YAP1_MOUSE
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 03-AUG-2022, entry version 181.
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; 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, Pancreas,
RC 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).
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. The core of this pathway is composed of a kinase
CC cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory
CC protein SAV1, phosphorylates and activates LATS1/2 in complex with its
CC regulatory protein MOB1, which in turn phosphorylates and inactivates
CC YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and
CC 3D tissue shape by regulating cortical actomyosin network formation.
CC Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-
CC actin polymerization. Plays a key role in controlling cell
CC proliferation in response to cell contact. Phosphorylation of YAP1 by
CC LATS1/2 inhibits its translocation into the nucleus to regulate
CC cellular genes important for cell proliferation, cell death, and cell
CC migration. The presence of TEAD transcription factors are required for
CC it to stimulate gene expression, cell growth, anchorage-independent
CC growth, and epithelial mesenchymal transition (EMT) induction.
CC Suppresses ciliogenesis via acting as a transcriptional corepressor of
CC the TEAD4 target genes AURKA and PLK1 (By similarity). In conjunction
CC with WWTR1, involved in the regulation of TGFB1-dependent SMAD2 and
CC SMAD3 nuclear accumulation (PubMed:21145499).
CC {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:21145499}.
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).
CC {ECO:0000250|UniProtKB:P46937, ECO:0000269|PubMed:20123908,
CC ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:7644498,
CC 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:0000250|UniProtKB:P46937}. Nucleus
CC {ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:28087714}. Note=Both
CC phosphorylation and cell density can regulate its subcellular
CC localization (By similarity). Phosphorylation sequesters it in the
CC cytoplasm by inhibiting its translocation into the nucleus (By
CC similarity). At low density, predominantly nuclear and is translocated
CC to the cytoplasm at high density. PTPN14 induces translocation from the
CC nucleus to the cytoplasm (By similarity). 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 (PubMed:21145499). {ECO:0000250|UniProtKB:P46937,
CC 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}.
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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 complex.
DR CORUM; P46938; -.
DR DIP; DIP-40015N; -.
DR ELM; P46938; -.
DR IntAct; P46938; 35.
DR MINT; P46938; -.
DR STRING; 10090.ENSMUSP00000069554; -.
DR iPTMnet; P46938; -.
DR PhosphoSitePlus; P46938; -.
DR jPOST; P46938; -.
DR MaxQB; P46938; -.
DR PaxDb; P46938; -.
DR PeptideAtlas; P46938; -.
DR PRIDE; P46938; -.
DR ProteomicsDB; 299617; -. [P46938-1]
DR ProteomicsDB; 299618; -. [P46938-2]
DR Antibodypedia; 3994; 977 antibodies from 43 providers.
DR DNASU; 22601; -.
DR Ensembl; ENSMUST00000065353; ENSMUSP00000069554; ENSMUSG00000053110. [P46938-1]
DR Ensembl; ENSMUST00000086580; ENSMUSP00000083772; ENSMUSG00000053110. [P46938-2]
DR GeneID; 22601; -.
DR KEGG; mmu:22601; -.
DR UCSC; uc009ode.2; mouse. [P46938-2]
DR UCSC; uc009odf.2; mouse. [P46938-1]
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; YYLNHIT; -.
DR OrthoDB; 1006566at2759; -.
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 71 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 251 other tissues.
DR ExpressionAtlas; P46938; baseline and differential.
DR Genevisible; P46938; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0008022; F:protein C-terminus 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:0006974; P:cellular response to DNA damage stimulus; ISO: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:0006975; P:DNA damage induced protein phosphorylation; ISS:UniProtKB.
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: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:2000648; P:positive regulation of stem cell proliferation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:MGI.
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:0035019; P:somatic stem cell population maintenance; IDA:MGI.
DR GO; GO:0072089; P:stem cell proliferation; 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 IDEAL; IID50281; -.
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..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
