TCF7_HUMAN
ID TCF7_HUMAN Reviewed; 384 AA.
AC P36402; B3KSH3; Q86WR9; Q9UKI4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Transcription factor 7;
DE Short=TCF-7;
DE AltName: Full=T-cell-specific transcription factor 1;
DE Short=T-cell factor 1;
DE Short=TCF-1;
GN Name=TCF7; Synonyms=TCF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4L).
RC TISSUE=T-cell;
RX PubMed=1989880;
RA van de Wetering M., Oosterwegel M.A., Dooijes D., Clevers H.;
RT "Identification and cloning of TCF-1, a T lymphocyte-specific transcription
RT factor containing a sequence-specific HMG box.";
RL EMBO J. 10:123-132(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=T-cell;
RX PubMed=1569101; DOI=10.1016/s0021-9258(18)42476-3;
RA van de Wetering M., Oosterwegel M.A., Holstege F., Dooyes D.,
RA Suijkerbuijk R., Geurts van Kessel A., Clevers H.;
RT "The human T cell transcription factor-1 gene. Structure, localization, and
RT promoter characterization.";
RL J. Biol. Chem. 267:8530-8536(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5S; 6S; 7S AND 8S).
RC TISSUE=T-cell lymphoma;
RX PubMed=7640309; DOI=10.1016/0167-4781(95)00108-s;
RA Mayer K., Wolff E., Clevers H., Ballhausen W.G.;
RT "The human high mobility group (HMG)-box transcription factor TCF-1: novel
RT isoforms due to alternative splicing and usage of a new exon IXA.";
RL Biochim. Biophys. Acta 1263:169-172(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2S).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2L).
RC TISSUE=Liver, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68 (ISOFORM 4L), TISSUE SPECIFICITY,
RP AND INDUCTION BY TCF7L2 AND CTNNB1.
RX PubMed=10489374; DOI=10.1126/science.285.5435.1923;
RA Roose J., Huls G., van Beest M., Moerer P., van der Horn K.,
RA Goldschmeding R., Logtenberg T., Clevers H.;
RT "Synergy between tumor suppressor APC and the beta-catenin-Tcf4 target
RT Tcf1.";
RL Science 285:1923-1926(1999).
RN [8]
RP UTILIZATION OF AN UPSTREAM PROMOTER, AND IDENTIFICATION (ISOFORMS 1S AND
RP 4L).
RX PubMed=8622675; DOI=10.1128/mcb.16.3.745;
RA Van de Wetering M., Castrop J., Korinek V., Clevers H.;
RT "Extensive alternative splicing and dual promoter usage generate Tcf-1
RT protein isoforms with differential transcription control properties.";
RL Mol. Cell. Biol. 16:745-752(1996).
RN [9]
RP INTERACTION WITH CTNNB1.
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 [10]
RP INTERACTION WITH CTNNB1; TLE5 AND TLE4.
RX PubMed=9783587; DOI=10.1038/26989;
RA Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H., Moerer P.,
RA van de Wetering M., Destree O., Clevers H.;
RT "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT transcriptional repressors.";
RL Nature 395:608-612(1998).
RN [11]
RP INTERACTION WITH TLE5; TLE1; TLE2; TLE3 AND TLE4.
RX PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT "All Tcf HMG box transcription factors interact with Groucho-related co-
RT repressors.";
RL Nucleic Acids Res. 29:1410-1419(2001).
RN [12]
RP INTERACTION WITH SOX13.
RX PubMed=17218525; DOI=10.1126/science.1135344;
RA Melichar H.J., Narayan K., Der S.D., Hiraoka Y., Gardiol N., Jeannet G.,
RA Held W., Chambers C.A., Kang J.;
RT "Regulation of gammadelta versus alphabeta T lymphocyte differentiation by
RT the transcription factor SOX13.";
RL Science 315:230-233(2007).
RN [13]
RP INTERACTION WITH SOX13.
RX PubMed=20028982; DOI=10.1074/jbc.m109.046649;
RA Marfil V., Moya M., Pierreux C.E., Castell J.V., Lemaigre F.P., Real F.X.,
RA Bort R.;
RT "Interaction between Hhex and SOX13 modulates Wnt/TCF activity.";
RL J. Biol. Chem. 285:5726-5737(2010).
RN [14]
RP INTERACTION WITH MLLT11.
RX PubMed=26079538; DOI=10.18632/oncotarget.4136;
RA Park J., Schlederer M., Schreiber M., Ice R., Merkel O., Bilban M.,
RA Hofbauer S., Kim S., Addison J., Zou J., Ji C., Bunting S.T., Wang Z.,
RA Shoham M., Huang G., Bago-Horvath Z., Gibson L.F., Rojanasakul Y.,
RA Remick S., Ivanov A., Pugacheva E., Bunting K.D., Moriggl R., Kenner L.,
RA Tse W.;
RT "AF1q is a novel TCF7 co-factor which activates CD44 and promotes breast
RT cancer metastasis.";
RL Oncotarget 6:20697-20710(2015).
CC -!- FUNCTION: Transcriptional activator involved in T-cell lymphocyte
CC differentiation. Necessary for the survival of CD4(+) CD8(+) immature
CC thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain
CC cannot fulfill this role. Binds to the T-lymphocyte-specific enhancer
CC element (5'-WWCAAAG-3') found in the promoter of the CD3E gene.
CC Represses expression of the T-cell receptor gamma gene in alpha-beta T-
CC cell lineages (By similarity). Required for the development of natural
CC killer receptor-positive lymphoid tissue inducer T-cells (By
CC similarity). TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated
CC by TCF7 and CTNNB1.May also act as feedback transcriptional repressor
CC of CTNNB1 and TCF7L2 target genes. {ECO:0000250|UniProtKB:Q00417}.
CC -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable
CC complex (PubMed:9488439 PubMed:9783587). Interacts with TLE5, TLE1,
CC TLE2, TLE3 and TLE4 (PubMed:9783587, PubMed:11266540). Interacts with
CC MLLT11 (PubMed:26079538). Long isoform interacts (via N-terminus) with
CC SOX13; inhibits WNT-mediated transcriptional activity (PubMed:17218525,
CC PubMed:20028982). {ECO:0000269|PubMed:11266540,
CC ECO:0000269|PubMed:17218525, ECO:0000269|PubMed:20028982,
CC ECO:0000269|PubMed:26079538, ECO:0000269|PubMed:9488439,
CC ECO:0000269|PubMed:9783587}.
CC -!- INTERACTION:
CC P36402; P35222: CTNNB1; NbExp=4; IntAct=EBI-2119465, EBI-491549;
CC P36402; Q13015: MLLT11; NbExp=2; IntAct=EBI-2119465, EBI-6269719;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=16;
CC Comment=2 series of isoforms, L and S, are produced by alternative
CC promoter usage. Additional isoforms seem to exist.;
CC Name=4L; Synonyms=D;
CC IsoId=P36402-1; Sequence=Displayed;
CC Name=4S;
CC IsoId=P36402-2; Sequence=VSP_006961;
CC Name=1L;
CC IsoId=P36402-3; Sequence=VSP_006960;
CC Name=1S; Synonyms=E;
CC IsoId=P36402-4; Sequence=VSP_006961, VSP_006960;
CC Name=5L; Synonyms=D;
CC IsoId=P36402-9; Sequence=VSP_012160;
CC Name=5S;
CC IsoId=P36402-10; Sequence=VSP_006961, VSP_012160;
CC Name=6L; Synonyms=E;
CC IsoId=P36402-11; Sequence=VSP_012161;
CC Name=6S;
CC IsoId=P36402-12; Sequence=VSP_006961, VSP_012161;
CC Name=7L; Synonyms=F;
CC IsoId=P36402-13; Sequence=VSP_012162;
CC Name=7S;
CC IsoId=P36402-14; Sequence=VSP_006961, VSP_012162;
CC Name=8L; Synonyms=G;
CC IsoId=P36402-15; Sequence=VSP_012163;
CC Name=8S;
CC IsoId=P36402-16; Sequence=VSP_006961, VSP_012163;
CC Name=2L;
CC IsoId=P36402-5; Sequence=VSP_002191;
CC Name=2S; Synonyms=B;
CC IsoId=P36402-6; Sequence=VSP_006961, VSP_002191;
CC Name=3L;
CC IsoId=P36402-7; Sequence=VSP_002192;
CC Name=3S; Synonyms=C;
CC IsoId=P36402-8; Sequence=VSP_006961, VSP_002192;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in T-cells. Also detected
CC in proliferating intestinal epithelial cells and in the basal
CC epithelial cells of mammary gland epithelium.
CC {ECO:0000269|PubMed:10489374}.
CC -!- INDUCTION: By TCF7L2 and CTNNB1. {ECO:0000269|PubMed:10489374}.
CC -!- MISCELLANEOUS: [Isoform 1L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 1S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3L]: Produced by alternative splicing of
CC isoform 4L. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3S]: Produced by alternative splicing of
CC isoform 4S. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA87441.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; X59869; CAA42526.1; -; mRNA.
DR EMBL; X59870; CAA42527.1; -; mRNA.
DR EMBL; X59871; CAA42528.1; -; mRNA.
DR EMBL; X63901; CAB56795.1; -; Genomic_DNA.
DR EMBL; Z47361; CAA87439.1; -; mRNA.
DR EMBL; Z47362; CAA87440.1; -; mRNA.
DR EMBL; Z47363; CAA87441.1; ALT_SEQ; mRNA.
DR EMBL; Z47364; CAA87442.1; -; mRNA.
DR EMBL; AK093530; BAG52735.1; -; mRNA.
DR EMBL; CH471062; EAW62277.1; -; Genomic_DNA.
DR EMBL; BC048769; AAH48769.1; -; mRNA.
DR EMBL; BC072023; AAH72023.1; -; mRNA.
DR EMBL; AF163776; AAF00616.1; -; Genomic_DNA.
DR CCDS; CCDS4169.1; -. [P36402-5]
DR CCDS; CCDS4170.1; -. [P36402-6]
DR CCDS; CCDS43362.1; -. [P36402-8]
DR CCDS; CCDS47263.2; -. [P36402-2]
DR PIR; A38095; A38095.
DR PIR; B38095; B38095.
DR PIR; C38095; C38095.
DR PIR; D38095; D38095.
DR PIR; S61796; S61796.
DR RefSeq; NP_001128323.2; NM_001134851.3. [P36402-2]
DR RefSeq; NP_001333354.1; NM_001346425.1.
DR RefSeq; NP_001333379.1; NM_001346450.1.
DR RefSeq; NP_003193.2; NM_003202.4. [P36402-5]
DR RefSeq; NP_963963.1; NM_201632.4. [P36402-6]
DR RefSeq; NP_963965.1; NM_201634.4. [P36402-8]
DR RefSeq; NP_998813.1; NM_213648.4. [P36402-6]
DR RefSeq; XP_006714747.1; XM_006714684.2. [P36402-9]
DR AlphaFoldDB; P36402; -.
DR SMR; P36402; -.
DR BioGRID; 112794; 21.
DR IntAct; P36402; 6.
DR MINT; P36402; -.
DR STRING; 9606.ENSP00000340347; -.
DR iPTMnet; P36402; -.
DR PhosphoSitePlus; P36402; -.
DR BioMuta; TCF7; -.
DR DMDM; 209572716; -.
DR jPOST; P36402; -.
DR MassIVE; P36402; -.
DR MaxQB; P36402; -.
DR PaxDb; P36402; -.
DR PeptideAtlas; P36402; -.
DR PRIDE; P36402; -.
DR ProteomicsDB; 55182; -. [P36402-1]
DR ProteomicsDB; 55183; -. [P36402-10]
DR ProteomicsDB; 55184; -. [P36402-11]
DR ProteomicsDB; 55185; -. [P36402-12]
DR ProteomicsDB; 55186; -. [P36402-13]
DR ProteomicsDB; 55187; -. [P36402-14]
DR ProteomicsDB; 55188; -. [P36402-15]
DR ProteomicsDB; 55189; -. [P36402-16]
DR ProteomicsDB; 55190; -. [P36402-2]
DR ProteomicsDB; 55191; -. [P36402-3]
DR ProteomicsDB; 55192; -. [P36402-4]
DR ProteomicsDB; 55193; -. [P36402-5]
DR ProteomicsDB; 55194; -. [P36402-6]
DR ProteomicsDB; 55195; -. [P36402-7]
DR ProteomicsDB; 55196; -. [P36402-8]
DR ProteomicsDB; 55197; -. [P36402-9]
DR Antibodypedia; 14629; 490 antibodies from 37 providers.
DR DNASU; 6932; -.
DR Ensembl; ENST00000342854.10; ENSP00000340347.5; ENSG00000081059.20. [P36402-5]
DR Ensembl; ENST00000378560.8; ENSP00000367822.4; ENSG00000081059.20. [P36402-8]
DR Ensembl; ENST00000395023.5; ENSP00000378469.1; ENSG00000081059.20. [P36402-6]
DR Ensembl; ENST00000518915.5; ENSP00000430179.1; ENSG00000081059.20. [P36402-2]
DR Ensembl; ENST00000520958.5; ENSP00000429547.1; ENSG00000081059.20. [P36402-6]
DR GeneID; 6932; -.
DR KEGG; hsa:6932; -.
DR MANE-Select; ENST00000342854.10; ENSP00000340347.5; NM_003202.5; NP_003193.2. [P36402-5]
DR UCSC; uc003kyt.4; human. [P36402-1]
DR CTD; 6932; -.
DR DisGeNET; 6932; -.
DR GeneCards; TCF7; -.
DR HGNC; HGNC:11639; TCF7.
DR HPA; ENSG00000081059; Tissue enriched (lymphoid).
DR MIM; 189908; gene.
DR neXtProt; NX_P36402; -.
DR OpenTargets; ENSG00000081059; -.
DR PharmGKB; PA36392; -.
DR VEuPathDB; HostDB:ENSG00000081059; -.
DR eggNOG; KOG3248; Eukaryota.
DR GeneTree; ENSGT00940000159831; -.
DR HOGENOM; CLU_013229_5_0_1; -.
DR InParanoid; P36402; -.
DR OMA; MHYPAPS; -.
DR OrthoDB; 807716at2759; -.
DR PhylomeDB; P36402; -.
DR TreeFam; TF318448; -.
DR PathwayCommons; P36402; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
DR SignaLink; P36402; -.
DR SIGNOR; P36402; -.
DR BioGRID-ORCS; 6932; 18 hits in 1101 CRISPR screens.
DR ChiTaRS; TCF7; human.
DR GeneWiki; TCF7; -.
DR GenomeRNAi; 6932; -.
DR Pharos; P36402; Tbio.
DR PRO; PR:P36402; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P36402; protein.
DR Bgee; ENSG00000081059; Expressed in thymus and 205 other tissues.
DR ExpressionAtlas; P36402; baseline and differential.
DR Genevisible; P36402; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0045586; P:regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:InterPro.
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 InterPro; IPR028785; Tcf7.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF33; PTHR10373:SF33; 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 promoter usage; Alternative splicing; DNA-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..384
FT /note="Transcription factor 7"
FT /id="PRO_0000048612"
FT DNA_BIND 269..337
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..59
FT /note="CTNNB1-binding"
FT REGION 133..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..348
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 1S, isoform 2S, isoform 3S,
FT isoform 4S, isoform 5S, isoform 6S, isoform 7S and isoform
FT 8S)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7640309"
FT /id="VSP_006961"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRARFGLNQQTDWCG
FT PCRRKKKCIRYLPGEGRCPSPVPSDDSALGCPGSPAPQDSPSYHLLPRFPTELLTSPAE
FT RHLHPQVSPLLSASQPQGPHRPPAAPCRAHRYSNRNLRDRWPSRHRTPGRLQEPTP
FT (in isoform 1L and isoform 1S)"
FT /evidence="ECO:0000305"
FT /id="VSP_006960"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> GGKRNAFGTYPEKAAAPAPFLP
FT MTVL (in isoform 2L and isoform 2S)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_002191"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRARFGLNQQTDWCG
FT PCR (in isoform 3L and isoform 3S)"
FT /evidence="ECO:0000305"
FT /id="VSP_002192"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> DNSLHYS (in isoform 5L
FT and isoform 5S)"
FT /evidence="ECO:0000303|PubMed:7640309"
FT /id="VSP_012160"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRARFGLNQQTDWCG
FT PCRKKKCIRYLPGEGRCPSPVPSDDSALGCPGSPAPQDSPSYHLLPRFPTELLTSPAER
FT HLHPQVSPLLSASQPQGPHRPPAAPCRAHRYSNRNLRDRWPSRHRTPGRLQEPTP (in
FT isoform 6L and isoform 6S)"
FT /evidence="ECO:0000303|PubMed:7640309"
FT /id="VSP_012161"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> DGIPACTILSP (in
FT isoform 7L and isoform 7S)"
FT /evidence="ECO:0000303|PubMed:7640309"
FT /id="VSP_012162"
FT VAR_SEQ 359..384
FT /note="ETNWPRELKDGNGQESLSMSSSSSPA -> QLEDWDGWARKP (in
FT isoform 8L and isoform 8S)"
FT /evidence="ECO:0000303|PubMed:7640309"
FT /id="VSP_012163"
FT CONFLICT 21
FT /note="D -> N (in Ref. 7; AAF00616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 41642 MW; 5088C962F2FD0C00 CRC64;
MPQLDSGGGG AGGGDDLGAP DELLAFQDEG EEQDDKSRDS AAGPERDLAE LKSSLVNESE
GAAGGAGIPG VPGAGAGARG EAEALGREHA AQRLFPDKLP EPLEDGLKAP ECTSGMYKET
VYSAFNLLMH YPPPSGAGQH PQPQPPLHKA NQPPHGVPQL SLYEHFNSPH PTPAPADISQ
KQVHRPLQTP DLSGFYSLTS GSMGQLPHTV SWFTHPSLML GSGVPGHPAA IPHPAIVPPS
GKQELQPFDR NLKTQAESKA EKEAKKPTIK KPLNAFMLYM KEMRAKVIAE CTLKESAAIN
QILGRRWHAL SREEQAKYYE LARKERQLHM QLYPGWSARD NYGKKKRRSR EKHQESTTET
NWPRELKDGN GQESLSMSSS SSPA
