TLE4_HUMAN
ID TLE4_HUMAN Reviewed; 773 AA.
AC Q04727; F8W6T6; Q3ZCS1; Q5T1Y2; Q6PCB3; Q9BZ07; Q9BZ08; Q9BZ09; Q9NSL3;
AC Q9ULF9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Transducin-like enhancer protein 4;
DE AltName: Full=Grg-4;
DE AltName: Full=Groucho-related protein 4;
GN Name=TLE4; Synonyms=GRG4, KIAA1261;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Thalamus;
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 MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-773 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 326-773.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250 AND SER-269, AND
RP IDENTIFICATION BY 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 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237 AND LYS-281, 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 [13]
RP Q; GP; CCN AND SP DOMAIN BOUNDARIES.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-292, AND
RP IDENTIFICATION 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 [17]
RP INTERACTION WITH PAX2.
RX PubMed=24676634; DOI=10.1681/asn.2013070686;
RA Barua M., Stellacci E., Stella L., Weins A., Genovese G., Muto V.,
RA Caputo V., Toka H.R., Charoonratana V.T., Tartaglia M., Pollak M.R.;
RT "Mutations in PAX2 associate with adult-onset FSGS.";
RL J. Am. Soc. Nephrol. 25:1942-1953(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation mediated
CC by PAX5, and by CTNNB1 and TCF family members in Wnt signaling. The
CC effects of full-length TLE family members may be modulated by
CC association with dominant-negative AES. Essential for the
CC transcriptional repressor activity of SIX3 during retina and lens
CC development and for SIX3 transcriptional auto-repression (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC Interacts with PAX5 (By similarity). Interacts with LEF1, TCF7, TCF7L1
CC and TCF7L2 (By similarity). Interacts with ZNF703; TLE4 may mediate
CC ZNF703 transcriptional repression (By similarity). Interacts with SIX3
CC and SIX6 (By similarity). Interacts with PAX2 (PubMed:24676634).
CC Interacts with TLE1 (By similarity). {ECO:0000250|UniProtKB:Q62441,
CC ECO:0000269|PubMed:24676634}.
CC -!- INTERACTION:
CC Q04727-2; P37198: NUP62; NbExp=3; IntAct=EBI-12117860, EBI-347978;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q04727-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04727-2; Sequence=VSP_030497;
CC Name=3;
CC IsoId=Q04727-3; Sequence=VSP_030498;
CC Name=4;
CC IsoId=Q04727-4; Sequence=VSP_055169;
CC -!- TISSUE SPECIFICITY: In all tissues examined, mostly in brain, 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. PAX5 binding increases phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000269|PubMed:22304967}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86575.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033087; BAA86575.1; ALT_INIT; mRNA.
DR EMBL; AK296342; BAG59027.1; -; mRNA.
DR EMBL; AL353813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045650; AAH45650.1; -; mRNA.
DR EMBL; BC059405; AAH59405.2; -; mRNA.
DR EMBL; AL162059; CAB82397.1; -; mRNA.
DR EMBL; M99439; AAA61195.1; -; mRNA.
DR CCDS; CCDS43837.1; -. [Q04727-1]
DR CCDS; CCDS65069.1; -. [Q04727-3]
DR CCDS; CCDS65070.1; -. [Q04727-4]
DR CCDS; CCDS75851.1; -. [Q04727-2]
DR PIR; T47149; T47149.
DR RefSeq; NP_001269677.1; NM_001282748.1. [Q04727-3]
DR RefSeq; NP_001269678.1; NM_001282749.1. [Q04727-4]
DR RefSeq; NP_001269682.1; NM_001282753.1. [Q04727-2]
DR RefSeq; NP_008936.2; NM_007005.4. [Q04727-1]
DR AlphaFoldDB; Q04727; -.
DR SMR; Q04727; -.
DR BioGRID; 112946; 79.
DR CORUM; Q04727; -.
DR IntAct; Q04727; 30.
DR MINT; Q04727; -.
DR STRING; 9606.ENSP00000365720; -.
DR GlyGen; Q04727; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q04727; -.
DR PhosphoSitePlus; Q04727; -.
DR BioMuta; TLE4; -.
DR DMDM; 158518541; -.
DR EPD; Q04727; -.
DR jPOST; Q04727; -.
DR MassIVE; Q04727; -.
DR MaxQB; Q04727; -.
DR PaxDb; Q04727; -.
DR PeptideAtlas; Q04727; -.
DR PRIDE; Q04727; -.
DR ProteomicsDB; 29836; -.
DR ProteomicsDB; 58272; -. [Q04727-1]
DR ProteomicsDB; 58273; -. [Q04727-2]
DR ProteomicsDB; 58274; -. [Q04727-3]
DR Antibodypedia; 27418; 281 antibodies from 29 providers.
DR DNASU; 7091; -.
DR Ensembl; ENST00000265284.10; ENSP00000265284.6; ENSG00000106829.20. [Q04727-4]
DR Ensembl; ENST00000376537.8; ENSP00000365720.4; ENSG00000106829.20. [Q04727-3]
DR Ensembl; ENST00000376544.7; ENSP00000365727.4; ENSG00000106829.20. [Q04727-2]
DR Ensembl; ENST00000376552.8; ENSP00000365735.2; ENSG00000106829.20. [Q04727-1]
DR GeneID; 7091; -.
DR KEGG; hsa:7091; -.
DR MANE-Select; ENST00000376552.8; ENSP00000365735.2; NM_007005.6; NP_008936.2.
DR UCSC; uc004alc.5; human. [Q04727-1]
DR CTD; 7091; -.
DR DisGeNET; 7091; -.
DR GeneCards; TLE4; -.
DR HGNC; HGNC:11840; TLE4.
DR HPA; ENSG00000106829; Tissue enhanced (testis).
DR MIM; 605132; gene.
DR neXtProt; NX_Q04727; -.
DR OpenTargets; ENSG00000106829; -.
DR PharmGKB; PA36542; -.
DR VEuPathDB; HostDB:ENSG00000106829; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR HOGENOM; CLU_007612_3_0_1; -.
DR InParanoid; Q04727; -.
DR OMA; QELHRPE; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q04727; -.
DR TreeFam; TF314167; -.
DR PathwayCommons; Q04727; -.
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; Q04727; -.
DR SIGNOR; Q04727; -.
DR BioGRID-ORCS; 7091; 18 hits in 1085 CRISPR screens.
DR ChiTaRS; TLE4; human.
DR GenomeRNAi; 7091; -.
DR Pharos; Q04727; Tbio.
DR PRO; PR:Q04727; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q04727; protein.
DR Bgee; ENSG00000106829; Expressed in cranial nerve II and 201 other tissues.
DR ExpressionAtlas; Q04727; baseline and differential.
DR Genevisible; Q04727; 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; HDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..773
FT /note="Transducin-like enhancer protein 4"
FT /id="PRO_0000051283"
FT REPEAT 485..523
FT /note="WD 1"
FT REPEAT 531..570
FT /note="WD 2"
FT REPEAT 575..614
FT /note="WD 3"
FT REPEAT 617..656
FT /note="WD 4"
FT REPEAT 658..697
FT /note="WD 5"
FT REPEAT 699..738
FT /note="WD 6"
FT REPEAT 740..773
FT /note="WD 7"
FT REGION 1..136
FT /note="Q domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..204
FT /note="GP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..274
FT /note="CcN domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT REGION 275..452
FT /note="SP domain"
FT /evidence="ECO:0000305|PubMed:21429299"
FT COMPBIAS 182..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62441"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT VAR_SEQ 106..130
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055169"
FT VAR_SEQ 244..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030497"
FT VAR_SEQ 312
FT /note="L -> LKRDMGKLSETRLSEDEQCTLGLQRWFCRLWFM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030498"
FT CONFLICT 131
FT /note="Q -> QQ (in Ref. 5; CAB82397)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="A -> P (in Ref. 6; AAA61195)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="C -> A (in Ref. 6; AAA61195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 83755 MW; DA138F1DA29E81B6 CRC64;
MIRDLSKMYP QTRHPAPHQP AQPFKFTISE SCDRIKEEFQ FLQAQYHSLK LECEKLASEK
TEMQRHYVMY YEMSYGLNIE MHKQAEIVKR LNAICAQVIP FLSQEHQQQV VQAVERAKQV
TMAELNAIIG QQLQAQHLSH GHGLPVPLTP HPSGLQPPAI PPIGSSAGLL ALSSALGGQS
HLPIKDEKKH HDNDHQRDRD SIKSSSVSPS ASFRGAEKHR NSADYSSESK KQKTEEKEIA
ARYDSDGEKS DDNLVVDVSN EDPSSPRGSP AHSPRENGLD KTRLLKKDAP ISPASIASSS
STPSSKSKEL SLNEKSTTPV SKSNTPTPRT DAPTPGSNST PGLRPVPGKP PGVDPLASSL
RTPMAVPCPY PTPFGIVPHA GMNGELTSPG AAYAGLHNIS PQMSAAAAAA AAAAAYGRSP
VVGFDPHHHM RVPAIPPNLT GIPGGKPAYS FHVSADGQMQ PVPFPPDALI GPGIPRHARQ
INTLNHGEVV CAVTISNPTR HVYTGGKGCV KVWDISHPGN KSPVSQLDCL NRDNYIRSCR
LLPDGRTLIV GGEASTLSIW DLAAPTPRIK AELTSSAPAC YALAISPDSK VCFSCCSDGN
IAVWDLHNQT LVRQFQGHTD GASCIDISND GTKLWTGGLD NTVRSWDLRE GRQLQQHDFT
SQIFSLGYCP TGEWLAVGME NSNVEVLHVT KPDKYQLHLH ESCVLSLKFA HCGKWFVSTG
KDNLLNAWRT PYGASIFQSK ESSSVLSCDI SVDDKYIVTG SGDKKATVYE VIY
