O14641 · DVL2_HUMAN
- ProteinSegment polarity protein dishevelled homolog DVL-2
- GeneDVL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids736 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSegment polarity protein dishevelled homolog DVL-2
- Short namesDishevelled-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO14641
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity).
Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136).
Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 250 | No effect on interaction with FOXK2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 250-252 | Almost abolishes interaction with FOXK2. | ||||
Sequence: TSS → AAA | ||||||
Mutagenesis | 251 | No effect on interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 252 | Almost abolishes interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 254 | Reduces interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 254-257 | Almost abolishes interaction with FOXK2. | ||||
Sequence: SSVT → AAVA | ||||||
Mutagenesis | 255 | Almost abolishes interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 257 | Almost abolishes interaction with FOXK2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 259 | Almost abolishes interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 259-262 | Almost abolishes interaction with FOXK2. | ||||
Sequence: STMS → AAMA | ||||||
Mutagenesis | 260 | No effect on interaction with FOXK2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 262 | Almost abolishes interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 267 | Almost abolishes interaction with FOXK2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 267-269 | Almost abolishes interaction with FOXK2. | ||||
Sequence: TVT → AVA | ||||||
Mutagenesis | 269 | Almost abolishes interaction with FOXK2. | ||||
Sequence: T → A | ||||||
Mutagenesis | 275 | No effect on interaction with FOXK2. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 281 | No effect on interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_064708 | 282 | found in a renal cell carcinoma case; somatic mutation | |||
Sequence: I → T | ||||||
Mutagenesis | 286 | No effect on interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 295 | No effect on interaction with FOXK2. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 298 | No effect on interaction with FOXK2. | ||||
Sequence: S → A | ||||||
Mutagenesis | 329 | No effect on interaction with FOXK2. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 904 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000145746 | 1-736 | UniProt | Segment polarity protein dishevelled homolog DVL-2 | |||
Sequence: MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHTDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 211 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 640 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 641 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 715 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 717 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by CSNK1D (PubMed:21422228, PubMed:9192851).
WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (PubMed:25805136).
WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (PubMed:25805136).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
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 (By similarity).
Interacts with DACT1 and FAM105B/otulin. Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (PubMed:25805136).
Interacts with MAPK15 (By similarity).
Interacts with PKD1 (via extracellular domain) (PubMed:27214281).
Interacts with LMBR1L (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 (By similarity).
Interacts with DACT1 and FAM105B/otulin. Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (PubMed:25805136).
Interacts with MAPK15 (By similarity).
Interacts with PKD1 (via extracellular domain) (PubMed:27214281).
Interacts with LMBR1L (By similarity).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-93 | DIX | ||||
Sequence: VGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSD | ||||||
Region | 92-254 | Disordered | ||||
Sequence: SDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFS | ||||||
Compositional bias | 99-123 | Pro residues | ||||
Sequence: MAPPVHEPRAELAPPAPPLPPLPPE | ||||||
Compositional bias | 147-174 | Basic and acidic residues | ||||
Sequence: LEPETETESVVSLRRERPRRRDSSEHGA | ||||||
Region | 250-355 | Required for interaction with FOXK2 | ||||
Sequence: TSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCW | ||||||
Domain | 267-339 | PDZ | ||||
Sequence: TVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRD | ||||||
Domain | 433-507 | DEP | ||||
Sequence: PESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGD | ||||||
Region | 558-675 | Disordered | ||||
Sequence: PHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMAL | ||||||
Compositional bias | 575-599 | Polar residues | ||||
Sequence: TYGGGSASSQHSEGSRSSGSTRSDG | ||||||
Compositional bias | 602-616 | Basic and acidic residues | ||||
Sequence: GRTGRPEERAPESKS |
Domain
The DIX domain mediates homooligomerization.
Sequence similarities
Belongs to the DSH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length736
- Mass (Da)78,948
- Last updated1998-01-01 v1
- Checksum4BAD95B6C3FE531B
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 99-123 | Pro residues | ||||
Sequence: MAPPVHEPRAELAPPAPPLPPLPPE | ||||||
Compositional bias | 147-174 | Basic and acidic residues | ||||
Sequence: LEPETETESVVSLRRERPRRRDSSEHGA | ||||||
Compositional bias | 575-599 | Polar residues | ||||
Sequence: TYGGGSASSQHSEGSRSSGSTRSDG | ||||||
Compositional bias | 602-616 | Basic and acidic residues | ||||
Sequence: GRTGRPEERAPESKS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF006012 EMBL· GenBank· DDBJ | AAB65243.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009822 EMBL· GenBank· DDBJ | AAP88824.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471108 EMBL· GenBank· DDBJ | EAW90245.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC014844 EMBL· GenBank· DDBJ | AAH14844.1 EMBL· GenBank· DDBJ | mRNA |