ID TF7L2_MOUSE Reviewed; 459 AA. AC Q924A0; O70574; Q8C834; Q91XP2; Q91XP3; Q91XP4; Q924A1; Q9Z0V3; Q9Z0V4; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 2. DT 26-FEB-2020, entry version 174. DE RecName: Full=Transcription factor 7-like 2; DE AltName: Full=HMG box transcription factor 4; DE AltName: Full=T-cell-specific transcription factor 4; DE Short=T-cell factor 4; DE Short=TCF-4; DE Short=mTCF-4; GN Name=Tcf7l2; Synonyms=Tcf4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=9488439; DOI=10.1128/mcb.18.3.1248; RA Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G., RA Markman M., Lamers W., Destree O., Clevers H.; RT "Two members of the Tcf family implicated in Wnt/b-catenin signaling during RT embryogenesis in the mouse."; RL Mol. Cell. Biol. 18:1248-1256(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL NUCLEOTIDE SEQUENCE RP [MRNA] (ISOFORMS 1 AND 4). RC STRAIN=ICR; TISSUE=Fetal intestine; RX PubMed=9880534; DOI=10.1074/jbc.274.3.1566; RA Lee Y.J., Swencki B., Shoichet S., Shivdasani R.A.; RT "A possible role for the high mobility group box transcription factor Tcf-4 RT in vertebrate gut epithelial cell differentiation."; RL J. Biol. Chem. 274:1566-1572(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 6 AND 7), AND PARTIAL RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5). RC STRAIN=C57BL/6J, and CD-1; TISSUE=Pituitary; RX PubMed=11845287; DOI=10.1007/s00335-001-2076-0; RA Douglas K.R., Brinkmeier M.L., Kennell J.A., Eswara P., Harrison T.A., RA Patrianakos A.I., Sprecher B.S., Potok M.A., Lyons R.H. Jr., RA MacDougald O.A., Camper S.A.; RT "Identification of members of the Wnt signaling pathway in the embryonic RT pituitary gland."; RL Mamm. Genome 12:843-851(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). RA Bayarsaihan D.; RT "A novel isoform of the HMG transcription factor Tcf4."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9). RC STRAIN=C57BL/6J; TISSUE=Head; 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [7] RP FUNCTION. RX PubMed=9697701; DOI=10.1038/1270; RA Korinek V., Barker N., Moerer P., van Donselaar E., Huls G., Peters P.J., RA Clevers H.; RT "Depletion of epithelial stem-cell compartments in the small intestine of RT mice lacking Tcf-4."; RL Nat. Genet. 19:379-383(1998). RN [8] RP INTERACTION WITH TGFB1I1. RX PubMed=16291758; DOI=10.1074/jbc.m505869200; RA Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.; RT "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor- RT driven transcription."; RL J. Biol. Chem. 281:1755-1764(2006). RN [9] RP INTERACTION WITH TNIK AND CTNNB1. RX PubMed=19816403; DOI=10.1038/emboj.2009.285; RA Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., RA Heck A.J., Clevers H.; RT "The kinase TNIK is an essential activator of Wnt target genes."; RL EMBO J. 28:3329-3340(2009). RN [10] RP FUNCTION. RX PubMed=21856776; DOI=10.1101/gad.17227011; RA Vacik T., Stubbs J.L., Lemke G.; RT "A novel mechanism for the transcriptional regulation of Wnt signaling in RT development."; RL Genes Dev. 25:1783-1795(2011). CC -!- FUNCTION: Participates in the Wnt signaling pathway and modulates MYC CC expression by binding to its promoter in a sequence-specific manner. CC Acts as repressor in the absence of CTNNB1, and as activator in its CC presence. Activates transcription from promoters with several copies of CC the Tcf motif CCTTTGATC in the presence of CTNNB1. TLE1, TLE2, TLE3 and CC TLE4 repress transactivation mediated by TCF7L2/TCF4 and CTNNB1. CC Expression of dominant-negative mutants results in cell-cycle arrest in CC G1 (By similarity). Necessary for the maintenance of the epithelial CC stem-cell compartment of the small intestine. {ECO:0000250, CC ECO:0000269|PubMed:21856776, ECO:0000269|PubMed:9697701}. CC -!- SUBUNIT: Interacts with TGFB1I1 (PubMed:16291758). Interacts with SPIN1 CC (By similarity). Interacts with CTNNB1 (via the armadillo repeat); CC forms stable transcription complex (PubMed:19816403). Interacts with CC EP300. Interacts with NLK. Interacts with CCDC85B (probably through the CC HMG box); prevents interaction with CTNNB1 (By similarity). Interacts CC with TNIK (PubMed:19816403). Interacts with MAD2L2; prevents CC TCF7L2/TCF4 binding to promZIPK/DAPK3oters, negatively modulating its CC transcriptional activity. Interacts with ZIPK/DAPK3. Interacts with CC XIAP/BIRC4 and TLE3. Interacts with DDIT3/CHOP. The CTNNB1 and CC TCF7L2/TCF4 complex interacts with PML (isoform PML-4). Identified in a CC complex with CTNNB1 and FERMT2. Interacts with C11orf84/SPINDOC in a CC SPIN1-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9NQB0, CC ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:19816403}. CC -!- INTERACTION: CC Q9R1Y5:Hic1; NbExp=4; IntAct=EBI-646713, EBI-5236187; CC P39428:Traf1; NbExp=6; IntAct=EBI-646713, EBI-520123; CC -!- SUBCELLULAR LOCATION: Nucleus, PML body. Note=Diffuse pattern. CC Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic CC leukemia) nuclear bodies (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; CC IsoId=Q924A0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q924A0-2; Sequence=VSP_006976, VSP_006979; CC Name=3; CC IsoId=Q924A0-3; Sequence=VSP_006975; CC Name=4; CC IsoId=Q924A0-4; Sequence=VSP_006978, VSP_006981; CC Name=5; CC IsoId=Q924A0-5; Sequence=VSP_006974, VSP_006977; CC Name=6; CC IsoId=Q924A0-6; Sequence=VSP_006977; CC Name=7; CC IsoId=Q924A0-7; Sequence=VSP_006973, VSP_006975, VSP_006977; CC Name=8; CC IsoId=Q924A0-8; Sequence=VSP_006976, VSP_006980; CC Name=9; Synonyms=dnTcf7l2 exon1b/c; CC IsoId=Q924A0-9; Sequence=VSP_043205; CC -!- TISSUE SPECIFICITY: Detected in adult brain and liver, and at lower CC levels in intestine, with a clear increase from the distal colon to the CC duodenum. Detected at low levels in heart, lung, kidney, pituitary and CC testis. CC -!- DEVELOPMENTAL STAGE: First detected at 10.5 dpc. Highly expressed at CC 13.5 dpc-16.5 dpc in the central nervous system, in particular in the CC roof of the mesencephalon, at the ditelencephalic junction and in CC dorsal thalamus. At 13.5 dpc, detected at low levels in CC gastrointestinal epithelia. CC -!- PTM: Phosphorylated at Thr-178 and/or Thr-189 by NLK. Phosphorylation CC by NLK at these sites inhibits DNA-binding by TCF7L2/TCF4, thereby CC preventing transcriptional activation of target genes of the canonical CC Wnt/beta-catenin signaling pathway (By similarity). {ECO:0000250}. CC -!- PTM: Polysumoylated. Sumoylation is enhanced by PIAS family members and CC desumoylation is enhanced by SENP2. Sumoylation/desumoylation regulates CC TCF7L2/TCF4 transcription activity in the Wnt/beta-catenin signaling CC pathway without altering interaction with CTNNB1 nor binding to DNA (By CC similarity). {ECO:0000250}. CC -!- DISEASE: Note=Constitutive activation and subsequent transactivation of CC target genes may lead to the maintenance of stem-cell characteristics CC (cycling and longevity) in cells that should normally undergo terminal CC differentiation and constitute the primary transforming event in CC colorectal cancer (CRC). CC -!- MISCELLANEOUS: [Isoform 8]: May result from the retention of an intron CC in the cDNA. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Dominant negative form which cannot bind CC CTNNB1. Expression is VAX2-dependent. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TCF/LEF 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; AJ223070; CAA11071.1; -; mRNA. DR EMBL; AF107298; AAD16967.1; -; mRNA. DR EMBL; AF107299; AAD16968.1; -; mRNA. DR EMBL; AF363722; AAK77485.1; -; Genomic_DNA. DR EMBL; AF363722; AAK77486.1; -; Genomic_DNA. DR EMBL; AF363724; AAK77488.1; -; mRNA. DR EMBL; AF363725; AAK77489.1; -; mRNA. DR EMBL; AF363726; AAK77490.1; -; mRNA. DR EMBL; AY072035; AAL58534.1; -; mRNA. DR EMBL; AK048536; BAC33366.1; -; mRNA. DR EMBL; AC118695; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC137148; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157916; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS50470.1; -. [Q924A0-2] DR CCDS; CCDS50471.1; -. [Q924A0-1] DR CCDS; CCDS50474.1; -. [Q924A0-9] DR RefSeq; NP_001136390.1; NM_001142918.2. DR RefSeq; NP_001136393.1; NM_001142921.2. DR RefSeq; NP_001136396.1; NM_001142924.2. [Q924A0-9] DR SMR; Q924A0; -. DR BioGrid; 204009; 10. DR DIP; DIP-40920N; -. DR IntAct; Q924A0; 5. DR MINT; Q924A0; -. DR STRING; 10090.ENSMUSP00000107283; -. DR iPTMnet; Q924A0; -. DR PhosphoSitePlus; Q924A0; -. DR PaxDb; Q924A0; -. DR PeptideAtlas; Q924A0; -. DR PRIDE; Q924A0; -. DR Ensembl; ENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9] DR GeneID; 21416; -. DR KEGG; mmu:21416; -. DR UCSC; uc008hya.2; mouse. [Q924A0-6] DR UCSC; uc008hyb.2; mouse. [Q924A0-5] DR UCSC; uc008hyk.2; mouse. [Q924A0-2] DR UCSC; uc008hyn.2; mouse. [Q924A0-9] DR CTD; 6934; -. DR MGI; MGI:1202879; Tcf7l2. DR eggNOG; KOG3248; Eukaryota. DR eggNOG; ENOG41109RU; LUCA. DR GeneTree; ENSGT00940000155535; -. DR HOGENOM; CLU_013229_1_0_1; -. DR InParanoid; Q924A0; -. DR KO; K04491; -. DR OrthoDB; 807716at2759; -. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR Reactome; R-MMU-4641265; Repression of WNT target genes. DR Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling. DR ChiTaRS; Tcf7l2; mouse. DR PRO; PR:Q924A0; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q924A0; protein. DR Bgee; ENSMUSG00000024985; Expressed in inferior colliculus and 347 other tissues. DR ExpressionAtlas; Q924A0; baseline and differential. DR Genevisible; Q924A0; MM. DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISO:MGI. DR GO; GO:0071664; C:catenin-TCF7L2 complex; IDA:BHF-UCL. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0000790; C:nuclear chromatin; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0005667; C:transcription factor complex; IDA:MGI. DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI. DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI. DR GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0008134; F:transcription factor binding; ISO:MGI. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI. DR GO; GO:0001568; P:blood vessel development; ISO:MGI. DR GO; GO:0030282; P:bone mineralization; IGI:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISO:MGI. DR GO; GO:0007050; P:cell cycle arrest; ISO:MGI. DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:MGI. DR GO; GO:0009267; P:cellular response to starvation; IMP:MGI. DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:MGI. DR GO; GO:0030538; P:embryonic genitalia morphogenesis; IGI:MGI. DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IGI:MGI. DR GO; GO:0060325; P:face morphogenesis; IGI:MGI. DR GO; GO:0045444; P:fat cell differentiation; ISO:MGI. DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI. DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI. DR GO; GO:0005977; P:glycogen metabolic process; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:1901142; P:insulin metabolic process; IMP:MGI. DR GO; GO:0043570; P:maintenance of DNA repeat elements; ISO:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0048625; P:myoblast fate commitment; IMP:MGI. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI. DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI. DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISO:MGI. DR GO; GO:0021915; P:neural tube development; IGI:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI. DR GO; GO:0014003; P:oligodendrocyte development; IMP:MGI. DR GO; GO:0021983; P:pituitary gland development; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:MGI. DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISO:MGI. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL. DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:MGI. DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL. DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0035947; P:regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter; IMP:MGI. DR GO; GO:0032350; P:regulation of hormone metabolic process; ISO:MGI. DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI. DR GO; GO:0031641; P:regulation of myelination; IMP:MGI. DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:MGI. DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:MGI. DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI. DR GO; GO:0009749; P:response to glucose; IMP:BHF-UCL. DR GO; GO:0032252; P:secretory granule localization; IMP:MGI. DR GO; GO:0043588; P:skin development; IGI:MGI. DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central. DR Gene3D; 1.10.30.10; -; 1. DR Gene3D; 4.10.900.10; -; 1. DR InterPro; IPR027397; Catenin_binding_dom_sf. DR InterPro; IPR013558; CTNNB1-bd_N. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR024940; TCF/LEF. DR PANTHER; PTHR10373; PTHR10373; 1. DR Pfam; PF08347; CTNNB1_binding; 1. DR Pfam; PF00505; HMG_box; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; SSF47095; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1..459 FT /note="Transcription factor 7-like 2" FT /id="PRO_0000048624" FT DNA_BIND 327..395 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..53 FT /note="CTNNB1-binding" FT REGION 178..372 FT /note="Mediates interaction with MAD2L2" FT /evidence="ECO:0000250" FT MOTIF 402..408 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 155..294 FT /note="Pro-rich" FT MOD_RES 178 FT /note="Phosphothreonine; by NLK" FT /evidence="ECO:0000250|UniProtKB:Q9NQB0" FT MOD_RES 189 FT /note="Phosphothreonine; by NLK" FT /evidence="ECO:0000250|UniProtKB:Q9NQB0" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9NQB0" FT CROSSLNK 297 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VAR_SEQ 1..161 FT /note="MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDLADVKSSLVNES FT ETNQDSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDL FT TSPYLPNGSLSPTARTYLQMKWPLLDVQAGSLQSRQTLKDARSPSPAHIV -> M (in FT isoform 9)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_043205" FT VAR_SEQ 127 FT /note="T -> TLHFQSGSTHYSAYKTIEHQIAIQ (in isoform 7)" FT /evidence="ECO:0000303|PubMed:11845287" FT /id="VSP_006973" FT VAR_SEQ 161 FT /note="V -> VQSPLPCCTQGHACPHFYTPSDFTVSTQVFRDTKSSHSLQKVGEPWY FT LE (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_006974" FT VAR_SEQ 237..240 FT /note="Missing (in isoform 3 and isoform 7)" FT /evidence="ECO:0000303|PubMed:11845287" FT /id="VSP_006975" FT VAR_SEQ 268 FT /note="S -> SSFLSS (in isoform 2 and isoform 8)" FT /evidence="ECO:0000303|PubMed:9880534, ECO:0000303|Ref.4" FT /id="VSP_006976" FT VAR_SEQ 270..459 FT /note="Missing (in isoform 5, isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:11845287" FT /id="VSP_006977" FT VAR_SEQ 417..459 FT /note="EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL -> GEKKS FT AFATYKVKAAASAHPLQMEAY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9880534" FT /id="VSP_006979" FT VAR_SEQ 417..459 FT /note="EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCSL -> GERGE FT SGRWRLEDHSYVRLPSGGGRRNPRPGHCGEPILGSLFCLCVF (in isoform 8)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_006980" FT VAR_SEQ 417..433 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_006978" FT VAR_SEQ 457..459 FT /note="CSL -> ADANTPKKCRALFGLDRQTLWCKPCRRKKKCVRYIQGEGSCLSPP FT SSDGSLLDSPPPSPHLLGSPPQDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAE FT AAHGKASALCPNGALDLPPAALQPSMVPSSSLAQPSTSSLHSHNSLAGTQPQPLSLVTK FT SLE (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_006981" FT CONFLICT 57 FT /note="D -> N (in Ref. 2; AAD16967 and 3; AAK77488/ FT AAK77489/AAK77490)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="W -> R (in Ref. 4; AAL58534)" FT /evidence="ECO:0000305" FT CONFLICT 410 FT /note="K -> Q (in Ref. 2; AAD16968)" FT /evidence="ECO:0000305" SQ SEQUENCE 459 AA; 51217 MW; 43BC307DC258E83F CRC64; MPQLNGGGGD DLGANDELIS FKDEGEQEEK NSENSSAERD LADVKSSLVN ESETNQDSSS DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS LSPTARTYLQ MKWPLLDVQA GSLQSRQTLK DARSPSPAHI VSNKVPVVQH PHHVHPLTPL ITYSNEHFTP GNPPPHLPAD VDPKTGIPRP PHPPDISPYY PLSPGTVGQI PHPLGWLVPQ QGQPVYPITT GGFRHPYPTA LTVNASMSRF PPHMVPPHHT LHTTGIPHPA IVTPTVKQES SQSDVGSLHS SKHQDSKKEE EKKKPHIKKP LNAFMLYMKE MRAKVVAECT LKESAAINQI LGRRWHALSR EEQAKYYELA RKERQLHMQL YPGWSARDNY GKKKKRKRDK QPGETNEHSE CFLNPCLSLP PITDLSAPKK CRARFGLDQQ NNWCGPCSL //