| 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 |