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YAP1 (Yes-associated protein 1, 65kDa)

Written2010-01Silvia Di Agostino, Sabrina Strano, Giovanni Blandino
Molecular Medicine Department, Regina Elena Cancer Institute, Rome 00144, Italy

(Note : for Links provided by Atlas : click)


HGNC (Hugo) YAP1
HGNC Alias symbYAP65
HGNC Previous nameYes-associated protein 1, 65kDa
 Yes associated protein 1
LocusID (NCBI) 10413
Atlas_Id 42855
Location 11q22.1  [Link to chromosome band 11q22]
Location_base_pair Starts at 102110447 and ends at 102233424 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping YAP1.png]
Local_order Genes flanking YAP1 on 11q22.1 are:
- CNTN5, contactin-5, 11q22.1
- FLJ42335, Hypothetical protein LOC100128386, 11q22.1
- FLJ32810, Rho-type GTPase-activating protein FLJ32810, 11q22.1
- TMEM133, transmembrane protein 133, 11q22.1
- PGR, progesterone receptor, 11q22-q23
- TRPC6, transient receptor potential cation channel, subfamily C, member 6, 11q22.1
- ANGPTL5, angiopoietin-like 5, 11q22.1
- YAP1, Yes-associated protein 1, 11q22.1
- RPS6P17, ribosomal protein S6 pseudogene 17, 11q22.2
- BIRC3, baculoviral IAP repeat-containing protein 3, 11q22.2
- BIRC2, baculoviral IAP repeat-containing protein 2, 11q22.2
- MMP20, matrix metalloproteinase 20, 11q22.2
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
C11orf95 (11q13.1)::YAP1 (11q22.1)DDX10 (11q22.3)::YAP1 (11q22.1)METAP1D (2q31.1)::YAP1 (11q22.1)
MRE11 (11q21)::YAP1 (11q22.1)PPP6R3 (11q13.2)::YAP1 (11q22.1)TMEM123 (11q22.2)::YAP1 (11q22.1)
YAP1 (11q22.1)::C11orf70 (11q22.1)YAP1 (11q22.1)::CUL5 (11q22.3)YAP1 (11q22.1)::MAML2 (11q21)
YAP1 (11q22.1)::STIM1 (11p15.4)YAP1 (11q22.1)::TFE3 (Xp11.23)
Note YAP interacts with the SH3 domain of c-Yes (and also c-Src), through a stretch of proline residues. YAP protein contains a WW domain that is found in various structural, regulatory and signaling molecules in yeast, nematode, and mammals, and it is involved in protein-protein interaction.


  YAP1 mRNA spans approximately 5218 bases and has 7 exons.
Description The genomic size is 122863 bases and the gene is located on plus strand. YAP1 gene is composed of 7 exons. The open reading frame of the coding region is 1364 bp. No polymorphisms of YAP1 is known.
SNP: 1590 single nucleotide polymorphisms are present in the human gene according to NCBI database.
Transcription The human YAP1 coding sequence consists of 1364 bp from the start codon to the stop codon. A differentially spliced isoform of YAP1 (9 exons), with two WW domains known as YAP2 also exists (Sudol et al., 1995).
Pseudogene No pseudogene of YAP1 is known.


Note The Yes-associated protein (YAP), a critical mediator of p73 function, binds p73 to regulate its transcriptional activity (Strano et al., 2001) and subsequent cell-death induction (Basu et al., 2003). This binding is negatively regulated by AKT-mediated YAP phosphorylation (Basu et al., 2003) and enhanced by DNA damage (Strano et al., 2005). In addition to increase p73 transcriptional activity via the p300 acetyltansferase (Strano et al., 2005), YAP can stabilize p73 protein in a posttranslational manner by competing with the ITCH E3-ligase for binding to p73 (Levy et al., 2007).
  Structure of human YAP isoforms. The protein domains and their length (indicated by number of limiting residues) are reported. YAP1 contains a proline-rich domain, a WW domain, a glutamine rich domain and portion of protein that regulates the transcription activation.
Description Structure: YAP protein consists of 454 amino acids, with a molecular weight of 65 kDa. It was identified as a protein that interacted with the non receptor tyrosine kinase c-Yes, which is a member of the Src family (Sudol, 1994). In fact, Yap is able to interact with the SH3 domain of c-Yes (and also c-Src), through a stretch of proline residues; this proline-rich region is able to interact with SH3 domains of many other proteins. In addition Yap contains another binding domain of a different nature. Due to the presence of two tryptophan residues, which appear to be conserved along evolution and that play an important role in the domain structure and function, it was named WW domain (Sudol et al., 1995; Sudol and Hunter, 2000).
The WW domain binds to short stretches of prolines (PY motif), and therefore mediating the interaction between proteins. The WW domain of Yap belongs to the first of four different classes that differ in terms of the sequence of the interacting motif, a PPxY in the case of WW type I. Yap has been found to interact with many proteins, whose function often is quite substantially different, and the majority of these interactions are mostly mediated by the WW domain (Bertini et al., 2009).
The interaction with PEBP2 (a RunX transcription factor) was the first example of Yap1 as a co-activator of transcription. The WW domain of Yap1 interacts with the PY motif present in the transcription activation domain of PEBP2 and in this occasion Yap1 was reported for the first time to have a strong intrinsic transactivation activity (Yagi et al., 1999). The transcriptional coactivator Yes-associated protein (YAP) was shown to interact with and to enhance p73-dependent apoptosis in response to DNA damage (Strano et al., 2001; Strano et al., 2005).
Interactors of YAPReference
YES Sudol et al., 1995
WBP1 and WBP2Chen and Sudol, 1995
NFE2Gavva et al., 1997
RUNX1 and RUNX2Yagi et al., 1999
EBP50Mohler et al., 1999
TP53BP2Espanel and Sudol, 2001
TP73 Strano et al., 2001
TEAD1, 2, 3, 4 Vassilev et al., 2001
SMAD7Ferrigno et al., 2002
AKTBasu et al., 2003
ERBB4Komuro et al., 2003
HNRNPUHowell et al., 2004
LATS1Hao et al., 2008
ABL1Levy et al., 2008
PMLLapi et al., 2008
EGR1Zagurovskaya et al., 2009
Table 1: Modified by Bertini et al., 2009.
Expression By Northern blot analysis YAP1 expression shows a major transcript of approximately 5 kb in several human tissues. High expression was found in placenta, prostate, testis, ovary, and small intestine, and lower expression was found in brain, liver, and spleen. No expression was found in peripheral blood leukocytes (Sudol et al., 1995).
YAP1 is the predominant isoform and is ubiquitously expressed in the major part of tissues for twelve normal human tissues (out of 28 tissues shown) hybridized against Affymetrix GeneChips HG-U95A-E (GeneNote data) and for 22 normal human tissues hybridized against HG-U133A (GNF Symatlas data) (Su et al., 2004).
Localisation Posttranslational modification of YAP determines its binding and localisation. Lapi et al. (2008) have shown Akt-mediated phosphorylation promotes YAP cytoplasmic retention, demonstrating that active Akt counters cisplatin-induced increases in PML transcription via the YAP-p73 complex. Recently, Levy et al. (2008) have also shown that cisplatin induces ABL1-mediated YAP phosphorylation, resulting in YAP nuclear localization and increased p73 binding and activation of pro-apoptotic genes.
YAP binding of p73 and its coordination of other binding proteins probably depend on an integration of phosphorylation by AKT, ABL1, and other kinases. However, the shuttling of Yap between nucleus and cytoplasm has emerged as an important means for regulating the activity of this protein.
Function Yap is a small protein that binds to many transcription factors and modulates their activity. Yap increases the ability of p73 to induce apoptosis as a consequence of damage to the DNA, and therefore its activity was thought to favor tumor suppression. However, other studies have recently shown a role for Yap in cell differentiation, cell transformation and in the regulation of organ size. It has been demonstrated that the Drosophila Hippo pathway has a mammalian equivalent, and that Yap is part of this pathway, where it could stimulate proliferation (Pan, 2007; Harvey et al., 2007).
Apoptosis: The transcriptional coactivator Yes-associated protein (YAP) has demonstrated to interact with and to enhance p73-dependent apoptosis in response to DNA damage (Strano et al., 2001; Strano et al., 2005). It has been reported that YAP is phosphorylated by AKT, and such modification impairs YAP-nuclear translocation and attenuates p73-mediated apoptosis (Basu et al., 2003). Recently, it was demonstrated that p73 is required for the nuclear translocation of endogenous YAP in cells exposed to cisplatin and that YAP is recruited by PML into nuclear bodies to promote p73 transcriptional activity (Strano et al., 2005). It was found that YAP contributes to p73 stabilization in response to DNA damage and promotes p73-dependent apoptosis through the specific and selective coactivation of apoptotic p73 target genes and potentiation of p300-mediated acetylation of p73 (Strano et al., 2005). Then, it was described the existence of a proapoptotic autoregulatory feedback loop between p73, YAP, and the promyelocytic leukemia (PML) tumor suppressor gene (Lapi et al., 2008). PML is a direct transcriptional target of p73/YAP. PML contributes to the p73-dependent apoptotic response by regulating YAP stability. Importantly, PML and YAP physically interact through their PVPVY and WW domains, respectively, causing YAP stabilization upon cisplatin treatment, which occurs through PML mediated sumoylation (Lapi et al., 2008).
Together with this proapoptotic role, YAP recently was identified as a tumor suppressor in breast cancer (Yuan et al., 2008). The findings that YAP plays opposing roles in tissue growth/development and DNA damage/apoptosis appear at first contradictory, but this can be explained if YAP binds and activates or inactivates different transcription factors to differentially regulate either pro-growth or pro-apoptotic genes.
Organ size and cell differentiation: Yap plays an important role in controlling organ growth. The works done on Drosophila show how a disrupted Hippo signalling pathway has a negative impact on the growth of imaginal discs (Pan et al., 2007) and how the presence of mutated forms of Yap in particular has an effect on size and shape of fly wings (Zhao et al., 2007).
In addition Dong et al. (2007) reported that overexpression of Yap in mice increases liver size, and in the long term it induces nodules which present characteristics of HCC (Dong et al., 2007). This is in accordance with another important study where increased levels of Yap are shown to enlarge liver size in a reversible manner (Camargo et al., 2007).
However, many questions are unsolved. For instance, it would be interesting to check whether the Hippo pathway plays a role in choices taken by Yap during cell differentiation; to verify whether activity of Yap could be extended to a cellular context beside intestine epithelium; to find the molecular mechanism used by Yap to control transcription of those genes that are in charge of cell differentiation; and obviously, a screen for these genes.
Homology Orthologs: YAP1 is evolutionarily principally conserved in 8 eukaryotes: Canis familiaris, Pan troglodytes, Bos taurus, Mus musculus, Galus gallus, Danio rerio, Xenopus laevis, Silurana tropicalis. Orthologies between human and Drosophyla melanogaster, Caenorabditis elegans and Saccaromyces cerevisiae are quite low. For details see: HomoloGene.


Note No mutations of YAP1 are known.

Implicated in

Entity Various cancers
Note Overholtzer and collaborators identified a mouse mammary tumor with a small amplicon involving the Yap1 gene. They noted that amplification of the syntenic locus on human chromosome 11q22 is present in different cancers (breast, colon, prostate). Overexpression of human YAP1 in nontransformed mammary epithelial cells induced epithelial-to-mesenchymal transition, suppression of apoptosis, growth factor-independent proliferation, and anchorage-independent growth in soft agar (Overholtzer et al., 2006). They concluded that YAP1 contributes to malignant transformation in cancers harboring the 11q22 amplicon.
Entity Tumor suppression
Note As previously described, the regulation of p73 activity by YAP has been investigated in the context of DNA-damage signaling. As an activating cofactor for a proapoptotic transcription factor, it was assumed that YAP plays a tumor suppressor role in cancer. YAP has also been identified as an oncogenic progrowth, cell size regulator in both Drosophila melanogaster and mammalian cells (Dong et al., 2007; Zhao et al., 2007). The mechanism for the growth control role of YAP or its fly homolog, Yki, is the result of its inactivation by the MST2 (HIPPO in fly) pathway, where the tumor suppressor LATS1 kinase (WTS in fly) directly phosphorylates YAP (Yki), inhibiting its coactivation of the TEAD (Scalloped in fly) transcription factor to upregulate pro-growth genes (Zhao et al., 2008).
The MST2/LATS1 pathway can also enhance YAP-p73 binding and activation of proapoptotic genes downstream of Fas signaling in breast cancer cells (Matallanas et al., 2007).


Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis.
Basu S, Totty NF, Irwin MS, Sudol M, Downward J.
Mol Cell. 2003 Jan;11(1):11-23.
PMID 12535517
YAP: at the crossroad between transformation and tumor suppression.
Bertini E, Oka T, Sudol M, Strano S, Blandino G.
Cell Cycle. 2009 Jan 1;8(1):49-57. Epub 2009 Jan 24. (REVIEW)
PMID 19106601
YAP1 increases organ size and expands undifferentiated progenitor cells.
Camargo FD, Gokhale S, Johnnidis JB, Fu D, Bell GW, Jaenisch R, Brummelkamp TR.
Curr Biol. 2007 Dec 4;17(23):2054-60. Epub 2007 Nov 1.
PMID 17980593
The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules.
Chen HI, Sudol M.
Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7819-23.
PMID 7644498
Elucidation of a universal size-control mechanism in Drosophila and mammals.
Dong J, Feldmann G, Huang J, Wu S, Zhang N, Comerford SA, Gayyed MF, Anders RA, Maitra A, Pan D.
Cell. 2007 Sep 21;130(6):1120-33.
PMID 17889654
A single point mutation in a group I WW domain shifts its specificity to that of group II WW domains.
Espanel X, Sudol M.
J Biol Chem. 1999 Jun 11;274(24):17284-9.
PMID 10358088
Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-beta/Smad signaling.
Ferrigno O, Lallemand F, Verrecchia F, L'Hoste S, Camonis J, Atfi A, Mauviel A.
Oncogene. 2002 Jul 25;21(32):4879-84.
PMID 12118366
Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II.
Gavva NR, Gavva R, Ermekova K, Sudol M, Shen CJ.
J Biol Chem. 1997 Sep 26;272(39):24105-8.
PMID 9305852
Tumor suppressor LATS1 is a negative regulator of oncogene YAP.
Hao Y, Chun A, Cheung K, Rashidi B, Yang X.
J Biol Chem. 2008 Feb 29;283(9):5496-509. Epub 2007 Dec 24.
PMID 18158288
The Salvador-Warts-Hippo pathway - an emerging tumour-suppressor network.
Harvey K, Tapon N.
Nat Rev Cancer. 2007 Mar;7(3):182-91. (REVIEW)
PMID 17318211
Heterogeneous nuclear ribonuclear protein U associates with YAP and regulates its co-activation of Bax transcription.
Howell M, Borchers C, Milgram SL.
J Biol Chem. 2004 Jun 18;279(25):26300-6. Epub 2004 Apr 19.
PMID 15096513
WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus.
Komuro A, Nagai M, Navin NE, Sudol M.
J Biol Chem. 2003 Aug 29;278(35):33334-41. Epub 2003 Jun 13.
PMID 12807903
PML, YAP, and p73 are components of a proapoptotic autoregulatory feedback loop.
Lapi E, Di Agostino S, Donzelli S, Gal H, Domany E, Rechavi G, Pandolfi PP, Givol D, Strano S, Lu X, Blandino G.
Mol Cell. 2008 Dec 26;32(6):803-14.
PMID 19111660
Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage.
Levy D, Adamovich Y, Reuven N, Shaul Y.
Mol Cell. 2008 Feb 15;29(3):350-61.
PMID 18280240
RASSF1A elicits apoptosis through an MST2 pathway directing proapoptotic transcription by the p73 tumor suppressor protein.
Matallanas D, Romano D, Yee K, Meissl K, Kucerova L, Piazzolla D, Baccarini M, Vass JK, Kolch W, O'neill E.
Mol Cell. 2007 Sep 21;27(6):962-75.
PMID 17889669
Yes-associated protein 65 localizes p62(c-Yes) to the apical compartment of airway epithelia by association with EBP50.
Mohler PJ, Kreda SM, Boucher RC, Sudol M, Stutts MJ, Milgram SL.
J Cell Biol. 1999 Nov 15;147(4):879-90.
PMID 10562288
Transforming properties of YAP, a candidate oncogene on the chromosome 11q22 amplicon.
Overholtzer M, Zhang J, Smolen GA, Muir B, Li W, Sgroi DC, Deng CX, Brugge JS, Haber DA.
Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12405-10. Epub 2006 Aug 7.
PMID 16894141
Hippo signaling in organ size control.
Pan D.
Genes Dev. 2007 Apr 15;21(8):886-97. (REVIEW)
PMID 17437995
The transcriptional coactivator Yes-associated protein drives p73 gene-target specificity in response to DNA Damage.
Strano S, Monti O, Pediconi N, Baccarini A, Fontemaggi G, Lapi E, Mantovani F, Damalas A, Citro G, Sacchi A, Del Sal G, Levrero M, Blandino G.
Mol Cell. 2005 May 13;18(4):447-59.
PMID 15893728
Physical interaction with Yes-associated protein enhances p73 transcriptional activity.
Strano S, Munarriz E, Rossi M, Castagnoli L, Shaul Y, Sacchi A, Oren M, Sudol M, Cesareni G, Blandino G.
J Biol Chem. 2001 May 4;276(18):15164-73. Epub 2001 Jan 24.
PMID 11278685
A gene atlas of the mouse and human protein-encoding transcriptomes.
Su AI, Wiltshire T, Batalov S, Lapp H, Ching KA, Block D, Zhang J, Soden R, Hayakawa M, Kreiman G, Cooke MP, Walker JR, Hogenesch JB.
Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6062-7. Epub 2004 Apr 9.
PMID 15075390
Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain.
Sudol M, Bork P, Einbond A, Kastury K, Druck T, Negrini M, Huebner K, Lehman D.
J Biol Chem. 1995 Jun 16;270(24):14733-41.
PMID 7782338
NeW wrinkles for an old domain.
Sudol M, Hunter T.
Cell. 2000 Dec 22;103(7):1001-4. (REVIEW)
PMID 11163176
Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product.
Sudol M.
Oncogene. 1994 Aug;9(8):2145-52.
PMID 8035999
TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm.
Vassilev A, Kaneko KJ, Shu H, Zhao Y, DePamphilis ML.
Genes Dev. 2001 May 15;15(10):1229-41.
PMID 11358867
A WW domain-containing yes-associated protein (YAP) is a novel transcriptional co-activator.
Yagi R, Chen LF, Shigesada K, Murakami Y, Ito Y.
EMBO J. 1999 May 4;18(9):2551-62.
PMID 10228168
Yes-associated protein (YAP) functions as a tumor suppressor in breast.
Yuan M, Tomlinson V, Lara R, Holliday D, Chelala C, Harada T, Gangeswaran R, Manson-Bishop C, Smith P, Danovi SA, Pardo O, Crook T, Mein CA, Lemoine NR, Jones LJ, Basu S.
Cell Death Differ. 2008 Nov;15(11):1752-9. Epub 2008 Jul 11.
PMID 18617895
EGR-1 forms a complex with YAP-1 and upregulates Bax expression in irradiated prostate carcinoma cells.
Zagurovskaya M, Shareef MM, Das A, Reeves A, Gupta S, Sudol M, Bedford MT, Prichard J, Mohiuddin M, Ahmed MM.
Oncogene. 2009 Feb 26;28(8):1121-31. Epub 2009 Jan 12.
PMID 19137013
Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control.
Zhao B, Wei X, Li W, Udan RS, Yang Q, Kim J, Xie J, Ikenoue T, Yu J, Li L, Zheng P, Ye K, Chinnaiyan A, Halder G, Lai ZC, Guan KL.
Genes Dev. 2007 Nov 1;21(21):2747-61.
PMID 17974916
TEAD mediates YAP-dependent gene induction and growth control.
Zhao B, Ye X, Yu J, Li L, Li W, Li S, Yu J, Lin JD, Wang CY, Chinnaiyan AM, Lai ZC, Guan KL.
Genes Dev. 2008 Jul 15;22(14):1962-71. Epub 2008 Jun 25.
PMID 18579750


This paper should be referenced as such :
Di, Agostino S ; Strano, S ; Blandino, G
YAP1 (Yes-associated protein 1, 65kDa)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(11):1054-1058.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)YAP1   16262
Entrez_Gene (NCBI)YAP1    Yes1 associated transcriptional regulator
AliasesCOB1; YAP; YAP2; YAP65; 
GeneCards (Weizmann)YAP1
Ensembl hg19 (Hinxton)ENSG00000137693 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000137693 [Gene_View]  ENSG00000137693 [Sequence]  chr11:102110447-102233424 [Contig_View]  YAP1 [Vega]
ICGC DataPortalENSG00000137693
TCGA cBioPortalYAP1
AceView (NCBI)YAP1
Genatlas (Paris)YAP1
SOURCE (Princeton)YAP1
Genetics Home Reference (NIH)YAP1
Genomic and cartography
GoldenPath hg38 (UCSC)YAP1  -     chr11:102110447-102233424 +  11q22.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)YAP1  -     11q22.1   [Description]    (hg19-Feb_2009)
GoldenPathYAP1 - 11q22.1 [CytoView hg19]  YAP1 - 11q22.1 [CytoView hg38]
Genome Data Viewer NCBIYAP1 [Mapview hg19]  
OMIM120433   606608   
Gene and transcription
Genbank (Entrez)AA854862 AB567720 AB567721 AI128142 AK300414
RefSeq transcript (Entrez)NM_001130145 NM_001195044 NM_001195045 NM_001282097 NM_001282098 NM_001282099 NM_001282100 NM_001282101 NM_006106
Consensus coding sequences : CCDS (NCBI)YAP1
Gene ExpressionYAP1 [ NCBI-GEO ]   YAP1 [ EBI - ARRAY_EXPRESS ]   YAP1 [ SEEK ]   YAP1 [ MEM ]
Gene Expression Viewer (FireBrowse)YAP1 [ Firebrowse - Broad ]
GenevisibleExpression of YAP1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10413
GTEX Portal (Tissue expression)YAP1
Human Protein AtlasENSG00000137693-YAP1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)YAP1
Human Protein Atlas [tissue]ENSG00000137693-YAP1 [tissue]
Protein Interaction databases
Complex Portal (EBI) CPX-256 YAP1-TEAD1 complex
Ontologies - Pathways
PubMed499 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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