ID CTND1_MOUSE Reviewed; 938 AA. AC P30999; Q3TSU9; Q80XQ4; Q8CHF8; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 20-JUN-2018, entry version 164. 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=Catns, Kiaa0384; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=SWR/J; RX PubMed=1334250; RA Reynolds A.B., Herbert L., Cleveland J.L., Berg S.T., Gaut J.R.; RT "p120, a novel substrate of protein tyrosine kinase receptors and of RT p60v-src, is related to cadherin-binding factors beta-catenin, RT plakoglobin and armadillo."; RL Oncogene 7:2439-2445(1992). RN [2] RP SEQUENCE REVISION. RA Reynolds A.B.; RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=12465718; DOI=10.1093/dnares/9.5.179; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., RA Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT I. The complete nucleotide sequences of 100 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 9:179-188(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP 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 RT zinc finger transcription factor."; RL Mol. Cell. Biol. 19:3614-3623(1999). RN [7] RP INTERACTION WITH ZBTB33. RX PubMed=12087177; DOI=10.1093/nar/gkf398; RA Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.; RT "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein RT that recognizes both a sequence-specific consensus and methylated CpG RT dinucleotides."; RL Nucleic Acids Res. 30:2911-2919(2002). RN [8] RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF 622-LYS-LYS-623. RX PubMed=15138284; DOI=10.1242/jcs.01101; RA Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.; RT "NLS-dependent nuclear localization of p120ctn is necessary to relieve RT Kaiso-mediated transcriptional repression."; RL J. Cell Sci. 117:2675-2686(2004). RN [9] RP ERRATUM. RA Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.; RL J. Cell Sci. 117:3405-3405(2004). RN [10] RP INTERACTION WITH GNA12 AND GNA13. 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 [11] RP FUNCTION. RX PubMed=15817151; DOI=10.1016/j.yexcr.2005.01.007; RA Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., RA Daniel J.M.; RT "The catenin p120ctn inhibits Kaiso-mediated transcriptional RT repression of the beta-catenin/TCF target gene matrilysin."; RL Exp. Cell Res. 305:253-265(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217; TYR-221 AND RP TYR-280, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [14] RP INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17344476; DOI=10.1091/mbc.E06-10-0941; RA Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., RA Gevaert K., Birchmeier W., Briscoe J., Fujita Y.; RT "The transcriptional repressor Glis2 is a novel binding partner for RT p120 catenin."; RL Mol. Biol. Cell 18:1918-1927(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-288; RP SER-349; SER-847; SER-857; TYR-865 AND SER-899, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion RT affinity chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349; RP SER-352 AND TYR-904, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-59; SER-225; RP SER-230; SER-252; SER-269; SER-288; TYR-291; SER-300; THR-304; RP SER-320; SER-349; SER-352; SER-713; SER-847; SER-857; SER-864; RP TYR-865; SER-868; THR-869; SER-899 AND SER-920, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Binds to and inhibits the transcriptional repressor CC ZBTB33, which may lead to activation of target genes of the Wnt CC signaling pathway (By similarity). Associates with and regulates CC the cell adhesion properties of both C-, E- and N-cadherins, being CC critical for their surface stability. Implicated both in cell CC transformation by SRC and in ligand-induced receptor signaling CC through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 CC C-terminal cleavage. {ECO:0000250, ECO:0000269|PubMed:15138284, CC ECO:0000269|PubMed:15817151, ECO:0000269|PubMed:17344476}. CC -!- SUBUNIT: Belongs to a multiprotein cell-cell adhesion complex that CC also contains E-cadherin/CDH1, alpha-catenin/CTNNA1, beta- CC catenin/CTNNB1, and gamma-catenin/JUP. Binds to the C-terminal CC fragment of PSEN1 and mutually competes for CDH1 (By similarity). CC Interacts with ZBTB33 (PubMed:10207085, PubMed:12087177). CC Interacts with GLIS2 (PubMed:17344476). Interacts with FER (By CC similarity). Interacts with NANOS1 (via N-terminal region) (By CC similarity). Interacts (via N-terminus) with GNA12; the CC interaction regulates CDH1-mediated cell-cell adhesion CC (PubMed:15240885). Interacts with GNA13 (PubMed:15240885). CC {ECO:0000250|UniProtKB:O60716, ECO:0000269|PubMed:10207085, CC ECO:0000269|PubMed:12087177, ECO:0000269|PubMed:15240885, CC ECO:0000269|PubMed:17344476}. CC -!- INTERACTION: CC Q60598:Cttn; NbExp=4; IntAct=EBI-529924, EBI-397955; CC P35235:Ptpn11; NbExp=3; IntAct=EBI-529924, EBI-397236; CC Q8BN78:Zbtb33; NbExp=3; IntAct=EBI-529924, EBI-1216314; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15138284, CC ECO:0000269|PubMed:17344476}. Nucleus CC {ECO:0000269|PubMed:15138284, ECO:0000269|PubMed:17344476}. Cell CC membrane {ECO:0000269|PubMed:17344476}. Note=Interaction with CC GLIS2 promotes nuclear translocation (PubMed:17344476). Detected CC at cell-cell contacts (By similarity). NANOS1 induces its CC translocation from sites of cell-cell contact to the cytoplasm (By CC similarity). CDH1 enhances cell membrane localization (By CC similarity). {ECO:0000250|UniProtKB:O60716, CC ECO:0000269|PubMed:17344476}. CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus CC {ECO:0000269|PubMed:15138284}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P30999-1; Sequence=Displayed; CC Name=2; CC IsoId=P30999-2; Sequence=VSP_030567, VSP_030568; CC Note=Contains a nuclear localization signal (NLS) domain at CC positions 622-629. {ECO:0000269|PubMed:15138284}; CC Name=3; CC IsoId=P30999-3; Sequence=VSP_030568; CC -!- DOMAIN: ARM repeats 1 to 5 mediate interaction with cadherins. CC {ECO:0000250}. CC -!- PTM: Phosphorylated by FER and other protein-tyrosine kinases. CC Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC41421.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z17804; CAA79078.1; -; mRNA. DR EMBL; AB093237; BAC41421.1; ALT_INIT; mRNA. DR EMBL; AK133193; BAE21551.1; -; mRNA. DR EMBL; AK161790; BAE36576.1; -; mRNA. DR EMBL; BC043108; AAH43108.1; -; mRNA. DR EMBL; BC054544; AAH54544.1; -; mRNA. DR CCDS; CCDS16186.1; -. [P30999-1] DR CCDS; CCDS50622.1; -. [P30999-2] DR CCDS; CCDS50623.1; -. [P30999-3] DR PIR; I48701; S28498. DR RefSeq; NP_001078917.1; NM_001085448.1. [P30999-3] DR RefSeq; NP_001078918.1; NM_001085449.1. DR RefSeq; NP_001078919.1; NM_001085450.1. [P30999-1] DR RefSeq; NP_001078922.1; NM_001085453.1. [P30999-2] DR RefSeq; NP_031641.2; NM_007615.4. [P30999-1] DR RefSeq; XP_006498698.1; XM_006498635.1. DR RefSeq; XP_017170690.1; XM_017315201.1. [P30999-1] DR RefSeq; XP_017170697.1; XM_017315208.1. [P30999-3] DR UniGene; Mm.35738; -. DR ProteinModelPortal; P30999; -. DR SMR; P30999; -. DR BioGrid; 198513; 25. DR CORUM; P30999; -. DR DIP; DIP-31972N; -. DR IntAct; P30999; 23. DR MINT; P30999; -. DR STRING; 10090.ENSMUSP00000064518; -. DR iPTMnet; P30999; -. DR PhosphoSitePlus; P30999; -. DR SwissPalm; P30999; -. DR MaxQB; P30999; -. DR PaxDb; P30999; -. DR PeptideAtlas; P30999; -. DR PRIDE; P30999; -. DR Ensembl; ENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3] DR Ensembl; ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2] DR Ensembl; ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1] DR Ensembl; ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1] DR Ensembl; ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3] DR Ensembl; ENSMUST00000189772; ENSMUSP00000141166; ENSMUSG00000101645. [P30999-1] DR GeneID; 12388; -. DR KEGG; mmu:12388; -. DR UCSC; uc008kio.1; mouse. [P30999-3] DR UCSC; uc008kip.1; mouse. [P30999-1] DR UCSC; uc008kit.1; mouse. [P30999-2] DR CTD; 1500; -. DR MGI; MGI:105100; Ctnnd1. DR eggNOG; KOG1048; Eukaryota. DR eggNOG; ENOG410Y21Q; LUCA. DR GeneTree; ENSGT00760000119167; -. DR HOGENOM; HOG000231862; -. DR HOVERGEN; HBG004284; -. DR InParanoid; P30999; -. DR KO; K05690; -. DR PhylomeDB; P30999; -. DR TreeFam; TF321877; -. DR Reactome; R-MMU-418990; Adherens junctions interactions. DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability. DR ChiTaRS; Ctnnd1; mouse. DR PRO; PR:P30999; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; ENSMUSG00000034101; -. DR CleanEx; MM_CTNND1; -. DR ExpressionAtlas; P30999; baseline and differential. DR Genevisible; P30999; MM. DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI. DR GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0005915; C:zonula adherens; ISO:MGI. DR GO; GO:0045296; F:cadherin binding; ISO:MGI. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0007155; P:cell adhesion; IMP:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI. DR GO; GO:0060690; P:epithelial cell differentiation involved in salivary gland development; IMP:MGI. DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0001822; P:kidney development; IMP:MGI. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IGI:MGI. DR GO; GO:0010954; P:positive regulation of protein processing; IMP:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. 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; 2. DR PROSITE; PS50176; ARM_REPEAT; 3. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell adhesion; Cell membrane; KW Coiled coil; Complete proteome; Cytoplasm; Isopeptide bond; Membrane; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1 938 Catenin delta-1. FT /FTId=PRO_0000064297. FT REPEAT 358 395 ARM 1. FT REPEAT 398 437 ARM 2. FT REPEAT 441 475 ARM 3. FT REPEAT 476 516 ARM 4. FT REPEAT 534 573 ARM 5. FT REPEAT 583 624 ARM 6. FT REPEAT 653 693 ARM 7. FT REPEAT 700 739 ARM 8. FT REPEAT 740 780 ARM 9. FT REPEAT 781 826 ARM 10. FT COILED 10 46 {ECO:0000255}. FT SITE 401 401 Essential for interaction with cadherins. FT {ECO:0000250}. FT SITE 478 478 Essential for interaction with cadherins. FT {ECO:0000250}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 4 4 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 47 47 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 59 59 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 112 112 Phosphotyrosine; by FYN. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 125 125 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 217 217 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT MOD_RES 221 221 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT MOD_RES 225 225 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 228 228 Phosphotyrosine. FT {ECO:0000244|PubMed:19131326}. FT MOD_RES 230 230 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 252 252 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 257 257 Phosphotyrosine. FT {ECO:0000244|PubMed:19131326}. FT MOD_RES 268 268 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 269 269 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 280 280 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT MOD_RES 288 288 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 291 291 Phosphotyrosine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 300 300 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 304 304 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 320 320 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 346 346 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 349 349 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:18630941, FT ECO:0000244|PubMed:19131326, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 352 352 Phosphoserine. FT {ECO:0000244|PubMed:19131326, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 617 617 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 713 713 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 811 811 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 847 847 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 857 857 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 859 859 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 861 861 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 864 864 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 865 865 Phosphotyrosine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 868 868 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 869 869 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 879 879 Phosphoserine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 899 899 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 904 904 Phosphotyrosine. FT {ECO:0000244|PubMed:17947660, FT ECO:0000244|PubMed:19131326}. FT MOD_RES 906 906 Phosphothreonine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 916 916 Phosphothreonine. FT {ECO:0000250|UniProtKB:O60716}. FT MOD_RES 920 920 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT CROSSLNK 421 421 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:O60716}. FT CROSSLNK 517 517 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:O60716}. FT CROSSLNK 882 882 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:O60716}. FT VAR_SEQ 626 631 Missing (in isoform 2). FT {ECO:0000303|PubMed:1334250}. FT /FTId=VSP_030567. FT VAR_SEQ 880 900 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:12465718, FT ECO:0000303|PubMed:1334250, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_030568. FT MUTAGEN 622 623 KK->AA: Abolishes nuclear localization. FT {ECO:0000269|PubMed:15138284}. FT CONFLICT 405 405 R -> A (in Ref. 1; CAA79078). FT {ECO:0000305}. FT CONFLICT 676 676 K -> N (in Ref. 1; CAA79078). FT {ECO:0000305}. FT CONFLICT 715 715 I -> R (in Ref. 1; CAA79078). FT {ECO:0000305}. FT CONFLICT 752 752 I -> R (in Ref. 1; CAA79078). FT {ECO:0000305}. SQ SEQUENCE 938 AA; 104925 MW; 2F13DB7350355832 CRC64; MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI //