ID CTND1_HUMAN Reviewed; 968 AA. AC O60716; A8K939; O15088; O60713; O60714; O60715; O60935; Q6DHZ7; Q6RBX8; AC Q9UP71; Q9UP72; Q9UP73; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 221. DE RecName: Full=Catenin delta-1; DE AltName: Full=Cadherin-associated Src substrate; DE Short=CAS; DE AltName: Full=p120 catenin; DE Short=p120(ctn); DE AltName: Full=p120(cas); GN Name=CTNND1; Synonyms=KIAA0384; 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], AND ALTERNATIVE SPLICING. RC TISSUE=Fetal kidney; RX PubMed=9653641; DOI=10.1006/geno.1998.5325; RA Keirsebilck A., Bonne S., Staes K., van Hengel J., Nollet F., Reynolds A., RA van Roy F.; RT "Molecular cloning of the human p120ctn catenin gene (CTNND1): expression RT of multiple alternatively spliced isoforms."; RL Genomics 50:129-146(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1AC). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1AC). RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-217; CYS-464 AND RP LYS-915. RG NIEHS SNPs program; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. 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., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., 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 MRNA] (ISOFORM 1A). RC TISSUE=Testis; 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 [7] RP PHOSPHORYLATION BY FER, AND INTERACTION WITH FER. RX PubMed=7623846; DOI=10.1128/mcb.15.8.4553; RA Kim L., Wong T.W.; RT "The cytoplasmic tyrosine kinase FER is associated with the catenin-like RT substrate pp120 and is activated by growth factors."; RL Mol. Cell. Biol. 15:4553-4561(1995). RN [8] RP FUNCTION, AND INTERACTION WITH ZBTB33. RX PubMed=10207085; DOI=10.1128/mcb.19.5.3614; RA Daniel J.M., Reynolds A.B.; RT "The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc RT finger transcription factor."; RL Mol. Cell. Biol. 19:3614-3623(1999). RN [9] RP ALTERNATIVE INITIATION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=11896187; DOI=10.1242/jcs.115.7.1391; RA Aho S., Levansuo L., Montonen O., Kari C., Rodeck U., Uitto J.; RT "Specific sequences in p120ctn determine subcellular distribution of its RT multiple isoforms involved in cellular adhesion of normal and malignant RT epithelial cells."; RL J. Cell Sci. 115:1391-1402(2002). RN [10] RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRJ. RX PubMed=12370829; DOI=10.1038/sj.onc.1205858; RA Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.; RT "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts RT with p120(ctn)."; RL Oncogene 21:7067-7076(2002). RN [11] RP FUNCTION. RX PubMed=14610055; DOI=10.1083/jcb.200307111; RA Davis M.A., Ireton R.C., Reynolds A.B.; RT "A core function for p120-catenin in cadherin turnover."; RL J. Cell Biol. 163:525-534(2003). RN [12] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=14699141; DOI=10.1074/jbc.m306057200; RA Kondapalli J., Flozak A.S., Albuquerque M.L.C.; RT "Laminar shear stress differentially modulates gene expression of p120 RT catenin, Kaiso transcription factor, and vascular endothelial cadherin in RT human coronary artery endothelial cells."; RL J. Biol. Chem. 279:11417-11424(2004). RN [13] RP INTERACTION WITH CDH1; GNA12 AND GNA13, AND SUBCELLULAR LOCATION. RX PubMed=15240885; DOI=10.1073/pnas.0401366101; RA Krakstad B.F., Ardawatia V.V., Aragay A.M.; RT "A role for Galpha12/Galpha13 in p120ctn regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004). RN [14] RP SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS1. RX PubMed=17047063; DOI=10.1158/0008-5472.can-05-3096; RA Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., RA Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.; RT "E-cadherin regulates human Nanos1, which interacts with p120ctn and RT induces tumor cell migration and invasion."; RL Cancer Res. 66:10007-10015(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-268; SER-269; SER-349 RP AND SER-352, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [17] RP SUBCELLULAR LOCATION. RX PubMed=17115030; DOI=10.1038/ncb1504; RA Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., RA Huttelmaier S., Hatzfeld M.; RT "The armadillo protein p0071 regulates Rho signalling during cytokinesis."; RL Nat. Cell Biol. 8:1432-1440(2006). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [19] RP INTERACTION WITH GLIS2, AND FUNCTION. RX PubMed=17344476; DOI=10.1091/mbc.e06-10-0941; RA Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., RA Birchmeier W., Briscoe J., Fujita Y.; RT "The transcriptional repressor Glis2 is a novel binding partner for p120 RT catenin."; RL Mol. Biol. Cell 18:1918-1927(2007). RN [20] RP PHOSPHORYLATION AT TYR-112 BY FYN. RX PubMed=17194753; DOI=10.1128/mcb.01974-06; RA Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P., RA Bustelo X.R., Garcia de Herreros A., Dunach M.; RT "Specific phosphorylation of p120-catenin regulatory domain differently RT modulates its binding to RhoA."; RL Mol. Cell. Biol. 27:1745-1757(2007). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-230 AND SER-288, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-889 (ISOFORM 1), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-910 (ISOFORM 1A), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916 (ISOFORM 1AC), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-895 (ISOFORM 1C), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-835 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-856 (ISOFORM 2A), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-862 (ISOFORM 2AC), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-841 (ISOFORM 2C), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-788 (ISOFORM 3), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-809 (ISOFORM 3A), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-815 (ISOFORM 3AC), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-794 (ISOFORM 3C), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-566 (ISOFORM 4), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587 (ISOFORM 4A), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-593 (ISOFORM 4AC), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-572 (ISOFORM 4C), AND 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [24] RP PHOSPHORYLATION AT SER-288 BY PAK5. RX PubMed=20564219; DOI=10.1002/jcb.22639; RA Wong L.E., Reynolds A.B., Dissanayaka N.T., Minden A.; RT "p120-catenin is a binding partner and substrate for Group B Pak kinases."; RL J. Cell. Biochem. 110:1244-1254(2010). RN [25] RP INTERACTION WITH PLPP3. RX PubMed=20123964; DOI=10.1128/mcb.00038-09; RA Humtsoe J.O., Liu M., Malik A.B., Wary K.K.; RT "Lipid phosphate phosphatase 3 stabilization of beta-catenin induces RT endothelial cell migration and formation of branching point structures."; RL Mol. Cell. Biol. 30:1593-1606(2010). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-4; SER-47; SER-811; THR-916 AND SER-920, AND 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-320; SER-349; RP SER-847; SER-857; SER-859; SER-864; SER-879 AND SER-920, AND IDENTIFICATION RP BY 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 [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-47; THR-59; SER-252; RP SER-268; SER-269; SER-288; SER-346; SER-349; SER-352; SER-861; SER-864; RP THR-869; THR-906 AND SER-920, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-225; SER-252; RP SER-268; SER-269; SER-346; SER-349; SER-352; SER-617; SER-847; SER-857; RP SER-864; TYR-865; SER-868; THR-869; SER-920 AND SER-943, 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., 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 [33] RP INTERACTION WITH CCDC85B, AND REGION. RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492; RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J., RA McCrea P.D., Gamse J.T., Reynolds A.B.; RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of RT p120-catenin family: potential roles in hydrocephalus and heterotopia."; RL Mol. Biol. Cell 25:2592-2603(2014). RN [34] RP INVOLVEMENT IN BCDS2, AND VARIANTS BCDS2 365-GLN--ILE-968 DEL AND RP 700-ARG--ILE-968 DEL. RX PubMed=28301459; DOI=10.1038/gim.2017.11; RA Ghoumid J., Stichelbout M., Jourdain A.S., Frenois F., Lejeune-Dumoulin S., RA Alex-Cordier M.P., Lebrun M., Guerreschi P., Duquennoy-Martinot V., RA Vinchon M., Ferri J., Jung M., Vicaire S., Vanlerberghe C., Escande F., RA Petit F., Manouvrier-Hanu S.; RT "Blepharocheilodontic syndrome is a CDH1 pathway-related disorder due to RT mutations in CDH1 and CTNND1."; RL Genet. Med. 19:1013-1021(2017). RN [35] RP IDENTIFICATION IN A CADHERIN/CATENIN ADHESION COMPLEX. RX PubMed=28051089; DOI=10.1038/mi.2016.120; RA Caldwell J.M., Collins M.H., Kemme K.A., Sherrill J.D., Wen T., Rochman M., RA Stucke E.M., Amin L., Tai H., Putnam P.E., Jimenez-Dalmaroni M.J., RA Wormald M.R., Porollo A., Abonia J.P., Rothenberg M.E.; RT "Cadherin 26 is an alpha integrin-binding epithelial receptor regulated RT during allergic inflammation."; RL Mucosal Immunol. 10:1190-1201(2017). RN [36] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-421; LYS-517 AND LYS-882, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 324-937 IN COMPLEX WITH CDH1, RP FUNCTION, SUBUNIT, SITE, AND MUTAGENESIS OF TRP-363; LYS-401; LYS-444; RP TRP-477 AND ASN-478. RX PubMed=20371349; DOI=10.1016/j.cell.2010.01.017; RA Ishiyama N., Lee S.H., Liu S., Li G.Y., Smith M.J., Reichardt L.F., RA Ikura M.; RT "Dynamic and static interactions between p120 catenin and E-cadherin RT regulate the stability of cell-cell adhesion."; RL Cell 141:117-128(2010). CC -!- FUNCTION: Key regulator of cell-cell adhesion that associates with and CC regulates the cell adhesion properties of both C-, E- and N-cadherins, CC being critical for their surface stability (PubMed:14610055, CC PubMed:20371349). Beside cell-cell adhesion, regulates gene CC transcription through several transcription factors including CC ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and CC downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). CC Implicated both in cell transformation by SRC and in ligand-induced CC receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors CC (PubMed:17344476). {ECO:0000269|PubMed:10207085, CC ECO:0000269|PubMed:14610055, ECO:0000269|PubMed:17344476, CC ECO:0000269|PubMed:20371349}. CC -!- SUBUNIT: Belongs to a multiprotein cell-cell adhesion complex that also CC contains E-cadherin/CDH1, alpha-catenin/CTNNA1, beta-catenin/CTNNB1, CC and gamma-catenin/JUP (PubMed:20371349, PubMed:15240885). Component of CC a cadherin:catenin adhesion complex composed of at least of CDH26, CC beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 CC (PubMed:28051089). Binds to the C-terminal fragment of PSEN1 and CC mutually competes for CDH1. Interacts with ZBTB33 (PubMed:10207085). CC Interacts with GLIS2 (PubMed:17344476). Interacts with FER CC (PubMed:7623846). Interacts with NANOS1 (via N-terminal region) CC (PubMed:17047063). Interacts (via N-terminus) with GNA12; the CC interaction regulates CDH1-mediated cell-cell adhesion CC (PubMed:15240885). Interacts with GNA13 (PubMed:15240885). Interacts CC with CCDC85B (PubMed:25009281). Interacts with PLPP3; negatively CC regulates the PLPP3-mediated stabilization of CTNNB1 (PubMed:20123964). CC {ECO:0000269|PubMed:10207085, ECO:0000269|PubMed:15240885, CC ECO:0000269|PubMed:17047063, ECO:0000269|PubMed:17344476, CC ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:20371349, CC ECO:0000269|PubMed:25009281, ECO:0000269|PubMed:28051089, CC ECO:0000269|PubMed:7623846}. CC -!- INTERACTION: CC O60716; P00533: EGFR; NbExp=5; IntAct=EBI-701927, EBI-297353; CC O60716; Q7Z6J6: FRMD5; NbExp=3; IntAct=EBI-701927, EBI-727282; CC O60716; O14495: PLPP3; NbExp=9; IntAct=EBI-701927, EBI-766232; CC O60716; Q12913: PTPRJ; NbExp=5; IntAct=EBI-701927, EBI-2264500; CC O60716-5; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-701963, EBI-2511344; CC O60716-5; Q86T24: ZBTB33; NbExp=3; IntAct=EBI-701963, EBI-2515625; CC O60716-21; Q8WY41: NANOS1; NbExp=2; IntAct=EBI-9634525, EBI-9630165; CC O60716-29; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-702059, EBI-2511344; CC O60716-29; P09803: Cdh1; Xeno; NbExp=3; IntAct=EBI-702059, EBI-984420; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction CC {ECO:0000269|PubMed:11896187}. Cytoplasm {ECO:0000269|PubMed:15240885, CC ECO:0000269|PubMed:17047063}. Nucleus {ECO:0000269|PubMed:11896187, CC ECO:0000269|PubMed:17115030}. Cell membrane CC {ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17047063}. CC Note=Interaction with GLIS2 promotes nuclear translocation (By CC similarity). Detected at cell-cell contacts (PubMed:15240885, CC PubMed:17047063). NANOS1 induces its translocation from sites of cell- CC cell contact to the cytoplasm (PubMed:17047063). CDH1 enhances cell CC membrane localization (PubMed:15240885). Isoforms 4A and 1AB are CC excluded from the nucleus (PubMed:11896187). CC {ECO:0000250|UniProtKB:P30999, ECO:0000269|PubMed:11896187, CC ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:17047063}. CC -!- SUBCELLULAR LOCATION: [Isoform 1A]: Nucleus CC {ECO:0000269|PubMed:11896187}. CC -!- SUBCELLULAR LOCATION: [Isoform 2A]: Nucleus CC {ECO:0000269|PubMed:11896187}. CC -!- SUBCELLULAR LOCATION: [Isoform 3A]: Nucleus CC {ECO:0000269|PubMed:11896187}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=32; CC Comment=Isoforms result of a combination of four transcription start CC sites and three alternatively spliced exons(A, B and C).; CC Name=1ABC; CC IsoId=O60716-1; Sequence=Displayed; CC Name=1AB; Synonyms=p120-1AB {ECO:0000303|PubMed:25009281}; CC IsoId=O60716-2; Sequence=VSP_006743; CC Name=1AC; CC IsoId=O60716-3; Sequence=VSP_006745; CC Name=1BC; Synonyms=p120-1A {ECO:0000303|PubMed:25009281}; CC IsoId=O60716-4; Sequence=VSP_006744; CC Name=1A; CC IsoId=O60716-5; Sequence=VSP_006743, VSP_006745; CC Name=1B; CC IsoId=O60716-6; Sequence=VSP_006743, VSP_006744; CC Name=1C; CC IsoId=O60716-7; Sequence=VSP_006744, VSP_006745; CC Name=1; CC IsoId=O60716-8; Sequence=VSP_006743, VSP_006744, VSP_006745; CC Name=2ABC; CC IsoId=O60716-9; Sequence=VSP_006740; CC Name=2AB; CC IsoId=O60716-10; Sequence=VSP_006740, VSP_006743; CC Name=2AC; CC IsoId=O60716-11; Sequence=VSP_006740, VSP_006745; CC Name=2BC; CC IsoId=O60716-12; Sequence=VSP_006740, VSP_006744; CC Name=2A; CC IsoId=O60716-13; Sequence=VSP_006740, VSP_006743, VSP_006745; CC Name=2B; CC IsoId=O60716-14; Sequence=VSP_006740, VSP_006743, VSP_006744; CC Name=2C; CC IsoId=O60716-15; Sequence=VSP_006740, VSP_006744, VSP_006745; CC Name=2; CC IsoId=O60716-16; Sequence=VSP_006740, VSP_006743, VSP_006744, CC VSP_006745; CC Name=3ABC; CC IsoId=O60716-17; Sequence=VSP_006741; CC Name=3AB; CC IsoId=O60716-18; Sequence=VSP_006741, VSP_006743; CC Name=3AC; CC IsoId=O60716-19; Sequence=VSP_006741, VSP_006745; CC Name=3BC; CC IsoId=O60716-20; Sequence=VSP_006741, VSP_006744; CC Name=3A; CC IsoId=O60716-21; Sequence=VSP_006741, VSP_006743, VSP_006745; CC Name=3B; CC IsoId=O60716-22; Sequence=VSP_006741, VSP_006743, VSP_006744; CC Name=3C; CC IsoId=O60716-23; Sequence=VSP_006741, VSP_006744, VSP_006745; CC Name=3; CC IsoId=O60716-24; Sequence=VSP_006741, VSP_006743, VSP_006744, CC VSP_006745; CC Name=4ABC; CC IsoId=O60716-25; Sequence=VSP_006742; CC Name=4AB; CC IsoId=O60716-26; Sequence=VSP_006742, VSP_006743; CC Name=4AC; CC IsoId=O60716-27; Sequence=VSP_006742, VSP_006745; CC Name=4BC; CC IsoId=O60716-28; Sequence=VSP_006742, VSP_006744; CC Name=4A; CC IsoId=O60716-29; Sequence=VSP_006742, VSP_006743, VSP_006745; CC Name=4B; CC IsoId=O60716-30; Sequence=VSP_006742, VSP_006743, VSP_006744; CC Name=4C; CC IsoId=O60716-31; Sequence=VSP_006742, VSP_006744, VSP_006745; CC Name=4; CC IsoId=O60716-32; Sequence=VSP_006742, VSP_006743, VSP_006744, CC VSP_006745; CC -!- TISSUE SPECIFICITY: Expressed in vascular endothelium. Melanocytes and CC melanoma cells primarily express the long isoform 1A, whereas CC keratinocytes express shorter isoforms, especially 3A. The shortest CC isoform 4A, is detected in normal keratinocytes and melanocytes, and CC generally lost from cells derived from squamous cell carcinomas or CC melanomas. The C-terminal alternatively spliced exon B is present in CC the p120ctn transcripts in the colon, intestine and prostate, but lost CC in several tumor tissues derived from these organs. CC {ECO:0000269|PubMed:11896187, ECO:0000269|PubMed:14699141}. CC -!- INDUCTION: Induced in vascular endothelium by wounding. This effect is CC potentiated by prior laminar shear stress, which enhances wound CC closure. {ECO:0000269|PubMed:14699141}. CC -!- DOMAIN: A possible nuclear localization signal exists in all isoforms CC where Asp-626--631-Arg are deleted. CC -!- DOMAIN: ARM repeats 1 to 5 mediate interaction with cadherins. CC -!- PTM: Phosphorylated by FER and other protein-tyrosine kinases. CC Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ. CC {ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:17194753, CC ECO:0000269|PubMed:20564219, ECO:0000269|PubMed:7623846}. CC -!- DISEASE: Blepharocheilodontic syndrome 2 (BCDS2) [MIM:617681]: A form CC of blepharocheilodontic syndrome, a rare autosomal dominant disorder. CC It is characterized by lower eyelid ectropion, upper eyelid CC distichiasis, euryblepharon, bilateral cleft lip and palate, and CC features of ectodermal dysplasia, including hair anomalies, conical CC teeth and tooth agenesis. An additional rare manifestation is CC imperforate anus. There is considerable phenotypic variability among CC affected individuals. {ECO:0000269|PubMed:28301459}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20838.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ctnnd1/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40197/CTNND1"; 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; AF062319; AAC39804.1; -; mRNA. DR EMBL; AF062323; AAC39808.1; -; mRNA. DR EMBL; AF062341; AAC39826.1; -; mRNA. DR EMBL; AF062342; AAC39827.1; -; mRNA. DR EMBL; AF062322; AAC39807.1; -; mRNA. DR EMBL; AF062326; AAC39811.1; -; mRNA. DR EMBL; AF062328; AAC39813.1; -; mRNA. DR EMBL; AF062338; AAC39823.1; -; mRNA. DR EMBL; AF062324; AAC39809.1; -; mRNA. DR EMBL; AF062327; AAC39812.1; -; mRNA. DR EMBL; AF062329; AAC39814.1; -; mRNA. DR EMBL; AF062330; AAC39815.1; -; mRNA. DR EMBL; AF062331; AAC39816.1; -; mRNA. DR EMBL; AF062333; AAC39818.1; -; mRNA. DR EMBL; AF062334; AAC39819.1; -; mRNA. DR EMBL; AF062335; AAC39820.1; -; mRNA. DR EMBL; AF062336; AAC39821.1; -; mRNA. DR EMBL; AF062339; AAC39824.1; -; mRNA. DR EMBL; AF062340; AAC39825.1; -; mRNA. DR EMBL; AF062343; AAC39828.1; -; mRNA. DR EMBL; AF062317; AAC39802.1; -; mRNA. DR EMBL; AF062325; AAC39810.1; -; mRNA. DR EMBL; AF062332; AAC39817.1; -; mRNA. DR EMBL; AF062344; AAC39829.1; -; mRNA. DR EMBL; AF062321; AAC39806.1; -; mRNA. DR EMBL; AF062320; AAC39805.1; -; mRNA. DR EMBL; AF062337; AAC39822.1; -; mRNA. DR EMBL; AF062318; AAC39803.1; -; mRNA. DR EMBL; AB002382; BAA20838.2; ALT_INIT; mRNA. DR EMBL; AK292554; BAF85243.1; -; mRNA. DR EMBL; AY505564; AAR84236.1; -; Genomic_DNA. DR EMBL; AP001931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC075795; AAH75795.1; -; mRNA. DR CCDS; CCDS44604.1; -. [O60716-1] DR CCDS; CCDS44605.1; -. [O60716-2] DR CCDS; CCDS44606.1; -. [O60716-5] DR CCDS; CCDS44607.1; -. [O60716-6] DR CCDS; CCDS44608.1; -. [O60716-17] DR CCDS; CCDS44609.1; -. [O60716-21] DR CCDS; CCDS53632.1; -. [O60716-19] DR CCDS; CCDS53633.1; -. [O60716-18] DR CCDS; CCDS53634.1; -. [O60716-22] DR CCDS; CCDS55763.1; -. [O60716-9] DR CCDS; CCDS55764.1; -. [O60716-11] DR CCDS; CCDS55765.1; -. [O60716-10] DR CCDS; CCDS55766.1; -. [O60716-13] DR CCDS; CCDS55767.1; -. [O60716-14] DR CCDS; CCDS73290.1; -. [O60716-3] DR RefSeq; NP_001078927.1; NM_001085458.1. [O60716-1] DR RefSeq; NP_001078928.1; NM_001085459.1. [O60716-2] DR RefSeq; NP_001078929.1; NM_001085460.1. [O60716-5] DR RefSeq; NP_001078930.1; NM_001085461.1. [O60716-5] DR RefSeq; NP_001078931.1; NM_001085462.1. [O60716-5] DR RefSeq; NP_001078932.1; NM_001085463.1. [O60716-17] DR RefSeq; NP_001078933.1; NM_001085464.1. [O60716-18] DR RefSeq; NP_001078934.1; NM_001085465.1. [O60716-22] DR RefSeq; NP_001078935.1; NM_001085466.1. [O60716-19] DR RefSeq; NP_001078936.1; NM_001085467.1. [O60716-21] DR RefSeq; NP_001078937.1; NM_001085468.1. [O60716-21] DR RefSeq; NP_001078938.1; NM_001085469.1. [O60716-21] DR RefSeq; NP_001193812.1; NM_001206883.1. [O60716-9] DR RefSeq; NP_001193813.1; NM_001206884.1. [O60716-11] DR RefSeq; NP_001193814.1; NM_001206885.1. [O60716-3] DR RefSeq; NP_001193815.1; NM_001206886.1. [O60716-10] DR RefSeq; NP_001193816.1; NM_001206887.1. [O60716-14] DR RefSeq; NP_001193817.1; NM_001206888.1. [O60716-13] DR RefSeq; NP_001193818.1; NM_001206889.1. [O60716-13] DR RefSeq; NP_001193819.1; NM_001206890.1. [O60716-21] DR RefSeq; NP_001193820.1; NM_001206891.1. [O60716-13] DR RefSeq; NP_001322.1; NM_001331.2. [O60716-6] DR PDB; 3L6X; X-ray; 2.40 A; A=324-937. DR PDB; 3L6Y; X-ray; 3.00 A; A/C/E=324-937. DR PDBsum; 3L6X; -. DR PDBsum; 3L6Y; -. DR AlphaFoldDB; O60716; -. DR SMR; O60716; -. DR BioGRID; 107881; 232. DR CORUM; O60716; -. DR DIP; DIP-33850N; -. DR ELM; O60716; -. DR IntAct; O60716; 94. DR MINT; O60716; -. DR STRING; 9606.ENSP00000382004; -. DR TCDB; 8.A.160.1.1; the catenin (catenin) family. DR CarbonylDB; O60716; -. DR GlyConnect; 1078; 4 N-Linked glycans (1 site). DR GlyCosmos; O60716; 1 site, 3 glycans. DR GlyGen; O60716; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O60716; -. DR MetOSite; O60716; -. DR PhosphoSitePlus; O60716; -. DR SwissPalm; O60716; -. DR BioMuta; CTNND1; -. DR EPD; O60716; -. DR jPOST; O60716; -. DR MassIVE; O60716; -. DR MaxQB; O60716; -. DR PaxDb; 9606-ENSP00000382004; -. DR PeptideAtlas; O60716; -. DR ProteomicsDB; 49537; -. [O60716-1] DR ProteomicsDB; 49538; -. [O60716-10] DR ProteomicsDB; 49539; -. [O60716-11] DR ProteomicsDB; 49540; -. [O60716-12] DR ProteomicsDB; 49541; -. [O60716-13] DR ProteomicsDB; 49542; -. [O60716-14] DR ProteomicsDB; 49543; -. [O60716-15] DR ProteomicsDB; 49544; -. [O60716-16] DR ProteomicsDB; 49545; -. [O60716-17] DR ProteomicsDB; 49546; -. [O60716-18] DR ProteomicsDB; 49547; -. [O60716-19] DR ProteomicsDB; 49548; -. [O60716-2] DR ProteomicsDB; 49549; -. [O60716-20] DR ProteomicsDB; 49550; -. [O60716-21] DR ProteomicsDB; 49551; -. [O60716-22] DR ProteomicsDB; 49552; -. [O60716-23] DR ProteomicsDB; 49553; -. [O60716-24] DR ProteomicsDB; 49554; -. [O60716-25] DR ProteomicsDB; 49555; -. [O60716-26] DR ProteomicsDB; 49556; -. [O60716-27] DR ProteomicsDB; 49557; -. [O60716-28] DR ProteomicsDB; 49558; -. [O60716-29] DR ProteomicsDB; 49559; -. [O60716-3] DR ProteomicsDB; 49560; -. [O60716-30] DR ProteomicsDB; 49561; -. [O60716-31] DR ProteomicsDB; 49562; -. [O60716-32] DR ProteomicsDB; 49563; -. [O60716-4] DR ProteomicsDB; 49564; -. [O60716-5] DR ProteomicsDB; 49565; -. [O60716-6] DR ProteomicsDB; 49566; -. [O60716-7] DR ProteomicsDB; 49567; -. [O60716-8] DR ProteomicsDB; 49568; -. [O60716-9] DR Pumba; O60716; -. DR Antibodypedia; 2886; 1358 antibodies from 43 providers. DR DNASU; 1500; -. DR Ensembl; ENST00000358694.10; ENSP00000351527.6; ENSG00000198561.16. [O60716-5] DR Ensembl; ENST00000361332.8; ENSP00000354823.4; ENSG00000198561.16. [O60716-2] DR Ensembl; ENST00000361391.10; ENSP00000354785.6; ENSG00000198561.16. [O60716-6] DR Ensembl; ENST00000361796.9; ENSP00000354907.5; ENSG00000198561.16. [O60716-3] DR Ensembl; ENST00000399050.10; ENSP00000382004.5; ENSG00000198561.16. [O60716-1] DR Ensembl; ENST00000415361.6; ENSP00000403518.2; ENSG00000198561.16. [O60716-17] DR Ensembl; ENST00000426142.6; ENSP00000409930.2; ENSG00000198561.16. [O60716-21] DR Ensembl; ENST00000428599.6; ENSP00000413586.2; ENSG00000198561.16. [O60716-5] DR Ensembl; ENST00000524630.5; ENSP00000436543.1; ENSG00000198561.16. [O60716-5] DR Ensembl; ENST00000525902.5; ENSP00000434672.1; ENSG00000198561.16. [O60716-27] DR Ensembl; ENST00000526357.5; ENSP00000433334.1; ENSG00000198561.16. [O60716-10] DR Ensembl; ENST00000526772.5; ENSP00000433158.1; ENSG00000198561.16. [O60716-29] DR Ensembl; ENST00000526938.5; ENSP00000432041.1; ENSG00000198561.16. [O60716-7] DR Ensembl; ENST00000527467.5; ENSP00000434900.1; ENSG00000198561.16. [O60716-25] DR Ensembl; ENST00000528232.5; ENSP00000435266.1; ENSG00000198561.16. [O60716-19] DR Ensembl; ENST00000528621.5; ENSP00000432243.1; ENSG00000198561.16. [O60716-13] DR Ensembl; ENST00000529526.5; ENSP00000436323.1; ENSG00000198561.16. [O60716-13] DR Ensembl; ENST00000529873.5; ENSP00000435494.1; ENSG00000198561.16. [O60716-14] DR Ensembl; ENST00000529986.5; ENSP00000437156.1; ENSG00000198561.16. [O60716-21] DR Ensembl; ENST00000530094.5; ENSP00000437327.1; ENSG00000198561.16. [O60716-18] DR Ensembl; ENST00000530748.5; ENSP00000436744.1; ENSG00000198561.16. [O60716-11] DR Ensembl; ENST00000531014.5; ENSP00000432623.1; ENSG00000198561.16. [O60716-26] DR Ensembl; ENST00000532245.5; ENSP00000434017.1; ENSG00000198561.16. [O60716-21] DR Ensembl; ENST00000532463.5; ENSP00000432075.1; ENSG00000198561.16. [O60716-21] DR Ensembl; ENST00000532649.5; ENSP00000435379.1; ENSG00000198561.16. [O60716-13] DR Ensembl; ENST00000532787.5; ENSP00000434949.1; ENSG00000198561.16. [O60716-22] DR Ensembl; ENST00000532844.5; ENSP00000433276.1; ENSG00000198561.16. [O60716-9] DR Ensembl; ENST00000533667.5; ENSP00000437051.1; ENSG00000198561.16. [O60716-30] DR Ensembl; ENST00000534579.5; ENSP00000435789.1; ENSG00000198561.16. [O60716-13] DR Ensembl; ENST00000673683.1; ENSP00000500962.1; ENSG00000198561.16. [O60716-5] DR GeneID; 1500; -. DR KEGG; hsa:1500; -. DR MANE-Select; ENST00000399050.10; ENSP00000382004.5; NM_001085458.2; NP_001078927.1. DR UCSC; uc001nli.5; human. [O60716-1] DR AGR; HGNC:2515; -. DR CTD; 1500; -. DR DisGeNET; 1500; -. DR GeneCards; CTNND1; -. DR HGNC; HGNC:2515; CTNND1. DR HPA; ENSG00000198561; Low tissue specificity. DR MalaCards; CTNND1; -. DR MIM; 601045; gene. DR MIM; 617681; phenotype. DR neXtProt; NX_O60716; -. DR OpenTargets; ENSG00000198561; -. DR Orphanet; 1997; Blepharo-cheilo-odontic syndrome. DR PharmGKB; PA27016; -. DR VEuPathDB; HostDB:ENSG00000198561; -. DR eggNOG; KOG1048; Eukaryota. DR GeneTree; ENSGT00940000156045; -. DR HOGENOM; CLU_009111_4_1_1; -. DR InParanoid; O60716; -. DR OMA; GDQMSYP; -. DR OrthoDB; 5473239at2759; -. DR PhylomeDB; O60716; -. DR TreeFam; TF321877; -. DR PathwayCommons; O60716; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells. DR Reactome; R-HSA-9762292; Regulation of CDH11 function. DR Reactome; R-HSA-9764302; Regulation of CDH19 Expression and Function. DR Reactome; R-HSA-9833576; CDH11 homotypic and heterotypic interactions. DR SignaLink; O60716; -. DR SIGNOR; O60716; -. DR BioGRID-ORCS; 1500; 32 hits in 1170 CRISPR screens. DR ChiTaRS; CTNND1; human. DR EvolutionaryTrace; O60716; -. DR GeneWiki; CTNND1; -. DR GenomeRNAi; 1500; -. DR Pharos; O60716; Tbio. DR PRO; PR:O60716; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O60716; Protein. DR Bgee; ENSG00000198561; Expressed in ventricular zone and 102 other cell types or tissues. DR ExpressionAtlas; O60716; baseline and differential. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0016342; C:catenin complex; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IMP:BHF-UCL. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0005915; C:zonula adherens; IEA:Ensembl. DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl. DR GO; GO:0045296; F:cadherin binding; IDA:UniProt. DR GO; GO:0140311; F:protein sequestering activity; IDA:UniProt. DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:UniProtKB. DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR028435; Plakophilin/d_Catenin. DR PANTHER; PTHR10372:SF6; CATENIN DELTA-1; 1. DR PANTHER; PTHR10372; PLAKOPHILLIN-RELATED; 1. DR Pfam; PF00514; Arm; 4. DR SMART; SM00185; ARM; 7. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 3. DR Genevisible; O60716; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW Cell adhesion; Cell junction; Cell membrane; Coiled coil; Cytoplasm; KW Disease variant; Ectodermal dysplasia; Isopeptide bond; Membrane; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1..968 FT /note="Catenin delta-1" FT /id="PRO_0000064296" FT REPEAT 358..395 FT /note="ARM 1" FT REPEAT 398..437 FT /note="ARM 2" FT REPEAT 441..475 FT /note="ARM 3" FT REPEAT 476..516 FT /note="ARM 4" FT REPEAT 534..573 FT /note="ARM 5" FT REPEAT 583..624 FT /note="ARM 6" FT REPEAT 653..693 FT /note="ARM 7" FT REPEAT 700..739 FT /note="ARM 8" FT REPEAT 740..780 FT /note="ARM 9" FT REPEAT 781..826 FT /note="ARM 10" FT REGION 1..357 FT /note="Necessary and sufficient for interaction with FT CCDC85B" FT /evidence="ECO:0000269|PubMed:25009281" FT REGION 855..944 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 10..46 FT /evidence="ECO:0000255" FT COMPBIAS 855..872 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 873..888 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..910 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 911..925 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 401 FT /note="Essential for interaction with cadherins" FT /evidence="ECO:0000269|PubMed:20371349" FT SITE 478 FT /note="Essential for interaction with cadherins" FT /evidence="ECO:0000269|PubMed:20371349" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 59 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 112 FT /note="Phosphotyrosine; by FYN" FT /evidence="ECO:0000269|PubMed:17194753" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 217 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 221 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 228 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 257 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 280 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 288 FT /note="Phosphoserine; by PAK5" FT /evidence="ECO:0000269|PubMed:20564219, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 291 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 304 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 617 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 713 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 811 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 847 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 857 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 859 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 861 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 864 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 865 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 869 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 879 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 904 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES 906 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 916 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 920 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 943 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 421 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 517 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 882 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..323 FT /note="Missing (in isoform 4ABC, isoform 4AB, isoform 4AC, FT isoform 4BC, isoform 4A, isoform 4B, isoform 4C and isoform FT 4)" FT /evidence="ECO:0000305" FT /id="VSP_006742" FT VAR_SEQ 1..101 FT /note="Missing (in isoform 3ABC, isoform 3AB, isoform 3AC, FT isoform 3BC, isoform 3A, isoform 3B, isoform 3C and isoform FT 3)" FT /evidence="ECO:0000305" FT /id="VSP_006741" FT VAR_SEQ 1..54 FT /note="Missing (in isoform 2ABC, isoform 2AB, isoform 2AC, FT isoform 2BC, isoform 2A, isoform 2B, isoform 2C and isoform FT 2)" FT /evidence="ECO:0000305" FT /id="VSP_006740" FT VAR_SEQ 626..631 FT /note="Missing (in isoform 1AB, isoform 1A, isoform 1B, FT isoform 1, isoform 2AB, isoform 2A, isoform 2B, isoform 2, FT isoform 3AB, isoform 3A, isoform 3B, isoform 3, isoform FT 4AB, isoform 4A, isoform 4B and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_006743" FT VAR_SEQ 880..900 FT /note="Missing (in isoform 1BC, isoform 1B, isoform 1C, FT isoform 1, isoform 2BC, isoform 2B, isoform 2C, isoform 2, FT isoform 3BC, isoform 3B, isoform 3C, isoform 3, isoform FT 4BC, isoform 4B, isoform 4C and isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_006744" FT VAR_SEQ 937..965 FT /note="Missing (in isoform 1AC, isoform 1A, isoform 1C, FT isoform 1, isoform 2AC, isoform 2A, isoform 2C, isoform 2, FT isoform 3AC, isoform 3A, isoform 3C, isoform 3, isoform FT 4AC, isoform 4A, isoform 4C and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9205841" FT /id="VSP_006745" FT VARIANT 171 FT /note="S -> F (in dbSNP:rs11229133)" FT /id="VAR_038255" FT VARIANT 217 FT /note="Y -> C (in dbSNP:rs11570194)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_020929" FT VARIANT 365..968 FT /note="Missing (in BCDS2)" FT /evidence="ECO:0000269|PubMed:28301459" FT /id="VAR_079395" FT VARIANT 464 FT /note="R -> C (in dbSNP:rs11570199)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_020930" FT VARIANT 700..968 FT /note="Missing (in BCDS2)" FT /evidence="ECO:0000269|PubMed:28301459" FT /id="VAR_079396" FT VARIANT 915 FT /note="R -> K (in dbSNP:rs11570222)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_020931" FT MUTAGEN 363 FT /note="W->A: Severely disrupts cadherin interaction." FT /evidence="ECO:0000269|PubMed:20371349" FT MUTAGEN 401 FT /note="K->M: Complete loss of cadherin interaction." FT /evidence="ECO:0000269|PubMed:20371349" FT MUTAGEN 444 FT /note="K->M: Severely disrupts cadherin interaction." FT /evidence="ECO:0000269|PubMed:20371349" FT MUTAGEN 477 FT /note="W->A: Severely disrupts cadherin interaction." FT /evidence="ECO:0000269|PubMed:20371349" FT MUTAGEN 478 FT /note="N->A: Complete loss of cadherin interaction." FT /evidence="ECO:0000269|PubMed:20371349" FT CONFLICT 319 FT /note="R -> M (in Ref. 2; BAA20838)" FT /evidence="ECO:0000305" FT CONFLICT 380 FT /note="D -> G (in Ref. 6; AAH75795)" FT /evidence="ECO:0000305" FT HELIX 368..374 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 380..394 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 398..406 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 409..415 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 422..435 FT /evidence="ECO:0007829|PDB:3L6X" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 441..449 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 452..462 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 466..479 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 486..492 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 494..500 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 502..506 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 524..537 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 542..550 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 554..567 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 574..587 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 590..593 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 655..660 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 662..674 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 678..692 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 697..706 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 709..717 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 718..720 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 724..738 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 744..757 FT /evidence="ECO:0007829|PDB:3L6X" FT STRAND 759..763 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 766..768 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 772..786 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 790..798 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 801..809 FT /evidence="ECO:0007829|PDB:3L6X" FT STRAND 812..814 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 816..830 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 833..840 FT /evidence="ECO:0007829|PDB:3L6X" FT TURN 841..843 FT /evidence="ECO:0007829|PDB:3L6X" FT HELIX 846..849 FT /evidence="ECO:0007829|PDB:3L6X" FT MOTIF O60716-2:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-3:916 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-5:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-5:910 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18669648" FT MOTIF O60716-6:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-7:895 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-8:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-8:889 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-10:568..575 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-11:862 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-13:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-13:856 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18669648" FT MOTIF O60716-14:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-15:841 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-16:622..629 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-16:835 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-18:521..528 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-19:815 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-21:521..528 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-21:809 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18669648" FT MOTIF O60716-22:521..528 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-23:794 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-24:521..528 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-24:788 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18669648" FT MOTIF O60716-26:299..306 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-27:593 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-29:299..306 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-29:587 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-30:299..306 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-31:572 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOTIF O60716-32:299..306 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:P30999" FT MOD_RES O60716-32:566 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18669648" SQ SEQUENCE 968 AA; 108170 MW; D5C37489A891F292 CRC64; MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANPLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HSHLLYSTIP RMQEPGQIVE TYTEEDPEGA MSVVSVETSD DGTTRRTETT VKKVVKTVTT RTVQPVAMGP DGLPVDASSV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYSRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS DYGTARRTGT PSDPRRRLRS YEDMIGEEVP SDQYYWAPLA QHERGSLASL DSLRKGGPPP PNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PVLVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY QEAAPNVANN TGPHAASCFG AKKGKDEWFS RGKKPIEDPA NDTVDFPKRT SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIADLLT NEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVISILN TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIQM SNMGSNTKSL DNNYSTPNER GDHNRTLDRS GDLGDMEPLK GTTPLMQDEG QESLEEELDV LVLDDEGGQV SYPSMQKI //