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Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (mTCF-4)

 TF7L2_MOUSE             Reviewed;         459 AA.
Q924A0; O70574; Q8C834; Q91XP2; Q91XP3; Q91XP4; Q924A1; Q9Z0V3;
Q9Z0V4;
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
30-AUG-2017, entry version 152.
RecName: Full=Transcription factor 7-like 2;
AltName: Full=HMG box transcription factor 4;
AltName: Full=T-cell-specific transcription factor 4;
Short=T-cell factor 4;
Short=TCF-4;
Short=mTCF-4;
Name=Tcf7l2; Synonyms=Tcf4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=9488439; DOI=10.1128/MCB.18.3.1248;
Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G.,
Markman M., Lamers W., Destree O., Clevers H.;
"Two members of the Tcf family implicated in Wnt/b-catenin signaling
during embryogenesis in the mouse.";
Mol. Cell. Biol. 18:1248-1256(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
STRAIN=ICR; TISSUE=Fetal intestine;
PubMed=9880534; DOI=10.1074/jbc.274.3.1566;
Lee Y.J., Swencki B., Shoichet S., Shivdasani R.A.;
"A possible role for the high mobility group box transcription factor
Tcf-4 in vertebrate gut epithelial cell differentiation.";
J. Biol. Chem. 274:1566-1572(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 6 AND 7), AND
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5).
STRAIN=C57BL/6J, and CD-1; TISSUE=Pituitary;
PubMed=11845287; DOI=10.1007/s00335-001-2076-0;
Douglas K.R., Brinkmeier M.L., Kennell J.A., Eswara P., Harrison T.A.,
Patrianakos A.I., Sprecher B.S., Potok M.A., Lyons R.H. Jr.,
MacDougald O.A., Camper S.A.;
"Identification of members of the Wnt signaling pathway in the
embryonic pituitary gland.";
Mamm. Genome 12:843-851(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
Bayarsaihan D.;
"A novel isoform of the HMG transcription factor Tcf4.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
FUNCTION.
PubMed=9697701; DOI=10.1038/1270;
Korinek V., Barker N., Moerer P., van Donselaar E., Huls G.,
Peters P.J., Clevers H.;
"Depletion of epithelial stem-cell compartments in the small intestine
of mice lacking Tcf-4.";
Nat. Genet. 19:379-383(1998).
[8]
INTERACTION WITH TGFB1I1.
PubMed=16291758; DOI=10.1074/jbc.M505869200;
Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.;
"HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-
driven transcription.";
J. Biol. Chem. 281:1755-1764(2006).
[9]
INTERACTION WITH TNIK AND CTNNB1.
PubMed=19816403; DOI=10.1038/emboj.2009.285;
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
Mohammed S., Heck A.J., Clevers H.;
"The kinase TNIK is an essential activator of Wnt target genes.";
EMBO J. 28:3329-3340(2009).
[10]
FUNCTION.
PubMed=21856776; DOI=10.1101/gad.17227011;
Vacik T., Stubbs J.L., Lemke G.;
"A novel mechanism for the transcriptional regulation of Wnt signaling
in development.";
Genes Dev. 25:1783-1795(2011).
-!- FUNCTION: Participates in the Wnt signaling pathway and modulates
MYC expression by binding to its promoter in a sequence-specific
manner. Acts as repressor in the absence of CTNNB1, and as
activator in its presence. Activates transcription from promoters
with several copies of the Tcf motif CCTTTGATC in the presence of
CTNNB1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated
by TCF7L2/TCF4 and CTNNB1. Expression of dominant-negative mutants
results in cell-cycle arrest in G1 (By similarity). Necessary for
the maintenance of the epithelial stem-cell compartment of the
small intestine. {ECO:0000250, ECO:0000269|PubMed:21856776,
ECO:0000269|PubMed:9697701}.
-!- SUBUNIT: Interacts with TGFB1I1. Interacts with SPIN1 (By
similarity). Interacts with CTNNB1 (via the armadillo repeat);
forms stable transcription complex. Interacts with EP300.
Interacts with NLK. Interacts with CCDC85B (probably through the
HMG box); prevents interaction with CTNNB1. Interacts with TNIK.
Interacts with MAD2L2; prevents TCF7L2/TCF4 binding to
promZIPK/DAPK3oters, negatively modulating its transcriptional
activity. Interacts with ZIPK/DAPK3. Interacts with XIAP/BIRC4 and
TLE3. Interacts with DDIT3/CHOP. The CTNNB1 and TCF7L2/TCF4
complex interacts with PML (isoform PML-4). Identified in a
complex with CTNNB1 and FERMT2. {ECO:0000250,
ECO:0000269|PubMed:16291758, ECO:0000269|PubMed:19816403}.
-!- INTERACTION:
Q9R1Y5:Hic1; NbExp=4; IntAct=EBI-646713, EBI-5236187;
P39428:Traf1; NbExp=6; IntAct=EBI-646713, EBI-520123;
-!- SUBCELLULAR LOCATION: Nucleus, PML body. Note=Diffuse pattern.
Colocalizes with SUMO1 and PIAS4 in a subset of PML (promyelocytic
leukemia) nuclear bodies (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q924A0-1; Sequence=Displayed;
Name=2;
IsoId=Q924A0-2; Sequence=VSP_006976, VSP_006979;
Name=3;
IsoId=Q924A0-3; Sequence=VSP_006975;
Name=4;
IsoId=Q924A0-4; Sequence=VSP_006978, VSP_006981;
Name=5;
IsoId=Q924A0-5; Sequence=VSP_006974, VSP_006977;
Name=6;
IsoId=Q924A0-6; Sequence=VSP_006977;
Name=7;
IsoId=Q924A0-7; Sequence=VSP_006973, VSP_006975, VSP_006977;
Name=8;
IsoId=Q924A0-8; Sequence=VSP_006976, VSP_006980;
Note=May result from the retention of an intron in the cDNA.;
Name=9; Synonyms=dnTcf7l2 exon1b/c;
IsoId=Q924A0-9; Sequence=VSP_043205;
Note=Dominant negative form which cannot bind CTNNB1. Expression
is VAX2-dependent.;
-!- TISSUE SPECIFICITY: Detected in adult brain and liver, and at
lower levels in intestine, with a clear increase from the distal
colon to the duodenum. Detected at low levels in heart, lung,
kidney, pituitary and testis.
-!- DEVELOPMENTAL STAGE: First detected at E10.5. Highly expressed at
E13.5-E16.5 in the central nervous system, in particular in the
roof of the mesencephalon, at the ditelencephalic junction and in
dorsal thalamus. At E13.5, detected at low levels in
gastrointestinal epithelia.
-!- PTM: Phosphorylated at Thr-178 and/or Thr-189 by NLK.
Phosphorylation by NLK at these sites inhibits DNA-binding by
TCF7L2/TCF4, thereby preventing transcriptional activation of
target genes of the canonical Wnt/beta-catenin signaling pathway
(By similarity). {ECO:0000250}.
-!- PTM: Polysumoylated. Sumoylation is enhanced by PIAS family
members and desumoylation is enhanced by SENP2.
Sumoylation/desumoylation regulates TCF7L2/TCF4 transcription
activity in the Wnt/beta-catenin signaling pathway without
altering interaction with CTNNB1 nor binding to DNA (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=Constitutive activation and subsequent
transactivation of target genes may lead to the maintenance of
stem-cell characteristics (cycling and longevity) in cells that
should normally undergo terminal differentiation and constitute
the primary transforming event in colorectal cancer (CRC).
-!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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EMBL; AJ223070; CAA11071.1; -; mRNA.
EMBL; AF107298; AAD16967.1; -; mRNA.
EMBL; AF107299; AAD16968.1; -; mRNA.
EMBL; AF363722; AAK77485.1; -; Genomic_DNA.
EMBL; AF363722; AAK77486.1; -; Genomic_DNA.
EMBL; AF363724; AAK77488.1; -; mRNA.
EMBL; AF363725; AAK77489.1; -; mRNA.
EMBL; AF363726; AAK77490.1; -; mRNA.
EMBL; AY072035; AAL58534.1; -; mRNA.
EMBL; AK048536; BAC33366.1; -; mRNA.
EMBL; AC118695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC157916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS50470.1; -. [Q924A0-2]
CCDS; CCDS50471.1; -. [Q924A0-1]
CCDS; CCDS50474.1; -. [Q924A0-9]
RefSeq; NP_001136390.1; NM_001142918.2.
RefSeq; NP_001136393.1; NM_001142921.2.
RefSeq; NP_001136396.1; NM_001142924.2. [Q924A0-9]
UniGene; Mm.139815; -.
ProteinModelPortal; Q924A0; -.
SMR; Q924A0; -.
BioGrid; 204009; 10.
DIP; DIP-40920N; -.
IntAct; Q924A0; 4.
MINT; MINT-421706; -.
STRING; 10090.ENSMUSP00000107284; -.
iPTMnet; Q924A0; -.
PhosphoSitePlus; Q924A0; -.
PaxDb; Q924A0; -.
PeptideAtlas; Q924A0; -.
PRIDE; Q924A0; -.
Ensembl; ENSMUST00000111646; ENSMUSP00000107273; ENSMUSG00000024985. [Q924A0-9]
GeneID; 21416; -.
KEGG; mmu:21416; -.
UCSC; uc008hya.2; mouse. [Q924A0-6]
UCSC; uc008hyb.2; mouse. [Q924A0-5]
UCSC; uc008hyk.2; mouse. [Q924A0-2]
UCSC; uc008hyn.2; mouse. [Q924A0-9]
CTD; 6934; -.
MGI; MGI:1202879; Tcf7l2.
eggNOG; KOG3248; Eukaryota.
eggNOG; ENOG41109RU; LUCA.
GeneTree; ENSGT00390000009964; -.
HOGENOM; HOG000116032; -.
HOVERGEN; HBG000419; -.
InParanoid; Q924A0; -.
KO; K04491; -.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-MMU-4086398; Ca2+ pathway.
Reactome; R-MMU-4641265; Repression of WNT target genes.
Reactome; R-MMU-8951430; RUNX3 regulates WNT signaling.
ChiTaRS; Tcf7l2; mouse.
PRO; PR:Q924A0; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024985; -.
CleanEx; MM_TCF4; -.
ExpressionAtlas; Q924A0; baseline and differential.
Genevisible; Q924A0; MM.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISO:MGI.
GO; GO:0071664; C:catenin-TCF7L2 complex; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0001568; P:blood vessel development; ISO:MGI.
GO; GO:0030282; P:bone mineralization; IGI:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0035411; P:catenin import into nucleus; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0001678; P:cellular glucose homeostasis; IMP:MGI.
GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:MGI.
GO; GO:0030538; P:embryonic genitalia morphogenesis; IGI:MGI.
GO; GO:0048619; P:embryonic hindgut morphogenesis; IGI:MGI.
GO; GO:0060325; P:face morphogenesis; IGI:MGI.
GO; GO:0045444; P:fat cell differentiation; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
GO; GO:1901142; P:insulin metabolic process; IMP:MGI.
GO; GO:0043570; P:maintenance of DNA repeat elements; ISO:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0048625; P:myoblast fate commitment; IMP:MGI.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISO:MGI.
GO; GO:0021915; P:neural tube development; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
GO; GO:0021983; P:pituitary gland development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:MGI.
GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISO:MGI.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:MGI.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0035947; P:regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0032350; P:regulation of hormone metabolic process; ISO:MGI.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0031641; P:regulation of myelination; IMP:MGI.
GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:MGI.
GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:MGI.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0009749; P:response to glucose; IMP:BHF-UCL.
GO; GO:0032252; P:secretory granule localization; IMP:MGI.
GO; GO:0043588; P:skin development; IGI:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR027397; Catenin_binding_dom.
InterPro; IPR013558; CTNNB1-bd_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR024940; TCF/LEF.
InterPro; IPR028773; TCF7L2.
PANTHER; PTHR10373; PTHR10373; 1.
PANTHER; PTHR10373:SF44; PTHR10373:SF44; 1.
Pfam; PF08347; CTNNB1_binding; 1.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation;
Wnt signaling pathway.
CHAIN 1 459 Transcription factor 7-like 2.
/FTId=PRO_0000048624.
DNA_BIND 327 395 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 53 CTNNB1-binding.
REGION 178 372 Mediates interaction with MAD2L2.
{ECO:0000250}.
MOTIF 402 408 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 155 294 Pro-rich.
MOD_RES 178 178 Phosphothreonine; by NLK. {ECO:0000250}.
MOD_RES 189 189 Phosphothreonine; by NLK. {ECO:0000250}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NQB0}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 161 MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDL
ADVKSSLVNESETNQDSSSDSEAERRPPPRSESFRDKSRES
LEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSP
TARTYLQMKWPLLDVQAGSLQSRQTLKDARSPSPAHIV ->
M (in isoform 9).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_043205.
VAR_SEQ 127 127 T -> TLHFQSGSTHYSAYKTIEHQIAIQ (in isoform
7). {ECO:0000303|PubMed:11845287}.
/FTId=VSP_006973.
VAR_SEQ 161 161 V -> VQSPLPCCTQGHACPHFYTPSDFTVSTQVFRDTKSS
HSLQKVGEPWYLE (in isoform 5).
{ECO:0000305}.
/FTId=VSP_006974.
VAR_SEQ 237 240 Missing (in isoform 3 and isoform 7).
{ECO:0000303|PubMed:11845287}.
/FTId=VSP_006975.
VAR_SEQ 268 268 S -> SSFLSS (in isoform 2 and isoform 8).
{ECO:0000303|PubMed:9880534,
ECO:0000303|Ref.4}.
/FTId=VSP_006976.
VAR_SEQ 270 459 Missing (in isoform 5, isoform 6 and
isoform 7).
{ECO:0000303|PubMed:11845287}.
/FTId=VSP_006977.
VAR_SEQ 417 459 EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPC
SL -> GEKKSAFATYKVKAAASAHPLQMEAY (in
isoform 2). {ECO:0000303|PubMed:9880534}.
/FTId=VSP_006979.
VAR_SEQ 417 459 EHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPC
SL -> GERGESGRWRLEDHSYVRLPSGGGRRNPRPGHCGE
PILGSLFCLCVF (in isoform 8).
{ECO:0000303|Ref.4}.
/FTId=VSP_006980.
VAR_SEQ 417 433 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_006978.
VAR_SEQ 457 459 CSL -> ADANTPKKCRALFGLDRQTLWCKPCRRKKKCVRY
IQGEGSCLSPPSSDGSLLDSPPPSPHLLGSPPQDAKSQTEQ
TQPLSLSLKPDPLAHLSMMPPPPALLLAEAAHGKASALCPN
GALDLPPAALQPSMVPSSSLAQPSTSSLHSHNSLAGTQPQP
LSLVTKSLE (in isoform 4). {ECO:0000305}.
/FTId=VSP_006981.
CONFLICT 57 57 D -> N (in Ref. 2; AAD16967 and 3;
AAK77488/AAK77489/AAK77490).
{ECO:0000305}.
CONFLICT 236 236 W -> R (in Ref. 4; AAL58534).
{ECO:0000305}.
CONFLICT 410 410 K -> Q (in Ref. 2; AAD16968).
{ECO:0000305}.
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


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