CTND1_HUMAN
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 03-AUG-2022, entry version 212.
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="http://atlasgeneticsoncology.org/Genes/CTNND1ID40197ch11q11.html";
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; 184.
DR CORUM; O60716; -.
DR DIP; DIP-33850N; -.
DR ELM; O60716; -.
DR IntAct; O60716; 80.
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 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; O60716; -.
DR PeptideAtlas; O60716; -.
DR PRIDE; 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 Antibodypedia; 2886; 1134 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 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; 233858at2759; -.
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 SignaLink; O60716; -.
DR SIGNOR; O60716; -.
DR BioGRID-ORCS; 1500; 30 hits in 1090 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 100 other tissues.
DR ExpressionAtlas; O60716; baseline and differential.
DR Genevisible; O60716; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IDA:UniProtKB.
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:UniProtKB.
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; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
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; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028439; Catenin_d1.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF6; PTHR10372:SF6; 1.
DR Pfam; PF00514; Arm; 3.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
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
