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 27-MAR-2024, entry version 224. 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). Involved in transcriptional repression of GNRHR and CC enhances MSX1-mediated transcriptional repression of CGA/alpha-GSU (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62441}. 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. CC {ECO:0000250|UniProtKB:Q62441}. 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}; 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; 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; 85. DR CORUM; Q04727; -. DR IntAct; Q04727; 30. DR MINT; Q04727; -. DR STRING; 9606.ENSP00000365720; -. DR GlyCosmos; Q04727; 6 sites, 2 glycans. DR GlyGen; Q04727; 13 sites, 2 O-linked glycans (13 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; 9606-ENSP00000365720; -. DR PeptideAtlas; Q04727; -. DR ProteomicsDB; 29836; -. DR ProteomicsDB; 58272; -. [Q04727-1] DR ProteomicsDB; 58273; -. [Q04727-2] DR ProteomicsDB; 58274; -. [Q04727-3] DR Pumba; Q04727; -. DR Antibodypedia; 27418; 310 antibodies from 29 providers. DR DNASU; 7091; -. DR Ensembl; ENST00000265284.10; ENSP00000265284.6; ENSG00000106829.21. [Q04727-4] DR Ensembl; ENST00000376537.8; ENSP00000365720.4; ENSG00000106829.21. [Q04727-3] DR Ensembl; ENST00000376544.7; ENSP00000365727.4; ENSG00000106829.21. [Q04727-2] DR Ensembl; ENST00000376552.8; ENSP00000365735.2; ENSG00000106829.21. [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 AGR; HGNC:11840; -. 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; RXSPSAS; -. DR OrthoDB; 1333122at2759; -. 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 1164 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 203 other cell types or tissues. DR ExpressionAtlas; Q04727; 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; 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; ISS:UniProtKB. 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:SF31; TRANSDUCIN-LIKE ENHANCER PROTEIN 4; 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; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR Genevisible; Q04727; HS. 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 //