ID YAP1_MOUSE Reviewed; 488 AA. AC P46938; Q52KJ5; Q91WL1; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 2. DT 27-MAR-2024, entry version 190. 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=Yap, Yap65; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=NIH Swiss; TISSUE=Embryo; 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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. 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 [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=129, C57BL/6J, and FVB/N; RC TISSUE=Brain, Kidney, and Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH WBP1 AND WBP2. RX PubMed=7644498; DOI=10.1073/pnas.92.17.7819; RA Chen H.I., Sudol M.; RT "The WW domain of Yes-associated protein binds a proline-rich ligand that RT differs from the consensus established for Src homology 3-binding RT modules."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7819-7823(1995). RN [6] RP INTERACTION WITH ENAH. RX PubMed=9407065; DOI=10.1074/jbc.272.52.32869; RA Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., RA Sudol M.; RT "The WW domain of neural protein FE65 interacts with proline-rich motifs in RT Mena, the mammalian homolog of Drosophila enabled."; RL J. Biol. Chem. 272:32869-32877(1997). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [8] 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-94; SER-112; SER-123 RP AND SER-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP FUNCTION, INTERACTION WITH WWTR1; SMAD2 AND SMAD3, AND SUBCELLULAR RP 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 [14] RP INTERACTION WITH TEAD4, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 47-85 RP IN COMPLEX WITH TEAD4. 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 [15] RP TISSUE SPECIFICITY. 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 [16] RP SUBCELLULAR LOCATION. RX PubMed=28087714; DOI=10.1101/gad.284539.116; RA Kwan J., Sczaniecka A., Arash E.H., Nguyen L., Chen C.C., Ratkovic S., RA Klezovitch O., Attisano L., McNeill H., Emili A., Vasioukhin V.; RT "DLG5 connects cell polarity and Hippo signaling protein networks by RT linking PAR-1 with MST1/2."; RL Genes Dev. 30:2696-2709(2016). RN [17] RP FUNCTION, INTERACTION WITH CLDN18, AND SUBCELLULAR LOCATION. RX PubMed=29400695; DOI=10.1172/jci90429; RA Zhou B., Flodby P., Luo J., Castillo D.R., Liu Y., Yu F.X., McConnell A., RA Varghese B., Li G., Chimge N.O., Sunohara M., Koss M.N., Elatre W., RA Conti P., Liebler J.M., Yang C., Marconett C.N., Laird-Offringa I.A., RA Minoo P., Guan K., Stripp B.R., Crandall E.D., Borok Z.; RT "Claudin-18-mediated YAP activity regulates lung stem and progenitor cell RT homeostasis and tumorigenesis."; RL J. Clin. Invest. 128:970-984(2018). 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:29400695). The core of this pathway is CC composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in CC complex with its regulatory protein SAV1, phosphorylates and activates CC LATS1/2 in complex with its regulatory protein MOB1, which in turn CC phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Plays a CC 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. Plays a key CC role in controlling cell proliferation in response to cell contact. CC Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the CC nucleus to regulate cellular genes important for cell proliferation, CC cell death, and cell migration. The presence of TEAD transcription CC factors are required for it to stimulate gene expression, cell growth, CC anchorage-independent growth, and epithelial mesenchymal transition CC (EMT) induction. Suppresses ciliogenesis via acting as a CC transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 CC (By similarity). In conjunction with WWTR1, involved in the regulation CC of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation CC (PubMed:21145499). {ECO:0000250|UniProtKB:P46937, CC ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:29400695}. CC -!- SUBUNIT: Binds to the SH3 domain of the YES kinase (By similarity). CC Binds to WBP1 and WBP2 (PubMed:7644498). Binds, in vitro, through the CC WW1 domain, to neural isoforms of ENAH that contain the PPSY motif CC (PubMed:9407065). The phosphorylated form interacts with YWHAB (By CC similarity). Interacts (via WW domains) with LATS1 (via PPxY motif 2) CC (By similarity). Interacts with LATS2 (By similarity). Interacts (via CC WW domain 1) with isoform JM-A of ERBB4 (via PPxY motif 2) (By CC similarity). Interacts with TEAD1, TEAD2 and TEAD3 (By similarity). CC Interacts with TP73 and HCK (By similarity). Interacts with RUNX1 (By CC similarity). Interacts with TEAD4 (PubMed:20123908). Interacts (via WW CC domains) with PTPN14 (via PPxY motif 2); this interaction leads to the CC cytoplasmic sequestration of YAP1 and inhibits its transcriptional co- CC activator activity (By similarity). Interacts (when phosphorylated at CC Ser-112) with SMAD2, SMAD3 and WWTR1 (PubMed:21145499). Interacts with CC PRRG2 (via cytoplasmic domain) (By similarity). Interacts (via WW CC domains) with PRRG4 (via cytoplasmic domain) (By similarity). Interacts CC (phosphorylated) with CLDN18; the interaction sequesters YAP1 away from CC the nucleus and thereby restricts transcription of YAP1 target genes CC (PubMed:29400695). Interacts with SMAD1 (By similarity). CC {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:20123908, CC ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:29400695, CC ECO:0000269|PubMed:7644498, ECO:0000269|PubMed:9407065}. CC -!- INTERACTION: CC P46938; Q501J6: Ddx17; NbExp=3; IntAct=EBI-1211949, EBI-911206; CC P46938; P97474: Pitx2; NbExp=2; IntAct=EBI-1211949, EBI-1175125; CC P46938; P30051: Tead1; NbExp=4; IntAct=EBI-1211949, EBI-3953905; CC P46938; Q9JJP2: Tp73; NbExp=2; IntAct=EBI-1211949, EBI-1770138; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29400695}. Nucleus CC {ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:28087714, CC ECO:0000269|PubMed:29400695}. Cell junction CC {ECO:0000269|PubMed:29400695}. Note=Both phosphorylation and cell CC density can regulate its subcellular localization (By similarity). CC Phosphorylation sequesters it in the cytoplasm by inhibiting its CC translocation into the nucleus (By similarity). At low density, CC predominantly nuclear and is translocated to the cytoplasm at high CC density. PTPN14 induces translocation from the nucleus to the cytoplasm CC (By similarity). Localized mainly to the nucleus in the early stages of CC embryo development with expression becoming evident in the cytoplasm at CC the blastocyst and epiblast stages (PubMed:21145499). CC {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:21145499}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms lacking the transactivation domain CC exist.; CC Name=1; Synonyms=YAP2L; CC IsoId=P46938-1; Sequence=Displayed; CC Name=2; Synonyms=YAP2; CC IsoId=P46938-2; Sequence=VSP_039056; CC -!- TISSUE SPECIFICITY: Isoforms lacking the transactivation domain seen in CC striatal neurons (at protein level). Ubiquitous. Isoform 2 is expressed CC at higher levels in the neural tissues. In the embryo, it is expressed CC in brain, eye, and the maxillary and frontonasal components of the CC primary palate. {ECO:0000269|PubMed:12807903, CC ECO:0000269|PubMed:16461361, ECO:0000269|PubMed:24462371}. CC -!- DOMAIN: The first coiled-coil region mediates most of the interaction CC with TEAD transcription factors. {ECO:0000250|UniProtKB:P46937}. CC -!- PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic CC translocation and inactivation. Phosphorylated by ABL1; leading to YAP1 CC stabilization, enhanced interaction with TP73 and recruitment onto CC proapoptotic genes; in response to DNA damage. Phosphorylation at Ser- CC 385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser- CC 382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) CC E3 ubiquitin ligase and subsequent degradation (By similarity). CC Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 CC and MAPK9/JNK2, which is required for the regulation of apoptosis by CC YAP1 (By similarity). {ECO:0000250|UniProtKB:P46937}. CC -!- PTM: Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase. CC {ECO:0000250|UniProtKB:P46937}. CC -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80508; CAA56673.1; -; mRNA. DR EMBL; CH466522; EDL24950.1; -; Genomic_DNA. DR EMBL; BC014733; AAH14733.1; -; mRNA. DR EMBL; BC039125; AAH39125.1; -; mRNA. DR EMBL; BC094313; AAH94313.1; -; mRNA. DR CCDS; CCDS40533.1; -. [P46938-2] DR CCDS; CCDS52718.1; -. [P46938-1] DR PIR; B56954; B56954. DR RefSeq; NP_001164618.1; NM_001171147.1. [P46938-1] DR RefSeq; NP_033560.1; NM_009534.3. [P46938-2] DR PDB; 3JUA; X-ray; 3.00 A; B/D/F/H=47-85. DR PDB; 6JK0; X-ray; 3.10 A; A=156-247. DR PDB; 6JK1; X-ray; 2.00 A; A/B=156-247. DR PDBsum; 3JUA; -. DR PDBsum; 6JK0; -. DR PDBsum; 6JK1; -. DR AlphaFoldDB; P46938; -. DR SMR; P46938; -. DR BioGRID; 204611; 96. DR ComplexPortal; CPX-394; YAP1-TEAD1 transcription factor complex. DR CORUM; P46938; -. DR DIP; DIP-40015N; -. DR ELM; P46938; -. DR IntAct; P46938; 36. DR MINT; P46938; -. DR STRING; 10090.ENSMUSP00000069554; -. DR GlyGen; P46938; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P46938; -. DR PhosphoSitePlus; P46938; -. DR jPOST; P46938; -. DR MaxQB; P46938; -. DR PaxDb; 10090-ENSMUSP00000069554; -. DR PeptideAtlas; P46938; -. DR ProteomicsDB; 299617; -. [P46938-1] DR ProteomicsDB; 299618; -. [P46938-2] DR Pumba; P46938; -. DR Antibodypedia; 3994; 1194 antibodies from 44 providers. DR CPTC; P46938; 4 antibodies. DR DNASU; 22601; -. DR Ensembl; ENSMUST00000065353.13; ENSMUSP00000069554.7; ENSMUSG00000053110.14. [P46938-1] DR Ensembl; ENSMUST00000086580.12; ENSMUSP00000083772.6; ENSMUSG00000053110.14. [P46938-2] DR GeneID; 22601; -. DR KEGG; mmu:22601; -. DR UCSC; uc009ode.2; mouse. [P46938-2] DR UCSC; uc009odf.2; mouse. [P46938-1] DR AGR; MGI:103262; -. DR CTD; 10413; -. DR MGI; MGI:103262; Yap1. DR VEuPathDB; HostDB:ENSMUSG00000053110; -. DR eggNOG; KOG0940; Eukaryota. DR GeneTree; ENSGT00510000046760; -. DR HOGENOM; CLU_041917_0_1_1; -. DR InParanoid; P46938; -. DR OMA; LPMRMRN; -. DR OrthoDB; 2593247at2759; -. DR PhylomeDB; P46938; -. DR TreeFam; TF326941; -. DR Reactome; R-MMU-1251985; Nuclear signaling by ERBB4. DR Reactome; R-MMU-2028269; Signaling by Hippo. DR Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression. DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-MMU-8951671; RUNX3 regulates YAP1-mediated transcription. DR BioGRID-ORCS; 22601; 13 hits in 75 CRISPR screens. DR ChiTaRS; Yap1; mouse. DR EvolutionaryTrace; P46938; -. DR PRO; PR:P46938; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P46938; Protein. DR Bgee; ENSMUSG00000053110; Expressed in animal zygote and 255 other cell types or tissues. DR ExpressionAtlas; P46938; baseline and differential. DR GO; GO:0030054; C:cell junction; ISO:MGI. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0140552; C:TEAD-YAP complex; IPI:ComplexPortal. DR GO; GO:0005667; C:transcription regulator complex; IGI:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0070064; F:proline-rich region binding; IPI:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0001824; P:blastocyst development; IMP:MGI. DR GO; GO:0060449; P:bud elongation involved in lung branching; IMP:MGI. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0061026; P:cardiac muscle tissue regeneration; IMP:ARUK-UCL. DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IDA:MGI. DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB. DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI. DR GO; GO:0060242; P:contact inhibition; ISO:MGI. DR GO; GO:0006974; P:DNA damage response; ISO:MGI. DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IGI:MGI. DR GO; GO:1903703; P:enterocyte differentiation; IDA:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:MGI. DR GO; GO:0002067; P:glandular epithelial cell differentiation; IDA:MGI. DR GO; GO:0003015; P:heart process; IMP:ARUK-UCL. DR GO; GO:0035329; P:hippo signaling; IGI:MGI. 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:0060575; P:intestinal epithelial cell differentiation; IDA:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0048368; P:lateral mesoderm development; IGI:MGI. DR GO; GO:0060487; P:lung epithelial cell differentiation; IMP:MGI. DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB. DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; ISO:MGI. DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IDA:MGI. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IGI:MGI. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0030903; P:notochord development; IGI:MGI. DR GO; GO:0035265; P:organ growth; IDA:MGI. DR GO; GO:0048339; P:paraxial mesoderm development; IGI:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:MGI. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:ARUK-UCL. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:MGI. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:MGI. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB. DR GO; GO:0046622; P:positive regulation of organ growth; IDA:MGI. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:MGI. DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IGI:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI. DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI. DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:MGI. DR GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; IGI:MGI. DR GO; GO:0050767; P:regulation of neurogenesis; ISO:MGI. DR GO; GO:0072091; P:regulation of stem cell proliferation; IDA:MGI. DR GO; GO:0032570; P:response to progesterone; ISO:MGI. DR GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB. DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI. DR GO; GO:0001894; P:tissue homeostasis; IMP:ARUK-UCL. DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI. DR GO; GO:0001570; P:vasculogenesis; IMP:MGI. DR GO; GO:0042060; P:wound healing; IMP:ARUK-UCL. DR CDD; cd00201; WW; 2. DR DisProt; DP02451; -. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 6.20.430.10; -; 1. DR IDEAL; IID50281; -. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR17616:SF9; TRANSCRIPTIONAL COACTIVATOR YAP1; 1. DR PANTHER; PTHR17616; YES-ASSOCIATED PROTEIN YAP1 FAMILY MEMBER; 1. DR Pfam; PF00397; WW; 2. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 2. DR PROSITE; PS50020; WW_DOMAIN_2; 2. DR Genevisible; P46938; MM. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cell junction; Coiled coil; KW Cytoplasm; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..488 FT /note="Transcriptional coactivator YAP1" FT /id="PRO_0000076072" FT DOMAIN 156..189 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 215..248 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 76..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..293 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 276..488 FT /note="Transactivation domain" FT REGION 339..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 71..85 FT /evidence="ECO:0000250" FT COILED 283..344 FT /evidence="ECO:0000255" FT COMPBIAS 1..34 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..293 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 48 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q2EJA0" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 95 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q2EJA0" FT MOD_RES 104 FT /note="Phosphothreonine; by MAPK8 and MAPK9" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 112 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21145499, FT ECO:0007744|PubMed:21183079" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 149 FT /note="Phosphoserine; by LATS1 and LATS2" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 352 FT /note="Phosphoserine; by MAPK8 and MAPK9" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 366 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 382 FT /note="Phosphoserine; by LATS1 and LATS2" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 385 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 388 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 392 FT /note="Phosphotyrosine; by ABL1" FT /evidence="ECO:0000250|UniProtKB:P46937" FT MOD_RES 397 FT /note="Phosphothreonine; by MAPK8 and MAPK9" FT /evidence="ECO:0000250|UniProtKB:P46937" FT VAR_SEQ 313..328 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12807903, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7782338" FT /id="VSP_039056" FT HELIX 51..58 FT /evidence="ECO:0007829|PDB:3JUA" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:3JUA" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:3JUA" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:3JUA" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:6JK1" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:6JK1" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:6JK1" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:6JK1" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:6JK0" FT STRAND 221..225 FT /evidence="ECO:0007829|PDB:6JK1" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:6JK1" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:6JK1" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:6JK1" SQ SEQUENCE 488 AA; 52383 MW; 5A2221B74B1400F9 CRC64; MEPAQQPPPQ PAPQGPAPPS VSPAGTPAAP PAPPAGHQVV HVRGDSETDL EALFNAVMNP KTANVPQTVP MRLRKLPDSF FKPPEPKSHS RQASTDAGTA GALTPQHVRA HSSPASLQLG AVSPGTLTAS GVVSGPAAAP AAQHLRQSSF EIPDDVPLPA GWEMAKTSSG QRYFLNHNDQ TTTWQDPRKA MLSQLNVPAP ASPAVPQTLM NSASGPLPDG WEQAMTQDGE VYYINHKNKT TSWLDPRLDP RFAMNQRITQ SAPVKQPPPL APQSPQGGVL GGGSSNQQQQ IQLQQLQMEK ERLRLKQQEL FRQAIRNINP STANAPKCQE LALRSQLPTL EQDGGTPNAV SSPGMSQELR TMTTNSSDPF LNSGTYHSRD ESTDSGLSMS SYSIPRTPDD FLNSVDEMDT GDTISQSTLP SQQSRFPDYL EALPGTNVDL GTLEGDAMNI EGEELMPSLQ EALSSEILDV ESVLAATKLD KESFLTWL //