ID TEAD2_HUMAN Reviewed; 447 AA. AC Q15562; B4DTJ6; M0R1T9; Q8NA25; Q96IG3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 11-NOV-2015, entry version 141. DE RecName: Full=Transcriptional enhancer factor TEF-4; DE AltName: Full=TEA domain family member 2; DE Short=TEAD-2; GN Name=TEAD2; Synonyms=TEF4; 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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Placenta, and Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Eye, and Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-367. RC TISSUE=Brain; 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 [6] RP FUNCTION, AND INTERACTION WITH YAP1. 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., RA Wang C.Y., 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH RP 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., RA Lei Q.Y., Guan K.L.; RT "TEAD transcription factors mediate the function of TAZ in cell growth RT and epithelial-mesenchymal transition."; RL J. Biol. Chem. 284:13355-13362(2009). CC -!- FUNCTION: Transcription factor which plays a key role in the Hippo CC signaling pathway, a pathway involved in organ size control and CC tumor suppression by restricting proliferation and promoting CC apoptosis. The core of this pathway is composed of a kinase CC cascade wherein MST1/MST2, in complex with its regulatory protein CC SAV1, phosphorylates and activates LATS1/2 in complex with its CC regulatory protein MOB1, which in turn phosphorylates and CC inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene CC expression of YAP1 and WWTR1/TAZ, thereby regulating cell CC proliferation, migration and epithelial mesenchymal transition CC (EMT) induction. Binds to the SPH and GT-IIC 'enhansons' (5'- CC GTGGAATGT-3'). May be involved in the gene regulation of neural CC development. Binds to the M-CAT motif. CC {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. CC -!- SUBUNIT: Interacts with YAP1 and WWTR1/TAZ. CC {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}. CC -!- INTERACTION: CC Q5TBC7:BCL2L15; NbExp=4; IntAct=EBI-6427252, EBI-10247136; CC Q15853:USF2; NbExp=3; IntAct=EBI-6427252, EBI-1055994; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q15562-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15562-2; Sequence=VSP_045127; CC Name=3; CC IsoId=Q15562-3; Sequence=VSP_045126, VSP_045127; CC Name=4; CC IsoId=Q15562-4; Sequence=VSP_055673; CC Note=No experimental confirmation available.; CC -!- SIMILARITY: Contains 1 TEA DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00505}. 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; AK093236; BAC04104.1; -; mRNA. DR EMBL; AK290736; BAF83425.1; -; mRNA. DR EMBL; AK300241; BAG62008.1; -; mRNA. DR EMBL; AC010524; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471177; EAW52469.1; -; Genomic_DNA. DR EMBL; BC051301; AAH51301.1; -; mRNA. DR EMBL; BC007556; AAH07556.1; -; mRNA. DR EMBL; BC018803; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X94440; CAA64214.1; -; mRNA. DR CCDS; CCDS12761.1; -. [Q15562-1] DR CCDS; CCDS58670.1; -. [Q15562-3] DR CCDS; CCDS58671.1; -. [Q15562-2] DR CCDS; CCDS59406.1; -. [Q15562-4] DR PIR; G01116; G01116. DR RefSeq; NP_001243587.1; NM_001256658.1. [Q15562-2] DR RefSeq; NP_001243588.1; NM_001256659.1. [Q15562-2] DR RefSeq; NP_001243589.1; NM_001256660.1. [Q15562-4] DR RefSeq; NP_001243590.1; NM_001256661.1. [Q15562-4] DR RefSeq; NP_001243591.1; NM_001256662.1. [Q15562-3] DR RefSeq; NP_003589.1; NM_003598.1. [Q15562-1] DR RefSeq; XP_006723487.1; XM_006723424.1. [Q15562-4] DR RefSeq; XP_011525705.1; XM_011527403.1. [Q15562-2] DR UniGene; Hs.515534; -. DR PDB; 3L15; X-ray; 2.00 A; A/B=217-447. DR PDBsum; 3L15; -. DR ProteinModelPortal; Q15562; -. DR SMR; Q15562; 40-115, 221-446. DR BioGrid; 114041; 17. DR DIP; DIP-59318N; -. DR IntAct; Q15562; 4. DR STRING; 9606.ENSP00000310701; -. DR PhosphoSite; Q15562; -. DR BioMuta; TEAD2; -. DR DMDM; 21264529; -. DR MaxQB; Q15562; -. DR PaxDb; Q15562; -. DR PRIDE; Q15562; -. DR DNASU; 8463; -. DR Ensembl; ENST00000311227; ENSP00000310701; ENSG00000074219. [Q15562-1] DR Ensembl; ENST00000377214; ENSP00000366419; ENSG00000074219. [Q15562-2] DR Ensembl; ENST00000539846; ENSP00000437928; ENSG00000074219. [Q15562-3] DR Ensembl; ENST00000593945; ENSP00000469640; ENSG00000074219. [Q15562-4] DR Ensembl; ENST00000598810; ENSP00000472109; ENSG00000074219. [Q15562-4] DR Ensembl; ENST00000601519; ENSP00000469672; ENSG00000074219. [Q15562-2] DR GeneID; 8463; -. DR KEGG; hsa:8463; -. DR UCSC; uc002png.4; human. DR UCSC; uc002pnh.4; human. [Q15562-1] DR UCSC; uc010yao.3; human. DR CTD; 8463; -. DR GeneCards; TEAD2; -. DR HGNC; HGNC:11715; TEAD2. DR MIM; 601729; gene. DR neXtProt; NX_Q15562; -. DR PharmGKB; PA36433; -. DR eggNOG; KOG3841; Eukaryota. DR eggNOG; ENOG410XQMP; LUCA. DR GeneTree; ENSGT00390000008670; -. DR HOGENOM; HOG000253933; -. DR HOVERGEN; HBG056905; -. DR InParanoid; Q15562; -. DR KO; K09448; -. DR OMA; TPWNVPD; -. DR OrthoDB; EOG7288RP; -. DR PhylomeDB; Q15562; -. DR TreeFam; TF313443; -. DR Reactome; R-HSA-1989781; PPARA activates gene expression. DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression. DR ChiTaRS; TEAD2; human. DR EvolutionaryTrace; Q15562; -. DR GeneWiki; TEAD2; -. DR GenomeRNAi; 8463; -. DR NextBio; 31676; -. DR PRO; PR:Q15562; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; Q15562; -. DR CleanEx; HS_TEAD2; -. DR ExpressionAtlas; Q15562; baseline and differential. DR Genevisible; Q15562; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0005667; C:transcription factor complex; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0035329; P:hippo signaling; IDA:UniProtKB. DR GO; GO:0048368; P:lateral mesoderm development; IEA:Ensembl. DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0030903; P:notochord development; IEA:Ensembl. DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR InterPro; IPR000818; TEA/ATTS. DR InterPro; IPR016361; TEF_metazoa. DR PANTHER; PTHR11834; PTHR11834; 1. DR Pfam; PF01285; TEA; 1. DR PIRSF; PIRSF002603; TEF; 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; Complete proteome; KW DNA-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 447 Transcriptional enhancer factor TEF-4. FT /FTId=PRO_0000205932. FT DNA_BIND 40 107 TEA. {ECO:0000255|PROSITE- FT ProRule:PRU00505}. FT REGION 172 447 Transcriptional activation. FT {ECO:0000255}. FT COMPBIAS 152 216 Pro-rich. FT VAR_SEQ 1 131 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045126. FT VAR_SEQ 120 120 K -> KALNV (in isoform 4). {ECO:0000305}. FT /FTId=VSP_055673. FT VAR_SEQ 155 155 P -> PQVV (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045127. FT CONFLICT 144 144 P -> L (in Ref. 5; CAA64214). FT {ECO:0000305}. FT STRAND 229 238 {ECO:0000244|PDB:3L15}. FT HELIX 240 243 {ECO:0000244|PDB:3L15}. FT STRAND 249 255 {ECO:0000244|PDB:3L15}. FT STRAND 268 270 {ECO:0000244|PDB:3L15}. FT HELIX 271 277 {ECO:0000244|PDB:3L15}. FT HELIX 285 291 {ECO:0000244|PDB:3L15}. FT HELIX 294 296 {ECO:0000244|PDB:3L15}. FT STRAND 297 304 {ECO:0000244|PDB:3L15}. FT STRAND 326 337 {ECO:0000244|PDB:3L15}. FT STRAND 340 349 {ECO:0000244|PDB:3L15}. FT STRAND 352 362 {ECO:0000244|PDB:3L15}. FT STRAND 364 366 {ECO:0000244|PDB:3L15}. FT STRAND 369 378 {ECO:0000244|PDB:3L15}. FT HELIX 381 390 {ECO:0000244|PDB:3L15}. FT HELIX 396 403 {ECO:0000244|PDB:3L15}. FT STRAND 406 414 {ECO:0000244|PDB:3L15}. FT TURN 415 417 {ECO:0000244|PDB:3L15}. FT STRAND 420 430 {ECO:0000244|PDB:3L15}. FT STRAND 433 435 {ECO:0000244|PDB:3L15}. FT STRAND 438 445 {ECO:0000244|PDB:3L15}. SQ SEQUENCE 447 AA; 49243 MW; A9077F55638A3AC7 CRC64; MGEPRAGAAL DDGSGWTGSE EGSEEGTGGS EGAGGDGGPD AEGVWSPDIE QSFQEALAIY PPCGRRKIIL SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARR KSREIQSKLK DQVSKDKAFQ TMATMSSAQL ISAPSLQAKL GPTGPQASEL FQFWSGGSGP PWNVPDVKPF SQTPFTLSLT PPSTDLPGYE PPQALSPLPP PTPSPPAWQA RGLGTARLQL VEFSAFVEPP DAVDSYQRHL FVHISQHCPS PGAPPLESVD VRQIYDKFPE KKGGLRELYD RGPPHAFFLV KFWADLNWGP SGEEAGAGGS ISSGGFYGVS SQYESLEHMT LTCSSKVCSF GKQVVEKVET ERAQLEDGRF VYRLLRSPMC EYLVNFLHKL RQLPERYMMN SVLENFTILQ VVTNRDTQEL LLCTAYVFEV STSERGAQHH IYRLVRD //