TEAD4_HUMAN
ID TEAD4_HUMAN Reviewed; 434 AA.
AC Q15561; H0Y308; Q6MZR9; Q8NEV5; Q92883; Q96BK2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcriptional enhancer factor TEF-3;
DE AltName: Full=TEA domain family member 4;
DE Short=TEAD-4;
DE AltName: Full=Transcription factor 13-like 1;
DE AltName: Full=Transcription factor RTEF-1;
GN Name=TEAD4; Synonyms=RTEF1, TCF13L1, TEF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=8921372; DOI=10.1006/geno.1996.0522;
RA Stewart A.F.R., Richard C.W. III, Suzow J., Stephan D., Weremowicz S.,
RA Morton C.C., Adra C.N.;
RT "Cloning of human RTEF-1, a transcriptional enhancer factor-1-related gene
RT preferentially expressed in skeletal muscle: evidence for an ancient
RT multigene family.";
RL Genomics 37:68-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 8-434 (ISOFORM 1).
RX PubMed=8702974; DOI=10.1074/jbc.271.36.21775;
RA Jacquemin P., Hwang J.-J., Martial J.A., Dolle P., Davidson I.;
RT "A novel family of developmentally regulated mammalian transcription
RT factors containing the TEA/ATTS DNA binding domain.";
RL J. Biol. Chem. 271:21775-21785(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-391 (ISOFORM 3).
RA Tsika R.W., Karasseva N.G., Tsika G.L.;
RT "Role of MCAT binding factors during muscle hypertrophy.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, INTERACTION WITH YAP1, AND MUTAGENESIS OF TYR-429.
RX PubMed=18579750; DOI=10.1101/gad.1664408;
RA Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y.,
RA Chinnaiyan A.M., Lai Z.C., Guan K.L.;
RT "TEAD mediates YAP-dependent gene induction and growth control.";
RL Genes Dev. 22:1962-1971(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH WWTR1.
RX PubMed=19324877; DOI=10.1074/jbc.m900843200;
RA Zhang H., Liu C.Y., Zha Z.Y., Zhao B., Yao J., Zhao S., Xiong Y., Lei Q.Y.,
RA Guan K.L.;
RT "TEAD transcription factors mediate the function of TAZ in cell growth and
RT epithelial-mesenchymal transition.";
RL J. Biol. Chem. 284:13355-13362(2009).
RN [10]
RP INTERACTION WITH YAP1, AND MUTAGENESIS OF ASP-266; LYS-297; TRP-299;
RP PHE-337; PHE-373; LEU-380; GLU-391; PHE-393; HIS-427 AND TYR-429.
RX PubMed=20123908; DOI=10.1101/gad.1865310;
RA Chen L., Chan S.W., Zhang X., Walsh M., Lim C.J., Hong W., Song H.;
RT "Structural basis of YAP recognition by TEAD4 in the hippo pathway.";
RL Genes Dev. 24:290-300(2010).
CC -!- FUNCTION: Transcription factor which plays a key role in the Hippo
CC signaling pathway, a pathway involved in organ size control and tumor
CC suppression by restricting proliferation and promoting apoptosis. The
CC core of this pathway is composed of a kinase cascade wherein MST1/MST2,
CC in complex with its regulatory protein SAV1, phosphorylates and
CC activates LATS1/2 in complex with its regulatory protein MOB1, which in
CC turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ.
CC Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby
CC regulating cell proliferation, migration and epithelial mesenchymal
CC transition (EMT) induction. Binds specifically and non-cooperatively to
CC the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates
CC transcription. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750,
CC ECO:0000269|PubMed:19324877}.
CC -!- SUBUNIT: Interacts with YAP1 and WWTR1/TAZ.
CC {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877,
CC ECO:0000269|PubMed:20123908}.
CC -!- INTERACTION:
CC Q15561; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-747736, EBI-11977221;
CC Q15561; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-747736, EBI-2548868;
CC Q15561; Q01850: CDR2; NbExp=3; IntAct=EBI-747736, EBI-1181367;
CC Q15561; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-747736, EBI-747776;
CC Q15561; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-747736, EBI-740680;
CC Q15561; Q08379: GOLGA2; NbExp=6; IntAct=EBI-747736, EBI-618309;
CC Q15561; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-747736, EBI-5916454;
CC Q15561; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-747736, EBI-2514791;
CC Q15561; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-747736, EBI-10172004;
CC Q15561; Q0VD86: INCA1; NbExp=3; IntAct=EBI-747736, EBI-6509505;
CC Q15561; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-747736, EBI-3044087;
CC Q15561; Q15323: KRT31; NbExp=3; IntAct=EBI-747736, EBI-948001;
CC Q15561; Q6A162: KRT40; NbExp=6; IntAct=EBI-747736, EBI-10171697;
CC Q15561; O95751: LDOC1; NbExp=3; IntAct=EBI-747736, EBI-740738;
CC Q15561; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-747736, EBI-741037;
CC Q15561; Q5JR59-3: MTUS2; NbExp=6; IntAct=EBI-747736, EBI-11522433;
CC Q15561; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-747736, EBI-302345;
CC Q15561; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-747736, EBI-3957793;
CC Q15561; P31321: PRKAR1B; NbExp=3; IntAct=EBI-747736, EBI-2805516;
CC Q15561; A6NK89: RASSF10; NbExp=3; IntAct=EBI-747736, EBI-6912267;
CC Q15561; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-747736, EBI-11957366;
CC Q15561; Q01196-8: RUNX1; NbExp=5; IntAct=EBI-747736, EBI-12001422;
CC Q15561; P21673: SAT1; NbExp=3; IntAct=EBI-747736, EBI-711613;
CC Q15561; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-747736, EBI-6117072;
CC Q15561; O60504: SORBS3; NbExp=3; IntAct=EBI-747736, EBI-741237;
CC Q15561; Q08117-2: TLE5; NbExp=3; IntAct=EBI-747736, EBI-11741437;
CC Q15561; Q13077: TRAF1; NbExp=6; IntAct=EBI-747736, EBI-359224;
CC Q15561; P14373: TRIM27; NbExp=6; IntAct=EBI-747736, EBI-719493;
CC Q15561; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-747736, EBI-2130429;
CC Q15561; Q99990: VGLL1; NbExp=3; IntAct=EBI-747736, EBI-11983165;
CC Q15561; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-747736, EBI-11957216;
CC Q15561; Q14135: VGLL4; NbExp=3; IntAct=EBI-747736, EBI-5278589;
CC Q15561; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-747736, EBI-2799833;
CC Q15561; Q9NP79: VTA1; NbExp=4; IntAct=EBI-747736, EBI-740160;
CC Q15561; Q9GZV5: WWTR1; NbExp=9; IntAct=EBI-747736, EBI-747743;
CC Q15561; P46937: YAP1; NbExp=10; IntAct=EBI-747736, EBI-1044059;
CC Q15561; Q80V24: Vgll4; Xeno; NbExp=3; IntAct=EBI-747736, EBI-9253433;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15561-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15561-2; Sequence=VSP_043099;
CC Name=3;
CC IsoId=Q15561-3; Sequence=VSP_045657;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in skeletal muscle. Lower
CC levels in pancreas, placenta, and heart.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64212.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
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DR EMBL; U63824; AAC50763.1; -; mRNA.
DR EMBL; BX640921; CAE45959.1; -; mRNA.
DR EMBL; AC005911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88872.1; -; Genomic_DNA.
DR EMBL; BC015497; AAH15497.2; -; mRNA.
DR EMBL; X94438; CAA64212.2; ALT_SEQ; mRNA.
DR EMBL; AY101179; AAM89497.1; -; mRNA.
DR CCDS; CCDS31729.1; -. [Q15561-1]
DR CCDS; CCDS31730.1; -. [Q15561-3]
DR CCDS; CCDS41737.1; -. [Q15561-2]
DR RefSeq; NP_003204.2; NM_003213.3. [Q15561-1]
DR RefSeq; NP_958849.1; NM_201441.2. [Q15561-3]
DR RefSeq; NP_958851.1; NM_201443.2. [Q15561-2]
DR PDB; 5GZB; X-ray; 2.70 A; A=36-139.
DR PDB; 5NO6; X-ray; 2.88 A; I/N=40-112.
DR PDB; 5OAQ; X-ray; 1.95 A; A=217-434.
DR PDB; 6GE3; X-ray; 1.85 A; A=216-434.
DR PDB; 6GE4; X-ray; 1.97 A; A=216-434.
DR PDB; 6GE5; X-ray; 2.05 A; A=216-434.
DR PDB; 6GE6; X-ray; 1.80 A; A=216-434.
DR PDB; 6GEC; X-ray; 1.70 A; A=216-434.
DR PDB; 6GEE; X-ray; 1.96 A; A=216-434.
DR PDB; 6GEG; X-ray; 2.23 A; A=216-434.
DR PDB; 6GEI; X-ray; 1.65 A; A=216-434.
DR PDB; 6GEK; X-ray; 2.28 A; A/B=216-434.
DR PDB; 6HIK; X-ray; 1.65 A; A=216-434.
DR PDB; 6Q2X; X-ray; 2.10 A; A=217-434.
DR PDB; 6Q36; X-ray; 2.01 A; A/B=217-434.
DR PDB; 6SEN; X-ray; 1.65 A; A/B=217-434.
DR PDB; 6SEO; X-ray; 2.55 A; A=217-434.
DR PDBsum; 5GZB; -.
DR PDBsum; 5NO6; -.
DR PDBsum; 5OAQ; -.
DR PDBsum; 6GE3; -.
DR PDBsum; 6GE4; -.
DR PDBsum; 6GE5; -.
DR PDBsum; 6GE6; -.
DR PDBsum; 6GEC; -.
DR PDBsum; 6GEE; -.
DR PDBsum; 6GEG; -.
DR PDBsum; 6GEI; -.
DR PDBsum; 6GEK; -.
DR PDBsum; 6HIK; -.
DR PDBsum; 6Q2X; -.
DR PDBsum; 6Q36; -.
DR PDBsum; 6SEN; -.
DR PDBsum; 6SEO; -.
DR AlphaFoldDB; Q15561; -.
DR SMR; Q15561; -.
DR BioGRID; 112863; 71.
DR DIP; DIP-61626N; -.
DR IntAct; Q15561; 48.
DR MINT; Q15561; -.
DR STRING; 9606.ENSP00000352926; -.
DR BindingDB; Q15561; -.
DR ChEMBL; CHEMBL4295828; -.
DR iPTMnet; Q15561; -.
DR PhosphoSitePlus; Q15561; -.
DR SwissPalm; Q15561; -.
DR BioMuta; TEAD4; -.
DR EPD; Q15561; -.
DR jPOST; Q15561; -.
DR MassIVE; Q15561; -.
DR MaxQB; Q15561; -.
DR PaxDb; Q15561; -.
DR PeptideAtlas; Q15561; -.
DR PRIDE; Q15561; -.
DR ProteomicsDB; 34410; -.
DR ProteomicsDB; 60634; -. [Q15561-1]
DR ProteomicsDB; 60635; -. [Q15561-2]
DR Antibodypedia; 22199; 283 antibodies from 30 providers.
DR DNASU; 7004; -.
DR Ensembl; ENST00000358409.7; ENSP00000351184.3; ENSG00000197905.10. [Q15561-3]
DR Ensembl; ENST00000359864.8; ENSP00000352926.3; ENSG00000197905.10. [Q15561-1]
DR Ensembl; ENST00000397122.6; ENSP00000380311.2; ENSG00000197905.10. [Q15561-2]
DR GeneID; 7004; -.
DR KEGG; hsa:7004; -.
DR MANE-Select; ENST00000359864.8; ENSP00000352926.3; NM_003213.4; NP_003204.2.
DR UCSC; uc001qln.4; human. [Q15561-1]
DR CTD; 7004; -.
DR DisGeNET; 7004; -.
DR GeneCards; TEAD4; -.
DR HGNC; HGNC:11717; TEAD4.
DR HPA; ENSG00000197905; Tissue enhanced (skeletal).
DR MIM; 601714; gene.
DR neXtProt; NX_Q15561; -.
DR OpenTargets; ENSG00000197905; -.
DR PharmGKB; PA36435; -.
DR VEuPathDB; HostDB:ENSG00000197905; -.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR HOGENOM; CLU_012515_0_0_1; -.
DR InParanoid; Q15561; -.
DR OMA; AISGFWQ; -.
DR OrthoDB; 823827at2759; -.
DR PhylomeDB; Q15561; -.
DR PathwayCommons; Q15561; -.
DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR SignaLink; Q15561; -.
DR SIGNOR; Q15561; -.
DR BioGRID-ORCS; 7004; 54 hits in 1100 CRISPR screens.
DR ChiTaRS; TEAD4; human.
DR GeneWiki; TEAD4; -.
DR GenomeRNAi; 7004; -.
DR Pharos; Q15561; Tchem.
DR PRO; PR:Q15561; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15561; protein.
DR Bgee; ENSG00000197905; Expressed in hindlimb stylopod muscle and 153 other tissues.
DR ExpressionAtlas; Q15561; baseline and differential.
DR Genevisible; Q15561; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001830; P:trophectodermal cell fate commitment; IEA:Ensembl.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR InterPro; IPR027255; TEF-3.
DR InterPro; IPR016361; TEF_metazoa.
DR InterPro; IPR041086; YBD.
DR Pfam; PF01285; TEA; 1.
DR Pfam; PF17725; YBD; 1.
DR PIRSF; PIRSF002603; TEF; 1.
DR PIRSF; PIRSF500722; TEF-3; 1.
DR PRINTS; PR00065; TEADOMAIN.
DR SMART; SM00426; TEA; 1.
DR PROSITE; PS00554; TEA_1; 1.
DR PROSITE; PS51088; TEA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..434
FT /note="Transcriptional enhancer factor TEF-3"
FT /id="PRO_0000205937"
FT DNA_BIND 36..112
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_043099"
FT VAR_SEQ 119..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_045657"
FT VARIANT 323
FT /note="P -> S (in dbSNP:rs11550887)"
FT /id="VAR_052279"
FT MUTAGEN 266
FT /note="D->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 297
FT /note="K->A: Important loss of interaction with YAP1 and
FT complete loss of transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 299
FT /note="W->A: Important loss of interaction with YAP1 and
FT complete loss of transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 337
FT /note="F->A: Reduced interaction with YAP1."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 373
FT /note="F->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 380
FT /note="L->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 391
FT /note="E->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 393
FT /note="F->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 427
FT /note="H->A: Reduced transforming ability."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 429
FT /note="Y->A,H: Loss of interaction with YAP1 and also
FT activation by YAP1."
FT /evidence="ECO:0000269|PubMed:18579750,
FT ECO:0000269|PubMed:20123908"
FT MUTAGEN 429
FT /note="Y->A: Important loss of interaction with YAP1 and
FT complete loss of transforming ability."
FT /evidence="ECO:0000269|PubMed:18579750,
FT ECO:0000269|PubMed:20123908"
FT CONFLICT 39
FT /note="A -> G (in Ref. 1; AAC50763)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> R (in Ref. 1; AAC50763)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="G -> E (in Ref. 1; AAC50763)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..220
FT /note="SVA -> RRG (in Ref. 1; AAC50763)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="SD -> LR (in Ref. 1; AAC50763)"
FT /evidence="ECO:0000305"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5GZB"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:5NO6"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:5GZB"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:5GZB"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5GZB"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:5GZB"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6SEO"
FT STRAND 225..238
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 241..254
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6Q36"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 312..324
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 327..336
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 356..365
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 368..378
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6HIK"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:6GEI"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 407..417
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6GEK"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:6GEI"
SQ SEQUENCE 434 AA; 48329 MW; 544DDFD86E88D9A8 CRC64;
MEGTAGTITS NEWSSPTSPE GSTASGGSQA LDKPIDNDAE GVWSPDIEQS FQEALAIYPP
CGRRKIILSD EGKMYGRNEL IARYIKLRTG KTRTRKQVSS HIQVLARRKA REIQAKLKDQ
AAKDKALQSM AAMSSAQIIS ATAFHSSMAL ARGPGRPAVS GFWQGALPGQ AGTSHDVKPF
SQQTYAVQPP LPLPGFESPA GPAPSPSAPP APPWQGRSVA SSKLWMLEFS AFLEQQQDPD
TYNKHLFVHI GQSSPSYSDP YLEAVDIRQI YDKFPEKKGG LKDLFERGPS NAFFLVKFWA
DLNTNIEDEG SSFYGVSSQY ESPENMIITC STKVCSFGKQ VVEKVETEYA RYENGHYSYR
IHRSPLCEYM INFIHKLKHL PEKYMMNSVL ENFTILQVVT NRDTQETLLC IAYVFEVSAS
EHGAQHHIYR LVKE
