DVL3_HUMAN
ID DVL3_HUMAN Reviewed; 716 AA.
AC Q92997; B4E3E5; D3DNT0; O14642; Q13531; Q8N5E9; Q92607;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-3;
DE Short=Dishevelled-3;
DE AltName: Full=DSH homolog 3;
GN Name=DVL3; Synonyms=KIAA0208;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8817329; DOI=10.1093/hmg/5.7.953;
RA Pizzuti A., Amati F., Calabrese G., Mari A., Colosimo A., Silani V.,
RA Giardino L., Ratti A., Penso D., Calza L., Palka G., Scarlato G.,
RA Novelli G., Dallapiccola B.;
RT "cDNA characterization and chromosomal mapping of two human homologues of
RT the Drosophila dishevelled polarity gene.";
RL Hum. Mol. Genet. 5:953-958(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9344861; DOI=10.1006/bbrc.1997.7500;
RA Bui T.D., Beier D.R., Jonssen M., Smith K., Dorrington S.M., Kaklamanis L.,
RA Kearney L., Regan R., Sussman D.J., Harris A.L.;
RT "cDNA cloning of a human dishevelled DVL-3 gene, mapping to 3q27, and
RT expression in human breast and colon carcinomas.";
RL Biochem. Biophys. Res. Commun. 239:510-516(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9192851; DOI=10.1006/geno.1997.4713;
RA Semenov M.V., Snyder M.;
RT "Human dishevelled genes constitute a DHR-containing multigene family.";
RL Genomics 42:302-310(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-433.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH DAB2.
RX PubMed=12805222; DOI=10.1093/emboj/cdg286;
RA Howe P.H.;
RT "Regulation of the Wnt signaling pathway by disabled-2 (Dab2).";
RL EMBO J. 22:3084-3094(2003).
RN [10]
RP INTERACTION WITH LRRFIP2.
RX PubMed=15677333; DOI=10.1073/pnas.0409472102;
RA Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S.,
RA Schultz P.G.;
RT "Identification of the Wnt signaling activator leucine-rich repeat in
RT Flightless interaction protein 2 by a genome-wide functional analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH CYLD.
RX PubMed=20227366; DOI=10.1016/j.molcel.2010.01.035;
RA Tauriello D.V., Haegebarth A., Kuper I., Edelmann M.J., Henraat M.,
RA Canninga-van Dijk M.R., Kessler B.M., Clevers H., Maurice M.M.;
RT "Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling
RT through K63-linked ubiquitination of Dvl.";
RL Mol. Cell 37:607-619(2010).
RN [13]
RP PHOSPHORYLATION BY CSNK1D/CK1.
RX PubMed=21422228; DOI=10.1083/jcb.201011111;
RA Greer Y.E., Rubin J.S.;
RT "Casein kinase 1 delta functions at the centrosome to mediate Wnt-3a-
RT dependent neurite outgrowth.";
RL J. Cell Biol. 192:993-1004(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH CEP164.
RX PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA Hildebrandt F.;
RT "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT ciliopathies to DNA damage response signaling.";
RL Cell 150:533-548(2012).
RN [16]
RP PHOSPHORYLATION AT SER-192; THR-346 AND SER-700, AND METHYLATION AT ARG-27;
RP ARG-212; ARG-342 AND ARG-698.
RX PubMed=22612246; DOI=10.1021/pr300314d;
RA Wu C., Wei W., Li C., Li Q., Sheng Q., Zeng R.;
RT "Delicate analysis of post-translational modifications on Dishevelled 3.";
RL J. Proteome Res. 11:3829-3837(2012).
RN [17]
RP METHYLATION AT ARG-271; ARG-342 AND ARG-614, AND MUTAGENESIS OF ARG-271;
RP ARG-342 AND ARG-614.
RX PubMed=23150776; DOI=10.1038/srep00805;
RA Bikkavilli R.K., Avasarala S., Vanscoyk M., Sechler M., Kelley N.,
RA Malbon C.C., Winn R.A.;
RT "Dishevelled3 is a novel arginine methyl transferase substrate.";
RL Sci. Rep. 2:805-805(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-697, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP INTERACTION WITH DCDC2.
RX PubMed=25557784; DOI=10.1016/j.ajhg.2014.12.002;
RA Schueler M., Braun D.A., Chandrasekar G., Gee H.Y., Klasson T.D.,
RA Halbritter J., Bieder A., Porath J.D., Airik R., Zhou W., LoTurco J.J.,
RA Che A., Otto E.A., Boeckenhauer D., Sebire N.J., Honzik T., Harris P.C.,
RA Koon S.J., Gunay-Aygun M., Saunier S., Zerres K., Bruechle N.O.,
RA Drenth J.P., Pelletier L., Tapia-Paez I., Lifton R.P., Giles R.H., Kere J.,
RA Hildebrandt F.;
RT "DCDC2 mutations cause a renal-hepatic ciliopathy by disrupting Wnt
RT signaling.";
RL Am. J. Hum. Genet. 96:81-92(2015).
RN [21]
RP INTERACTION WITH FOXK1 AND FOXK2.
RX PubMed=25805136; DOI=10.1016/j.devcel.2015.01.031;
RA Wang W., Li X., Lee M., Jun S., Aziz K.E., Feng L., Tran M.K., Li N.,
RA McCrea P.D., Park J.I., Chen J.;
RT "FOXKs promote Wnt/beta-catenin signaling by translocating DVL into the
RT nucleus.";
RL Dev. Cell 32:707-718(2015).
RN [22]
RP INVOLVEMENT IN DRS3.
RX PubMed=26924530; DOI=10.1016/j.ajhg.2016.01.005;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA White J.J., Mazzeu J.F., Hoischen A., Bayram Y., Withers M., Gezdirici A.,
RA Kimonis V., Steehouwer M., Jhangiani S.N., Muzny D.M., Gibbs R.A.,
RA van Bon B.W., Sutton V.R., Lupski J.R., Brunner H.G., Carvalho C.M.;
RT "DVL3 alleles resulting in a -1 frameshift of the last exon mediate
RT autosomal-dominant Robinow syndrome.";
RL Am. J. Hum. Genet. 98:553-561(2016).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] THR-216.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in the signal transduction pathway mediated by
CC multiple Wnt genes. {ECO:0000250|UniProtKB:Q61062}.
CC -!- SUBUNIT: Interacts (via the PDZ domain) with the C-terminal regions of
CC VANGL1 and VANGL2 (By similarity). Interacts (via the region containing
CC both the PDZ and DEP domains) with LRRFIP2; the DIX domain may inhibit
CC this interaction. Interacts with CYLD, CEP164 and DAB2. Interacts with
CC DCDC2. Interacts with FOXK1 and FOXK2 (PubMed:25805136). Interacts with
CC DAAM2 (By similarity). {ECO:0000250|UniProtKB:Q61062,
CC ECO:0000269|PubMed:12805222, ECO:0000269|PubMed:15677333,
CC ECO:0000269|PubMed:20227366, ECO:0000269|PubMed:22863007,
CC ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25805136}.
CC -!- INTERACTION:
CC Q92997; Q9ULW3: ABT1; NbExp=5; IntAct=EBI-739789, EBI-2602396;
CC Q92997; O75689: ADAP1; NbExp=3; IntAct=EBI-739789, EBI-714732;
CC Q92997; Q02040: AKAP17A; NbExp=3; IntAct=EBI-739789, EBI-1042725;
CC Q92997; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-739789, EBI-12170453;
CC Q92997; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-739789, EBI-2371151;
CC Q92997; P05067: APP; NbExp=3; IntAct=EBI-739789, EBI-77613;
CC Q92997; Q8TBE0: BAHD1; NbExp=4; IntAct=EBI-739789, EBI-742750;
CC Q92997; Q8N7W2-2: BEND7; NbExp=5; IntAct=EBI-739789, EBI-10181188;
CC Q92997; O14503: BHLHE40; NbExp=3; IntAct=EBI-739789, EBI-711810;
CC Q92997; Q9HC52: CBX8; NbExp=3; IntAct=EBI-739789, EBI-712912;
CC Q92997; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-739789, EBI-2836773;
CC Q92997; Q8N8U2: CDYL2; NbExp=3; IntAct=EBI-739789, EBI-8467076;
CC Q92997; Q9UPV0: CEP164; NbExp=5; IntAct=EBI-739789, EBI-3937015;
CC Q92997; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-739789, EBI-1104570;
CC Q92997; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-739789, EBI-739624;
CC Q92997; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739789, EBI-742887;
CC Q92997; P49759-3: CLK1; NbExp=3; IntAct=EBI-739789, EBI-11981867;
CC Q92997; P21964-2: COMT; NbExp=3; IntAct=EBI-739789, EBI-10200977;
CC Q92997; P48730: CSNK1D; NbExp=4; IntAct=EBI-739789, EBI-751621;
CC Q92997; P49674: CSNK1E; NbExp=9; IntAct=EBI-739789, EBI-749343;
CC Q92997; P68400: CSNK2A1; NbExp=4; IntAct=EBI-739789, EBI-347804;
CC Q92997; P0DMU9: CT45A10; NbExp=3; IntAct=EBI-739789, EBI-12153495;
CC Q92997; Q8NHU0: CT45A3; NbExp=3; IntAct=EBI-739789, EBI-8643558;
CC Q92997; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-739789, EBI-3867333;
CC Q92997; O14640: DVL1; NbExp=5; IntAct=EBI-739789, EBI-723489;
CC Q92997; Q86TH3: DVL1; NbExp=3; IntAct=EBI-739789, EBI-10185025;
CC Q92997; O60739: EIF1B; NbExp=3; IntAct=EBI-739789, EBI-1043343;
CC Q92997; O15371: EIF3D; NbExp=3; IntAct=EBI-739789, EBI-353818;
CC Q92997; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-739789, EBI-751248;
CC Q92997; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-739789, EBI-6658203;
CC Q92997; O95363: FARS2; NbExp=3; IntAct=EBI-739789, EBI-2513774;
CC Q92997; O43320: FGF16; NbExp=3; IntAct=EBI-739789, EBI-11479104;
CC Q92997; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-739789, EBI-11533409;
CC Q92997; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-739789, EBI-372506;
CC Q92997; P28799-2: GRN; NbExp=3; IntAct=EBI-739789, EBI-25860013;
CC Q92997; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-739789, EBI-748420;
CC Q92997; P20719: HOXA5; NbExp=3; IntAct=EBI-739789, EBI-8470697;
CC Q92997; Q00444: HOXC5; NbExp=3; IntAct=EBI-739789, EBI-11955357;
CC Q92997; P31273: HOXC8; NbExp=3; IntAct=EBI-739789, EBI-1752118;
CC Q92997; Q9C086: INO80B; NbExp=3; IntAct=EBI-739789, EBI-715611;
CC Q92997; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-739789, EBI-1055254;
CC Q92997; Q674X7-2: KAZN; NbExp=3; IntAct=EBI-739789, EBI-12024294;
CC Q92997; Q9H3F6: KCTD10; NbExp=3; IntAct=EBI-739789, EBI-2505886;
CC Q92997; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-739789, EBI-11954971;
CC Q92997; O60333-2: KIF1B; NbExp=3; IntAct=EBI-739789, EBI-10975473;
CC Q92997; Q13351: KLF1; NbExp=3; IntAct=EBI-739789, EBI-8284732;
CC Q92997; Q9UIH9: KLF15; NbExp=5; IntAct=EBI-739789, EBI-2796400;
CC Q92997; P57682: KLF3; NbExp=3; IntAct=EBI-739789, EBI-8472267;
CC Q92997; O43474: KLF4; NbExp=3; IntAct=EBI-739789, EBI-7232405;
CC Q92997; Q53G59: KLHL12; NbExp=4; IntAct=EBI-739789, EBI-740929;
CC Q92997; Q96PV6: LENG8; NbExp=3; IntAct=EBI-739789, EBI-739546;
CC Q92997; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-739789, EBI-2341787;
CC Q92997; Q9Y608: LRRFIP2; NbExp=2; IntAct=EBI-739789, EBI-1023718;
CC Q92997; Q5S007: LRRK2; NbExp=4; IntAct=EBI-739789, EBI-5323863;
CC Q92997; Q9P127: LUZP4; NbExp=3; IntAct=EBI-739789, EBI-10198848;
CC Q92997; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-739789, EBI-10268010;
CC Q92997; O15481: MAGEB4; NbExp=3; IntAct=EBI-739789, EBI-751857;
CC Q92997; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-739789, EBI-746778;
CC Q92997; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-739789, EBI-742459;
CC Q92997; P23511-2: NFYA; NbExp=3; IntAct=EBI-739789, EBI-11061759;
CC Q92997; Q969G9: NKD1; NbExp=3; IntAct=EBI-739789, EBI-1538217;
CC Q92997; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-739789, EBI-716098;
CC Q92997; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-739789, EBI-398874;
CC Q92997; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-739789, EBI-11022007;
CC Q92997; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-739789, EBI-2339674;
CC Q92997; P78337: PITX1; NbExp=4; IntAct=EBI-739789, EBI-748265;
CC Q92997; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-739789, EBI-2876622;
CC Q92997; Q96T60: PNKP; NbExp=3; IntAct=EBI-739789, EBI-1045072;
CC Q92997; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-739789, EBI-10293968;
CC Q92997; Q96MT3: PRICKLE1; NbExp=3; IntAct=EBI-739789, EBI-2348662;
CC Q92997; P54646: PRKAA2; NbExp=3; IntAct=EBI-739789, EBI-1383852;
CC Q92997; Q99633: PRPF18; NbExp=3; IntAct=EBI-739789, EBI-2798416;
CC Q92997; O43395: PRPF3; NbExp=2; IntAct=EBI-739789, EBI-744322;
CC Q92997; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-739789, EBI-1567797;
CC Q92997; Q8NAV1: PRPF38A; NbExp=3; IntAct=EBI-739789, EBI-715374;
CC Q92997; P60891: PRPS1; NbExp=3; IntAct=EBI-739789, EBI-749195;
CC Q92997; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-739789, EBI-740924;
CC Q92997; P86480: PRR20D; NbExp=3; IntAct=EBI-739789, EBI-12754095;
CC Q92997; P61289: PSME3; NbExp=3; IntAct=EBI-739789, EBI-355546;
CC Q92997; Q8NDT2-2: RBM15B; NbExp=3; IntAct=EBI-739789, EBI-10269922;
CC Q92997; Q14498: RBM39; NbExp=3; IntAct=EBI-739789, EBI-395290;
CC Q92997; Q2KHN1: RNF151; NbExp=3; IntAct=EBI-739789, EBI-12002474;
CC Q92997; P62913-2: RPL11; NbExp=3; IntAct=EBI-739789, EBI-11027771;
CC Q92997; O43159: RRP8; NbExp=3; IntAct=EBI-739789, EBI-2008793;
CC Q92997; P57060: RWDD2B; NbExp=3; IntAct=EBI-739789, EBI-724442;
CC Q92997; Q9HAJ7: SAP30L; NbExp=3; IntAct=EBI-739789, EBI-2340040;
CC Q92997; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-739789, EBI-11955083;
CC Q92997; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-739789, EBI-1802965;
CC Q92997; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-739789, EBI-749336;
CC Q92997; Q96L94-2: SNX22; NbExp=3; IntAct=EBI-739789, EBI-12310305;
CC Q92997; O60504: SORBS3; NbExp=3; IntAct=EBI-739789, EBI-741237;
CC Q92997; P27105: STOM; NbExp=3; IntAct=EBI-739789, EBI-1211440;
CC Q92997; O43463: SUV39H1; NbExp=3; IntAct=EBI-739789, EBI-349968;
CC Q92997; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-739789, EBI-10246152;
CC Q92997; Q96C24: SYTL4; NbExp=3; IntAct=EBI-739789, EBI-747142;
CC Q92997; P62380: TBPL1; NbExp=3; IntAct=EBI-739789, EBI-716225;
CC Q92997; Q15560: TCEA2; NbExp=3; IntAct=EBI-739789, EBI-710310;
CC Q92997; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-739789, EBI-11955057;
CC Q92997; Q92734: TFG; NbExp=3; IntAct=EBI-739789, EBI-357061;
CC Q92997; Q9BT49: THAP7; NbExp=3; IntAct=EBI-739789, EBI-741350;
CC Q92997; Q08117-2: TLE5; NbExp=3; IntAct=EBI-739789, EBI-11741437;
CC Q92997; Q8WVP5: TNFAIP8L1; NbExp=6; IntAct=EBI-739789, EBI-752102;
CC Q92997; P09430: TNP1; NbExp=3; IntAct=EBI-739789, EBI-10196343;
CC Q92997; Q12933: TRAF2; NbExp=3; IntAct=EBI-739789, EBI-355744;
CC Q92997; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-739789, EBI-725997;
CC Q92997; Q15631: TSN; NbExp=3; IntAct=EBI-739789, EBI-1044160;
CC Q92997; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-739789, EBI-723389;
CC Q92997; Q8N831: TSPYL6; NbExp=3; IntAct=EBI-739789, EBI-12023322;
CC Q92997; Q9NQZ2: UTP3; NbExp=3; IntAct=EBI-739789, EBI-714067;
CC Q92997; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-739789, EBI-12227803;
CC Q92997; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-739789, EBI-12032042;
CC Q92997; O76024: WFS1; NbExp=3; IntAct=EBI-739789, EBI-720609;
CC Q92997; P19544: WT1; NbExp=3; IntAct=EBI-739789, EBI-2320534;
CC Q92997; P23025: XPA; NbExp=3; IntAct=EBI-739789, EBI-295222;
CC Q92997; Q96MU7: YTHDC1; NbExp=6; IntAct=EBI-739789, EBI-2849854;
CC Q92997; O43167: ZBTB24; NbExp=3; IntAct=EBI-739789, EBI-744471;
CC Q92997; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-739789, EBI-3918996;
CC Q92997; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-739789, EBI-7781767;
CC Q92997; P10074: ZBTB48; NbExp=4; IntAct=EBI-739789, EBI-744864;
CC Q92997; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-739789, EBI-742740;
CC Q92997; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-739789, EBI-12879708;
CC Q92997; P49910: ZNF165; NbExp=3; IntAct=EBI-739789, EBI-741694;
CC Q92997; Q9BSG1: ZNF2; NbExp=3; IntAct=EBI-739789, EBI-8489229;
CC Q92997; O43296: ZNF264; NbExp=3; IntAct=EBI-739789, EBI-4395808;
CC Q92997; Q14C61: ZNF264; NbExp=3; IntAct=EBI-739789, EBI-2826570;
CC Q92997; Q9P2F9: ZNF319; NbExp=3; IntAct=EBI-739789, EBI-11993110;
CC Q92997; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-739789, EBI-347633;
CC Q92997; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-739789, EBI-740727;
CC Q92997; Q8N8Z8: ZNF441; NbExp=3; IntAct=EBI-739789, EBI-17216366;
CC Q92997; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-739789, EBI-12010736;
CC Q92997; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-739789, EBI-10486136;
CC Q92997; Q9H707: ZNF552; NbExp=3; IntAct=EBI-739789, EBI-2555731;
CC Q92997; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-739789, EBI-745520;
CC Q92997; Q5T619: ZNF648; NbExp=3; IntAct=EBI-739789, EBI-11985915;
CC Q92997; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-739789, EBI-11090299;
CC Q92997; Q8N508: ZNF697; NbExp=3; IntAct=EBI-739789, EBI-10265733;
CC Q92997; Q32M78: ZNF699; NbExp=3; IntAct=EBI-739789, EBI-10217363;
CC Q92997; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-739789, EBI-7138235;
CC Q92997; Q96H86: ZNF764; NbExp=3; IntAct=EBI-739789, EBI-745775;
CC Q92997; Q6NX45: ZNF774; NbExp=6; IntAct=EBI-739789, EBI-10251462;
CC Q92997; Q96BV0: ZNF775; NbExp=3; IntAct=EBI-739789, EBI-7149881;
CC Q92997; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-739789, EBI-10240849;
CC Q92997; O75541-2: ZNF821; NbExp=3; IntAct=EBI-739789, EBI-14544035;
CC Q92997; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-739789, EBI-11962574;
CC Q92997; Q15696: ZRSR2; NbExp=3; IntAct=EBI-739789, EBI-6657923;
CC Q92997; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-739789, EBI-10281938;
CC Q92997; P10073: ZSCAN22; NbExp=3; IntAct=EBI-739789, EBI-10178224;
CC Q92997; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-739789, EBI-14650477;
CC Q92997; P98078: Dab2; Xeno; NbExp=2; IntAct=EBI-739789, EBI-1391846;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92997-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92997-2; Sequence=VSP_053371;
CC -!- PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-
CC linked ubiquitin chains. {ECO:0000269|PubMed:20227366}.
CC -!- PTM: Phosphorylated by CSNK1D. {ECO:0000269|PubMed:21422228,
CC ECO:0000269|PubMed:22612246}.
CC -!- PTM: Arginine methylation may function as a switch in regulation of
CC function in Wnt signaling. {ECO:0000269|PubMed:22612246,
CC ECO:0000269|PubMed:23150776}.
CC -!- DISEASE: Robinow syndrome, autosomal dominant 3 (DRS3) [MIM:616894]: A
CC form of Robinow syndrome, a rare skeletal dysplasia syndrome
CC characterized by dysmorphic features resembling a fetal face, mesomelic
CC limb shortening, genital hypoplasia, renal anomalies, and
CC costovertebral segmentation defects. {ECO:0000269|PubMed:26924530}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13199.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U49262; AAB47447.1; -; mRNA.
DR EMBL; U75651; AAB84228.1; -; mRNA.
DR EMBL; AF006013; AAB65244.1; -; mRNA.
DR EMBL; D86963; BAA13199.2; ALT_INIT; mRNA.
DR EMBL; AK304686; BAG65457.1; -; mRNA.
DR EMBL; AC131235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78295.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78296.1; -; Genomic_DNA.
DR EMBL; BC032459; AAH32459.1; -; mRNA.
DR CCDS; CCDS3253.1; -. [Q92997-1]
DR PIR; JC5763; JC5763.
DR RefSeq; NP_004414.3; NM_004423.3. [Q92997-1]
DR PDB; 6V7O; X-ray; 2.90 A; C/D=679-688.
DR PDB; 6ZC6; X-ray; 1.58 A; A=243-335.
DR PDB; 6ZC8; X-ray; 2.76 A; A/B=243-335.
DR PDBsum; 6V7O; -.
DR PDBsum; 6ZC6; -.
DR PDBsum; 6ZC8; -.
DR AlphaFoldDB; Q92997; -.
DR SMR; Q92997; -.
DR BioGRID; 108190; 251.
DR DIP; DIP-34509N; -.
DR IntAct; Q92997; 224.
DR MINT; Q92997; -.
DR STRING; 9606.ENSP00000316054; -.
DR BindingDB; Q92997; -.
DR ChEMBL; CHEMBL6028; -.
DR MoonDB; Q92997; Predicted.
DR GlyGen; Q92997; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q92997; -.
DR PhosphoSitePlus; Q92997; -.
DR BioMuta; DVL3; -.
DR DMDM; 6919875; -.
DR EPD; Q92997; -.
DR jPOST; Q92997; -.
DR MassIVE; Q92997; -.
DR MaxQB; Q92997; -.
DR PaxDb; Q92997; -.
DR PeptideAtlas; Q92997; -.
DR PRIDE; Q92997; -.
DR ProteomicsDB; 5895; -.
DR ProteomicsDB; 75666; -. [Q92997-1]
DR Antibodypedia; 33790; 328 antibodies from 36 providers.
DR DNASU; 1857; -.
DR Ensembl; ENST00000313143.9; ENSP00000316054.3; ENSG00000161202.20. [Q92997-1]
DR Ensembl; ENST00000431765.6; ENSP00000405885.1; ENSG00000161202.20. [Q92997-2]
DR GeneID; 1857; -.
DR KEGG; hsa:1857; -.
DR MANE-Select; ENST00000313143.9; ENSP00000316054.3; NM_004423.4; NP_004414.3.
DR UCSC; uc003fms.4; human. [Q92997-1]
DR CTD; 1857; -.
DR DisGeNET; 1857; -.
DR GeneCards; DVL3; -.
DR GeneReviews; DVL3; -.
DR HGNC; HGNC:3087; DVL3.
DR HPA; ENSG00000161202; Low tissue specificity.
DR MalaCards; DVL3; -.
DR MIM; 601368; gene.
DR MIM; 616894; phenotype.
DR neXtProt; NX_Q92997; -.
DR OpenTargets; ENSG00000161202; -.
DR Orphanet; 3107; Autosomal dominant Robinow syndrome.
DR PharmGKB; PA27543; -.
DR VEuPathDB; HostDB:ENSG00000161202; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; Q92997; -.
DR OMA; RKYASHM; -.
DR OrthoDB; 474724at2759; -.
DR PhylomeDB; Q92997; -.
DR TreeFam; TF318198; -.
DR PathwayCommons; Q92997; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5368598; Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; Q92997; -.
DR SIGNOR; Q92997; -.
DR BioGRID-ORCS; 1857; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; DVL3; human.
DR GeneWiki; DVL3; -.
DR GenomeRNAi; 1857; -.
DR Pharos; Q92997; Tbio.
DR PRO; PR:Q92997; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92997; protein.
DR Bgee; ENSG00000161202; Expressed in stromal cell of endometrium and 195 other tissues.
DR ExpressionAtlas; Q92997; baseline and differential.
DR Genevisible; Q92997; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISS:BHF-UCL.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:BHF-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IGI:ParkinsonsUK-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:BHF-UCL.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR024580; Dishevelled_C-dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR008342; DVL3.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10878; PTHR10878; 1.
DR PANTHER; PTHR10878:SF6; PTHR10878:SF6; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF12316; Dsh_C; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR01760; DISHEVELLED.
DR PRINTS; PR01763; DISHEVELLED3.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Dwarfism; Methylation; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..716
FT /note="Segment polarity protein dishevelled homolog DVL-3"
FT /id="PRO_0000145749"
FT DOMAIN 1..82
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 249..321
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 422..496
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 85..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:22612246"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22612246,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:22612246"
FT MOD_RES 271
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23150776"
FT MOD_RES 271
FT /note="Symmetric dimethylarginine; by PRMT7; alternate"
FT /evidence="ECO:0000269|PubMed:23150776"
FT MOD_RES 342
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:22612246,
FT ECO:0000269|PubMed:23150776"
FT MOD_RES 342
FT /note="Symmetric dimethylarginine; by PRMT7; alternate"
FT /evidence="ECO:0000269|PubMed:22612246,
FT ECO:0000269|PubMed:23150776"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22612246"
FT MOD_RES 614
FT /note="Symmetric dimethylarginine; by PRMT7"
FT /evidence="ECO:0000269|PubMed:23150776"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 698
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|PubMed:22612246"
FT MOD_RES 698
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:22612246"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22612246"
FT VAR_SEQ 350..367
FT /note="SEPIRPIDPAAWVSHTAA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053371"
FT VARIANT 216
FT /note="R -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036116"
FT VARIANT 433
FT /note="W -> L (in dbSNP:rs17853048)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025519"
FT MUTAGEN 271
FT /note="R->K: Localizes to plasma membranes."
FT /evidence="ECO:0000269|PubMed:23150776"
FT MUTAGEN 342
FT /note="R->K: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:23150776"
FT MUTAGEN 614
FT /note="R->K: Localizes to plasma membranes."
FT /evidence="ECO:0000269|PubMed:23150776"
FT CONFLICT 2
FT /note="G -> D (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> Y (in Ref. 2; AAB84228)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="P -> S (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="G -> W (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> R (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> N (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="R -> W (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="E -> D (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="S -> C (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> T (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="T -> S (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="T -> A (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="N -> K (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="R -> C (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="W -> C (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> P (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="L -> V (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="P -> R (in Ref. 3; AAB65244)"
FT /evidence="ECO:0000305"
FT CONFLICT 553..554
FT /note="FP -> LG (in Ref. 3; AAB65244)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="A -> T (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="S -> I (in Ref. 1; AAB47447)"
FT /evidence="ECO:0000305"
FT CONFLICT 682..716
FT /note="PPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM -> LRAATWPQCPRN
FT (in Ref. 4; BAA13199)"
FT /evidence="ECO:0000305"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6ZC6"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6ZC8"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6ZC6"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6ZC6"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:6ZC6"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6ZC6"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:6ZC6"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6ZC6"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:6ZC6"
SQ SEQUENCE 716 AA; 78055 MW; B1A55EBF9507D06E CRC64;
MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD DDFGVVKEEI
SDDNAKLPCF NGRVVSWLVS AEGSHPDPAP FCADNPSELP PPMERTGGIG DSRPPSFHPH
AGGGSQENLD NDTETDSLVS AQRERPRRRD GPEHATRLNG TAKGERRREP GGYDSSSTLM
SSELETTSFF DSDEDDSTSR FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD
STMSLNIITV TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL
QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS EPIRPIDPAA
WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER LDDFHLSIHS DMAAIVKAMA
SPESGLEVRD RMWLKITIPN AFIGSDVVDW LYHNVEGFTD RREARKYASN LLKAGFIRHT
VNKITFSEQC YYIFGDLCGN MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY
PPPPHPYNPH PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG
SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL ASSLRSHHTH PSYGPPGVPP
LYGPPMLMMP PPPAAMGPPG APPGRDLASV PPELTASRQS FRMAMGNPSE FFVDVM
