ID DIXC1_HUMAN Reviewed; 683 AA. AC Q155Q3; A1A5D8; E9PRV4; Q6P2J8; Q6PIK4; Q86SR7; Q8IVY4; Q96N69; AC Q9C0C8; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 30-NOV-2016, entry version 103. DE RecName: Full=Dixin; DE AltName: Full=Coiled-coil protein DIX1; DE Short=Coiled-coil-DIX1; DE AltName: Full=DIX domain-containing protein 1; GN Name=DIXDC1; Synonyms=CCD1, KIAA1735; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN. RX PubMed=16814745; DOI=10.1016/j.bbrc.2006.06.050; RA Wang X., Zheng L., Zeng Z., Zhou G., Chien J., Qian C., Vasmatzis G., RA Shridhar V., Chen L., Liu W.; RT "DIXDC1 isoform, l-DIXDC1, is a novel filamentous actin-binding RT protein."; RL Biochem. Biophys. Res. Commun. 347:22-30(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11214970; DOI=10.1093/dnares/7.6.347; RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIX. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 7:347-355(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-293 (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 3-218 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 327-683 (ISOFORMS 1/2). RC TISSUE=Brain, and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-683 (ISOFORMS 1/2). RC TISSUE=Mammary gland; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND INTERACTION WITH AXIN1; DVL2; MAP3K4 AND RAC. RX PubMed=15262978; DOI=10.1074/jbc.M404598200; RA Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.; RT "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal RT kinase activation by Axin and dishevelled through distinct RT mechanisms."; RL J. Biol. Chem. 279:39366-39373(2004). RN [8] RP IDENTIFICATION BY 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 [9] RP SUBCELLULAR LOCATION, AND INTERACTION WITH GAMMA TUBULIN. RX PubMed=19375513; DOI=10.1016/j.cellbi.2009.04.001; RA Wu Y., Jing X., Ma X., Wu Y., Ding X., Fan W., Fan M.; RT "DIXDC1 co-localizes and interacts with gamma-tubulin in HEK293 RT cells."; RL Cell Biol. Int. 33:697-701(2009). RN [10] RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND UBIQUITINATION. RX PubMed=20085589; DOI=10.1111/j.1349-7006.2009.01448.x; RA Wang L., Li H., Chen Q., Zhu T., Zhu H., Zheng L.; RT "Wnt signaling stabilizes the DIXDC1 protein through decreased RT ubiquitin-dependent degradation."; RL Cancer Sci. 101:700-706(2010). RN [11] RP MYRISTOYLATION AT GLY-2 (ISOFORM 2). RX PubMed=20213681; DOI=10.1002/pmic.200900783; RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., RA Tsunasawa S., Utsumi T.; RT "Strategy for comprehensive identification of human N-myristoylated RT proteins using an insect cell-free protein synthesis system."; RL Proteomics 10:1780-1793(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 597-683, FUNCTION, RP MUTAGENESIS OF ASP-648; PHE-651 AND LYS-655, DOMAIN, AND INTERACTION RP WITH DVL2. RX PubMed=21189423; DOI=10.1074/jbc.M110.186742; RA Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., RA Lin S.C., Wang Z.X., Wu J.W.; RT "Molecular basis of Wnt activation via the DIX-domain protein Ccd1."; RL J. Biol. Chem. 286:8597-8608(2011). CC -!- FUNCTION: Positive effector of the Wnt signaling pathway; CC activates WNT3A signaling via DVL2. Regulates JNK activation by CC AXIN1 and DVL2. {ECO:0000269|PubMed:15262978, CC ECO:0000269|PubMed:21189423}. CC -!- SUBUNIT: Isoform 1 but not isoform 2 binds filamentous actin. CC Interacts with the complex composed of DVL2 and Rac. Interacts CC with AXIN1; competes with MAP3K1. Interacts with MAP3K4 preventing CC MAP3K4 interaction with AXIN1. Directly interacts (via DIX domain) CC with DVL2 (via DIX domain). Interacts with gamma-tubulin. CC {ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:16814745, CC ECO:0000269|PubMed:19375513, ECO:0000269|PubMed:21189423}. CC -!- INTERACTION: CC O14641:DVL2; NbExp=2; IntAct=EBI-1104700, EBI-740850; CC Q60838:Dvl2 (xeno); NbExp=4; IntAct=EBI-1104700, EBI-641940; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000269|PubMed:16814745, ECO:0000269|PubMed:19375513, CC ECO:0000269|PubMed:20085589}. Note=Colocalizes with gamma-tubulin CC at the centrosome, both during interphase and mitosis. CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell junction, focal adhesion. CC Note=Associated with actin stress fiber at the filament ends. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=l-DIXDC1; CC IsoId=Q155Q3-1; Sequence=Displayed; CC Note=Major isoform. Ubiquitously expressed.; CC Name=2; Synonyms=s-DIXDC1; CC IsoId=Q155Q3-2; Sequence=VSP_025378, VSP_025379; CC Note=Major isoform. Preferentially expressed in cardiac and CC skeletal muscles. Initiator Met-1 is removed. Contains a CC N-myristoyl glycine at position 2.; CC Name=3; CC IsoId=Q155Q3-4; Sequence=VSP_025380, VSP_025381; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q155Q3-5; Sequence=VSP_054565, VSP_025380, VSP_025381; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression CC in cardiac and skeletal muscles. {ECO:0000269|PubMed:16814745}. CC -!- DOMAIN: The coiled-coil domain mediates interaction with MAP3K4 CC and inhibition of AXIN1-mediated JNK activation through MAP3K4. CC {ECO:0000269|PubMed:21189423}. CC -!- DOMAIN: The DIX domain mediates interaction with AXIN1 and CC inhibition of AXIN1-mediated JNK activation through MAP3K1. CC Mediates interaction with DVL2; this interaction is required for CC activation of Wnt signaling. {ECO:0000269|PubMed:21189423}. CC -!- PTM: Phosphorylated on tyrosine and serine residues. CC {ECO:0000269|PubMed:20085589}. CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation. CC WNT3A signaling increases DIXDC1 protein levels by inhibiting its CC ubiquitination and subsequent degradation. CC {ECO:0000269|PubMed:20085589}. CC -!- SIMILARITY: Belongs to the DIXDC1 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00044}. CC -!- SIMILARITY: Contains 1 DIX domain. {ECO:0000255|PROSITE- CC ProRule:PRU00069}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH35509.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH64479.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAB21826.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=BAB71039.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; 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; DQ642016; ABG25914.1; -; mRNA. DR EMBL; AB051522; BAB21826.1; ALT_INIT; mRNA. DR EMBL; AP000907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67171.1; -; Genomic_DNA. DR EMBL; BC033034; AAH33034.1; -; mRNA. DR EMBL; BC035509; AAH35509.1; ALT_SEQ; mRNA. DR EMBL; BC041626; AAH41626.2; -; mRNA. DR EMBL; BC048294; AAH48294.1; -; mRNA. DR EMBL; BC064479; AAH64479.1; ALT_SEQ; mRNA. DR EMBL; BC128600; AAI28601.1; -; mRNA. DR EMBL; AK055899; BAB71039.1; ALT_SEQ; mRNA. DR CCDS; CCDS60957.1; -. [Q155Q3-5] DR CCDS; CCDS73381.1; -. [Q155Q3-1] DR CCDS; CCDS73382.1; -. [Q155Q3-2] DR RefSeq; NP_001033043.1; NM_001037954.3. [Q155Q3-1] DR RefSeq; NP_001265471.1; NM_001278542.1. [Q155Q3-5] DR RefSeq; NP_219493.1; NM_033425.4. [Q155Q3-2] DR UniGene; Hs.655626; -. DR PDB; 3PZ7; X-ray; 2.44 A; A=597-683. DR PDBsum; 3PZ7; -. DR ProteinModelPortal; Q155Q3; -. DR SMR; Q155Q3; -. DR BioGrid; 124542; 19. DR IntAct; Q155Q3; 20. DR MINT; MINT-8080298; -. DR STRING; 9606.ENSP00000394352; -. DR iPTMnet; Q155Q3; -. DR PhosphoSitePlus; Q155Q3; -. DR DMDM; 147641721; -. DR EPD; Q155Q3; -. DR MaxQB; Q155Q3; -. DR PaxDb; Q155Q3; -. DR PeptideAtlas; Q155Q3; -. DR PRIDE; Q155Q3; -. DR Ensembl; ENST00000440460; ENSP00000394352; ENSG00000150764. [Q155Q3-1] DR Ensembl; ENST00000529225; ENSP00000434130; ENSG00000150764. [Q155Q3-5] DR Ensembl; ENST00000615255; ENSP00000480808; ENSG00000150764. [Q155Q3-2] DR GeneID; 85458; -. DR KEGG; hsa:85458; -. DR UCSC; uc001pmj.4; human. [Q155Q3-1] DR CTD; 85458; -. DR DisGeNET; 85458; -. DR GeneCards; DIXDC1; -. DR HGNC; HGNC:23695; DIXDC1. DR HPA; HPA039424; -. DR HPA; HPA039658; -. DR MIM; 610493; gene. DR neXtProt; NX_Q155Q3; -. DR OpenTargets; ENSG00000150764; -. DR PharmGKB; PA134988674; -. DR eggNOG; ENOG410IFNC; Eukaryota. DR eggNOG; ENOG410XPPR; LUCA. DR GeneTree; ENSGT00390000013552; -. DR HOVERGEN; HBG107812; -. DR InParanoid; Q155Q3; -. DR OMA; ETSWEEQ; -. DR OrthoDB; EOG091G03RC; -. DR PhylomeDB; Q155Q3; -. DR ChiTaRS; DIXDC1; human. DR GeneWiki; DIXDC1; -. DR GenomeRNAi; 85458; -. DR PRO; PR:Q155Q3; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000150764; -. DR CleanEx; HS_DIXDC1; -. DR ExpressionAtlas; Q155Q3; baseline and differential. DR Genevisible; Q155Q3; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0007049; P:cell cycle; IEA:Ensembl. DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl. DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; IEA:Ensembl. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl. DR CDD; cd00014; CH; 1. DR Gene3D; 1.10.418.10; -; 1. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR001158; DIX. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR Pfam; PF00307; CH; 1. DR Pfam; PF00778; DIX; 1. DR SMART; SM00033; CH; 1. DR SMART; SM00021; DAX; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS50841; DIX; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Cell junction; KW Coiled coil; Complete proteome; Cytoplasm; Developmental protein; KW Lipoprotein; Myristate; Phosphoprotein; Polymorphism; KW Reference proteome; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1 683 Dixin. FT /FTId=PRO_0000287223. FT DOMAIN 20 127 CH. {ECO:0000255|PROSITE- FT ProRule:PRU00044}. FT DOMAIN 600 680 DIX. {ECO:0000255|PROSITE- FT ProRule:PRU00069}. FT REGION 127 300 Actin-binding. FT COILED 279 452 {ECO:0000255}. FT MOD_RES 186 186 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80Y83}. FT MOD_RES 231 231 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80Y83}. FT MOD_RES 590 590 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT VAR_SEQ 1 211 Missing (in isoform 2). FT {ECO:0000303|PubMed:11214970, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025378. FT VAR_SEQ 1 20 MLACLTRGNLLDVLQEGFNE -> MGTQVVMRFNNSLLPTE FT PS (in isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_054565. FT VAR_SEQ 212 219 PSESSCSS -> MGGTQVKC (in isoform 2). FT {ECO:0000303|PubMed:11214970, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025379. FT VAR_SEQ 219 219 S -> R (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025380. FT VAR_SEQ 220 683 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025381. FT VARIANT 300 300 K -> R (in dbSNP:rs34575249). FT /FTId=VAR_032294. FT MUTAGEN 648 648 D->A: Loss of interaction with DVL2. FT Abolishes activation of Wnt signaling. FT {ECO:0000269|PubMed:21189423}. FT MUTAGEN 651 651 F->A: Loss of interaction with DVL2. FT Abolishes activation of Wnt signaling. FT {ECO:0000269|PubMed:21189423}. FT MUTAGEN 655 655 K->A: Loss of interaction with DVL2. FT Abolishes activation of Wnt signaling. FT {ECO:0000269|PubMed:21189423}. FT CONFLICT 140 140 S -> P (in Ref. 1; ABG25914). FT {ECO:0000305}. FT CONFLICT 144 144 L -> R (in Ref. 1; ABG25914). FT {ECO:0000305}. FT CONFLICT 168 168 H -> Q (in Ref. 1; ABG25914). FT {ECO:0000305}. FT CONFLICT 378 378 L -> S (in Ref. 3; BAB71039). FT {ECO:0000305}. FT STRAND 601 606 {ECO:0000244|PDB:3PZ7}. FT STRAND 614 620 {ECO:0000244|PDB:3PZ7}. FT HELIX 627 634 {ECO:0000244|PDB:3PZ7}. FT STRAND 640 648 {ECO:0000244|PDB:3PZ7}. FT TURN 649 651 {ECO:0000244|PDB:3PZ7}. FT STRAND 652 658 {ECO:0000244|PDB:3PZ7}. FT STRAND 671 678 {ECO:0000244|PDB:3PZ7}. SQ SEQUENCE 683 AA; 77478 MW; E643D1A69B00238C CRC64; MLACLTRGNL LDVLQEGFNE QQLQAYVAWV NAQLKKRPAV KPVQDLRQDL RDGVILAYLI EIVAGEKLSG VQLSPGNQQE MKNNVEKVLQ FVASKKIRMH QTSAKDIVDG NLKSIMRLVL ALAAHFKPGS SRTVNQGRDS RAPLQSHRPH CATAVAQGAA AALADVCHDM SRSGRDVFRY RQRNSSMDEE IENPYWSVRA LVQQYEGQQR SPSESSCSSL TSPSPIHSAK SESIITQSEE KADFVIIPAE GIENRTEGTD SPLSRDWRPG SPGTYLETSW EEQLLEQQEY LEKEMEEAKK MISGLQALLL NGSLPEDEQE RPLALCEPGV NPEEQLIIIQ SRLDQSMEEN QDLKKELLKC KQEARNLQGI KDALQQRLTQ QDTSVLQLKQ ELLRANMDKD ELHNQNVDLQ RKLDERNRLL GEYKKELGQK DRLLQQHQAK LEEALRKLSD VSYHQVDLER ELEHKDVLLA HCMKREADEA TNYNSHNSQS NGFLLPTAGK GATSVSNRGT SDLQLVRDAL RSLRNSFSGH DPQHHTIDSL EQGISSLMER LHVMETQKKQ ERKVRVKSPR TQVGSEYRES WPPNSKLPHS QSSPTVSSTC TKVLYFTDRS LTPFMVNIPK RLEEVTLKDF KAAIDREGNH RYHFKALDPE FGTVKEEIFH DDDAIPGWEG KIVAWVEEDH GEN //