CTNB1_CANLF
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 03-AUG-2022, entry version 110.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=CTNNB1;
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).
CC {ECO:0000250|UniProtKB:P35222, 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 SLC9A3R1.
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 {ECO:0000250|UniProtKB:P35222, ECO:0000250|UniProtKB:Q02248,
CC 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 unstabilized (high level of phosphorylation) or bound to
CC CDH1 (By similarity). Translocates to the nucleus when it is stabilized
CC (low level of phosphorylation) (By similarity). Interaction with GLIS2
CC and MUC1 promotes nuclear translocation (By similarity). Interaction
CC with 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 stabilizion 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}.
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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 CORUM; B6V8E6; -.
DR IntAct; B6V8E6; 7.
DR MINT; B6V8E6; -.
DR STRING; 9615.ENSCAFP00000007783; -.
DR iPTMnet; B6V8E6; -.
DR PaxDb; B6V8E6; -.
DR PRIDE; B6V8E6; -.
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; 321213at2759; -.
DR TreeFam; TF317997; -.
DR Proteomes; UP000002254; 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:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; 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:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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: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:0045893; P:positive regulation of transcription, DNA-templated; 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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 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
