TLE1_HUMAN
ID TLE1_HUMAN Reviewed; 770 AA.
AC Q04724; A8K495; Q5T3G4; Q969V9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Transducin-like enhancer protein 1;
DE AltName: Full=E(Sp1) homolog;
DE AltName: Full=Enhancer of split groucho-like protein 1;
DE Short=ESG1;
GN Name=TLE1;
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].
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].
RC TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Kidney;
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 727-739, INTERACTION WITH FOXA2, AND MODULATION BY AES.
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 INTERACTION WITH TLE1.
RX PubMed=8687460; DOI=10.1006/bbrc.1996.0959;
RA Grbavec D., Stifani S.;
RT "Molecular interaction between TLE1 and the carboxyl-terminal domain of
RT HES-1 containing the WRPW motif.";
RL Biochem. Biophys. Res. Commun. 223:701-705(1996).
RN [8]
RP INTERACTION WITH HES1.
RX PubMed=8649374; DOI=10.1128/mcb.16.6.2670;
RA Fisher A.L., Ohsako S., Caudy M.;
RT "The WRPW motif of the hairy-related basic helix-loop-helix repressor
RT proteins acts as a 4-amino-acid transcription repression and protein-
RT protein interaction domain.";
RL Mol. Cell. Biol. 16:2670-2677(1996).
RN [9]
RP OLIGOMERIZATION, ASSOCIATION WITH CHROMATIN, AND INTERACTION WITH HISTONE
RP H3.
RX PubMed=9334241; DOI=10.1074/jbc.272.42.26604;
RA Palaparti A., Baratz A., Stifani S.;
RT "The Groucho/transducin-like enhancer of split transcriptional repressors
RT interact with the genetically defined amino-terminal silencing domain of
RT histone H3.";
RL J. Biol. Chem. 272:26604-26610(1997).
RN [10]
RP OLIGOMERIZATION, AND INTERACTION WITH HES1.
RX PubMed=9874198; DOI=10.1046/j.1432-1327.1998.2580339.x;
RA Grbavec D., Lo R., Liu Y., Stifani S.;
RT "Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila
RT Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer
RT of split proteins, and is expressed during neuronal development.";
RL Eur. J. Biochem. 258:339-349(1998).
RN [11]
RP INTERACTION WITH RUNX1; RUNX3 AND LEF1.
RX PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
RA Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
RA Stifani S., Paroush Z., Groner Y.;
RT "Transcriptional repression by AML1 and LEF-1 is mediated by the
RT TLE/Groucho corepressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
RN [12]
RP INTERACTION WITH KDM6A AND UTY.
RX PubMed=9854018; DOI=10.1042/bj3370013;
RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT "Groucho/transducin-like enhancer of split (TLE) family members interact
RT with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related
RT proteins: implications for evolutionary conservation of transcription
RT repression mechanisms.";
RL Biochem. J. 337:13-17(1999).
RN [13]
RP FUNCTION, AND INTERACTION WITH RELA.
RX PubMed=10660609; DOI=10.1074/jbc.275.6.4383;
RA Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N.,
RA Asamitsu K., Okamoto T.;
RT "Inhibition of nuclear factor-kappaB-mediated transcription by association
RT with the amino-terminal enhancer of split, a Groucho-related protein
RT lacking WD40 repeats.";
RL J. Biol. Chem. 275:4383-4390(2000).
RN [14]
RP INTERACTION WITH HESX1, AND MUTAGENESIS OF VAL-486; TYR-532; LEU-702 AND
RP SER-715.
RX PubMed=11731482; DOI=10.1101/gad.932601;
RA Dasen J.S., Martinez-Barbera J.-P., Herman T.S., O'Connell S., Olson L.,
RA Ju B., Tollkuhn J., Baek S.H., Rose D.W., Rosenfeld M.G.;
RT "Temporal regulation of a paired-like homeodomain repressor/TLE corepressor
RT complex and a related activator is required for pituitary organogenesis.";
RL Genes Dev. 15:3193-3207(2001).
RN [15]
RP SUBCELLULAR LOCATION, AND DEGREE OF PHOSPHORYLATION.
RX PubMed=12397081; DOI=10.1074/jbc.m111660200;
RA Nuthall H.N., Joachim K., Palaparti A., Stifani S.;
RT "A role for cell cycle-regulated phosphorylation in Groucho-mediated
RT transcriptional repression.";
RL J. Biol. Chem. 277:51049-51057(2002).
RN [16]
RP INTERACTION WITH ESRRG.
RX PubMed=14651967; DOI=10.1016/j.bbrc.2003.11.025;
RA Hentschke M., Borgmeyer U.;
RT "Identification of PNRC2 and TLE1 as activation function-1 cofactors of the
RT orphan nuclear receptor ERRgamma.";
RL Biochem. Biophys. Res. Commun. 312:975-982(2003).
RN [17]
RP INTERACTION WITH SIX3.
RX PubMed=12441302; DOI=10.1242/dev.00185;
RA Lopez-Rios J., Tessmar K., Loosli F., Wittbrodt J., Bovolenta P.;
RT "Six3 and Six6 activity is modulated by members of the groucho family.";
RL Development 130:185-195(2003).
RN [18]
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 [19]
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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21]
RP INTERACTION WITH EFNB1.
RX PubMed=21429299; DOI=10.5483/bmbrep.2011.44.3.199;
RA Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.;
RT "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4.";
RL BMB Rep. 44:199-204(2011).
RN [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-286, AND
RP IDENTIFICATION BY MASS 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 [24]
RP UBIQUITINATION BY XIAP/BIRC4.
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 [25]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 443-770.
RX PubMed=12057191; DOI=10.1016/s0969-2126(02)00768-2;
RA Pickles L.M., Roe S.M., Hemingway E.J., Stifani S., Pearl L.H.;
RT "Crystal structure of the C-terminal WD40 repeat domain of the human
RT Groucho/TLE1 transcriptional corepressor.";
RL Structure 10:751-761(2002).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits NF-kappa-B-regulated gene expression.
CC Inhibits the transcriptional activation mediated by FOXA2, and by
CC CTNNB1 and TCF family members in Wnt signaling. Enhances FOXG1/BF-
CC 1- and HES1-mediated transcriptional repression (By similarity). The
CC effects of full-length TLE family members may be modulated by
CC association with dominant-negative AES. Unusual function as coactivator
CC for ESRRG. {ECO:0000250|UniProtKB:Q62440, ECO:0000269|PubMed:10660609}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC Binds RUNX1, RUNX3, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG and the
CC NF-kappa-B subunit RELA. Interacts with HES1 (via WRPW motif). Binds
CC TCF7, LEF1, TCF7L1 and TCF7L2 (By similarity). Interacts with SIX3.
CC Interacts with EFNB1. Interacts with TLE4 (By similarity). Interacts
CC with FOXG1/BF-1; the interaction is inhibited by TLE6/GRG6 (By
CC similarity). {ECO:0000250|UniProtKB:Q62440,
CC ECO:0000269|PubMed:10660609, ECO:0000269|PubMed:10748198,
CC ECO:0000269|PubMed:11731482, ECO:0000269|PubMed:12441302,
CC ECO:0000269|PubMed:14651967, ECO:0000269|PubMed:21429299,
CC ECO:0000269|PubMed:8649374, ECO:0000269|PubMed:8687460,
CC ECO:0000269|PubMed:9334241, ECO:0000269|PubMed:9751710,
CC ECO:0000269|PubMed:9854018, ECO:0000269|PubMed:9874198}.
CC -!- INTERACTION:
CC Q04724; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-711424, EBI-702390;
CC Q04724; Q15038: DAZAP2; NbExp=3; IntAct=EBI-711424, EBI-724310;
CC Q04724; P55316: FOXG1; NbExp=2; IntAct=EBI-711424, EBI-715416;
CC Q04724; P28799: GRN; NbExp=3; IntAct=EBI-711424, EBI-747754;
CC Q04724; P62805: H4C9; NbExp=6; IntAct=EBI-711424, EBI-302023;
CC Q04724; P07686: HEXB; NbExp=3; IntAct=EBI-711424, EBI-7133736;
CC Q04724; Q9HC29: NOD2; NbExp=2; IntAct=EBI-711424, EBI-7445625;
CC Q04724; O60260-5: PRKN; NbExp=3; IntAct=EBI-711424, EBI-21251460;
CC Q04724; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-711424, EBI-396669;
CC Q04724; Q01196-1: RUNX1; NbExp=4; IntAct=EBI-711424, EBI-925940;
CC Q04724; Q01196-2: RUNX1; NbExp=3; IntAct=EBI-711424, EBI-925944;
CC Q04724; Q13761: RUNX3; NbExp=3; IntAct=EBI-711424, EBI-925990;
CC Q04724; Q96EB6: SIRT1; NbExp=4; IntAct=EBI-711424, EBI-1802965;
CC Q04724; A4PIW0: SYT-SSX2; NbExp=11; IntAct=EBI-711424, EBI-6050533;
CC Q04724; Q04724: TLE1; NbExp=4; IntAct=EBI-711424, EBI-711424;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12397081}.
CC Note=Nuclear and chromatin-associated, depending on isoforms and
CC phosphorylation status. Hyperphosphorylation decreases the affinity for
CC nuclear components.
CC -!- TISSUE SPECIFICITY: In all tissues examined, mostly in brain, liver and
CC muscle.
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: Phosphorylated, probably by CDK1. The degree of phosphorylation
CC varies throughout the cell cycle, and is highest at the G2/M
CC transition. Becomes hyperphosphorylated in response to cell
CC differentiation and interaction with HES1 or RUNX1.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000269|PubMed:22304967}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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DR EMBL; M99435; AAA61192.1; -; mRNA.
DR EMBL; AK290860; BAF83549.1; -; mRNA.
DR EMBL; AL365190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62636.1; -; Genomic_DNA.
DR EMBL; BC010100; AAH10100.1; -; mRNA.
DR EMBL; BC015747; AAH15747.1; -; mRNA.
DR CCDS; CCDS6661.1; -.
DR PIR; B56695; B56695.
DR RefSeq; NP_001290032.1; NM_001303103.1.
DR RefSeq; NP_001290033.1; NM_001303104.1.
DR RefSeq; NP_005068.2; NM_005077.4.
DR PDB; 1GXR; X-ray; 1.65 A; A/B=443-770.
DR PDB; 2CE8; X-ray; 2.03 A; A/B/C/D=443-770.
DR PDB; 2CE9; X-ray; 2.12 A; A/B/C/D=443-770.
DR PDB; 4OM2; X-ray; 4.00 A; A/B/C/D=1-156.
DR PDB; 4OM3; X-ray; 2.86 A; A/B/C/D=15-156.
DR PDB; 5MWJ; X-ray; 2.04 A; A/B=443-770.
DR PDBsum; 1GXR; -.
DR PDBsum; 2CE8; -.
DR PDBsum; 2CE9; -.
DR PDBsum; 4OM2; -.
DR PDBsum; 4OM3; -.
DR PDBsum; 5MWJ; -.
DR AlphaFoldDB; Q04724; -.
DR SMR; Q04724; -.
DR BioGRID; 112943; 193.
DR CORUM; Q04724; -.
DR DIP; DIP-36665N; -.
DR IntAct; Q04724; 145.
DR MINT; Q04724; -.
DR STRING; 9606.ENSP00000365682; -.
DR iPTMnet; Q04724; -.
DR PhosphoSitePlus; Q04724; -.
DR BioMuta; TLE1; -.
DR DMDM; 29840816; -.
DR CPTAC; CPTAC-1189; -.
DR EPD; Q04724; -.
DR jPOST; Q04724; -.
DR MassIVE; Q04724; -.
DR MaxQB; Q04724; -.
DR PaxDb; Q04724; -.
DR PeptideAtlas; Q04724; -.
DR PRIDE; Q04724; -.
DR ProteomicsDB; 58266; -.
DR Antibodypedia; 3147; 595 antibodies from 36 providers.
DR DNASU; 7088; -.
DR Ensembl; ENST00000376499.8; ENSP00000365682.3; ENSG00000196781.16.
DR GeneID; 7088; -.
DR KEGG; hsa:7088; -.
DR MANE-Select; ENST00000376499.8; ENSP00000365682.3; NM_005077.5; NP_005068.2.
DR UCSC; uc004aly.4; human.
DR CTD; 7088; -.
DR DisGeNET; 7088; -.
DR GeneCards; TLE1; -.
DR HGNC; HGNC:11837; TLE1.
DR HPA; ENSG00000196781; Low tissue specificity.
DR MIM; 600189; gene.
DR neXtProt; NX_Q04724; -.
DR OpenTargets; ENSG00000196781; -.
DR PharmGKB; PA36539; -.
DR VEuPathDB; HostDB:ENSG00000196781; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR HOGENOM; CLU_007612_3_0_1; -.
DR InParanoid; Q04724; -.
DR OMA; QLICPLI; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q04724; -.
DR TreeFam; TF314167; -.
DR PathwayCommons; Q04724; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR SignaLink; Q04724; -.
DR SIGNOR; Q04724; -.
DR BioGRID-ORCS; 7088; 23 hits in 1085 CRISPR screens.
DR ChiTaRS; TLE1; human.
DR EvolutionaryTrace; Q04724; -.
DR GeneWiki; TLE1; -.
DR GenomeRNAi; 7088; -.
DR Pharos; Q04724; Tbio.
DR PRO; PR:Q04724; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q04724; protein.
DR Bgee; ENSG00000196781; Expressed in ventricular zone and 210 other tissues.
DR ExpressionAtlas; Q04724; baseline and differential.
DR Genevisible; Q04724; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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 IDEAL; IID00208; -.
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 3D-structure; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..770
FT /note="Transducin-like enhancer protein 1"
FT /id="PRO_0000051276"
FT REPEAT 470..501
FT /note="WD 1"
FT REPEAT 528..558
FT /note="WD 2"
FT REPEAT 572..602
FT /note="WD 3"
FT REPEAT 614..644
FT /note="WD 4"
FT REPEAT 696..726
FT /note="WD 5"
FT REPEAT 737..767
FT /note="WD 6"
FT REGION 1..131
FT /note="Q domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..199
FT /note="GP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 176..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..268
FT /note="CcN domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 269..450
FT /note="SP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT MOTIF 225..228
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 140..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 259
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 263
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 267
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MUTAGEN 486
FT /note="V->S: Abolishes HESX1 binding."
FT /evidence="ECO:0000269|PubMed:11731482"
FT MUTAGEN 532
FT /note="Y->H: Abolishes HESX1 binding."
FT /evidence="ECO:0000269|PubMed:11731482"
FT MUTAGEN 702
FT /note="L->S: Abolishes HESX1 binding."
FT /evidence="ECO:0000269|PubMed:11731482"
FT MUTAGEN 715
FT /note="S->P: Abolishes HESX1 binding."
FT /evidence="ECO:0000269|PubMed:11731482"
FT CONFLICT 407..412
FT /note="AAAVVA -> RGRRGR (in Ref. 1; AAA61192)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="DA -> TP (in Ref. 1; AAA61192)"
FT /evidence="ECO:0000305"
FT HELIX 22..92
FT /evidence="ECO:0007829|PDB:4OM3"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4OM3"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:4OM3"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:4OM3"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 494..502
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 542..558
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:2CE8"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 586..593
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:1GXR"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 628..635
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:1GXR"
FT TURN 645..648
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 681..685
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 710..717
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 720..726
FT /evidence="ECO:0007829|PDB:1GXR"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 732..737
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 742..747
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:1GXR"
FT STRAND 763..769
FT /evidence="ECO:0007829|PDB:1GXR"
SQ SEQUENCE 770 AA; 83201 MW; 695FD1A37410EFE5 CRC64;
MFPQSRHPTP HQAAGQPFKF TIPESLDRIK EEFQFLQAQY HSLKLECEKL ASEKTEMQRH
YVMYYEMSYG LNIEMHKQTE IAKRLNTICA QVIPFLSQEH QQQVAQAVER AKQVTMAELN
AIIGQQQLQA QHLSHGHGPP VPLTPHPSGL QPPGIPPLGG SAGLLALSSA LSGQSHLAIK
DDKKHHDAEH HRDREPGTSN SLLVPDSLRG TDKRRNGPEF SNDIKKRKVD DKDSSHYDSD
GDKSDDNLVV DVSNEDPSSP RASPAHSPRE NGIDKNRLLK KDASSSPAST ASSASSTSLK
SKEMSLHEKA STPVLKSSTP TPRSDMPTPG TSATPGLRPG LGKPPAIDPL VNQAAAGLRT
PLAVPGPYPA PFGMVPHAGM NGELTSPGAA YASLHNMSPQ MSAAAAAAAV VAYGRSPMVG
FDPPPHMRVP TIPPNLAGIP GGKPAYSFHV TADGQMQPVP FPPDALIGPG IPRHARQINT
LNHGEVVCAV TISNPTRHVY TGGKGCVKVW DISHPGNKSP VSQLDCLNRD NYIRSCKLLP
DGCTLIVGGE ASTLSIWDLA APTPRIKAEL TSSAPACYAL AISPDSKVCF SCCSDGNIAV
WDLHNQTLVR QFQGHTDGAS CIDISNDGTK LWTGGLDNTV RSWDLREGRQ LQQHDFTSQI
FSLGYCPTGE WLAVGMESSN VEVLHVNKPD KYQLHLHESC VLSLKFAYCG KWFVSTGKDN
LLNAWRTPYG ASIFQSKESS SVLSCDISVD DKYIVTGSGD KKATVYEVIY
