TLE3_HUMAN
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 03-AUG-2022, entry version 213.
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; 153.
DR CORUM; Q04726; -.
DR DIP; DIP-36666N; -.
DR IntAct; Q04726; 87.
DR MINT; Q04726; -.
DR STRING; 9606.ENSP00000452871; -.
DR GlyGen; Q04726; 4 sites, 1 O-linked glycan (4 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; Q04726; -.
DR PeptideAtlas; Q04726; -.
DR PRIDE; 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 Antibodypedia; 7320; 101 antibodies from 27 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 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; FDTQMRQ; -.
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; 40 hits in 1092 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 163 other tissues.
DR ExpressionAtlas; Q04726; baseline and differential.
DR Genevisible; Q04726; HS.
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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR005617; Groucho/TLE_N.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
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
