ID TLE3_HUMAN Reviewed; 772 AA. AC Q04726; B4DPT0; E9PD64; F8W964; Q6PI57; Q8IVV6; Q8WVR2; Q9HCM5; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 222. DE RecName: Full=Transducin-like enhancer protein 3; DE AltName: Full=Enhancer of split groucho-like protein 3; DE Short=ESG3; GN Name=TLE3; Synonyms=KIAA1547; 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 1), AND VARIANT VAL-229. RC TISSUE=Fetal brain; RX PubMed=1303260; DOI=10.1038/ng1092-119; RA Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., RA Artavanis-Tsakonas S.; RT "Human homologs of a Drosophila enhancer of split gene product define a RT novel family of nuclear proteins."; RL Nat. Genet. 2:119-127(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7). RC TISSUE=Trachea; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6). RC TISSUE=Pancreas, and Testis; 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 [6] RP PROTEIN SEQUENCE OF 324-338 AND 521-531, AND INTERACTION WITH FOXA2. RX PubMed=10748198; DOI=10.1074/jbc.m910211199; RA Wang J.-C., Waltner-Law M., Yamada K., Osawa H., Stifani S., Granner D.K.; RT "Transducin-like enhancer of split proteins, the human homologs of RT Drosophila groucho, interact with hepatic nuclear factor 3beta."; RL J. Biol. Chem. 275:18418-18423(2000). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-286 AND THR-334, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP REVIEW. RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205; RA Jennings B.H., Ish-Horowicz D.; RT "The Groucho/TLE/Grg family of transcriptional co-repressors."; RL Genome Biol. 9:R205.1-R205.7(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-207; THR-259; RP SER-263; SER-267; SER-286; THR-312; SER-317; THR-319; THR-321; THR-328; RP THR-334 AND SER-413, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-286; RP THR-328 AND THR-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343 (ISOFORMS 3 AND 5), RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-336 (ISOFORM 7), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-263; RP SER-267; THR-328 AND THR-334, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-240; SER-245; RP THR-259; SER-263; SER-267 AND SER-286, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP SUBUNIT, UBIQUITINATION BY XIAP/BIRC4, AND INTERACTION WITH XIAP/BIRC4 AND RP TCF7L2/TCF4. RX PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032; RA Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.; RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."; RL Mol. Cell 45:619-628(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-207; SER-211; RP SER-263; SER-267; SER-286; THR-312; THR-328 AND THR-334, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP INTERACTION WITH TBX18. RX PubMed=26235987; DOI=10.1016/j.ajhg.2015.07.001; RA Vivante A., Kleppa M.J., Schulz J., Kohl S., Sharma A., Chen J., Shril S., RA Hwang D.Y., Weiss A.C., Kaminski M.M., Shukrun R., Kemper M.J., RA Lehnhardt A., Beetz R., Sanna-Cherchi S., Verbitsky M., Gharavi A.G., RA Stuart H.M., Feather S.A., Goodship J.A., Goodship T.H., Woolf A.S., RA Westra S.J., Doody D.P., Bauer S.B., Lee R.S., Adam R.M., Lu W., RA Reutter H.M., Kehinde E.O., Mancini E.J., Lifton R.P., Tasic V., RA Lienkamp S.S., Jueppner H., Kispert A., Hildebrandt F.; RT "Mutations in TBX18 cause dominant urinary tract malformations via RT transcriptional dysregulation of ureter development."; RL Am. J. Hum. Genet. 97:291-301(2015). CC -!- FUNCTION: Transcriptional corepressor that binds to a number of CC transcription factors. Inhibits the transcriptional activation mediated CC by CTNNB1 and TCF family members in Wnt signaling. The effects of full- CC length TLE family members may be modulated by association with CC dominant-negative AES (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotetramer and heterooligomer with other family members. CC Binds LEF1, TCF7 and TCF7L1 (By similarity). Binds FOXA2. Interacts CC with XIAP/BIRC4 and TCF7L2/TCF4. Interacts with TBX18 (via engrailed CC homology 1 repressor motif), leading to decreased of TBX18 CC transcriptional activity. {ECO:0000250|UniProtKB:Q08122, CC ECO:0000269|PubMed:10748198, ECO:0000269|PubMed:22304967, CC ECO:0000269|PubMed:26235987}. CC -!- INTERACTION: CC Q04726-4; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-12014388, EBI-2555370; CC Q04726-4; P33240: CSTF2; NbExp=3; IntAct=EBI-12014388, EBI-711360; CC Q04726-4; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-12014388, EBI-11992140; CC Q04726-4; Q15475: SIX1; NbExp=3; IntAct=EBI-12014388, EBI-743675; CC Q04726-4; Q9NPC8: SIX2; NbExp=3; IntAct=EBI-12014388, EBI-12695166; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q04726-1; Sequence=Displayed; CC Name=2; CC IsoId=Q04726-2; Sequence=VSP_006788; CC Name=3; CC IsoId=Q04726-3; Sequence=VSP_006789, VSP_006790; CC Name=4; CC IsoId=Q04726-4; Sequence=VSP_007023, VSP_007024, VSP_006790; CC Name=5; CC IsoId=Q04726-5; Sequence=VSP_006789; CC Name=6; CC IsoId=Q04726-6; Sequence=VSP_054598; CC Name=7; CC IsoId=Q04726-7; Sequence=VSP_055168, VSP_006789; CC -!- TISSUE SPECIFICITY: Placenta and lung. CC -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5 CC regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a CC central CcN domain, containing a nuclear localization signal, and a CC serine/proline-rich SP domain. The most highly conserved are the N- CC terminal Q domain and the C-terminal WD-repeat domain. CC {ECO:0000305|PubMed:18254933}. CC -!- PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect CC its stability, nuclear localization, or capacity to tetramerize but CC inhibits its interaction with TCF7L2/TCF4. CC {ECO:0000269|PubMed:22304967}. CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13373.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M99438; AAA61194.1; -; mRNA. DR EMBL; AB046767; BAB13373.1; ALT_INIT; mRNA. DR EMBL; AK315058; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK298482; BAG60692.1; -; mRNA. DR EMBL; AC026583; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC068327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015729; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC041831; AAH41831.1; -; mRNA. DR EMBL; BC043247; AAH43247.1; -; mRNA. DR CCDS; CCDS45293.1; -. [Q04726-1] DR CCDS; CCDS45294.1; -. [Q04726-5] DR CCDS; CCDS58375.1; -. [Q04726-2] DR CCDS; CCDS61689.1; -. [Q04726-7] DR CCDS; CCDS61691.1; -. [Q04726-6] DR CCDS; CCDS61692.1; -. [Q04726-3] DR PIR; D56695; D56695. DR RefSeq; NP_001098662.1; NM_001105192.2. [Q04726-5] DR RefSeq; NP_001269908.1; NM_001282979.1. [Q04726-3] DR RefSeq; NP_001269909.1; NM_001282980.1. [Q04726-6] DR RefSeq; NP_001269910.1; NM_001282981.1. [Q04726-7] DR RefSeq; NP_001269911.1; NM_001282982.1. DR RefSeq; NP_005069.2; NM_005078.3. [Q04726-1] DR RefSeq; NP_065959.1; NM_020908.2. [Q04726-2] DR AlphaFoldDB; Q04726; -. DR SMR; Q04726; -. DR BioGRID; 112945; 358. DR CORUM; Q04726; -. DR DIP; DIP-36666N; -. DR IntAct; Q04726; 89. DR MINT; Q04726; -. DR STRING; 9606.ENSP00000452871; -. DR GlyCosmos; Q04726; 4 sites, 1 glycan. DR GlyGen; Q04726; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q04726; -. DR PhosphoSitePlus; Q04726; -. DR BioMuta; TLE3; -. DR DMDM; 20532417; -. DR EPD; Q04726; -. DR jPOST; Q04726; -. DR MassIVE; Q04726; -. DR MaxQB; Q04726; -. DR PaxDb; 9606-ENSP00000452871; -. DR PeptideAtlas; Q04726; -. DR ProteomicsDB; 19592; -. DR ProteomicsDB; 30271; -. DR ProteomicsDB; 58268; -. [Q04726-1] DR ProteomicsDB; 58269; -. [Q04726-2] DR ProteomicsDB; 58270; -. [Q04726-3] DR ProteomicsDB; 58271; -. [Q04726-4] DR ProteomicsDB; 67140; -. DR Pumba; Q04726; -. DR Antibodypedia; 7320; 111 antibodies from 28 providers. DR DNASU; 7090; -. DR Ensembl; ENST00000317509.12; ENSP00000319233.8; ENSG00000140332.18. [Q04726-2] DR Ensembl; ENST00000440567.7; ENSP00000415057.3; ENSG00000140332.18. [Q04726-7] DR Ensembl; ENST00000451782.7; ENSP00000394717.3; ENSG00000140332.18. [Q04726-5] DR Ensembl; ENST00000557907.5; ENSP00000453107.1; ENSG00000140332.18. [Q04726-3] DR Ensembl; ENST00000557997.5; ENSP00000453083.1; ENSG00000140332.18. [Q04726-3] DR Ensembl; ENST00000558379.5; ENSP00000453435.1; ENSG00000140332.18. [Q04726-6] DR Ensembl; ENST00000558939.5; ENSP00000452871.1; ENSG00000140332.18. [Q04726-1] DR Ensembl; ENST00000559048.5; ENSP00000453760.1; ENSG00000140332.18. [Q04726-4] DR GeneID; 7090; -. DR KEGG; hsa:7090; -. DR MANE-Select; ENST00000451782.7; ENSP00000394717.3; NM_001105192.3; NP_001098662.1. [Q04726-5] DR UCSC; uc002asl.4; human. [Q04726-1] DR AGR; HGNC:11839; -. DR CTD; 7090; -. DR DisGeNET; 7090; -. DR GeneCards; TLE3; -. DR HGNC; HGNC:11839; TLE3. DR HPA; ENSG00000140332; Tissue enhanced (bone). DR MIM; 600190; gene. DR neXtProt; NX_Q04726; -. DR OpenTargets; ENSG00000140332; -. DR PharmGKB; PA36541; -. DR VEuPathDB; HostDB:ENSG00000140332; -. DR eggNOG; KOG0639; Eukaryota. DR GeneTree; ENSGT01030000234519; -. DR HOGENOM; CLU_007612_3_0_1; -. DR InParanoid; Q04726; -. DR OMA; LTPDANW; -. DR OrthoDB; 1333122at2759; -. DR PhylomeDB; Q04726; -. DR TreeFam; TF314167; -. DR PathwayCommons; Q04726; -. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. [Q04726-3] DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-HSA-4641265; Repression of WNT target genes. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; Q04726; -. DR SIGNOR; Q04726; -. DR BioGRID-ORCS; 7090; 42 hits in 1176 CRISPR screens. DR ChiTaRS; TLE3; human. DR GeneWiki; TLE3; -. DR GenomeRNAi; 7090; -. DR Pharos; Q04726; Tbio. DR PRO; PR:Q04726; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q04726; Protein. DR Bgee; ENSG00000140332; Expressed in blood and 165 other cell types or tissues. DR ExpressionAtlas; Q04726; baseline and differential. DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR005617; Groucho/TLE_N. DR InterPro; IPR009146; Groucho_enhance. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR10814; TRANSDUCIN-LIKE ENHANCER PROTEIN; 1. DR PANTHER; PTHR10814:SF24; TRANSDUCIN-LIKE ENHANCER PROTEIN 3; 1. DR Pfam; PF03920; TLE_N; 1. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR01850; GROUCHOFAMLY. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR Genevisible; Q04726; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; WD repeat; KW Wnt signaling pathway. FT CHAIN 1..772 FT /note="Transducin-like enhancer protein 3" FT /id="PRO_0000051280" FT REPEAT 484..522 FT /note="WD 1" FT REPEAT 530..569 FT /note="WD 2" FT REPEAT 574..613 FT /note="WD 3" FT REPEAT 616..655 FT /note="WD 4" FT REPEAT 657..696 FT /note="WD 5" FT REPEAT 698..737 FT /note="WD 6" FT REPEAT 739..771 FT /note="WD 7" FT REGION 1..131 FT /note="Q domain" FT /evidence="ECO:0000250|UniProtKB:Q04724" FT REGION 130..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 132..199 FT /note="GP domain" FT /evidence="ECO:0000250|UniProtKB:Q04724" FT REGION 185..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..268 FT /note="CcN domain" FT /evidence="ECO:0000250|UniProtKB:Q04724" FT REGION 269..452 FT /note="SP domain" FT /evidence="ECO:0000250|UniProtKB:Q04724" FT MOTIF 225..228 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 141..155 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 285..301 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..338 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 232 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q04727" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 259 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 275 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q04727" FT MOD_RES 286 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 312 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 319 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 321 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 328 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 334 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..8 FT /note="MYPQGRHP -> MPPPPPLSCLRGLQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007023" FT VAR_SEQ 1..8 FT /note="MYPQGRHP -> M (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055168" FT VAR_SEQ 127 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007024" FT VAR_SEQ 342..353 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877" FT /id="VSP_006788" FT VAR_SEQ 351..353 FT /note="Missing (in isoform 3, isoform 5 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_006789" FT VAR_SEQ 416..420 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054598" FT VAR_SEQ 417..421 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_006790" FT VARIANT 229 FT /note="A -> V (in dbSNP:rs1057864)" FT /evidence="ECO:0000269|PubMed:1303260" FT /id="VAR_053421" FT CONFLICT 358 FT /note="R -> C (in Ref. 3; BAG60692)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="S -> G (in Ref. 3; BAG60692)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="A -> T (in Ref. 5; AAH41831)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="E -> G (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="T -> S (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 535 FT /note="I -> M (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="L -> H (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 549 FT /note="V -> E (in Ref. 3; BAG60692)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="A -> G (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 692 FT /note="D -> H (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT CONFLICT 736 FT /note="F -> S (in Ref. 1; AAA61194)" FT /evidence="ECO:0000305" FT MOD_RES Q04726-3:343 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES Q04726-5:343 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES Q04726-7:336 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" SQ SEQUENCE 772 AA; 83417 MW; A2A469D73BF04A43 CRC64; MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL ANEKTEMQRH YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN AIIGQQQLQA QHLSHATHGP PVQLPPHPSG LQPPGIPPVT GSSSGLLALG ALGSQAHLTV KDEKNHHELD HRERESSANN SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS DGDKSDDLVV DVSNEDPATP RVSPAHSPPE NGLDKARSLK KDAPTSPASV ASSSSTPSSK TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI GIMASALRTP ISITSSYAAP FAMMSHHEMN GSLTSPGAYA GLHNIPPQMS AAAAAAAAAY GRSPMVSFGA VGFDPHPPMR ATGLPSSLAS IPGGKPAYSF HVSADGQMQP VPFPHDALAG PGIPRHARQI NTLSHGEVVC AVTISNPTRH VYTGGKGCVK IWDISQPGSK SPISQLDCLN RDNYIRSCKL LPDGRTLIVG GEASTLTIWD LASPTPRIKA ELTSSAPACY ALAISPDAKV CFSCCSDGNI AVWDLHNQTL VRQFQGHTDG ASCIDISHDG TKLWTGGLDN TVRSWDLREG RQLQQHDFTS QIFSLGYCPT GEWLAVGMES SNVEVLHHTK PDKYQLHLHE SCVLSLKFAY CGKWFVSTGK DNLLNAWRTP YGASIFQSKE SSSVLSCDIS ADDKYIVTGS GDKKATVYEV IY //