Detail Information for IndEnz0002018696
IED ID IndEnz0002018696
Enzyme Type ID protease018696
Protein Name Segment polarity protein dishevelled homolog DVL-3
Dishevelled-3
DSH homolog 3
Gene Name Dvl3
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPEPAPFCADNPSELPPSMERTGGIGDSRPPSFHPHASGGSQENLDNDTETDSLVSAQRERPRRRDGPEHAARLNGTTKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYGGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLTSSLRSHHTHPSYGPPGVPPLYGPPMLMMTPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM
Enzyme Length 716
Uniprot Accession Number Q61062
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Involved in the signal transduction pathway mediated by multiple Wnt genes. {ECO:0000269|PubMed:22227309}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (7); Domain (3); Modified residue (15); Region (2); Sequence conflict (2)
Keywords Cytoplasm;Developmental protein;Methylation;Phosphoprotein;Reference proteome;Ubl conjugation;Wnt signaling pathway
Interact With O35625; Q60838; Q80Z96; Q91ZD4
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
Modified Residue MOD_RES 27; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 48; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 125; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 192; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 212; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 271; /note=Asymmetric dimethylarginine; by PRMT1; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 271; /note=Symmetric dimethylarginine; by PRMT7; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 342; /note=Omega-N-methylarginine; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 342; /note=Symmetric dimethylarginine; by PRMT7; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 346; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 614; /note=Symmetric dimethylarginine; by PRMT7; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 697; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 698; /note=Dimethylated arginine; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 698; /note=Omega-N-methylarginine; alternate; /evidence=ECO:0000250|UniProtKB:Q92997; MOD_RES 700; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q92997
Post Translational Modification PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250|UniProtKB:Q92997}.; PTM: Phosphorylated by CSNK1D. {ECO:0000250|UniProtKB:Q92997}.; PTM: Arginine methylation may function as a switch in regulation of function in Wnt signaling. {ECO:0000250|UniProtKB:Q92997}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10337614; 11274398; 11356022; 12165471; 12421720; 12433684; 15454084; 15637299; 15748172; 16487141; 16501258; 16602821; 16679559; 17005174; 17119020; 18093802; 18187455; 18351675; 18772438; 18799693; 18824165; 19008950; 19701191; 20098415; 20332102; 20558380; 20940260; 20970343; 21092292; 21267068; 21652632; 21677750; 21718540; 21880741; 22234184; 22771245; 22899650; 22940627; 23095888; 23109420; 23122850; 23177622; 23371553; 23437169; 24302887; 24852369; 24952961; 25043421; 25073924; 25198863; 25807483; 29445149; 30022023; 31138536; 31756413; 31884387; 32253237; 32579954; 32805026; 32907846; 33141892; 8973355; 9774969;
Motif
Gene Encoded By
Mass 78,123
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda