Full text data of TLE3
TLE3
(KIAA1547)
[Confidence: low (only semi-automatic identification from reviews)]
Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3; ESG3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transducin-like enhancer protein 3 (Enhancer of split groucho-like protein 3; ESG3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q04726
ID TLE3_HUMAN Reviewed; 772 AA.
AC Q04726; E9PD64; Q8IVV6; Q8WVR2; Q9HCM5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 145.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT a 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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
RT project: 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.,
RA 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-286 AND
RP THR-334, AND MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
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;
RP THR-328; THR-334 AND SER-413, AND MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-286;
RP THR-328 AND THR-334, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343 (ISOFORMS 3 AND 5), AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-263;
RP SER-267; THR-328 AND THR-334, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-240; SER-245;
RP THR-259; SER-263; SER-267 AND SER-286, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP SUBUNIT, UBIQUITINATION BY XIAP/BIRC4, AND INTERACTION WITH XIAP/BIRC4
RP AND 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.,
RA Lee E.;
RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt
RT signaling.";
RL Mol. Cell 45:619-628(2012).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation
CC mediated 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 (By similarity).
CC -!- SUBUNIT: Homotetramer and heterooligomer with other family
CC members. Binds LEF1, TCF7 and TCF7L1 (By similarity). Binds FOXA2.
CC Interacts with XIAP/BIRC4 and TCF7L2/TCF4.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some
CC 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 Note=Contains a N6-acetyllysine at position 343;
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 Note=No experimental confirmation available. Contains a
CC N6-acetyllysine at position 343;
CC -!- TISSUE SPECIFICITY: Placenta and lung.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not
CC affect its stability, nuclear localization, or capacity to
CC tetramerize but inhibits its interaction with TCF7L2/TCF4.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13373.1; Type=Erroneous initiation;
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DR EMBL; M99438; AAA61194.1; -; mRNA.
DR EMBL; AB046767; BAB13373.1; ALT_INIT; mRNA.
DR EMBL; AK315058; -; NOT_ANNOTATED_CDS; 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 PIR; D56695; D56695.
DR RefSeq; NP_001098662.1; NM_001105192.2.
DR RefSeq; NP_001269908.1; NM_001282979.1.
DR RefSeq; NP_001269909.1; NM_001282980.1.
DR RefSeq; NP_001269910.1; NM_001282981.1.
DR RefSeq; NP_001269911.1; NM_001282982.1.
DR RefSeq; NP_005069.2; NM_005078.3.
DR RefSeq; NP_065959.1; NM_020908.2.
DR RefSeq; XP_005254681.1; XM_005254624.1.
DR UniGene; Hs.287362; -.
DR ProteinModelPortal; Q04726; -.
DR SMR; Q04726; 443-772.
DR IntAct; Q04726; 8.
DR MINT; MINT-2805536; -.
DR STRING; 9606.ENSP00000319233; -.
DR PhosphoSite; Q04726; -.
DR DMDM; 20532417; -.
DR PaxDb; Q04726; -.
DR PRIDE; Q04726; -.
DR DNASU; 7090; -.
DR Ensembl; ENST00000317509; ENSP00000319233; ENSG00000140332.
DR Ensembl; ENST00000451782; ENSP00000394717; ENSG00000140332.
DR Ensembl; ENST00000557907; ENSP00000453107; ENSG00000140332.
DR Ensembl; ENST00000557997; ENSP00000453083; ENSG00000140332.
DR Ensembl; ENST00000558939; ENSP00000452871; ENSG00000140332.
DR Ensembl; ENST00000559048; ENSP00000453760; ENSG00000140332.
DR GeneID; 7090; -.
DR KEGG; hsa:7090; -.
DR UCSC; uc010bil.1; human.
DR CTD; 7090; -.
DR GeneCards; GC15M070341; -.
DR HGNC; HGNC:11839; TLE3.
DR HPA; HPA054116; -.
DR MIM; 600190; gene.
DR neXtProt; NX_Q04726; -.
DR PharmGKB; PA36541; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000293211; -.
DR HOVERGEN; HBG004689; -.
DR InParanoid; Q04726; -.
DR OrthoDB; EOG7HQNC3; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q04726; -.
DR GeneWiki; TLE3; -.
DR GenomeRNAi; 7090; -.
DR NextBio; 27731; -.
DR PRO; PR:Q04726; -.
DR ArrayExpress; Q04726; -.
DR Bgee; Q04726; -.
DR CleanEx; HS_TLE3; -.
DR Genevestigator; Q04726; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor 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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 5.
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; Complete proteome;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1 772 Transducin-like enhancer protein 3.
FT /FTId=PRO_0000051280.
FT REPEAT 484 522 WD 1.
FT REPEAT 530 569 WD 2.
FT REPEAT 574 613 WD 3.
FT REPEAT 616 655 WD 4.
FT REPEAT 657 696 WD 5.
FT REPEAT 698 737 WD 6.
FT REPEAT 739 771 WD 7.
FT REGION 199 268 CCN domain.
FT MOTIF 225 228 Nuclear localization signal (Potential).
FT COMPBIAS 1 131 Gln-rich.
FT COMPBIAS 132 198 Gly/Pro-rich.
FT COMPBIAS 269 451 Pro/Ser-rich.
FT COMPBIAS 401 409 Poly-Ala.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 207 207 Phosphoserine.
FT MOD_RES 217 217 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 259 259 Phosphothreonine.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 267 267 Phosphoserine.
FT MOD_RES 286 286 Phosphoserine.
FT MOD_RES 312 312 Phosphothreonine.
FT MOD_RES 317 317 Phosphoserine.
FT MOD_RES 319 319 Phosphothreonine.
FT MOD_RES 321 321 Phosphothreonine.
FT MOD_RES 328 328 Phosphothreonine.
FT MOD_RES 334 334 Phosphothreonine.
FT MOD_RES 413 413 Phosphoserine.
FT VAR_SEQ 1 8 MYPQGRHP -> MPPPPPLSCLRGLQ (in isoform
FT 4).
FT /FTId=VSP_007023.
FT VAR_SEQ 127 127 Missing (in isoform 4).
FT /FTId=VSP_007024.
FT VAR_SEQ 342 353 Missing (in isoform 2).
FT /FTId=VSP_006788.
FT VAR_SEQ 351 353 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_006789.
FT VAR_SEQ 417 421 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_006790.
FT VARIANT 229 229 A -> V (in dbSNP:rs1057864).
FT /FTId=VAR_053421.
FT CONFLICT 409 409 A -> T (in Ref. 5; AAH41831).
FT CONFLICT 487 487 E -> G (in Ref. 1; AAA61194).
FT CONFLICT 498 498 T -> S (in Ref. 1; AAA61194).
FT CONFLICT 535 535 I -> M (in Ref. 1; AAA61194).
FT CONFLICT 541 541 L -> H (in Ref. 1; AAA61194).
FT CONFLICT 553 553 A -> G (in Ref. 1; AAA61194).
FT CONFLICT 692 692 D -> H (in Ref. 1; AAA61194).
FT CONFLICT 736 736 F -> S (in Ref. 1; AAA61194).
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
//
ID TLE3_HUMAN Reviewed; 772 AA.
AC Q04726; E9PD64; Q8IVV6; Q8WVR2; Q9HCM5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 145.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT a 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.
RT XVIII. The complete sequences of 100 new cDNA clones from brain which
RT code for large proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human
RT chromosome 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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
RT project: 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.,
RA 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-286 AND
RP THR-334, AND MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
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;
RP THR-328; THR-334 AND SER-413, AND MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-286;
RP THR-328 AND THR-334, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343 (ISOFORMS 3 AND 5), AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-263;
RP SER-267; THR-328 AND THR-334, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-240; SER-245;
RP THR-259; SER-263; SER-267 AND SER-286, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP SUBUNIT, UBIQUITINATION BY XIAP/BIRC4, AND INTERACTION WITH XIAP/BIRC4
RP AND 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.,
RA Lee E.;
RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt
RT signaling.";
RL Mol. Cell 45:619-628(2012).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation
CC mediated 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 (By similarity).
CC -!- SUBUNIT: Homotetramer and heterooligomer with other family
CC members. Binds LEF1, TCF7 and TCF7L1 (By similarity). Binds FOXA2.
CC Interacts with XIAP/BIRC4 and TCF7L2/TCF4.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some
CC 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 Note=Contains a N6-acetyllysine at position 343;
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 Note=No experimental confirmation available. Contains a
CC N6-acetyllysine at position 343;
CC -!- TISSUE SPECIFICITY: Placenta and lung.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not
CC affect its stability, nuclear localization, or capacity to
CC tetramerize but inhibits its interaction with TCF7L2/TCF4.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13373.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; M99438; AAA61194.1; -; mRNA.
DR EMBL; AB046767; BAB13373.1; ALT_INIT; mRNA.
DR EMBL; AK315058; -; NOT_ANNOTATED_CDS; 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 PIR; D56695; D56695.
DR RefSeq; NP_001098662.1; NM_001105192.2.
DR RefSeq; NP_001269908.1; NM_001282979.1.
DR RefSeq; NP_001269909.1; NM_001282980.1.
DR RefSeq; NP_001269910.1; NM_001282981.1.
DR RefSeq; NP_001269911.1; NM_001282982.1.
DR RefSeq; NP_005069.2; NM_005078.3.
DR RefSeq; NP_065959.1; NM_020908.2.
DR RefSeq; XP_005254681.1; XM_005254624.1.
DR UniGene; Hs.287362; -.
DR ProteinModelPortal; Q04726; -.
DR SMR; Q04726; 443-772.
DR IntAct; Q04726; 8.
DR MINT; MINT-2805536; -.
DR STRING; 9606.ENSP00000319233; -.
DR PhosphoSite; Q04726; -.
DR DMDM; 20532417; -.
DR PaxDb; Q04726; -.
DR PRIDE; Q04726; -.
DR DNASU; 7090; -.
DR Ensembl; ENST00000317509; ENSP00000319233; ENSG00000140332.
DR Ensembl; ENST00000451782; ENSP00000394717; ENSG00000140332.
DR Ensembl; ENST00000557907; ENSP00000453107; ENSG00000140332.
DR Ensembl; ENST00000557997; ENSP00000453083; ENSG00000140332.
DR Ensembl; ENST00000558939; ENSP00000452871; ENSG00000140332.
DR Ensembl; ENST00000559048; ENSP00000453760; ENSG00000140332.
DR GeneID; 7090; -.
DR KEGG; hsa:7090; -.
DR UCSC; uc010bil.1; human.
DR CTD; 7090; -.
DR GeneCards; GC15M070341; -.
DR HGNC; HGNC:11839; TLE3.
DR HPA; HPA054116; -.
DR MIM; 600190; gene.
DR neXtProt; NX_Q04726; -.
DR PharmGKB; PA36541; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000293211; -.
DR HOVERGEN; HBG004689; -.
DR InParanoid; Q04726; -.
DR OrthoDB; EOG7HQNC3; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q04726; -.
DR GeneWiki; TLE3; -.
DR GenomeRNAi; 7090; -.
DR NextBio; 27731; -.
DR PRO; PR:Q04726; -.
DR ArrayExpress; Q04726; -.
DR Bgee; Q04726; -.
DR CleanEx; HS_TLE3; -.
DR Genevestigator; Q04726; -.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor 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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 5.
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; Complete proteome;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1 772 Transducin-like enhancer protein 3.
FT /FTId=PRO_0000051280.
FT REPEAT 484 522 WD 1.
FT REPEAT 530 569 WD 2.
FT REPEAT 574 613 WD 3.
FT REPEAT 616 655 WD 4.
FT REPEAT 657 696 WD 5.
FT REPEAT 698 737 WD 6.
FT REPEAT 739 771 WD 7.
FT REGION 199 268 CCN domain.
FT MOTIF 225 228 Nuclear localization signal (Potential).
FT COMPBIAS 1 131 Gln-rich.
FT COMPBIAS 132 198 Gly/Pro-rich.
FT COMPBIAS 269 451 Pro/Ser-rich.
FT COMPBIAS 401 409 Poly-Ala.
FT MOD_RES 203 203 Phosphoserine.
FT MOD_RES 207 207 Phosphoserine.
FT MOD_RES 217 217 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 259 259 Phosphothreonine.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 267 267 Phosphoserine.
FT MOD_RES 286 286 Phosphoserine.
FT MOD_RES 312 312 Phosphothreonine.
FT MOD_RES 317 317 Phosphoserine.
FT MOD_RES 319 319 Phosphothreonine.
FT MOD_RES 321 321 Phosphothreonine.
FT MOD_RES 328 328 Phosphothreonine.
FT MOD_RES 334 334 Phosphothreonine.
FT MOD_RES 413 413 Phosphoserine.
FT VAR_SEQ 1 8 MYPQGRHP -> MPPPPPLSCLRGLQ (in isoform
FT 4).
FT /FTId=VSP_007023.
FT VAR_SEQ 127 127 Missing (in isoform 4).
FT /FTId=VSP_007024.
FT VAR_SEQ 342 353 Missing (in isoform 2).
FT /FTId=VSP_006788.
FT VAR_SEQ 351 353 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_006789.
FT VAR_SEQ 417 421 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_006790.
FT VARIANT 229 229 A -> V (in dbSNP:rs1057864).
FT /FTId=VAR_053421.
FT CONFLICT 409 409 A -> T (in Ref. 5; AAH41831).
FT CONFLICT 487 487 E -> G (in Ref. 1; AAA61194).
FT CONFLICT 498 498 T -> S (in Ref. 1; AAA61194).
FT CONFLICT 535 535 I -> M (in Ref. 1; AAA61194).
FT CONFLICT 541 541 L -> H (in Ref. 1; AAA61194).
FT CONFLICT 553 553 A -> G (in Ref. 1; AAA61194).
FT CONFLICT 692 692 D -> H (in Ref. 1; AAA61194).
FT CONFLICT 736 736 F -> S (in Ref. 1; AAA61194).
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
//
MIM
600190
*RECORD*
*FIELD* NO
600190
*FIELD* TI
*600190 TRANSDUCIN-LIKE ENHANCER OF SPLIT 3; TLE3
;;ENHANCER OF SPLIT GROUCHO 3; ESG3
read more*FIELD* TX
DESCRIPTION
The TLE genes are human homologs of the Drosophila 'groucho' gene, a
member of the Notch signaling pathway (see 190198). The Notch signaling
pathway controls cellular interactions important for the specification
of a variety of fates in both invertebrates and vertebrates (summary by
Liu et al., 1996).
CLONING
Miyasaka et al. (1993) reported the cDNA cloning, nucleotide and deduced
amino acid sequencing, and tissue-specific expression of mouse and human
TLE genes. They determined that mouse Esg (enhancer of split groucho),
the homolog of human TLE3, was represented by transcripts of 3.3 kb and
4.0 kb only in testis.
GENE FUNCTION
By a combination of in situ hybridization and immunohistochemical
studies, Liu et al. (1996) showed that TLE1 (600189), TLE2 (601041), and
TLE3 are coexpressed in a number of epithelial tissues. Moreover, they
showed that the expression is elevated in cervical squamous metaplasias
and carcinomas.
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the CUL4 (see
603137)-DDB1 (600045)-ROC1 (RBX1; 603814) complex, including TLE1, TLE2,
and TLE3. Sequence alignment revealed that TLE1 and most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors for the CUL4-DDB1 complex.
MAPPING
By Southern analysis of genomic DNA from human/Chinese hamster somatic
hybrid cell lines, Miyasaka et al. (1993) mapped the TLE3 gene to
chromosome 15.
Richard et al. (1994) presented an integrated physical, expression, and
genetic map of human chromosome 15. By PCR analysis, they concluded that
the TLE3 gene lies in their region II: 15q14-q15.1.
By fluorescence in situ hybridization, Liu et al. (1996) mapped TLE3 to
15q22.
*FIELD* RF
1. Higa, L. A.; Wu, M.; Ye, T.; Kobayashi, R.; Sun, H.; Zhang, H.
: CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
and regulates histone methylation. Nature Cell Biol. 8: 1277-1283,
2006.
2. Liu, Y.; Dehni, G.; Purcell, K. J.; Sokolow, J.; Carcangiu, M.
L.; Artavanis-Tsakonas, S.; Stifani, S.: Epithelial expression and
chromosomal location of human TLE genes: implications for Notch signaling
and neoplasia. Genomics 31: 58-64, 1996.
3. Miyasaka, H.; Choudhury, B. K.; Hou, E. W.; Li, S. S.-L.: Molecular
cloning and expression of mouse and human cDNA encoding AES and ESG
proteins with strong similarity to Drosophila enhancer of split groucho
protein. Europ. J. Biochem. 216: 343-352, 1993.
4. Richard, I.; Broux, O.; Chiannilkulchai, N.; Fougerousse, F.; Allamand,
V.; Bourg, N.; Brenguier, L.; Devaud, C.; Pasturaud, P.; Roudaut,
C.; Lorenzo, F.; Sebastiani-Kabatchis, C.; Schultz, R. A.; Polymeropoulos,
M. H.; Gyapay, G.; Auffray, C.; Beckmann, J. S.: Regional localization
of human chromosome 15 loci. Genomics 23: 619-627, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
*FIELD* CD
Victor A. McKusick: 11/11/1994
*FIELD* ED
mgross: 03/05/2013
carol: 11/29/2012
mark: 2/7/1996
terry: 2/1/1996
carol: 12/14/1994
terry: 11/11/1994
*RECORD*
*FIELD* NO
600190
*FIELD* TI
*600190 TRANSDUCIN-LIKE ENHANCER OF SPLIT 3; TLE3
;;ENHANCER OF SPLIT GROUCHO 3; ESG3
read more*FIELD* TX
DESCRIPTION
The TLE genes are human homologs of the Drosophila 'groucho' gene, a
member of the Notch signaling pathway (see 190198). The Notch signaling
pathway controls cellular interactions important for the specification
of a variety of fates in both invertebrates and vertebrates (summary by
Liu et al., 1996).
CLONING
Miyasaka et al. (1993) reported the cDNA cloning, nucleotide and deduced
amino acid sequencing, and tissue-specific expression of mouse and human
TLE genes. They determined that mouse Esg (enhancer of split groucho),
the homolog of human TLE3, was represented by transcripts of 3.3 kb and
4.0 kb only in testis.
GENE FUNCTION
By a combination of in situ hybridization and immunohistochemical
studies, Liu et al. (1996) showed that TLE1 (600189), TLE2 (601041), and
TLE3 are coexpressed in a number of epithelial tissues. Moreover, they
showed that the expression is elevated in cervical squamous metaplasias
and carcinomas.
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the CUL4 (see
603137)-DDB1 (600045)-ROC1 (RBX1; 603814) complex, including TLE1, TLE2,
and TLE3. Sequence alignment revealed that TLE1 and most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors for the CUL4-DDB1 complex.
MAPPING
By Southern analysis of genomic DNA from human/Chinese hamster somatic
hybrid cell lines, Miyasaka et al. (1993) mapped the TLE3 gene to
chromosome 15.
Richard et al. (1994) presented an integrated physical, expression, and
genetic map of human chromosome 15. By PCR analysis, they concluded that
the TLE3 gene lies in their region II: 15q14-q15.1.
By fluorescence in situ hybridization, Liu et al. (1996) mapped TLE3 to
15q22.
*FIELD* RF
1. Higa, L. A.; Wu, M.; Ye, T.; Kobayashi, R.; Sun, H.; Zhang, H.
: CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
and regulates histone methylation. Nature Cell Biol. 8: 1277-1283,
2006.
2. Liu, Y.; Dehni, G.; Purcell, K. J.; Sokolow, J.; Carcangiu, M.
L.; Artavanis-Tsakonas, S.; Stifani, S.: Epithelial expression and
chromosomal location of human TLE genes: implications for Notch signaling
and neoplasia. Genomics 31: 58-64, 1996.
3. Miyasaka, H.; Choudhury, B. K.; Hou, E. W.; Li, S. S.-L.: Molecular
cloning and expression of mouse and human cDNA encoding AES and ESG
proteins with strong similarity to Drosophila enhancer of split groucho
protein. Europ. J. Biochem. 216: 343-352, 1993.
4. Richard, I.; Broux, O.; Chiannilkulchai, N.; Fougerousse, F.; Allamand,
V.; Bourg, N.; Brenguier, L.; Devaud, C.; Pasturaud, P.; Roudaut,
C.; Lorenzo, F.; Sebastiani-Kabatchis, C.; Schultz, R. A.; Polymeropoulos,
M. H.; Gyapay, G.; Auffray, C.; Beckmann, J. S.: Regional localization
of human chromosome 15 loci. Genomics 23: 619-627, 1994.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
*FIELD* CD
Victor A. McKusick: 11/11/1994
*FIELD* ED
mgross: 03/05/2013
carol: 11/29/2012
mark: 2/7/1996
terry: 2/1/1996
carol: 12/14/1994
terry: 11/11/1994