."
  Luo W., Zou H., Jin L., Lin S., Li Q., Ye Z., Rui H., Lin S.C.
  J Biol Chem 280:5054-5060(2005) [PubMed] [Europe PMC] [Abstract]
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- "Wnt-5a induces Dishevelled phosphorylation and dopaminergic differentiation via a CK1-dependent mechanism."
  Bryja V., Schulte G., Rawal N., Grahn A., Arenas E.
  J Cell Sci 120:586-595(2007) [PubMed] [Europe PMC] [Abstract]
protein-macromolecule adaptor activity
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- "Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the differentiation of midbrain dopaminergic neurons."
  Cajanek L., Ganji R.S., Henriques-Oliveira C., Theofilopoulos S., Konik P., Bryja V., Arenas E.
  Mol Cell Biol 33:59-70(2013) [PubMed] [Europe PMC] [Abstract]
protein self-association
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.10
  "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.
small GTPase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- "Tiam1 regulates the Wnt/Dvl/Rac1 signaling pathway and the differentiation of midbrain dopaminergic neurons."
  Cajanek L., Ganji R.S., Henriques-Oliveira C., Theofilopoulos S., Konik P., Bryja V., Arenas E.
  Mol Cell Biol 33:59-70(2013) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein
Biological process	Wnt signaling pathway

Enzyme and pathway databases

Reactomeⁱ	R-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

Reactomeⁱ

R-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
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 11

Organism-specific databases

MGIⁱ	MGI:106613, Dvl2
VEuPathDBⁱ	HostDB:ENSMUSG00000020888

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	15	K → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	17	I → A: Reduces oligomerization. Abolishes interaction with DIXDC1. Reduces activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	27	Y → D: Loss of oligomerization. Abolishes interaction with DIXDC1. Abolishes activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	56	F → H: Reduces oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	61	D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	63	D → A: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	64	F → A: Reduces oligomerization. Reduces activation of Wnt signaling.	1
Mutagenesisⁱ	65	G → D: Loss of oligomerization. Abolishes activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	66	V → D: Reduces oligomerization. Reduces activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	68	K → A: Loss of oligomerization. Strongly reduced activation of Wnt signaling. 1 Publication	1
Mutagenesisⁱ	84	R → A: Strongly reduced interaction with DIXDC1.	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000145747	1 – 736	Segment polarity protein dishevelled homolog DVL-2Add BLAST		736

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	211	PhosphoserineCombined sources		1

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q60838
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q60838
PaxDbⁱ	Q60838
PRIDEⁱ	Q60838
ProteomicsDBⁱ	277616

PTM databases

iPTMnetⁱ	Q60838
PhosphoSitePlusⁱ	Q60838

Expressionⁱ

Tissue specificityⁱ

Ubiquitous.

Gene expression databases

Bgeeⁱ	ENSMUSG00000020888, Expressed in retina and 221 other tissues
Genevisibleⁱ	Q60838, 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).

Interacts with MAPK15 (PubMed:25823377).

Interacts with PKD1 (via extracellular domain) (PubMed:27214281).

Interacts with LMBR1L (PubMed:31073040).

By similarity9 Publications

Binary interactionsⁱ

Hide details

Q60838

With	#Exp.	IntAct
Ankrd6 - isoform 1 [Q69ZU8-1]	3	EBI-641940,EBI-15605686
Dact1 [Q8R4A3]	3	EBI-641940,EBI-3870250
itself	7	EBI-641940,EBI-641940
Dvl3 [Q61062]	3	EBI-641940,EBI-1538450
Vangl1 [Q80Z96]	4	EBI-641940,EBI-1750708
Vangl2 [Q91ZD4]	4	EBI-641940,EBI-1750744
Ap2m1 [P84092] from Rattus norvegicus.	4	EBI-641940,EBI-297693
CSNK1D [P48730] from Homo sapiens.	2	EBI-641940,EBI-751621
CSNK1E [P49674] from Homo sapiens.	3	EBI-641940,EBI-749343
DAAM1 - isoform 1 [Q9Y4D1-1] from Homo sapiens.	4	EBI-641940,EBI-15677700
DIXDC1 [Q155Q3] from Homo sapiens.	4	EBI-641940,EBI-1104700
PLK1 [P53350] from Homo sapiens.	12	EBI-641940,EBI-476768
WWOX [Q9NZC7] from Homo sapiens.	2	EBI-641940,EBI-4320739

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	199343, 22 interactors
CORUMⁱ	Q60838
Database of interacting proteins More...DIPⁱ	DIP-29399N
IntActⁱ	Q60838, 32 interactors
Molecular INTeraction database More...MINTⁱ	Q60838
STRINGⁱ	10090.ENSMUSP00000019362

Miscellaneous databases

RNActⁱ	Q60838, protein

RNActⁱ

Q60838, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	423 – 431	Combined sources	9
Beta strandⁱ	435 – 437	Combined sources	3
Beta strandⁱ	440 – 442	Combined sources	3
Beta strandⁱ	449 – 454	Combined sources	6
Helixⁱ	455 – 464	Combined sources	10
Helixⁱ	472 – 485	Combined sources	14
Beta strandⁱ	486 – 493	Combined sources	8
Beta strandⁱ	499 – 505	Combined sources	7

Show more details

3D structure databases

BMRBⁱ	Q60838
SMRⁱ	Q60838
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	11 – 93	DIXPROSITE-ProRule annotationAdd BLAST	83
Domainⁱ	267 – 339	PDZPROSITE-ProRule annotationAdd BLAST	73
Domainⁱ	433 – 507	DEPPROSITE-ProRule annotationAdd BLAST	75

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	93 – 255	DisorderedSequence analysisAdd BLAST		163
Regionⁱ	558 – 665	DisorderedSequence analysisAdd BLAST		108

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	107 – 123	Pro residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	147 – 174	Basic and acidic residuesSequence analysisAdd BLAST	28
Compositional biasⁱ	575 – 599	Polar residuesSequence analysisAdd BLAST	25
Compositional biasⁱ	602 – 616	Basic and acidic residuesSequence analysisAdd BLAST	15

Domainⁱ

The DIX domain mediates homooligomerization.1 Publication

Sequence similaritiesⁱ

Belongs to the DSH family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3571, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00950000182903
HOGENOMⁱ	CLU_012601_1_0_1
InParanoidⁱ	Q60838
OMAⁱ	FPTYPGS
Database of Orthologous Groups More...OrthoDBⁱ	474724at2759
PhylomeDBⁱ	Q60838
TreeFamⁱ	TF318198

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit 2.30.42.10, 1 hit 2.40.240.130, 1 hit
IDEALⁱ	IID50127
InterProⁱ	View protein in InterPro IPR000591, DEP_dom IPR024580, Dishevelled_C-dom IPR008339, Dishevelled_fam IPR003351, Dishevelled_protein_dom IPR001158, DIX IPR038207, DIX_dom_sf IPR015506, Dsh/Dvl-rel IPR008341, DVL2 IPR001478, PDZ IPR036034, PDZ_sf IPR029071, Ubiquitin-like_domsf IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf
PANTHERⁱ	PTHR10878, PTHR10878, 1 hit PTHR10878:SF8, PTHR10878:SF8, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00610, DEP, 1 hit PF02377, Dishevelled, 1 hit PF00778, DIX, 1 hit PF12316, Dsh_C, 1 hit PF00595, PDZ, 1 hit
PRINTSⁱ	PR01760, DISHEVELLED PR01762, DISHEVELLED2
SMARTⁱ	View protein in SMART SM00021, DAX, 1 hit SM00049, DEP, 1 hit SM00228, PDZ, 1 hit
SUPFAMⁱ	SSF46785, SSF46785, 1 hit SSF50156, SSF50156, 1 hit SSF54236, SSF54236, 1 hit
PROSITEⁱ	View protein in PROSITE PS50186, DEP, 1 hit PS50841, DIX, 1 hit PS50106, PDZ, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q60838-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	356	D → G in AAC52827 (PubMed:8887313).Curated		1

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 No translation available. CH466596 Genomic DNA Translation: EDL12520.1 BC053050 mRNA Translation: AAH53050.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS24930.1
NCBI Reference Sequences More...RefSeqⁱ	NP_031914.3, NM_007888.3

Genome annotation databases

Ensemblⁱ	ENSMUST00000019362; ENSMUSP00000019362; ENSMUSG00000020888 ENSMUST00000102575; ENSMUSP00000099635; ENSMUSG00000020888 ENSMUST00000190940; ENSMUSP00000140073; ENSMUSG00000020888
GeneIDⁱ	13543
KEGGⁱ	mmu:13543
UCSC genome browser More...UCSCⁱ	uc007jtm.1, mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q60838	Dishevelled segment polarity protein 2		MUSSI		736	UniRef100_Q60838
Uncharacterized protein		MOUSE		345

Protein	Similar proteins		Species	Score	Length	Source
Q60838	Segment polarity protein dishevelled homolog DVL-2	)	HUMAN		736	UniRef90_O14641
Dishevelled segment polarity protein 2		PANTR		736
Dishevelled segment polarity protein 2		PANPA		736
segment polarity protein dishevelled homolog DVL-2 isoform X3		TURTR		786
Dishevelled segment polarity protein 2		CAPHI		781
+278

Protein	Similar proteins		Species	Score	Length	Source
Q60838	Segment polarity protein dishevelled homolog DVL-2	)	HUMAN		736	UniRef50_O14641
Dishevelled segment polarity protein 2		PANTR		736
Dishevelled segment polarity protein 2		PANPA		736
segment polarity protein dishevelled homolog DVL-2 isoform X3		TURTR		786
Dishevelled segment polarity protein 2		CAPHI		781
+631

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 No translation available. CH466596 Genomic DNA Translation: EDL12520.1 BC053050 mRNA Translation: AAH53050.1
CCDSⁱ	CCDS24930.1
RefSeqⁱ	NP_031914.3, NM_007888.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3ML6	X-ray	3.50	A/B/C/D/E/F	417-510	[»]
	6VCC	electron microscopy	3.60	A/B/C/D/E/F/G/H/I/J/K/L	12-92	[»]
BMRBⁱ	Q60838
SMRⁱ	Q60838
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	199343, 22 interactors
CORUMⁱ	Q60838
DIPⁱ	DIP-29399N
IntActⁱ	Q60838, 32 interactors
MINTⁱ	Q60838
STRINGⁱ	10090.ENSMUSP00000019362

PTM databases

iPTMnetⁱ	Q60838
PhosphoSitePlusⁱ	Q60838

Proteomic databases

EPDⁱ	Q60838
MaxQBⁱ	Q60838
PaxDbⁱ	Q60838
PRIDEⁱ	Q60838
ProteomicsDBⁱ	277616

Protocols and materials databases

Antibodypediaⁱ	3985, 479 antibodies from 39 providers
The DNASU plasmid repository More...DNASUⁱ	13543

Genome annotation databases

Ensemblⁱ	ENSMUST00000019362; ENSMUSP00000019362; ENSMUSG00000020888 ENSMUST00000102575; ENSMUSP00000099635; ENSMUSG00000020888 ENSMUST00000190940; ENSMUSP00000140073; ENSMUSG00000020888
GeneIDⁱ	13543
KEGGⁱ	mmu:13543
UCSCⁱ	uc007jtm.1, mouse

Organism-specific databases

CTDⁱ	1856
MGIⁱ	MGI:106613, Dvl2
VEuPathDBⁱ	HostDB:ENSMUSG00000020888

Phylogenomic databases

eggNOGⁱ	KOG3571, Eukaryota
GeneTreeⁱ	ENSGT00950000182903
HOGENOMⁱ	CLU_012601_1_0_1
InParanoidⁱ	Q60838
OMAⁱ	FPTYPGS
OrthoDBⁱ	474724at2759
PhylomeDBⁱ	Q60838
TreeFamⁱ	TF318198

Enzyme and pathway databases

Reactomeⁱ	R-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

Reactomeⁱ

R-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

BioGRID-ORCSⁱ	13543, 0 hits in 49 CRISPR screens
ChiTaRSⁱ	Dvl2, mouse
Protein Ontology More...PROⁱ	PR:Q60838
RNActⁱ	Q60838, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000020888, Expressed in retina and 221 other tissues
Genevisibleⁱ	Q60838, MM

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit 2.30.42.10, 1 hit 2.40.240.130, 1 hit
IDEALⁱ	IID50127
InterProⁱ	View protein in InterPro IPR000591, DEP_dom IPR024580, Dishevelled_C-dom IPR008339, Dishevelled_fam IPR003351, Dishevelled_protein_dom IPR001158, DIX IPR038207, DIX_dom_sf IPR015506, Dsh/Dvl-rel IPR008341, DVL2 IPR001478, PDZ IPR036034, PDZ_sf IPR029071, Ubiquitin-like_domsf IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf
PANTHERⁱ	PTHR10878, PTHR10878, 1 hit PTHR10878:SF8, PTHR10878:SF8, 1 hit
Pfamⁱ	View protein in Pfam PF00610, DEP, 1 hit PF02377, Dishevelled, 1 hit PF00778, DIX, 1 hit PF12316, Dsh_C, 1 hit PF00595, PDZ, 1 hit
PRINTSⁱ	PR01760, DISHEVELLED PR01762, DISHEVELLED2
SMARTⁱ	View protein in SMART SM00021, DAX, 1 hit SM00049, DEP, 1 hit SM00228, PDZ, 1 hit
SUPFAMⁱ	SSF46785, SSF46785, 1 hit SSF50156, SSF50156, 1 hit SSF54236, SSF54236, 1 hit
PROSITEⁱ	View protein in PROSITE PS50186, DEP, 1 hit PS50841, DIX, 1 hit PS50106, PDZ, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DVL2_MOUSE
Accessionⁱ	Q60838Primary (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:	February 23, 2022
	This is version 189 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q60838 (DVL2_MOUSE)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Segment polarity protein dishevelled homolog DVL-2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Plasma membrane

Nucleus

Other locations

Cytoskeleton

Cytosol

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Q60838

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ