ID CTNB1_CANLF Reviewed; 781 AA. AC B6V8E6; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Catenin beta-1 {ECO:0000250|UniProtKB:Q02248}; DE AltName: Full=Beta-catenin {ECO:0000303|PubMed:10873669}; GN Name=CTNNB1 {ECO:0000250|UniProtKB:Q02248}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Han J.-I., Na K.-J.; RT "Cloning and sequencing of the full-length canine beta-catenin cDNA."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer; RX PubMed=16341006; DOI=10.1038/nature04338; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [3] RP INTERACTION WITH RAPGEF2, AND SUBCELLULAR LOCATION. RX PubMed=10873669; DOI=10.1006/bbrc.2000.3002; RA Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A., RA Kaibuchi K.; RT "Identification of a novel beta-catenin-interacting protein."; RL Biochem. Biophys. Res. Commun. 273:712-717(2000). CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling CC pathway (By similarity). In the absence of Wnt, forms a complex with CC AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on CC N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC CC and its subsequent degradation by the proteasome. In the presence of CC Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, CC where it acts as a coactivator for transcription factors of the TCF/LEF CC family, leading to activate Wnt responsive genes (By similarity). CC Involved in the regulation of cell adhesion, as component of an E- CC cadherin:catenin adhesion complex (By similarity). Acts as a negative CC regulator of centrosome cohesion. Involved in the CC CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks CC anoikis of malignant kidney and intestinal epithelial cells and CC promotes their anchorage-independent growth by down-regulating DAPK2. CC Disrupts PML function and PML-NB formation by inhibiting RANBP2- CC mediated sumoylation of PML (By similarity). Promotes neurogenesis by CC maintaining sympathetic neuroblasts within the cell cycle. Involved in CC chondrocyte differentiation via interaction with SOX9: SOX9-binding CC competes with the binding sites of TCF/LEF within CTNNB1, thereby CC inhibiting the Wnt signaling (By similarity). Acts as a positive CC regulator of odontoblast differentiation during mesenchymal tooth germ CC formation, via promoting the transcription of differentiation factors CC such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a CC MSX1-mediated manner at the bell stage of mesenchymal tooth germ CC formation which prevents premature differentiation of odontoblasts (By CC similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- SUBUNIT: Two separate complex-associated pools are found in the CC cytoplasm. The majority is present as part of an E-cadherin/ catenin CC adhesion complex composed of at least E-cadherin/CDH1 and beta- CC catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the complex is CC located to adherens junctions. The stable association of CTNNA1 is CC controversial as CTNNA1 was shown not to bind to F-actin when assembled CC in the complex. Alternatively, the CTNNA1-containing complex may be CC linked to F-actin by other proteins such as LIMA1. Binds NHERF1. CC Interacts with PTPRU (via the cytoplasmic juxtamembrane domain) and CC with EMD. Interacts with SESTD1 and TRPC4. Interacts with CAV1. CC Interacts with PTPRJ. Interacts with PKT7. Interacts with FAT1 (via the CC cytoplasmic domain). Interacts with CDK2, NDRG2 and NANOS1. Interacts CC with NEK2 and CDK5. Interacts with CARM1, CXADR, PCDH11Y and PTK6. CC Interacts with SOX7; this interaction may lead to proteasomal CC degradation of active CTNNB1 and thus inhibition of Wnt/beta-catenin- CC stimulated transcription. Identified in a complex with HINT1 and MITF. CC Interacts with FHIT. Interacts with FERMT2. Identified in a complex CC with TCF4 and FERMT2. Another cytoplasmic pool is part of a large CC complex containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes CC phosphorylation on N-terminal Ser and Thr residues and ubiquitination CC of CTNNB1 via BTRC and its subsequent degradation by the proteasome. CC Wnt-dependent activation of DVL antagonizes the action of GSK3B. When CC GSK3B activity is inhibited, the complex disassociates, CTNNB1 is CC dephosphorylated and is no longer targeted for destruction. The CC stabilized protein translocates to the nucleus, where it binds TCF/LEF- CC 1 family members, BCL9, BCL9L and possibly also RUVBL1 and CHD8. CC Interacts with TAX1BP3 (via the PDZ domain); this interaction inhibits CC the transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1 CC and CTNNA3. Interacts with TRPV4; the TRPV4 and CTNNB1 complex can CC interact with CDH1. Interacts with VCL. The CTNNB1 and TCF4 complex CC interacts with PML. Interacts with XIRP1. Binds CTNNBIP and EP300. CC CTNNB1 forms a ternary complex with LEF1 and EP300 that is disrupted by CC CTNNBIP1 binding. Interacts directly with AXIN1; the interaction is CC regulated by CDK2 phosphorylation of AXIN1. Interacts with GLIS2. CC Interacts with SCRIB. Interacts with TNIK and TCF7L2. Interacts with CC SLC30A9. Interacts with RORA. May interact with P-cadherin/CDH3 (By CC similarity). Interacts with RAPGEF2 (PubMed:10873669). Interacts with CC RNF220 (By similarity). Interacts with CTNND2 (By similarity). CC Interacts (via the C-terminal region) with CBY1 (By similarity). The CC complex composed, at least, of APC, CTNNB1 and GSK3B interacts with CC JPT1; the interaction requires the inactive form of GSK3B CC (phosphorylated at 'Ser-9'). Interacts with DLG5 (By similarity). CC Interacts with FAM53B; promoting translocation to the nucleus. CC Interacts with TMEM170B (By similarity). Interacts with AHI1 (By CC similarity). Interacts with GID8 (By similarity). Component of an CC cadherin:catenin adhesion complex composed of at least of CDH26, beta- CC catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By CC similarity). Forms a complex comprising APPL1, RUVBL2, APPL2, HDAC1 and CC HDAC2 (By similarity). Interacts with IRF2BPL; mediates the CC ubiquitination and degradation of CTNNB1 (By similarity). Interacts CC with AMFR (By similarity). Interacts with LMBR1L (By similarity). CC Interacts with SOX30; prevents interaction of CTNNB1 with TCF7L2/TCF4 CC and leads to inhibition of Wnt signaling (By similarity). Interacts CC with SOX9; inhibiting CTNNB1 activity by competing with the binding CC sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling CC (By similarity). Interacts with SPN/CD43 cytoplasmic tail (By CC similarity). Interacts (when phosphorylated at Tyr-333) with isoform M2 CC of PKM (PKM2); promoting transcription activation (By similarity). CC Interacts with PKP2 (via HEAD domain) (By similarity). Interacts with CC CDH1 (By similarity). Interacts (when unphosphorylated) with FLYWCH1, CC perhaps preventing interaction of CTNNB1 with TCF4, and thereby CC regulating transcription activation; phosphorylation of CTNNB1 may CC inhibit the interaction (By similarity). Interacts (via the central CC armadillo domains) with probable transcriptional regulator ADNP (via N- CC terminal region); interaction is direct and stabilizes CTNNB1 by CC modulating its phosphorylation by glycogen synthase kinase-3 beta GSK3B CC (By similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248, ECO:0000269|PubMed:10873669}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35222}. Nucleus CC {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10873669}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:Q02248}. Cell junction CC {ECO:0000269|PubMed:10873669}. Cell membrane CC {ECO:0000250|UniProtKB:P35222}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P35222}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P35222}. CC Synapse {ECO:0000250|UniProtKB:Q02248}. Cytoplasm, cytoskeleton, cilium CC basal body {ECO:0000250|UniProtKB:Q02248}. Note=Colocalized with CC RAPGEF2 and TJP1 at cell-cell contacts (PubMed:10873669). Cytoplasmic CC when it is un-stable (highly phosphorylated) or bound to CDH1 (By CC similarity). Translocates to the nucleus when it is stabilized (low CC level of phosphorylation) (By similarity). Interaction with GLIS2 and CC MUC1 promotes nuclear translocation (By similarity). Interaction with CC EMD inhibits nuclear localization (By similarity). The majority of CC beta-catenin is localized to the cell membrane (By similarity). In CC interphase, colocalizes with CROCC between CEP250 puncta at the CC proximal end of centrioles, and this localization is dependent on CROCC CC and CEP250 (By similarity). In mitosis, when NEK2 activity increases, CC it localizes to centrosomes at spindle poles independent of CROCC (By CC similarity). Colocalizes with CDK5 in the cell-cell contacts and plasma CC membrane of undifferentiated and differentiated neuroblastoma cells (By CC similarity). Interaction with FAM53B promotes translocation to the CC nucleus (By similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000269|PubMed:10873669}. CC -!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of Ser-45 CC by another kinase. Phosphorylation proceeds then from Thr-41 to Ser-33. CC Phosphorylated by NEK2. EGF stimulates tyrosine phosphorylation. CC Phosphorylated on Ser-33 and Ser-37 by HIPK2. This phosphorylation CC triggers proteasomal degradation. Phosphorylation at Ser-552 by AMPK CC promotes stabilization of the protein, enhancing TCF/LEF-mediated CC transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5. CC Phosphorylation by CDK2 regulates insulin internalization. CC Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331 and/or Tyr-333 with CC the predominant site at Tyr-64 is not essential for inhibition of CC transcriptional activity. Phosphorylation by SRC at Tyr-333 promotes CC interaction with isoform M2 of PKM (PKM2); promoting transcription CC activation. {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when CC phosphorylated by GSK3B, leading to its degradation. Ubiquitinated by a CC E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, CC APC and TBL1X, leading to its subsequent proteasomal degradation (By CC similarity). Ubiquitinated and degraded following interaction with SOX9 CC (By similarity). {ECO:0000250|UniProtKB:P35222, CC ECO:0000250|UniProtKB:Q02248}. CC -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes CC VEGF-induced, NO-dependent endothelial cell permeability by disrupting CC interaction with E-cadherin, thus mediating disassembly adherens CC junctions. {ECO:0000250}. CC -!- PTM: O-glycosylation at Ser-23 decreases nuclear localization and CC transcriptional activity, and increases localization to the plasma CC membrane and interaction with E-cadherin CDH1. CC {ECO:0000250|UniProtKB:Q96S06}. CC -!- PTM: Deacetylated at Lys-49 by SIRT1. {ECO:0000250|UniProtKB:P35222}. CC -!- SIMILARITY: Belongs to the beta-catenin family. {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; FJ268743; ACJ04159.1; -; mRNA. DR EMBL; AAEX03013510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001131124.1; NM_001137652.1. DR RefSeq; XP_013961954.1; XM_014106479.1. DR RefSeq; XP_013961955.1; XM_014106480.1. DR AlphaFoldDB; B6V8E6; -. DR SMR; B6V8E6; -. DR BioGRID; 142757; 1. DR CORUM; B6V8E6; -. DR IntAct; B6V8E6; 7. DR MINT; B6V8E6; -. DR STRING; 9615.ENSCAFP00000007783; -. DR GlyCosmos; B6V8E6; 1 site, No reported glycans. DR iPTMnet; B6V8E6; -. DR PaxDb; 9612-ENSCAFP00000007783; -. DR GeneID; 477032; -. DR KEGG; cfa:477032; -. DR CTD; 1499; -. DR eggNOG; KOG4203; Eukaryota. DR HOGENOM; CLU_008757_1_1_1; -. DR InParanoid; B6V8E6; -. DR OMA; YPKLVYT; -. DR OrthoDB; 50711at2759; -. DR TreeFam; TF317997; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB. DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB. DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB. DR GO; GO:0016342; C:catenin complex; ISS:UniProtKB. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0030054; C:cell junction; ISS:UniProtKB. DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB. DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central. DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB. DR GO; GO:0070830; P:bicellular tight junction assembly; IDA:UniProtKB. DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB. DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISS:UniProtKB. DR GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB. DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB. DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB. DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; ISS:UniProtKB. DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB. DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0032355; P:response to estradiol; ISS:UniProtKB. DR GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB. DR CDD; cd21724; CTNNAbd_CTNNB1; 1. 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; IPR013284; Beta-catenin. DR PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1. DR PANTHER; PTHR45976:SF4; CATENIN BETA-1; 1. DR Pfam; PF00514; Arm; 4. DR PRINTS; PR01869; BCATNINFAMLY. DR SMART; SM00185; ARM; 12. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 9. PE 1: Evidence at protein level; KW Acetylation; Activator; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW S-nitrosylation; Synapse; Transcription; Transcription regulation; KW Ubl conjugation; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P35222" FT CHAIN 2..781 FT /note="Catenin beta-1" FT /id="PRO_0000423871" FT REPEAT 141..180 FT /note="ARM 1" FT REPEAT 181..223 FT /note="ARM 2" FT REPEAT 224..264 FT /note="ARM 3" FT REPEAT 265..306 FT /note="ARM 4" FT REPEAT 308..349 FT /note="ARM 5" FT REPEAT 350..390 FT /note="ARM 6" FT REPEAT 392..429 FT /note="ARM 7" FT REPEAT 430..473 FT /note="ARM 8" FT REPEAT 478..519 FT /note="ARM 9" FT REPEAT 520..582 FT /note="ARM 10" FT REPEAT 583..623 FT /note="ARM 11" FT REPEAT 624..664 FT /note="ARM 12" FT REGION 2..23 FT /note="Interaction with VCL" FT /evidence="ECO:0000250" FT REGION 34..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..178 FT /note="Interaction with BCL9" FT /evidence="ECO:0000250" FT REGION 705..781 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 772..781 FT /note="Interaction with SCRIB" FT /evidence="ECO:0000250" FT COMPBIAS 34..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 23 FT /note="Phosphoserine; by GSK3-beta; alternate" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 29 FT /note="Phosphoserine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 33 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 37 FT /note="Phosphoserine; by GSK3-beta and HIPK2" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 41 FT /note="Phosphothreonine; by GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 64 FT /note="Phosphotyrosine; by PTK6" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 142 FT /note="Phosphotyrosine; by FYN and PTK6" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 191 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 246 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 331 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 333 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 552 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000250|UniProtKB:Q02248" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT MOD_RES 619 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:Q02248" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P35222" FT CARBOHYD 23 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q96S06" SQ SEQUENCE 781 AA; 85511 MW; 6148652F953F0723 CRC64; MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTT QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEPLGYR QDDPSYRSFH SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD L //