YAP1_HUMAN
ID YAP1_HUMAN Reviewed; 504 AA.
AC P46937; B4DTY1; B7ZA01; E3WEB5; E3WEB6; E9PRV2; F5H202; K0KQ18; K0KYZ8;
AC K0L195; K0L1G3; Q7Z574; Q8IUY9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Transcriptional coactivator YAP1;
DE Short=Yes-associated protein 1;
DE AltName: Full=Protein yorkie homolog;
DE AltName: Full=Yes-associated protein YAP65 homolog;
GN Name=YAP1; Synonyms=YAP65;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=7782338; DOI=10.1074/jbc.270.24.14733;
RA Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M.,
RA Huebner K., Lehman D.;
RT "Characterization of the mammalian YAP (Yes-associated protein) gene and
RT its role in defining a novel protein module, the WW domain.";
RL J. Biol. Chem. 270:14733-14741(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ERBB4,
RP AND MUTAGENESIS OF SER-127; TRP-199 AND PRO-202.
RX PubMed=12807903; DOI=10.1074/jbc.m305597200;
RA Komuro A., Nagai M., Navin N.E., Sudol M.;
RT "WW domain-containing protein YAP associates with ErbB-4 and acts as a co-
RT transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that
RT translocates to the nucleus.";
RL J. Biol. Chem. 278:33334-33341(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Esophagus;
RA Inazawa J., Imoto I., Muramatsu T.;
RT "YAP is a candidate oncogene for esophageal squamous-cell carcinoma.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 206-369 (ISOFORMS 3; 7; 8 AND 9), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Pancreas;
RX PubMed=22939869; DOI=10.1016/j.gene.2012.08.025;
RA Gaffney C.J., Oka T., Mazack V., Hilman D., Gat U., Muramatsu T.,
RA Inazawa J., Golden A., Carey D.J., Farooq A., Tromp G., Sudol M.;
RT "Identification, basic characterization and evolutionary analysis of
RT differentially spliced mRNA isoforms of human YAP1 gene.";
RL Gene 509:215-222(2012).
RN [9]
RP INTERACTION WITH WBP1 AND WBP2.
RX PubMed=9202023; DOI=10.1074/jbc.272.27.17070;
RA Chen H.I., Einbond A., Kwak S.-J., Linn H., Koepf E., Peterson S.,
RA Kelly J.W., Sudol M.;
RT "Characterization of the WW domain of human Yes-associated protein and its
RT polyproline containing ligands.";
RL J. Biol. Chem. 272:17070-17077(1997).
RN [10]
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 [11]
RP IDENTIFICATION OF ISOFORMS LACKING THE TRANSCRIPTIONAL ACTIVATION DOMAIN,
RP AND TISSUE SPECIFICITY.
RX PubMed=16461361; DOI=10.1083/jcb.200509132;
RA Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y.,
RA Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M.,
RA Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.;
RT "Transcriptional repression induces a slowly progressive atypical neuronal
RT death associated with changes of YAP isoforms and p73.";
RL J. Cell Biol. 172:589-604(2006).
RN [12]
RP INTERACTION WITH HCK.
RX PubMed=17535448; DOI=10.1186/1471-2199-8-45;
RA Paliwal P., Radha V., Swarup G.;
RT "Regulation of p73 by Hck through kinase-dependent and independent
RT mechanisms.";
RL BMC Mol. Biol. 8:45-45(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT
RP SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122;
RP SER-127 AND PRO-129, AND TISSUE SPECIFICITY.
RX PubMed=17974916; DOI=10.1101/gad.1602907;
RA Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T.,
RA Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C.,
RA Guan K.L.;
RT "Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell
RT contact inhibition and tissue growth control.";
RL Genes Dev. 21:2747-2761(2007).
RN [14]
RP INTERACTION WITH PRRG2.
RX PubMed=17502622; DOI=10.1073/pnas.0703195104;
RA Kulman J.D., Harris J.E., Xie L., Davie E.W.;
RT "Proline-rich Gla protein 2 is a cell-surface vitamin K-dependent protein
RT that binds to the transcriptional coactivator Yes-associated protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8767-8772(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP FUNCTION, INTERACTION WITH TEAD1; TEAD2; TEAD3 AND TEAD4, AND MUTAGENESIS
RP OF SER-94.
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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2,
RP PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, AND
RP MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397.
RX PubMed=18158288; DOI=10.1074/jbc.m709037200;
RA Hao Y., Chun A., Cheung K., Rashidi B., Yang X.;
RT "Tumor suppressor LATS1 is a negative regulator of oncogene YAP.";
RL J. Biol. Chem. 283:5496-5509(2008).
RN [18]
RP FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RUNX1 AND TP73.
RX PubMed=18280240; DOI=10.1016/j.molcel.2007.12.022;
RA Levy D., Adamovich Y., Reuven N., Shaul Y.;
RT "Yap1 phosphorylation by c-Abl is a critical step in selective activation
RT of proapoptotic genes in response to DNA damage.";
RL Mol. Cell 29:350-361(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-127; SER-131;
RP SER-138; THR-154; SER-274; SER-289 AND SER-367, AND IDENTIFICATION BY MASS
RP 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 [20]
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 [21]
RP IDENTIFICATION BY 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 [22]
RP PHOSPHORYLATION AT THR-119; SER-138; THR-154; SER-367 AND THR-412 BY
RP MAPK8/JNK1 AND MAPK9/JNK2, AND FUNCTION.
RX PubMed=21364637; DOI=10.1038/cddis.2010.7;
RA Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S.;
RT "JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis.";
RL Cell Death Dis. 1:E29-E29(2010).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA Larsen B.G., Rossant J., Wrana J.L.;
RT "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT of the TGF-beta-SMAD pathway.";
RL Dev. Cell 19:831-844(2010).
RN [24]
RP PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT
RP SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP),
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-61; SER-109; SER-127 AND
RP SER-164.
RX PubMed=20048001; DOI=10.1101/gad.1843810;
RA Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.;
RT "A coordinated phosphorylation by Lats and CK1 regulates YAP stability
RT through SCF(beta-TRCP).";
RL Genes Dev. 24:72-85(2010).
RN [25]
RP INTERACTION WITH TEAD4, AND MUTAGENESIS OF VAL-80; VAL-84 AND PRO-85.
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).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; THR-63; SER-109; THR-119;
RP SER-138; SER-274; SER-289 AND SER-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
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., Buerckstuemmer T.,
RA 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-289 AND SER-367, AND
RP IDENTIFICATION BY 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 [29]
RP INTERACTION WITH PRRG4, AND MUTAGENESIS OF TRP-199; PRO-202; SER-217;
RP TRP-258 AND PRO-261.
RX PubMed=23873930; DOI=10.1074/jbc.m113.484683;
RA Yazicioglu M.N., Monaldini L., Chu K., Khazi F.R., Murphy S.L., Huang H.,
RA Margaritis P., High K.A.;
RT "Cellular localization and characterization of cytosolic binding partners
RT for Gla domain-containing proteins PRRG4 and PRRG2.";
RL J. Biol. Chem. 288:25908-25914(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-109; THR-119;
RP SER-289; SER-381; SER-382 AND SER-388, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [31]
RP INTERACTION WITH PTPN14, AND SUBCELLULAR LOCATION.
RX PubMed=22525271; DOI=10.1038/onc.2012.147;
RA Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H.,
RA Zhang J.;
RT "PTPN14 interacts with and negatively regulates the oncogenic function of
RT YAP.";
RL Oncogene 32:1266-1273(2013).
RN [32]
RP INVOLVEMENT IN COB1, AND VARIANTS LEU-139; LEU-227; VAL-330 AND GLU-462.
RX PubMed=24462371; DOI=10.1016/j.ajhg.2014.01.001;
RG UK10K Consortium;
RA Williamson K.A., Rainger J., Floyd J.A., Ansari M., Meynert A.,
RA Aldridge K.V., Rainger J.K., Anderson C.A., Moore A.T., Hurles M.E.,
RA Clarke A., van Heyningen V., Verloes A., Taylor M.S., Wilkie A.O.,
RA Fitzpatrick D.R., Hurles M., FitzPatrick D.R., Al-Turki S., Anderson C.,
RA Barroso I., Beales P., Bentham J., Bhattacharya S., Carss K.,
RA Chatterjee K., Cirak S., Cosgrove C., Daly A., Floyd J., Franklin C.,
RA Futema M., Humphries S., McCarthy S., Mitchison H., Muntoni F.,
RA Onoufriadis A., Parker V., Payne F., Plagnol V., Raymond L., Savage D.,
RA Scambler P., Schmidts M., Semple R., Serra E., Stalker J.,
RA van Kogelenberg M., Vijayarangakannan P., Walter K., Wood G.;
RT "Heterozygous loss-of-function mutations in YAP1 cause both isolated and
RT syndromic optic fissure closure defects.";
RL Am. J. Hum. Genet. 94:295-302(2014).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-131, AND
RP IDENTIFICATION BY 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).
RN [34]
RP FUNCTION.
RX PubMed=25778702; DOI=10.1038/nature14215;
RA Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H.,
RA Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S.,
RA Miesfeld J.B., Link B.A., Senga T., Castillo-Morales A., Urrutia A.O.,
RA Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H.,
RA Heisenberg C.P., Furutani-Seiki M.;
RT "YAP is essential for tissue tension to ensure vertebrate 3D body shape.";
RL Nature 521:217-221(2015).
RN [35]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-94.
RX PubMed=25849865; DOI=10.1038/ncomms7781;
RA Kim J., Jo H., Hong H., Kim M.H., Kim J.M., Lee J.K., Heo W.D., Kim J.;
RT "Actin remodelling factors control ciliogenesis by regulating YAP/TAZ
RT activity and vesicle trafficking.";
RL Nat. Commun. 6:6781-6781(2015).
RN [36]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-127 AND SER-397.
RX PubMed=28169360; DOI=10.1038/srep42125;
RA Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C., Wang R.,
RA Chen H., Zhou C., Zhang J., Yang J., Liu P.;
RT "Loss of DLG5 promotes breast cancer malignancy by inhibiting the Hippo
RT signaling pathway.";
RL Sci. Rep. 7:42125-42125(2017).
RN [37]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30447097; DOI=10.1111/cas.13884;
RA Amisaki M., Tsuchiya H., Sakabe T., Fujiwara Y., Shiota G.;
RT "Identification of genes involved in the regulation of TERT in
RT hepatocellular carcinoma.";
RL Cancer Sci. 110:550-560(2019).
RN [38]
RP STRUCTURE BY NMR OF 165-210 OF WILD-TYPE AND MUTANT LYS-190 IN COMPLEX WITH
RP PRO-RICH PEPTIDES.
RX PubMed=11743730; DOI=10.1006/jmbi.2000.5199;
RA Pires J.R., Taha-Nejad F., Toepert F., Ast T., Hoffmueller U.,
RA Schneider-Mergener J., Kuehne R., Macias M.J., Oschkinat H.;
RT "Solution structures of the YAP65 WW domain and the variant L30 K in
RT complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the
RT application of peptide libraries reveal a minimal binding epitope.";
RL J. Mol. Biol. 314:1147-1156(2001).
RN [39]
RP STRUCTURE BY NMR OF 165-204.
RX PubMed=11687614; DOI=10.1073/pnas.221467398;
RA Ferguson N., Pires J.R., Toepert F., Johnson C.M., Pan Y.P.,
RA Volkmer-Engert R., Schneider-Mergener J., Daggett V., Oschkinat H.,
RA Fersht A.;
RT "Using flexible loop mimetics to extend phi-value analysis to secondary
RT structure interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13008-13013(2001).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 50-171 IN COMPLEX WITH TEAD1,
RP COILED-COIL REGION, INTERACTION WITH TEAD1, AND MUTAGENESIS OF MET-86;
RP ARG-89; LEU-91; SER-94; PHE-95 AND PHE-96.
RX PubMed=20123905; DOI=10.1101/gad.1865810;
RA Li Z., Zhao B., Wang P., Chen F., Dong Z., Yang H., Guan K.L., Xu Y.;
RT "Structural insights into the YAP and TEAD complex.";
RL Genes Dev. 24:235-240(2010).
CC -!- FUNCTION: Transcriptional regulator which can act both as a coactivator
CC and a corepressor and is the critical downstream regulatory target in
CC the Hippo signaling pathway that plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750,
CC PubMed:21364637, PubMed:30447097). The core of this pathway is composed
CC of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with
CC its regulatory protein SAV1, phosphorylates and activates LATS1/2 in
CC complex with its regulatory protein MOB1, which in turn phosphorylates
CC and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays
CC a key role in tissue tension and 3D tissue shape by regulating cortical
CC actomyosin network formation. Acts via ARHGAP18, a Rho GTPase
CC activating protein that suppresses F-actin polymerization
CC (PubMed:25778702). Plays a key role in controlling cell proliferation
CC in response to cell contact. Phosphorylation of YAP1 by LATS1/2
CC inhibits its translocation into the nucleus to regulate cellular genes
CC important for cell proliferation, cell death, and cell migration
CC (PubMed:18158288). The presence of TEAD transcription factors are
CC required for it to stimulate gene expression, cell growth, anchorage-
CC independent growth, and epithelial mesenchymal transition (EMT)
CC induction (PubMed:18579750). Suppresses ciliogenesis via acting as a
CC transcriptional corepressor of the TEAD4 target genes AURKA and PLK1
CC (PubMed:25849865). In conjunction with WWTR1, involved in the
CC regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By
CC similarity). {ECO:0000250|UniProtKB:P46938,
CC ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288,
CC ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:18579750,
CC ECO:0000269|PubMed:21364637, ECO:0000269|PubMed:25778702,
CC ECO:0000269|PubMed:25849865, ECO:0000269|PubMed:30447097}.
CC -!- FUNCTION: [Isoform 2]: Activates the C-terminal fragment (CTF) of ERBB4
CC (isoform 3). {ECO:0000269|PubMed:12807903}.
CC -!- FUNCTION: [Isoform 3]: Activates the C-terminal fragment (CTF) of ERBB4
CC (isoform 3). {ECO:0000269|PubMed:12807903}.
CC -!- SUBUNIT: Binds to the SH3 domain of the YES kinase. Binds to WBP1 and
CC WBP2 (PubMed:9202023). Binds, in vitro, through the WW1 domain, to
CC neural isoforms of ENAH that contain the PPSY motif (By similarity).
CC The phosphorylated form interacts with YWHAB (PubMed:17974916).
CC Interacts (via WW domains) with LATS1 (via PPxY motif 2)
CC (PubMed:18158288). Interacts with LATS2 (PubMed:18158288). Interacts
CC with TEAD1, TEAD2, TEAD3 and TEAD4 (PubMed:18579750, PubMed:20123905,
CC PubMed:20123908). Interacts with TP73 (PubMed:18280240). Interacts with
CC RUNX1 (PubMed:18280240). Interacts with HCK (PubMed:17535448).
CC Interacts (via WW domains) with PTPN14 (via PPxY motif 2); this
CC interaction leads to the cytoplasmic sequestration of YAP1 and inhibits
CC its transcriptional coactivator activity (PubMed:22525271). Interacts
CC (when phosphorylated at Ser-127) with SMAD2, SMAD3 and WWTR1 (By
CC similarity). Interacts with PRRG2 (via cytoplasmic domain)
CC (PubMed:17502622). Interacts (via WW domains) with PRRG4 (via
CC cytoplasmic domain) (PubMed:23873930). {ECO:0000250|UniProtKB:P46938,
CC ECO:0000269|PubMed:12807903, ECO:0000269|PubMed:17502622,
CC ECO:0000269|PubMed:17535448, ECO:0000269|PubMed:17974916,
CC ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:18280240,
CC ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:20123905,
CC ECO:0000269|PubMed:20123908, ECO:0000269|PubMed:22525271,
CC ECO:0000269|PubMed:23873930, ECO:0000269|PubMed:9202023}.
CC -!- SUBUNIT: [Isoform 3]: Interacts (via WW domain 1) with isoform 3 of
CC ERBB4 (via PPxY motif 2). {ECO:0000269|PubMed:12807903}.
CC -!- SUBUNIT: [Isoform 2]: Interacts (via WW domain 1) with isoform 3 of
CC ERBB4 (via PPxY motif 2). {ECO:0000269|PubMed:12807903}.
CC -!- INTERACTION:
CC P46937; Q68CP9: ARID2; NbExp=2; IntAct=EBI-1044059, EBI-637818;
CC P46937; P54259: ATN1; NbExp=2; IntAct=EBI-1044059, EBI-945980;
CC P46937; O15169: AXIN1; NbExp=11; IntAct=EBI-1044059, EBI-710484;
CC P46937; Q9H305: CDIP1; NbExp=2; IntAct=EBI-1044059, EBI-2876678;
CC P46937; P35222: CTNNB1; NbExp=13; IntAct=EBI-1044059, EBI-491549;
CC P46937; Q92841: DDX17; NbExp=7; IntAct=EBI-1044059, EBI-746012;
CC P46937; P11161: EGR2; NbExp=2; IntAct=EBI-1044059, EBI-625282;
CC P46937; Q15303: ERBB4; NbExp=4; IntAct=EBI-1044059, EBI-80371;
CC P46937; Q8NEA6: GLIS3; NbExp=2; IntAct=EBI-1044059, EBI-744456;
CC P46937; Q13887: KLF5; NbExp=2; IntAct=EBI-1044059, EBI-2696013;
CC P46937; O95835: LATS1; NbExp=10; IntAct=EBI-1044059, EBI-444209;
CC P46937; Q86YD5: LDLRAD3; NbExp=2; IntAct=EBI-1044059, EBI-30833221;
CC P46937; Q99732: LITAF; NbExp=2; IntAct=EBI-1044059, EBI-725647;
CC P46937; Q02750: MAP2K1; NbExp=3; IntAct=EBI-1044059, EBI-492564;
CC P46937; Q9NV92: NDFIP2; NbExp=2; IntAct=EBI-1044059, EBI-2933200;
CC P46937; Q8NI35: PATJ; NbExp=5; IntAct=EBI-1044059, EBI-724390;
CC P46937; P23759: PAX7; NbExp=2; IntAct=EBI-1044059, EBI-1042757;
CC P46937; Q9NR12: PDLIM7; NbExp=2; IntAct=EBI-1044059, EBI-350517;
CC P46937; Q13131: PRKAA1; NbExp=3; IntAct=EBI-1044059, EBI-1181405;
CC P46937; O14669: PRRG2; NbExp=6; IntAct=EBI-1044059, EBI-9824765;
CC P46937; Q9BZD6: PRRG4; NbExp=2; IntAct=EBI-1044059, EBI-3918643;
CC P46937; Q13635: PTCH1; NbExp=4; IntAct=EBI-1044059, EBI-8775406;
CC P46937; Q15678: PTPN14; NbExp=7; IntAct=EBI-1044059, EBI-1237156;
CC P46937; P62491: RAB11A; NbExp=2; IntAct=EBI-1044059, EBI-745098;
CC P46937; Q8TEU7: RAPGEF6; NbExp=2; IntAct=EBI-1044059, EBI-2693017;
CC P46937; Q7Z6E9: RBBP6; NbExp=2; IntAct=EBI-1044059, EBI-2117026;
CC P46937; Q01196: RUNX1; NbExp=3; IntAct=EBI-1044059, EBI-925904;
CC P46937; Q14160: SCRIB; NbExp=2; IntAct=EBI-1044059, EBI-357345;
CC P46937; Q15599: SLC9A3R2; NbExp=4; IntAct=EBI-1044059, EBI-1149760;
CC P46937; Q15797: SMAD1; NbExp=4; IntAct=EBI-1044059, EBI-1567153;
CC P46937; O15105: SMAD7; NbExp=7; IntAct=EBI-1044059, EBI-3861591;
CC P46937; O14544: SOCS6; NbExp=2; IntAct=EBI-1044059, EBI-3929549;
CC P46937; Q99593: TBX5; NbExp=4; IntAct=EBI-1044059, EBI-297043;
CC P46937; P28347: TEAD1; NbExp=11; IntAct=EBI-1044059, EBI-529156;
CC P46937; Q15562: TEAD2; NbExp=6; IntAct=EBI-1044059, EBI-6427252;
CC P46937; Q15562-2: TEAD2; NbExp=3; IntAct=EBI-1044059, EBI-9370956;
CC P46937; Q15561: TEAD4; NbExp=10; IntAct=EBI-1044059, EBI-747736;
CC P46937; Q8IV31: TMEM139; NbExp=2; IntAct=EBI-1044059, EBI-7238458;
CC P46937; Q8N4L1: TMEM151A; NbExp=2; IntAct=EBI-1044059, EBI-25600031;
CC P46937; O15417: TNRC18; NbExp=3; IntAct=EBI-1044059, EBI-2824620;
CC P46937; Q13625: TP53BP2; NbExp=6; IntAct=EBI-1044059, EBI-77642;
CC P46937; Q13625-2: TP53BP2; NbExp=9; IntAct=EBI-1044059, EBI-287091;
CC P46937; Q9H3D4: TP63; NbExp=2; IntAct=EBI-1044059, EBI-2337775;
CC P46937; O15350: TP73; NbExp=4; IntAct=EBI-1044059, EBI-389606;
CC P46937; O15350-1: TP73; NbExp=7; IntAct=EBI-1044059, EBI-389619;
CC P46937; Q96PN7: TRERF1; NbExp=2; IntAct=EBI-1044059, EBI-3505166;
CC P46937; Q9NRJ4: TULP4; NbExp=2; IntAct=EBI-1044059, EBI-1753487;
CC P46937; Q96G27: WBP1; NbExp=4; IntAct=EBI-1044059, EBI-3867685;
CC P46937; Q969T9: WBP2; NbExp=8; IntAct=EBI-1044059, EBI-727055;
CC P46937; P31946: YWHAB; NbExp=6; IntAct=EBI-1044059, EBI-359815;
CC P46937; P62258: YWHAE; NbExp=5; IntAct=EBI-1044059, EBI-356498;
CC P46937; P63104: YWHAZ; NbExp=9; IntAct=EBI-1044059, EBI-347088;
CC P46937; Q96JG9: ZNF469; NbExp=2; IntAct=EBI-1044059, EBI-12503573;
CC P46937; O35625: Axin1; Xeno; NbExp=3; IntAct=EBI-1044059, EBI-2365912;
CC P46937; Q5EG47: Prkaa1; Xeno; NbExp=2; IntAct=EBI-1044059, EBI-7282395;
CC P46937; P97764: Wbp1; Xeno; NbExp=13; IntAct=EBI-1044059, EBI-6304160;
CC P46937-1; Q9BZD6: PRRG4; NbExp=2; IntAct=EBI-26604877, EBI-3918643;
CC P46937-3; P35222: CTNNB1; NbExp=2; IntAct=EBI-6558686, EBI-491549;
CC P46937-3; Q9BZD6: PRRG4; NbExp=3; IntAct=EBI-6558686, EBI-3918643;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18158288,
CC ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:20048001,
CC ECO:0000269|PubMed:22525271, ECO:0000269|PubMed:25849865}. Nucleus
CC {ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288,
CC ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:20048001,
CC ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:22525271,
CC ECO:0000269|PubMed:25849865, ECO:0000269|PubMed:28169360,
CC ECO:0000269|PubMed:30447097}. Note=Both phosphorylation and cell
CC density can regulate its subcellular localization (PubMed:18158288,
CC PubMed:20048001). Phosphorylation sequesters it in the cytoplasm by
CC inhibiting its translocation into the nucleus (PubMed:18158288,
CC PubMed:20048001). At low density, predominantly nuclear and is
CC translocated to the cytoplasm at high density (PubMed:18158288,
CC PubMed:20048001, PubMed:25849865). PTPN14 induces translocation from
CC the nucleus to the cytoplasm (PubMed:22525271). Localized mainly to the
CC nucleus in the early stages of embryo development with expression
CC becoming evident in the cytoplasm at the blastocyst and epiblast stages
CC (By similarity). {ECO:0000250|UniProtKB:P46938,
CC ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001,
CC ECO:0000269|PubMed:22525271, ECO:0000269|PubMed:25849865}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Isoforms of the YAP1-1 form contain only one WW domain.;
CC Name=1; Synonyms=YAP1-2gamma, YAP2L;
CC IsoId=P46937-1; Sequence=Displayed;
CC Name=2; Synonyms=YAP1-2alpha, YAP2;
CC IsoId=P46937-2; Sequence=VSP_039054;
CC Name=3; Synonyms=YAP1-1beta;
CC IsoId=P46937-3; Sequence=VSP_039053, VSP_039055;
CC Name=4;
CC IsoId=P46937-4; Sequence=VSP_045190;
CC Name=5; Synonyms=YAP1-1alpha;
CC IsoId=P46937-5; Sequence=VSP_039053, VSP_039054;
CC Name=6; Synonyms=YAP1-1gamma;
CC IsoId=P46937-6; Sequence=VSP_039053;
CC Name=7; Synonyms=YAP1-1delta;
CC IsoId=P46937-7; Sequence=VSP_039053, VSP_053483;
CC Name=8; Synonyms=YAP1-2beta;
CC IsoId=P46937-8; Sequence=VSP_039055;
CC Name=9; Synonyms=YAP1-2delta;
CC IsoId=P46937-9; Sequence=VSP_053483;
CC -!- TISSUE SPECIFICITY: Increased expression seen in some liver and
CC prostate cancers. Isoforms lacking the transactivation domain found in
CC striatal neurons of patients with Huntington disease (at protein
CC level). {ECO:0000269|PubMed:16461361, ECO:0000269|PubMed:17974916,
CC ECO:0000269|PubMed:7782338}.
CC -!- DOMAIN: The first coiled-coil region mediates most of the interaction
CC with TEAD transcription factors. {ECO:0000269|PubMed:20123905}.
CC -!- PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic
CC translocation and inactivation (PubMed:18158288, PubMed:20048001).
CC Phosphorylated by ABL1; leading to YAP1 stabilization, enhanced
CC interaction with TP73 and recruitment onto proapoptotic genes; in
CC response to DNA damage (PubMed:18280240). Phosphorylation at Ser-400
CC and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397
CC by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3
CC ubiquitin ligase and subsequent degradation (PubMed:20048001).
CC Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by
CC MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of
CC apoptosis by YAP1 (PubMed:21364637). {ECO:0000269|PubMed:18158288,
CC ECO:0000269|PubMed:18280240, ECO:0000269|PubMed:20048001,
CC ECO:0000269|PubMed:21364637}.
CC -!- PTM: Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase.
CC {ECO:0000269|PubMed:20048001}.
CC -!- DISEASE: Coloboma, ocular, with or without hearing impairment, cleft
CC lip/palate, and/or intellectual disability (COB1) [MIM:120433]: An
CC autosomal dominant disease characterized by uveal colobomata,
CC microphthalmia, cataract and cleft lip/palate. Considerable variability
CC is observed among patients, uveal colobomata being the most constant
CC feature. Some patients manifest intellectual disability of varying
CC degree and/or sensorineural, mid-frequency hearing loss.
CC {ECO:0000269|PubMed:24462371}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 9]: Highest expression in ovary and placenta,
CC lowest in skeletal muscle and brain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/YAP1ID42855ch11q22.html";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shaping life - Issue 175 of
CC January 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/175/";
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DR EMBL; X80507; CAA56672.1; -; Genomic_DNA.
DR EMBL; AY316529; AAP92710.1; -; mRNA.
DR EMBL; AB567720; BAJ41471.1; -; mRNA.
DR EMBL; AB567721; BAJ41472.1; -; mRNA.
DR EMBL; AK300414; BAG62143.1; -; mRNA.
DR EMBL; AK316116; BAH14487.1; -; mRNA.
DR EMBL; AP000942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67011.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67015.1; -; Genomic_DNA.
DR EMBL; BC038235; AAH38235.1; -; mRNA.
DR EMBL; HE864159; CCI79618.1; -; mRNA.
DR EMBL; HE864160; CCI79619.1; -; mRNA.
DR EMBL; HE864161; CCI79620.1; -; mRNA.
DR EMBL; HE864162; CCI79621.1; -; mRNA.
DR CCDS; CCDS44716.1; -. [P46937-1]
DR CCDS; CCDS53699.1; -. [P46937-2]
DR CCDS; CCDS53700.1; -. [P46937-4]
DR CCDS; CCDS60944.1; -. [P46937-8]
DR CCDS; CCDS60945.1; -. [P46937-3]
DR CCDS; CCDS73373.1; -. [P46937-9]
DR CCDS; CCDS73374.1; -. [P46937-7]
DR CCDS; CCDS8314.2; -. [P46937-5]
DR PIR; A56954; A56954.
DR RefSeq; NP_001123617.1; NM_001130145.2. [P46937-1]
DR RefSeq; NP_001181973.1; NM_001195044.1. [P46937-2]
DR RefSeq; NP_001181974.1; NM_001195045.1. [P46937-4]
DR RefSeq; NP_001269026.1; NM_001282097.1. [P46937-6]
DR RefSeq; NP_001269027.1; NM_001282098.1. [P46937-3]
DR RefSeq; NP_001269028.1; NM_001282099.1. [P46937-7]
DR RefSeq; NP_001269029.1; NM_001282100.1. [P46937-8]
DR RefSeq; NP_001269030.1; NM_001282101.1. [P46937-9]
DR PDB; 1JMQ; NMR; -; A=165-210.
DR PDB; 1K5R; NMR; -; A=165-204.
DR PDB; 1K9Q; NMR; -; A=165-204.
DR PDB; 1K9R; NMR; -; A=165-204.
DR PDB; 2LAW; NMR; -; A=230-263.
DR PDB; 2LAX; NMR; -; A=170-205.
DR PDB; 2LAY; NMR; -; A=170-205.
DR PDB; 2LTV; NMR; -; A=230-265.
DR PDB; 2LTW; NMR; -; A=170-205.
DR PDB; 3KYS; X-ray; 2.80 A; B/D=50-171.
DR PDB; 3MHR; X-ray; 1.15 A; P=124-133.
DR PDB; 4RE1; X-ray; 2.20 A; C/D=50-171.
DR PDB; 4REX; X-ray; 1.60 A; A=165-209.
DR PDB; 5OAQ; X-ray; 1.95 A; L=60-100.
DR PDB; 5YDX; NMR; -; A=164-218.
DR PDB; 5YDY; NMR; -; A=229-287.
DR PDB; 6G6X; X-ray; 1.13 A; P=124-133.
DR PDB; 6G8I; X-ray; 1.60 A; P=125-133.
DR PDB; 6G8J; X-ray; 1.47 A; P=124-133.
DR PDB; 6G8K; X-ray; 1.25 A; P=124-133.
DR PDB; 6G8L; X-ray; 1.37 A; P=124-133.
DR PDB; 6G8P; X-ray; 1.90 A; P=124-133.
DR PDB; 6G8Q; X-ray; 1.85 A; P=124-132.
DR PDB; 6GE3; X-ray; 1.85 A; L=60-100.
DR PDB; 6GE4; X-ray; 1.97 A; L=60-100.
DR PDB; 6GE5; X-ray; 2.05 A; L=60-100.
DR PDB; 6GE6; X-ray; 1.80 A; L=60-100.
DR PDB; 6GEC; X-ray; 1.70 A; L=60-99.
DR PDB; 6GEE; X-ray; 1.96 A; L=60-99.
DR PDB; 6GEG; X-ray; 2.23 A; L=60-99.
DR PDB; 6GEI; X-ray; 1.65 A; L=60-100.
DR PDB; 6GEK; X-ray; 2.28 A; L/M=60-100.
DR PDB; 6HIK; X-ray; 1.65 A; L=60-99.
DR PDB; 6HIL; X-ray; 2.30 A; L/M/N/O=60-100.
DR PDB; 6Q2X; X-ray; 2.10 A; L=60-100.
DR PDBsum; 1JMQ; -.
DR PDBsum; 1K5R; -.
DR PDBsum; 1K9Q; -.
DR PDBsum; 1K9R; -.
DR PDBsum; 2LAW; -.
DR PDBsum; 2LAX; -.
DR PDBsum; 2LAY; -.
DR PDBsum; 2LTV; -.
DR PDBsum; 2LTW; -.
DR PDBsum; 3KYS; -.
DR PDBsum; 3MHR; -.
DR PDBsum; 4RE1; -.
DR PDBsum; 4REX; -.
DR PDBsum; 5OAQ; -.
DR PDBsum; 5YDX; -.
DR PDBsum; 5YDY; -.
DR PDBsum; 6G6X; -.
DR PDBsum; 6G8I; -.
DR PDBsum; 6G8J; -.
DR PDBsum; 6G8K; -.
DR PDBsum; 6G8L; -.
DR PDBsum; 6G8P; -.
DR PDBsum; 6G8Q; -.
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; 6HIL; -.
DR PDBsum; 6Q2X; -.
DR AlphaFoldDB; P46937; -.
DR SMR; P46937; -.
DR BioGRID; 115684; 710.
DR ComplexPortal; CPX-256; YAP1-TEAD1 complex.
DR CORUM; P46937; -.
DR DIP; DIP-40839N; -.
DR ELM; P46937; -.
DR IntAct; P46937; 327.
DR MINT; P46937; -.
DR STRING; 9606.ENSP00000478927; -.
DR ChEMBL; CHEMBL3334415; -.
DR GlyGen; P46937; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46937; -.
DR MetOSite; P46937; -.
DR PhosphoSitePlus; P46937; -.
DR BioMuta; YAP1; -.
DR DMDM; 294862479; -.
DR EPD; P46937; -.
DR jPOST; P46937; -.
DR MassIVE; P46937; -.
DR MaxQB; P46937; -.
DR PaxDb; P46937; -.
DR PeptideAtlas; P46937; -.
DR PRIDE; P46937; -.
DR ProteomicsDB; 23425; -.
DR ProteomicsDB; 25812; -.
DR ProteomicsDB; 5134; -.
DR ProteomicsDB; 55772; -. [P46937-1]
DR ProteomicsDB; 55773; -. [P46937-2]
DR ProteomicsDB; 55774; -. [P46937-3]
DR Antibodypedia; 3994; 977 antibodies from 43 providers.
DR DNASU; 10413; -.
DR Ensembl; ENST00000282441.10; ENSP00000282441.5; ENSG00000137693.14. [P46937-1]
DR Ensembl; ENST00000345877.6; ENSP00000331023.4; ENSG00000137693.14. [P46937-7]
DR Ensembl; ENST00000524575.5; ENSP00000435602.1; ENSG00000137693.14. [P46937-4]
DR Ensembl; ENST00000526343.5; ENSP00000434134.1; ENSG00000137693.14. [P46937-5]
DR Ensembl; ENST00000531439.5; ENSP00000431574.1; ENSG00000137693.14. [P46937-2]
DR Ensembl; ENST00000537274.5; ENSP00000445635.1; ENSG00000137693.14. [P46937-8]
DR Ensembl; ENST00000615667.4; ENSP00000478927.1; ENSG00000137693.14. [P46937-9]
DR Ensembl; ENST00000629586.2; ENSP00000487519.1; ENSG00000137693.14. [P46937-3]
DR GeneID; 10413; -.
DR KEGG; hsa:10413; -.
DR MANE-Select; ENST00000282441.10; ENSP00000282441.5; NM_001130145.3; NP_001123617.1.
DR UCSC; uc001pgt.3; human. [P46937-1]
DR CTD; 10413; -.
DR DisGeNET; 10413; -.
DR GeneCards; YAP1; -.
DR HGNC; HGNC:16262; YAP1.
DR HPA; ENSG00000137693; Low tissue specificity.
DR MalaCards; YAP1; -.
DR MIM; 120433; phenotype.
DR MIM; 606608; gene.
DR neXtProt; NX_P46937; -.
DR OpenTargets; ENSG00000137693; -.
DR Orphanet; 157791; Epithelioid hemangioendothelioma.
DR Orphanet; 1473; Uveal coloboma-cleft lip and palate-intellectual disability.
DR PharmGKB; PA38103; -.
DR VEuPathDB; HostDB:ENSG00000137693; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00510000046760; -.
DR HOGENOM; CLU_041917_0_1_1; -.
DR InParanoid; P46937; -.
DR OMA; YYLNHIT; -.
DR OrthoDB; 1006566at2759; -.
DR PhylomeDB; P46937; -.
DR TreeFam; TF326941; -.
DR PathwayCommons; P46937; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P46937; -.
DR SIGNOR; P46937; -.
DR BioGRID-ORCS; 10413; 151 hits in 1072 CRISPR screens.
DR ChiTaRS; YAP1; human.
DR EvolutionaryTrace; P46937; -.
DR GeneWiki; YAP1; -.
DR GenomeRNAi; 10413; -.
DR Pharos; P46937; Tchem.
DR PRO; PR:P46937; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P46937; protein.
DR Bgee; ENSG00000137693; Expressed in saphenous vein and 191 other tissues.
DR ExpressionAtlas; P46937; baseline and differential.
DR Genevisible; P46937; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140552; C:TEAD-YAP complex; IDA:CAFA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0070064; F:proline-rich region binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0060449; P:bud elongation involved in lung branching; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0061026; P:cardiac muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0060242; P:contact inhibition; IDA:UniProtKB.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IEA:Ensembl.
DR GO; GO:1903703; P:enterocyte differentiation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0003015; P:heart process; IEA:Ensembl.
DR GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0060576; P:intestinal epithelial cell development; IDA:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0048368; P:lateral mesoderm development; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:CACAO.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:ComplexPortal.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:CACAO.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:ARUK-UCL.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:CAFA.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IDA:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IDA:MGI.
DR GO; GO:0032570; P:response to progesterone; IDA:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00201; WW; 2.
DR DisProt; DP00702; -.
DR IDEAL; IID00304; -.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Coiled coil; Cytoplasm;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..504
FT /note="Transcriptional coactivator YAP1"
FT /id="PRO_0000076071"
FT DOMAIN 171..204
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 230..263
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..504
FT /note="Transactivation domain"
FT REGION 355..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..100
FT /evidence="ECO:0000269|PubMed:20123905"
FT COILED 298..359
FT /evidence="ECO:0000255"
FT COMPBIAS 1..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2EJA0"
FT MOD_RES 109
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2EJA0"
FT MOD_RES 119
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:21364637,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001,
FT ECO:0000269|PubMed:28169360, ECO:0007744|PubMed:18669648"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 138
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:21364637,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 154
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:21364637,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 164
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:21364637,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001,
FT ECO:0000269|PubMed:28169360"
FT MOD_RES 400
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:20048001"
FT MOD_RES 403
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:20048001"
FT MOD_RES 407
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:18280240"
FT MOD_RES 412
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000269|PubMed:21364637"
FT VAR_SEQ 1..178
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045190"
FT VAR_SEQ 230..267
FT /note="Missing (in isoform 3, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:22939869, ECO:0000303|Ref.3"
FT /id="VSP_039053"
FT VAR_SEQ 328..343
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12807903"
FT /id="VSP_039054"
FT VAR_SEQ 328
FT /note="Q -> QVRPQ (in isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:22939869"
FT /id="VSP_053483"
FT VAR_SEQ 329..343
FT /note="AMRNINPSTANSPKC -> VRP (in isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:22939869"
FT /id="VSP_039055"
FT VARIANT 139
FT /note="P -> L (in dbSNP:rs1162286204)"
FT /evidence="ECO:0000269|PubMed:24462371"
FT /id="VAR_071125"
FT VARIANT 227
FT /note="S -> L (in dbSNP:rs376161041)"
FT /evidence="ECO:0000269|PubMed:24462371"
FT /id="VAR_071126"
FT VARIANT 330
FT /note="M -> V (in dbSNP:rs777949318)"
FT /evidence="ECO:0000269|PubMed:24462371"
FT /id="VAR_071127"
FT VARIANT 462
FT /note="G -> E"
FT /evidence="ECO:0000269|PubMed:24462371"
FT /id="VAR_071128"
FT MUTAGEN 61
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-109; A-127 and A-164."
FT /evidence="ECO:0000269|PubMed:20048001"
FT MUTAGEN 80
FT /note="V->A: No change in interaction with TEAD4. Reduced
FT interaction with TEAD4 and transforming ability; when
FT associated with A-84 and A-85."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 84
FT /note="V->A: Reduced interaction with TEAD4 and
FT transforming ability; when associated with A-80 and A-85."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 85
FT /note="P->A: Reduced interaction with TEAD4 and
FT transforming ability; when associated with A-80 and A-84."
FT /evidence="ECO:0000269|PubMed:20123908"
FT MUTAGEN 86
FT /note="M->A: Complete loss of interaction with TEAD1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT MUTAGEN 89
FT /note="R->A: Complete loss of interaction with TEAD1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT MUTAGEN 91
FT /note="L->A: Complete loss of interaction with TEAD1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT MUTAGEN 94
FT /note="S->A: Loss of interaction with TEAD1, TEAD2, TEAD3
FT and TEAD4. Loss of transcriptional coactivation activity
FT towards TEAD1, TEAD2, TEAD3 and TEAD4 but no effect on its
FT activity towards RUNX2 and ERBB4. Abolishes suppression of
FT ciliogenesis."
FT /evidence="ECO:0000269|PubMed:18579750,
FT ECO:0000269|PubMed:20123905"
FT MUTAGEN 95
FT /note="F->A: Complete loss of interaction with TEAD1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT MUTAGEN 96
FT /note="F->A: Loss of interaction with TEAD1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT MUTAGEN 109
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-61; A-127 and A-164."
FT /evidence="ECO:0000269|PubMed:20048001"
FT MUTAGEN 122
FT /note="H->A,R,N,K: Loss of phosphorylation by LATS1."
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288"
FT MUTAGEN 122
FT /note="H->L,Y: Significantly decreased phosphorylation at
FT S-127 and decreased interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:17974916,
FT ECO:0000269|PubMed:18158288"
FT MUTAGEN 124
FT /note="R->A: Loss of phosphorylation by LATS1."
FT /evidence="ECO:0000269|PubMed:18158288"
FT MUTAGEN 127
FT /note="S->A: Reduced phosphorylation by LATS2, loss of
FT phosphorylation by LATS1, loss of interaction with YWHAB,
FT decreased interaction with ERBB4 and increased nuclear
FT localization and transcriptional coactivation activity
FT toward ERBB4. In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-61; A-109; A-127 and A-164."
FT /evidence="ECO:0000269|PubMed:12807903,
FT ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18158288,
FT ECO:0000269|PubMed:20048001"
FT MUTAGEN 129
FT /note="P->D: No effect on phosphorylation but loss of
FT interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:17974916"
FT MUTAGEN 164
FT /note="S->A: In YAP-4SA; prevents phosphorylation by LATS1
FT and LATS2, promoting retention in the nucleus; when
FT associated with A-61; A-109 and A-127."
FT /evidence="ECO:0000269|PubMed:20048001"
FT MUTAGEN 199
FT /note="W->A: Loss of interaction with ERBB4, loss of
FT transcriptional coactivation function toward CTF and
FT reduced interaction with PRRG4; when associated with A-
FT 202."
FT /evidence="ECO:0000269|PubMed:12807903,
FT ECO:0000269|PubMed:23873930"
FT MUTAGEN 202
FT /note="P->A: Loss of interaction with ERBB4, loss of
FT transcriptional coactivation function toward CTF and
FT reduced interaction with PRRG4; when associated with A-
FT 199."
FT /evidence="ECO:0000269|PubMed:12807903,
FT ECO:0000269|PubMed:23873930"
FT MUTAGEN 217
FT /note="S->A: No effect on interaction with PRRG4."
FT /evidence="ECO:0000269|PubMed:23873930"
FT MUTAGEN 258
FT /note="W->A: Reduced interaction with PRRG4; when
FT associated with A-261."
FT /evidence="ECO:0000269|PubMed:23873930"
FT MUTAGEN 261
FT /note="P->A: Reduced interaction with PRRG4; when
FT associated with A-258."
FT /evidence="ECO:0000269|PubMed:23873930"
FT MUTAGEN 397
FT /note="S->A: Loss of phosphorylation by LATS1."
FT /evidence="ECO:0000269|PubMed:18158288"
FT MUTAGEN 407
FT /note="Y->E: Enhanced interaction with TP73."
FT /evidence="ECO:0000269|PubMed:18280240"
FT MUTAGEN 407
FT /note="Y->F: No phosphorylation by ABL1 and partial loss of
FT binding to TP73."
FT /evidence="ECO:0000269|PubMed:18280240"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4RE1"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6GEI"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6GEI"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1K9Q"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4REX"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1K9Q"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4REX"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:4REX"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:4REX"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:4REX"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2LAW"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2LAW"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2LAW"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2LAW"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:2LAW"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2LAW"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5YDY"
SQ SEQUENCE 504 AA; 54462 MW; 6145F7049ED338AE CRC64;
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA GHQIVHVRGD
SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE PKSHSRQAST DAGTAGALTP
QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG PAATPTAQHL RQSSFEIPDD VPLPAGWEMA
KTSSGQRYFL NHIDQTTTWQ DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM
TQDGEIYYIN HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS
NQQQQMRLQQ LQMEKERLRL KQQELLRQAM RNINPSTANS PKCQELALRS QLPTLEQDGG
TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS GLSMSSYSVP RTPDDFLNSV
DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG TNVDLGTLEG DGMNIEGEEL MPSLQEALSS
DILNDMESVL AATKLDKESF LTWL
