TF7L2_MOUSE
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 03-AUG-2022, entry version 186.
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 Q924A0; Q9R1Y5: Hic1; NbExp=4; IntAct=EBI-646713, EBI-5236187;
CC Q924A0; 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}.
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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 AlphaFoldDB; Q924A0; -.
DR SMR; Q924A0; -.
DR BioGRID; 204009; 33.
DR DIP; DIP-40920N; -.
DR IntAct; Q924A0; 5.
DR MINT; Q924A0; -.
DR STRING; 10090.ENSMUSP00000107283; -.
DR iPTMnet; Q924A0; -.
DR PhosphoSitePlus; Q924A0; -.
DR MaxQB; Q924A0; -.
DR PaxDb; Q924A0; -.
DR PeptideAtlas; Q924A0; -.
DR PRIDE; Q924A0; -.
DR ProteomicsDB; 263113; -. [Q924A0-1]
DR ProteomicsDB; 263114; -. [Q924A0-2]
DR ProteomicsDB; 263115; -. [Q924A0-3]
DR ProteomicsDB; 263116; -. [Q924A0-4]
DR ProteomicsDB; 263117; -. [Q924A0-5]
DR ProteomicsDB; 263118; -. [Q924A0-6]
DR ProteomicsDB; 263119; -. [Q924A0-7]
DR ProteomicsDB; 263120; -. [Q924A0-8]
DR ProteomicsDB; 263121; -. [Q924A0-9]
DR Antibodypedia; 31824; 477 antibodies from 34 providers.
DR DNASU; 21416; -.
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 VEuPathDB; HostDB:ENSMUSG00000024985; -.
DR eggNOG; KOG3248; Eukaryota.
DR GeneTree; ENSGT00940000155535; -.
DR HOGENOM; CLU_013229_1_0_1; -.
DR InParanoid; Q924A0; -.
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-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling.
DR BioGRID-ORCS; 21416; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Tcf7l2; mouse.
DR PRO; PR:Q924A0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q924A0; protein.
DR Bgee; ENSMUSG00000024985; Expressed in medial dorsal nucleus of thalamus and 295 other tissues.
DR ExpressionAtlas; Q924A0; baseline and differential.
DR Genevisible; Q924A0; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
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:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
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 regulator 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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear 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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0001568; P:blood vessel development; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP: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: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:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IGI:MGI.
DR GO; GO:0045444; P:fat cell differentiation; ISO:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP: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: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: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:0035265; P:organ growth; 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:0006111; P:regulation of gluconeogenesis; 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 Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR027397; Catenin-bd_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..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..53
FT /note="CTNNB1-binding"
FT REGION 178..372
FT /note="Mediates interaction with MAD2L2"
FT /evidence="ECO:0000250"
FT REGION 295..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 402..408
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 16..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
