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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) (hTCF-4)

 TF7L2_HUMAN             Reviewed;         619 AA.
Q9NQB0; B4DRJ8; B9X074; C6ZRJ8; C6ZRK0; E2GH14; E2GH19; E2GH20;
E2GH24; E2GH25; E9PFH9; F8W742; F8W7T5; O00185; Q9NQB1; Q9NQB2;
Q9NQB3; Q9NQB4; Q9NQB5; Q9NQB6; Q9NQB7; Q9ULC2;
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
22-NOV-2017, entry version 182.
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=hTCF-4;
Name=TCF7L2; Synonyms=TCF4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9), AND INTERACTION WITH
CTNNB1.
TISSUE=Fetus;
PubMed=9065401; DOI=10.1126/science.275.5307.1784;
Korinek V., Barker N., Morin P.J., van Wichen D., de Weger R.,
Kinzler K.W., Vogelstein B., Clevers H.;
"Constitutive transcriptional activation by a beta-catenin-Tcf complex
in APC-/- colon carcinoma.";
Science 275:1784-1787(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND
9), AND VARIANT ASN-346.
PubMed=10919662;
Duval A., Rolland S., Tubacher E., Bui H., Thomas G., Hamelin R.;
"The human T cell transcription factor-4 gene: structure, extensive
characterization of alternative splicings, and mutational analysis in
colorectal cancer cell lines.";
Cancer Res. 60:3872-3879(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12; 13 AND 14), AND ALTERNATIVE
SPLICING.
TISSUE=Brain;
PubMed=19602480; DOI=10.1093/hmg/ddp321;
Prokunina-Olsson L., Welch C., Hansson O., Adhikari N., Scott L.J.,
Usher N., Tong M., Sprau A., Swift A., Bonnycastle L.L., Erdos M.R.,
He Z., Saxena R., Harmon B., Kotova O., Hoffman E.P., Altshuler D.,
Groop L., Boehnke M., Collins F.S., Hall J.L.;
"Tissue-specific alternative splicing of TCF7L2.";
Hum. Mol. Genet. 18:3795-3804(2009).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 9; 13; 14; 15 AND 17), AND
ALTERNATIVE SPLICING.
PubMed=21256126; DOI=10.1016/j.yexcr.2011.01.015;
Tsedensodnom O., Koga H., Rosenberg S.A., Nambotin S.B., Carroll J.J.,
Wands J.R., Kim M.;
"Identification of T-cell factor-4 isoforms that contribute to the
malignant phenotype of hepatocellular carcinoma cells.";
Exp. Cell Res. 317:920-931(2011).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
TISSUE=Colon;
Iseki H., Takeda A., Andou T., Takahashi N., Ban S., Kurochkin I.V.,
Okazaki Y., Koyama I.;
"ALEX1, a putative tumor suppressor, is regulated by CREB-dependent
Wnt signaling, and is silenced by promoter methylation in human
colorectal cancer.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 14).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 449-494.
TISSUE=Gastric carcinoma;
Saeki H., Tanaka S., Sugimachi K.;
"Human TCF-4 splice form B.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[11]
FUNCTION.
PubMed=9727977; DOI=10.1126/science.281.5382.1509;
He T.-C., Sparks A.B., Rago C., Hermeking H., Zawel L., da Costa L.T.,
Morin P.J., Vogelstein B., Kinzler K.W.;
"Identification of c-MYC as a target of the APC pathway.";
Science 281:1509-1512(1998).
[12]
TISSUE SPECIFICITY, INTERACTION WITH CTNNB1, AND SUBCELLULAR LOCATION.
PubMed=9916915; DOI=10.1016/S0002-9440(10)65247-9;
Barker N., Huls G., Korinek V., Clevers H.;
"Restricted high level expression of Tcf-4 protein in intestinal and
mammary gland epithelium.";
Am. J. Pathol. 154:29-35(1999).
[13]
INTERACTION WITH CTNNB1, AND MUTAGENESIS OF 10-ASP-ASP-11; ASP-16;
GLU-17; 23-ASP-GLU-24 AND LEU-48.
PubMed=10080941; DOI=10.1006/bbrc.1999.0379;
Omer C.A., Miller P.J., Diehl R.E., Kral A.M.;
"Identification of Tcf4 residues involved in high-affinity beta-
catenin binding.";
Biochem. Biophys. Res. Commun. 256:584-590(1999).
[14]
INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
PubMed=11266540; DOI=10.1093/nar/29.7.1410;
Brantjes H., Roose J., van De Wetering M., Clevers H.;
"All Tcf HMG box transcription factors interact with Groucho-related
co-repressors.";
Nucleic Acids Res. 29:1410-1419(2001).
[15]
FUNCTION.
PubMed=12408868; DOI=10.1016/S0092-8674(02)01014-0;
van de Wetering M., Sancho E., Verweij C., de Lau W., Oving I.,
Hurlstone A., van der Horn K., Batlle E., Coudreuse D., Haramis A.-P.,
Tjon-Pon-Fong M., Moerer P., van den Born M., Soete G., Pals S.,
Eilers M., Medema R., Clevers H.;
"The beta-catenin/TCF-4 complex imposes a crypt progenitor phenotype
on colorectal cancer cells.";
Cell 111:241-250(2002).
[16]
SUMOYLATION AT LYS-320, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-320 AND GLU-322.
PubMed=12727872; DOI=10.1093/emboj/cdg204;
Yamamoto H., Ihara M., Matsuura Y., Kikuchi A.;
"Sumoylation is involved in beta-catenin-dependent activation of Tcf-
4.";
EMBO J. 22:2047-2059(2003).
[17]
INTERACTION WITH EP300.
PubMed=12446687; DOI=10.1074/jbc.M210081200;
Hecht A., Stemmler M.P.;
"Identification of a promoter-specific transcriptional activation
domain at the C-terminus of the Wnt effector protein T-cell factor
4.";
J. Biol. Chem. 278:3776-3785(2003).
[18]
INTERACTION WITH NLK, PHOSPHORYLATION AT THR-201 AND/OR THR-212 BY
NLK, AND MUTAGENESIS OF THR-201 AND THR-212.
PubMed=12556497; DOI=10.1128/MCB.23.4.1379-1389.2003;
Ishitani T., Ninomiya-Tsuji J., Matsumoto K.;
"Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-
activated protein kinase-related Nemo-like kinase-dependent
phosphorylation in Wnt/beta-catenin signaling.";
Mol. Cell. Biol. 23:1379-1389(2003).
[19]
INTERACTION WITH NLK.
PubMed=16714285; DOI=10.1074/jbc.M602089200;
Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K.,
Hyodo-Miura J., Kawachi K., Natsume T., Shibuya H.;
"NARF, an nemo-like kinase (NLK)-associated ring finger protein
regulates the ubiquitylation and degradation of T cell factor/lymphoid
enhancer factor (TCF/LEF).";
J. Biol. Chem. 281:20749-20760(2006).
[20]
INVOLVEMENT IN NIDDM.
PubMed=16415884; DOI=10.1038/ng1732;
Grant S.F.A., Thorleifsson G., Reynisdottir I., Benediktsson R.,
Manolescu A., Sainz J., Helgason A., Stefansson H., Emilsson V.,
Helgadottir A., Styrkarsdottir U., Magnusson K.P., Walters G.B.,
Palsdottir E., Jonsdottir T., Gudmundsdottir T., Gylfason A.,
Saemundsdottir J., Wilensky R.L., Reilly M.P., Rader D.J., Bagger Y.,
Christiansen C., Gudnason V., Sigurdsson G., Thorsteinsdottir U.,
Gulcher J.R., Kong A., Stefansson K.;
"Variant of transcription factor 7-like 2 (TCF7L2) gene confers risk
of type 2 diabetes.";
Nat. Genet. 38:320-323(2006).
[21]
INTERACTION WITH DDIT3.
PubMed=16434966; DOI=10.1038/sj.onc.1209380;
Horndasch M., Lienkamp S., Springer E., Schmitt A., Pavenstaedt H.,
Walz G., Gloy J.;
"The C/EBP homologous protein CHOP (GADD153) is an inhibitor of
Wnt/TCF signals.";
Oncogene 25:3397-3407(2006).
[22]
INTERACTION WITH CCDC85B.
PubMed=17873903; DOI=10.1038/sj.onc.1210801;
Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K.;
"Coiled-coil domain containing 85B suppresses the beta-catenin
activity in a p53-dependent manner.";
Oncogene 27:1520-1526(2008).
[23]
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).
[24]
FUNCTION, AND INTERACTION WITH MAD2L2.
PubMed=19443654; DOI=10.1074/jbc.M109.005017;
Hong C.F., Chou Y.T., Lin Y.S., Wu C.W.;
"MAD2B, a novel TCF4-binding protein, modulates TCF4-mediated
epithelial-mesenchymal transdifferentiation.";
J. Biol. Chem. 284:19613-19622(2009).
[25]
INTERACTION WITH NLK AND ZIPK/DAPK3.
PubMed=21454679; DOI=10.1074/jbc.M110.189829;
Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R.,
Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T.;
"Zipper-interacting protein kinase (ZIPK) modulates canonical
Wnt/beta-catenin signaling through interaction with Nemo-like kinase
and T-cell factor 4 (NLK/TCF4).";
J. Biol. Chem. 286:19170-19177(2011).
[26]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH FERMT2 AND CTNNB1, AND
SUBCELLULAR LOCATION.
PubMed=22699938; DOI=10.1038/embor.2012.88;
Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G.,
Zhang H.;
"Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4
to enhance Wnt signalling.";
EMBO Rep. 13:750-758(2012).
[27]
INTERACTION WITH PML.
PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
Satow R., Shitashige M., Jigami T., Fukami K., Honda K.,
Kitabayashi I., Yamada T.;
"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
function in colorectal cancer cells.";
Gastroenterology 142:572-581(2012).
[28]
INTERACTION WITH SPIN1.
PubMed=22258766; DOI=10.1158/1541-7786.MCR-11-0440;
Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C.,
Zhou J.N., Jia Y.L., Yue W., Pei X.T.;
"SPINDLIN1 promotes cancer cell proliferation through activation of
WNT/TCF-4 signaling.";
Mol. Cancer Res. 10:326-335(2012).
[29]
INTERACTION WITH XIAP/BIRC4 AND TLE3.
PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A.,
Lee E.;
"XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt
signaling.";
Mol. Cell 45:619-628(2012).
[30]
INTERACTION WITH SPIN1.
PubMed=24589551; DOI=10.1101/gad.233239.113;
Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.;
"Molecular basis underlying histone H3 lysine-arginine methylation
pattern readout by Spin/Ssty repeats of Spindlin1.";
Genes Dev. 28:622-636(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
INVOLVEMENT IN NIDDM.
PubMed=24390345; DOI=10.1038/nature12828;
The SIGMA Type 2 Diabetes Consortium;
"Sequence variants in SLC16A11 are a common risk factor for type 2
diabetes in Mexico.";
Nature 506:97-101(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-539, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-49 IN COMPLEX WITH THE
ARMADILLO REPEAT REGION OF CTNNB1, AND MUTAGENESIS OF GLU-24; GLU-26;
GLU-28 AND GLU-29.
PubMed=11713475; DOI=10.1038/nsb718;
Graham T.A., Ferkey D.M., Mao F., Kimelman D., Xu W.;
"Tcf4 can specifically recognize beta-catenin using alternative
conformations.";
Nat. Struct. Biol. 8:1048-1052(2001).
[35]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 8-54 IN COMPLEX WITH THE
ARMADILLO REPEAT REGION OF CTNNB1, AND MUTAGENESIS OF ILE-19 AND
PHE-21.
PubMed=11713476; DOI=10.1038/nsb720;
Poy F., Lepourcelet M., Shivdasani R.A., Eck M.J.;
"Structure of a human Tcf4-beta-catenin complex.";
Nat. Struct. Biol. 8:1053-1057(2001).
[36]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-53 IN COMPLEX WITH BCL9
AND CTNNB1, AND INTERACTION WITH CTNNB1.
PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
"Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
Mol. Cell 24:293-300(2006).
[37]
VARIANT [LARGE SCALE ANALYSIS] CYS-465.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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 5'-CCTTTGATC-3' 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.
Necessary for the maintenance of the epithelial stem-cell
compartment of the small intestine. {ECO:0000269|PubMed:12408868,
ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:19443654,
ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:9727977}.
-!- SUBUNIT: Interacts with TGFB1I1 (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. Interacts with
SPIN1. {ECO:0000250, ECO:0000269|PubMed:10080941,
ECO:0000269|PubMed:11266540, ECO:0000269|PubMed:12446687,
ECO:0000269|PubMed:12556497, ECO:0000269|PubMed:12727872,
ECO:0000269|PubMed:16434966, ECO:0000269|PubMed:16714285,
ECO:0000269|PubMed:17052462, ECO:0000269|PubMed:17873903,
ECO:0000269|PubMed:19443654, ECO:0000269|PubMed:19816403,
ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:22155184,
ECO:0000269|PubMed:22258766, ECO:0000269|PubMed:22304967,
ECO:0000269|PubMed:22699938, ECO:0000269|PubMed:24589551,
ECO:0000269|PubMed:9065401, ECO:0000269|PubMed:9916915}.
-!- INTERACTION:
Q08117-2:AES; NbExp=4; IntAct=EBI-11746252, EBI-11741437;
P35222:CTNNB1; NbExp=34; IntAct=EBI-924724, EBI-491549;
Q9UER7:DAXX; NbExp=5; IntAct=EBI-924724, EBI-77321;
Q14526:HIC1; NbExp=6; IntAct=EBI-924724, EBI-2507362;
P14923:JUP; NbExp=13; IntAct=EBI-924724, EBI-702484;
Q13761:RUNX3; NbExp=14; IntAct=EBI-924724, EBI-925990;
Q9UKE5:TNIK; NbExp=3; IntAct=EBI-924724, EBI-1051794;
P12956:XRCC6; NbExp=9; IntAct=EBI-924724, EBI-353208;
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000269|PubMed:12727872, ECO:0000269|PubMed:22699938,
ECO:0000269|PubMed:9916915}. Note=Diffuse pattern. Colocalizes
with SUMO1 and PIAS4 in a subset of PML (promyelocytic leukemia)
nuclear bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=17;
Name=1; Synonyms=TCF-4M;
IsoId=Q9NQB0-1; Sequence=Displayed;
Name=2;
IsoId=Q9NQB0-2; Sequence=VSP_006970, VSP_006972;
Name=3;
IsoId=Q9NQB0-3; Sequence=VSP_006966;
Name=4;
IsoId=Q9NQB0-4; Sequence=VSP_006964, VSP_006970, VSP_006972;
Name=5;
IsoId=Q9NQB0-5; Sequence=VSP_006964;
Name=6; Synonyms=TCF-4I;
IsoId=Q9NQB0-6; Sequence=VSP_006967;
Name=7;
IsoId=Q9NQB0-7; Sequence=VSP_006964, VSP_006966;
Name=8;
IsoId=Q9NQB0-8; Sequence=VSP_006962;
Name=9; Synonyms=TCF-4G;
IsoId=Q9NQB0-9; Sequence=VSP_006965, VSP_006969;
Name=10;
IsoId=Q9NQB0-10; Sequence=VSP_006962, VSP_006963, VSP_006968,
VSP_006971;
Name=11;
IsoId=Q9NQB0-11; Sequence=VSP_006962, VSP_045821, VSP_006965,
VSP_006969;
Name=12;
IsoId=Q9NQB0-12; Sequence=VSP_006962, VSP_045822;
Note=Low expression in pancreas and colon.;
Name=13; Synonyms=TCF-4J;
IsoId=Q9NQB0-13; Sequence=VSP_006962, VSP_006964, VSP_006966;
Note=Common splicing form, lowest expression in skeletal
muscle.;
Name=14; Synonyms=TCF-4B, short;
IsoId=Q9NQB0-14; Sequence=VSP_006962, VSP_006965, VSP_006969;
Note=High transcriptional activity. Major isoform in liver.;
Name=15; Synonyms=TCF-4A;
IsoId=Q9NQB0-15; Sequence=VSP_006962, VSP_053750, VSP_006965,
VSP_006969;
Name=16; Synonyms=TCF-4K;
IsoId=Q9NQB0-16; Sequence=VSP_006962, VSP_053750, VSP_006964;
Name=17; Synonyms=TCF-4X2;
IsoId=Q9NQB0-17; Sequence=VSP_053748, VSP_053749;
-!- TISSUE SPECIFICITY: Detected in epithelium from small intestine,
with the highest expression at the top of the crypts and a
gradient of expression from crypt to villus. Detected in colon
epithelium and colon cancer, and in epithelium from mammary gland
and carcinomas derived therefrom. {ECO:0000269|PubMed:9916915}.
-!- DEVELOPMENTAL STAGE: Highly expressed in crypt regions and barely
detectable in villi in epithelium from fetal small intestine at
week 16. At week 22 expression in villi had increased strongly.
-!- DOMAIN: The promoter-specific activation domain interacts with the
transcriptional coactivator EP300.
-!- PTM: In vitro, phosphorylated by TNIK.
{ECO:0000269|PubMed:12556497}.
-!- PTM: Phosphorylated at Thr-201 and/or Thr-212 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.
{ECO:0000269|PubMed:12556497}.
-!- 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.
{ECO:0000269|PubMed:12727872}.
-!- 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).
-!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM)
[MIM:125853]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:16415884,
ECO:0000269|PubMed:24390345}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y11306; CAA72166.2; -; mRNA.
EMBL; AJ270770; CAB97212.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270776; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97212.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97213.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270776; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97213.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97214.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270777; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97214.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97215.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270777; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97215.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97216.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97216.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97217.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270778; CAB97217.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97218.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270776; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270777; CAB97218.1; JOINED; Genomic_DNA.
EMBL; AJ270770; CAB97219.1; -; Genomic_DNA.
EMBL; AJ270771; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270772; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270773; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270774; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270775; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270776; CAB97219.1; JOINED; Genomic_DNA.
EMBL; AJ270777; CAB97219.1; JOINED; Genomic_DNA.
EMBL; FJ010167; ACI28525.1; -; mRNA.
EMBL; FJ010169; ACI28527.1; -; mRNA.
EMBL; FJ010172; ACI28530.1; -; mRNA.
EMBL; HM352839; ADK35175.1; -; mRNA.
EMBL; HM352842; ADK35178.1; -; mRNA.
EMBL; HM352844; ADK35180.1; -; mRNA.
EMBL; HM352845; ADK35187.1; -; mRNA.
EMBL; HM352846; ADK35181.1; -; mRNA.
EMBL; HM352847; ADK35182.1; -; mRNA.
EMBL; HM352849; ADK35184.1; -; mRNA.
EMBL; HM352850; ADK35185.1; -; mRNA.
EMBL; AB440195; BAH24004.1; -; mRNA.
EMBL; AK299295; BAG61310.1; -; mRNA.
EMBL; AL135792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL158212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL451084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49513.1; -; Genomic_DNA.
EMBL; CH471066; EAW49515.1; -; Genomic_DNA.
EMBL; CH471066; EAW49516.1; -; Genomic_DNA.
EMBL; BC032656; AAH32656.1; -; mRNA.
EMBL; AB034691; BAA86225.1; -; mRNA.
CCDS; CCDS53577.1; -. [Q9NQB0-7]
CCDS; CCDS53578.1; -. [Q9NQB0-11]
CCDS; CCDS55729.1; -. [Q9NQB0-12]
CCDS; CCDS7576.1; -. [Q9NQB0-8]
PIR; S22807; S22807.
RefSeq; NP_001139746.1; NM_001146274.1. [Q9NQB0-7]
RefSeq; NP_001139755.1; NM_001146283.1. [Q9NQB0-11]
RefSeq; NP_001139756.1; NM_001146284.1. [Q9NQB0-10]
RefSeq; NP_001139758.1; NM_001146286.1. [Q9NQB0-14]
RefSeq; NP_001185455.1; NM_001198526.1. [Q9NQB0-13]
RefSeq; NP_001185457.1; NM_001198528.1. [Q9NQB0-12]
RefSeq; NP_001185460.1; NM_001198531.1. [Q9NQB0-9]
RefSeq; XP_005270141.1; XM_005270084.1. [Q9NQB0-1]
RefSeq; XP_005270146.1; XM_005270089.1.
RefSeq; XP_005270153.1; XM_005270096.2. [Q9NQB0-6]
RefSeq; XP_005270160.1; XM_005270103.1. [Q9NQB0-15]
RefSeq; XP_016872081.1; XM_017016592.1. [Q9NQB0-3]
RefSeq; XP_016872082.1; XM_017016593.1. [Q9NQB0-5]
UniGene; Hs.593995; -.
PDB; 1JDH; X-ray; 1.90 A; B=12-49.
PDB; 1JPW; X-ray; 2.50 A; D/E/F=6-54.
PDB; 2GL7; X-ray; 2.60 A; B/E=1-53.
PDBsum; 1JDH; -.
PDBsum; 1JPW; -.
PDBsum; 2GL7; -.
DisProt; DP00175; -.
ProteinModelPortal; Q9NQB0; -.
SMR; Q9NQB0; -.
BioGrid; 112795; 35.
CORUM; Q9NQB0; -.
DIP; DIP-36236N; -.
IntAct; Q9NQB0; 53.
MINT; MINT-222146; -.
STRING; 9606.ENSP00000444972; -.
BindingDB; Q9NQB0; -.
ChEMBL; CHEMBL3038511; -.
iPTMnet; Q9NQB0; -.
PhosphoSitePlus; Q9NQB0; -.
BioMuta; TCF7L2; -.
DMDM; 29337146; -.
MaxQB; Q9NQB0; -.
PaxDb; Q9NQB0; -.
PeptideAtlas; Q9NQB0; -.
PRIDE; Q9NQB0; -.
Ensembl; ENST00000352065; ENSP00000344823; ENSG00000148737. [Q9NQB0-12]
Ensembl; ENST00000355717; ENSP00000347949; ENSG00000148737. [Q9NQB0-11]
Ensembl; ENST00000355995; ENSP00000348274; ENSG00000148737. [Q9NQB0-1]
Ensembl; ENST00000369397; ENSP00000358404; ENSG00000148737. [Q9NQB0-8]
Ensembl; ENST00000538897; ENSP00000446172; ENSG00000148737. [Q9NQB0-6]
Ensembl; ENST00000627217; ENSP00000486891; ENSG00000148737. [Q9NQB0-7]
GeneID; 6934; -.
KEGG; hsa:6934; -.
UCSC; uc001lac.5; human. [Q9NQB0-1]
CTD; 6934; -.
DisGeNET; 6934; -.
EuPathDB; HostDB:ENSG00000148737.15; -.
GeneCards; TCF7L2; -.
HGNC; HGNC:11641; TCF7L2.
HPA; CAB013535; -.
HPA; HPA038800; -.
MalaCards; TCF7L2; -.
MIM; 125853; phenotype.
MIM; 602228; gene.
neXtProt; NX_Q9NQB0; -.
OpenTargets; ENSG00000148737; -.
PharmGKB; PA36394; -.
eggNOG; KOG3248; Eukaryota.
eggNOG; ENOG41109RU; LUCA.
GeneTree; ENSGT00390000009964; -.
HOVERGEN; HBG000419; -.
InParanoid; Q9NQB0; -.
KO; K04491; -.
OMA; EPWCLES; -.
OrthoDB; EOG091G0705; -.
PhylomeDB; Q9NQB0; -.
TreeFam; TF318448; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
Reactome; R-HSA-4641265; Repression of WNT target genes.
Reactome; R-HSA-5339700; TCF7L2 mutants don't bind CTBP.
Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
SignaLink; Q9NQB0; -.
SIGNOR; Q9NQB0; -.
ChiTaRS; TCF7L2; human.
EvolutionaryTrace; Q9NQB0; -.
GeneWiki; TCF7L2; -.
GenomeRNAi; 6934; -.
PRO; PR:Q9NQB0; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148737; -.
CleanEx; HS_TCF4; -.
ExpressionAtlas; Q9NQB0; baseline and differential.
Genevisible; Q9NQB0; HS.
GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IDA:BHF-UCL.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL.
GO; GO:0070016; F:armadillo repeat domain binding; IPI:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0001568; P:blood vessel development; IMP:BHF-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; IC:BHF-UCL.
GO; GO:0044334; P:canonical Wnt signaling pathway involved in positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IMP:BHF-UCL.
GO; GO:0008283; P:cell proliferation; IMP:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IDA:BHF-UCL.
GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:BHF-UCL.
GO; GO:0048625; P:myoblast fate commitment; IDA:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISS:BHF-UCL.
GO; GO:0031016; P:pancreas development; TAS:BHF-UCL.
GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; IMP:BHF-UCL.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032350; P:regulation of hormone metabolic process; IDA:BHF-UCL.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR027397; Catenin_binding_dom_sf.
InterPro; IPR013558; CTNNB1-bd_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR024940; TCF/LEF.
InterPro; IPR028773; TCF7L.
PANTHER; PTHR10373; PTHR10373; 1.
PANTHER; PTHR10373:SF25; PTHR10373:SF25; 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;
3D-structure; Activator; Alternative splicing; Complete proteome;
Diabetes mellitus; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation;
Wnt signaling pathway.
CHAIN 1 619 Transcription factor 7-like 2.
/FTId=PRO_0000048623.
DNA_BIND 350 418 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 53 CTNNB1-binding. {ECO:0000250}.
REGION 201 395 Mediates interaction with MAD2L2.
{ECO:0000269|PubMed:19443654}.
REGION 459 505 Promoter-specific activation domain.
MOTIF 425 430 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 178 317 Pro-rich.
MOD_RES 201 201 Phosphothreonine; by NLK.
{ECO:0000305|PubMed:12556497}.
MOD_RES 212 212 Phosphothreonine; by NLK.
{ECO:0000305|PubMed:12556497}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 320 320 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12727872}.
CROSSLNK 539 539 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 6 MPQLNG -> MSSFLS (in isoform 17).
{ECO:0000303|PubMed:21256126}.
/FTId=VSP_053748.
VAR_SEQ 7 290 Missing (in isoform 17).
{ECO:0000303|PubMed:21256126}.
/FTId=VSP_053749.
VAR_SEQ 128 150 Missing (in isoform 8, isoform 10,
isoform 11, isoform 12, isoform 13,
isoform 14, isoform 15 and isoform 16).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19602480,
ECO:0000303|PubMed:21256126,
ECO:0000303|PubMed:9065401}.
/FTId=VSP_006962.
VAR_SEQ 184 184 V -> VSPLPCCTQGHDCQHFYPPSDFTVSTQVFRDMKRSH
SLQKVGEPWCIE (in isoform 11).
{ECO:0000305}.
/FTId=VSP_045821.
VAR_SEQ 260 263 Missing (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006963.
VAR_SEQ 290 290 M -> MSSFLS (in isoform 15 and isoform
16). {ECO:0000303|PubMed:21256126}.
/FTId=VSP_053750.
VAR_SEQ 440 465 EHSECFLNPCLSLPPITDLSAPKKCR -> GEKKSAFATYK
VKAAASAHPLQMEAY (in isoform 9, isoform
11, isoform 14 and isoform 15).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:19602480,
ECO:0000303|PubMed:21256126,
ECO:0000303|PubMed:9065401,
ECO:0000303|Ref.5}.
/FTId=VSP_006965.
VAR_SEQ 440 456 Missing (in isoform 4, isoform 5, isoform
7, isoform 13 and isoform 16).
{ECO:0000303|PubMed:19602480,
ECO:0000303|PubMed:21256126}.
/FTId=VSP_006964.
VAR_SEQ 457 619 DLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCL
SPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSL
KPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAA
LQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE
-> GEKKSAFATYKVKAAASAHPLQMEAY (in isoform
6). {ECO:0000303|PubMed:21256126}.
/FTId=VSP_006967.
VAR_SEQ 457 482 DLSAPKKCRARFGLDQQNNWCGPCRR -> GEKKSAFATYK
VKAAASAHPLQMEAY (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006968.
VAR_SEQ 457 478 DLSAPKKCRARFGLDQQNNWCG -> DANTPKKCRALFGLD
RQTLWCK (in isoform 3, isoform 7 and
isoform 13).
{ECO:0000303|PubMed:19602480,
ECO:0000303|PubMed:21256126}.
/FTId=VSP_006966.
VAR_SEQ 466 619 Missing (in isoform 9, isoform 11,
isoform 14 and isoform 15).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:19602480,
ECO:0000303|PubMed:21256126,
ECO:0000303|PubMed:9065401,
ECO:0000303|Ref.5}.
/FTId=VSP_006969.
VAR_SEQ 481 619 RRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPP
RDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATH
KASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSL
AGTQPQPLSLVTKSLE -> SL (in isoform 12).
{ECO:0000303|PubMed:19602480}.
/FTId=VSP_045822.
VAR_SEQ 482 494 RKKKCVRYIQGEG -> CKYSKEVSGTVRA (in
isoform 2 and isoform 4). {ECO:0000305}.
/FTId=VSP_006970.
VAR_SEQ 483 619 Missing (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006971.
VAR_SEQ 495 619 Missing (in isoform 2 and isoform 4).
{ECO:0000305}.
/FTId=VSP_006972.
VARIANT 346 346 K -> N (in dbSNP:rs2757884).
{ECO:0000269|PubMed:10919662}.
/FTId=VAR_047126.
VARIANT 465 465 R -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035939.
MUTAGEN 10 11 DD->AA: Reduces CTNNB1 binding.
{ECO:0000269|PubMed:10080941}.
MUTAGEN 16 16 D->A: Abolishes CTNNB1 binding.
{ECO:0000269|PubMed:10080941}.
MUTAGEN 17 17 E->A: Reduces CTNNB1 binding.
{ECO:0000269|PubMed:10080941}.
MUTAGEN 19 19 I->A: Reduces transcription activation.
{ECO:0000269|PubMed:11713476}.
MUTAGEN 21 21 F->A: Reduces transcription activation.
{ECO:0000269|PubMed:11713476}.
MUTAGEN 23 24 DE->AA: Reduces CTNNB1 binding.
{ECO:0000269|PubMed:10080941}.
MUTAGEN 24 24 E->A: Reduces CTNNB1 binding, and
abolishes CTNNB1 binding; when associated
with A-26; A-28 and A-29.
{ECO:0000269|PubMed:11713475}.
MUTAGEN 26 26 E->A: Abolishes CTNNB1 binding; when
associated with A-24; A-28 and A-29.
{ECO:0000269|PubMed:11713475}.
MUTAGEN 28 28 E->A: Abolishes CTNNB1 binding; when
associated with A-24; A-26 and A-29.
{ECO:0000269|PubMed:11713475}.
MUTAGEN 29 29 E->A: Reduces CTNNB1 binding, and
abolishes CTNNB1 binding; when associated
with A-24; A-26 and A-28.
{ECO:0000269|PubMed:11713475}.
MUTAGEN 48 48 L->A: Abolishes CTNNB1 binding.
{ECO:0000269|PubMed:10080941}.
MUTAGEN 201 201 T->V: Reduced phosphorylation by NLK and
enhanced DNA-binding; when associated
with V-212.
{ECO:0000269|PubMed:12556497}.
MUTAGEN 212 212 T->V: Reduced phosphorylation by NLK and
enhanced DNA-binding; when associated
with V-201.
{ECO:0000269|PubMed:12556497}.
MUTAGEN 320 320 K->R: Loss of sumoylation. No effect on
localization to nuclear bodies.
{ECO:0000269|PubMed:12727872}.
MUTAGEN 322 322 E->A: Loss of sumoylation.
{ECO:0000269|PubMed:12727872}.
CONFLICT 118 121 NGSL -> KRSV (in Ref. 2; CAB97212/
CAB97213). {ECO:0000305}.
CONFLICT 167 167 Q -> R (in Ref. 4; ADK35180).
{ECO:0000305}.
CONFLICT 226 226 P -> L (in Ref. 4; ADK35180).
{ECO:0000305}.
CONFLICT 290 290 M -> V (in Ref. 1; CAA72166).
{ECO:0000305}.
CONFLICT 331 331 L -> H (in Ref. 3; ACI28527).
{ECO:0000305}.
CONFLICT 596 596 S -> W (in Ref. 1; CAA72166).
{ECO:0000305}.
HELIX 22 31 {ECO:0000244|PDB:1JDH}.
HELIX 38 48 {ECO:0000244|PDB:1JDH}.
SEQUENCE 619 AA; 67919 MW; 4DD2D3CC814AE16E CRC64;
MPQLNGGGGD DLGANDELIS FKDEGEQEEK SSENSSAERD LADVKSSLVN ESETNQNSSS
DSEAERRPPP RSESFRDKSR ESLEEAAKRQ DGGLFKGPPY PGYPFIMIPD LTSPYLPNGS
LSPTARTLHF QSGSTHYSAY KTIEHQIAVQ YLQMKWPLLD VQAGSLQSRQ ALKDARSPSP
AHIVSNKVPV VQHPHHVHPL TPLITYSNEH FTPGNPPPHL PADVDPKTGI PRPPHPPDIS
PYYPLSPGTV GQIPHPLGWL VPQQGQPVYP ITTGGFRHPY PTALTVNASM SRFPPHMVPP
HHTLHTTGIP HPAIVTPTVK QESSQSDVGS LHSSKHQDSK KEEEKKKPHI KKPLNAFMLY
MKEMRAKVVA ECTLKESAAI NQILGRRWHA LSREEQAKYY ELARKERQLH MQLYPGWSAR
DNYGKKKKRK RDKQPGETNE HSECFLNPCL SLPPITDLSA PKKCRARFGL DQQNNWCGPC
RRKKKCVRYI QGEGSCLSPP SSDGSLLDSP PPSPNLLGSP PRDAKSQTEQ TQPLSLSLKP
DPLAHLSMMP PPPALLLAEA THKASALCPN GALDLPPAAL QPAAPSSSIA QPSTSSLHSH
SSLAGTQPQP LSLVTKSLE


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