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 27-MAR-2024, entry version 217. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 6ZBQ; X-ray; 1.43 A; A/B=243-335. DR PDB; 6ZBZ; X-ray; 1.60 A; A/B/C/D=243-335. DR PDB; 6ZC3; X-ray; 1.67 A; A/B=243-335. DR PDB; 6ZC4; X-ray; 1.85 A; A/B=243-335. DR PDB; 6ZC6; X-ray; 1.58 A; A=243-335. DR PDB; 6ZC7; X-ray; 1.48 A; A/B=243-335. DR PDB; 6ZC8; X-ray; 2.76 A; A/B=243-335. DR PDBsum; 6V7O; -. DR PDBsum; 6ZBQ; -. DR PDBsum; 6ZBZ; -. DR PDBsum; 6ZC3; -. DR PDBsum; 6ZC4; -. DR PDBsum; 6ZC6; -. DR PDBsum; 6ZC7; -. DR PDBsum; 6ZC8; -. DR AlphaFoldDB; Q92997; -. DR SMR; Q92997; -. DR BioGRID; 108190; 266. DR DIP; DIP-34509N; -. DR IntAct; Q92997; 226. DR MINT; Q92997; -. DR STRING; 9606.ENSP00000316054; -. DR BindingDB; Q92997; -. DR ChEMBL; CHEMBL6028; -. DR MoonDB; Q92997; Predicted. DR GlyCosmos; Q92997; 2 sites, 1 glycan. DR GlyGen; Q92997; 4 sites, 1 O-linked glycan (4 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; 9606-ENSP00000316054; -. DR PeptideAtlas; Q92997; -. DR ProteomicsDB; 5895; -. DR ProteomicsDB; 75666; -. [Q92997-1] DR Pumba; Q92997; -. DR Antibodypedia; 33790; 360 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 AGR; HGNC:3087; -. 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; TPCTVIA; -. DR OrthoDB; 2910598at2759; -. 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 1153 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 197 other cell types or tissues. DR ExpressionAtlas; Q92997; baseline and differential. 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:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; 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:0050821; P:protein stabilization; IGI:ParkinsonsUK-UCL. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:BHF-UCL. DR GO; GO:0032880; P:regulation of protein localization; IDA:ParkinsonsUK-UCL. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:BHF-UCL. DR CDD; cd04438; DEP_dishevelled; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.40.240.130; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; SEGMENT POLARITY PROTEIN DISHEVELLED; 1. DR PANTHER; PTHR10878:SF6; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-3; 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; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50841; DIX; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q92997; HS. 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:6ZBQ" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:6ZC8" FT STRAND 262..266 FT /evidence="ECO:0007829|PDB:6ZBQ" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:6ZBZ" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:6ZBQ" FT HELIX 286..290 FT /evidence="ECO:0007829|PDB:6ZBQ" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:6ZBQ" FT HELIX 312..324 FT /evidence="ECO:0007829|PDB:6ZBQ" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:6ZC6" FT STRAND 329..334 FT /evidence="ECO:0007829|PDB:6ZBQ" 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 //