Detail Information for IndEnz0002018468
IED ID IndEnz0002018468
Enzyme Type ID protease018468
Protein Name Segment polarity protein dishevelled homolog DVL-3
Dishevelled-3
DSH homolog 3
Gene Name DVL3 KIAA0208
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPDPAPFCADNPSELPPPMERTGGIGDSRPPSFHPHAGGGSQENLDNDTETDSLVSAQRERPRRRDGPEHATRLNGTAKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYGGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLASSLRSHHTHPSYGPPGVPPLYGPPMLMMPPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM
Enzyme Length 716
Uniprot Accession Number Q92997
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:0000250|UniProtKB:Q61062}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Compositional bias (6); Domain (3); Erroneous initiation (1); Modified residue (15); Mutagenesis (3); Natural variant (2); Region (2); Sequence conflict (22)
Keywords 3D-structure;Alternative splicing;Cytoplasm;Developmental protein;Dwarfism;Methylation;Phosphoprotein;Reference proteome;Ubl conjugation;Wnt signaling pathway
Interact With Q9ULW3; O75689; Q02040; Q8N2N9-4; Q9Y2T2; P05067; Q8TBE0; Q8N7W2-2; O14503; Q9HC52; Q9UK58; Q8N8U2; Q9UPV0; Q8IYX8; Q8NHQ1; Q8TAP6; P49759-3; P21964-2; P48730; P49674; P68400; P0DMU9; Q8NHU0; A8MQ03; O14640; Q86TH3; O60739; O15371; Q8NE31; Q86YD7; O95363; O43320; Q96Q35-2; Q8TAE8; P28799-2; Q9NSC5; P20719; Q00444; P31273; Q9C086; Q8WXH2; Q674X7-2; Q9H3F6; Q96MP8-2; O60333-2; Q13351; Q9UIH9; P57682; O43474; Q53G59; Q96PV6; Q17RB8; Q9Y608; Q5S007; Q9P127; Q8N8X9; O15481; Q96A72; Q9BU76; P23511-2; Q969G9; Q9UGY1; Q9UBU9; Q9HBE1-4; Q5T6S3; P78337; Q9UPG8; Q96T60; Q96T49; Q96MT3; P54646; Q99633; O43395; Q8WWY3; Q8NAV1; P60891; Q9NZ81; P86480; P61289; Q8NDT2-2; Q14498; Q2KHN1; P62913-2; O43159; P57060; Q9HAJ7; Q9NUL5-4; Q96EB6; Q8TAD8; Q96L94-2; O60504; P27105; O43463; Q5T7P8-2; Q96C24; P62380; Q15560; Q8N8B7-2; Q92734; Q9BT49; Q08117-2; Q8WVP5; P09430; Q12933; Q8WV44; Q15631; Q6FI91; Q8N831; Q9NQZ2; Q5SQQ9-2; Q64LD2-2; O76024; P19544; P23025; Q96MU7; O43167; Q9HCK0; Q9UFB7; P10074; Q96BR9; Q9NU63-3; P49910; Q9BSG1; O43296; Q14C61; Q9P2F9; Q9H9D4; Q8TAU3; Q8N8Z8; Q8N0Y2-2; Q6ZNH5; Q9H707; Q9P0T4; Q5T619; Q9H7X3; Q8N508; Q32M78; Q9NQZ8; Q96H86; Q6NX45; Q96BV0; Q3KQV3; O75541-2; Q96EG3; Q15696; Q9Y5A6; P10073; Q6NSZ9-2; P98078
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
Modified Residue MOD_RES 27; /note="Omega-N-methylarginine"; /evidence="ECO:0000269|PubMed:22612246"; MOD_RES 48; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 125; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 192; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22612246, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"; MOD_RES 212; /note="Omega-N-methylarginine"; /evidence="ECO:0000269|PubMed:22612246"; MOD_RES 271; /note="Asymmetric dimethylarginine; by PRMT1; alternate"; /evidence="ECO:0000269|PubMed:23150776"; MOD_RES 271; /note="Symmetric dimethylarginine; by PRMT7; alternate"; /evidence="ECO:0000269|PubMed:23150776"; MOD_RES 342; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|PubMed:22612246, ECO:0000269|PubMed:23150776"; MOD_RES 342; /note="Symmetric dimethylarginine; by PRMT7; alternate"; /evidence="ECO:0000269|PubMed:22612246, ECO:0000269|PubMed:23150776"; MOD_RES 346; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:22612246"; MOD_RES 614; /note="Symmetric dimethylarginine; by PRMT7"; /evidence="ECO:0000269|PubMed:23150776"; MOD_RES 697; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 698; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000269|PubMed:22612246"; MOD_RES 698; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|PubMed:22612246"; MOD_RES 700; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:22612246"
Post Translational Modification PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains. {ECO:0000269|PubMed:20227366}.; PTM: Phosphorylated by CSNK1D. {ECO:0000269|PubMed:21422228, ECO:0000269|PubMed:22612246}.; PTM: Arginine methylation may function as a switch in regulation of function in Wnt signaling. {ECO:0000269|PubMed:22612246, ECO:0000269|PubMed:23150776}.
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 6V7O; 6ZC6; 6ZC8;
Mapped Pubmed ID 10330181; 10421629; 10517632; 10535959; 10644691; 10698942; 10944533; 11101902; 11336703; 11358862; 11425858; 11751577; 11779461; 11818547; 12015986; 12134165; 12533515; 12556519; 12716910; 14636582; 14731402; 14750955; 15084453; 15108311; 15143170; 15231748; 15459103; 15501440; 15608632; 15936275; 16169070; 16189514; 16329988; 16341016; 16341017; 16547521; 16636067; 16762923; 16965538; 17021034; 17030191; 17130287; 17234765; 17318175; 17373907; 17529994; 17569865; 17627283; 18077588; 18093802; 18162551; 18256687; 18339531; 18347018; 18362152; 18692936; 18719708; 18772438; 18798527; 19107203; 19365405; 19379695; 19447967; 19523939; 19561074; 19589360; 19625296; 20006983; 20064372; 20137080; 20412773; 20711500; 20803696; 21031079; 21183070; 21183076; 21252990; 21285348; 21667018; 21900206; 21988832; 22411803; 22569537; 22643886; 22682247; 22892949; 23022960; 23109420; 23256519; 23301094; 23396967; 23821037; 24040443; 24366813; 24427302; 24993822; 25156800; 25168481; 25416956; 25847080; 26008736; 26496610; 26638075; 26792835; 27008544; 27086035; 27744318; 28107606; 28455968; 28705114; 29575616; 30242173; 30266990; 30536315; 31000703; 31870452; 32032490; 32414668; 32900645; 33038884; 33496066; 7744250; 8947551; 9214626; 9520479; 9674432; 9716412;
Motif
Gene Encoded By
Mass 78,055
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda