YAP1 (Yes-associated protein 1) is a transcriptional coactivator and the main nuclear effector of the Hippo signaling pathway. It has no DNA-binding domain. An N-terminal TEAD-binding domain lets it bind TEAD1-4 and form a hybrid transcription factor (TEAD supplies the DNA-binding domain, YAP1 the activation domain). Its WW domains bind PPxY motifs in partners such as p73, angiomotins, PTPN14, LATS kinases and WBP2, and a C-terminal transactivation region and PDZ-binding motif complete the protein. When the Hippo kinase cascade is active, LATS1/2 phosphorylate YAP1 on HXRXXS motifs: phospho-S127 binds 14-3-3 and holds YAP1 in the cytoplasm, and a C-terminal phosphodegron targets it for SCF(beta-TrCP)-mediated degradation. Junctional and polarity proteins also sequester YAP1 according to cell density and mechanical cues. Nuclear YAP1-TEAD activates growth-promoting and anti-apoptotic genes (e.g. CTGF) at enhancers shared with AP-1. Through this program YAP1 promotes epithelial and progenitor proliferation, organ growth and regeneration, influences cell-fate choices such as osteogenic versus adipogenic differentiation, and drives oncogenic growth when deregulated. YAP1 also coactivates p73 proapoptotic genes after DNA damage. It is paralogous to WWTR1 (TAZ). Yorkie/YAP coactivators predate animals. The Capsaspora ortholog binds the Capsaspora TEAD ortholog and activates Hippo-responsive transcription in fly cells. In Capsaspora itself it controls cortical cytoskeletal dynamics and aggregate shape but not proliferation. This suggests that TEAD coactivation under Hippo-kinase control is ancestral, while control of proliferation and organ size was acquired in animals.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IMP PMID:25849865 Actin remodelling factors control ciliogenesis by regulating... | UNDECIDED | Summary: Negative regulation of transcription by RNA polymerase II (IMP) from a ciliogenesis study. Reason: Only the abstract of PMID:25849865 is cached; it reports that YAP/TAZ hyperactivation suppresses ciliogenesis but does not describe which genes are repressed. I cannot verify the transcriptional repression the curator recorded. Supporting Evidence: PMID:25849865 knockdown of YAP/TAZ is sufficient to induce ciliogenesis |
| GO:0000976 transcription cis-regulatory region binding | IDA PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | REMOVE | Summary: YAP1 has no DNA-binding domain; it occupies cis-regulatory regions only through DNA-binding partners (p73 in this paper; TEADs genome-wide). Reason: Direct sequence-specific DNA binding is contradicted by the domain structure: TEADs supply the DNA-binding domain and YAP supplies the activation domain [PMID:20368466]. Chromatin occupancy measured by ChIP in PMID:18280240 reflects recruitment by p73, which is captured by GO:0003713 and GO:0140297. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IEA GO_REF:0000107 | REMOVE | Summary: Electronic transfer of sequence-specific Pol II cis-regulatory DNA binding. YAP1 lacks a DNA-binding domain. Reason: Contradicted on biological grounds: YAP is recruited to DNA by TEAD and other DNA-binding factors [PMID:20368466]. Coactivator activity (GO:0003713) is the correct description. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0001894 tissue homeostasis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Tissue homeostasis (IEA). Reason: Consistent with YAP roles in epithelial homeostasis and regeneration [PMID:25731159, PMID:21376238]; non-core, animal-specific. Supporting Evidence: PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation |
| GO:0002009 morphogenesis of an epithelium | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Morphogenesis of an epithelium (ARBA). Reason: Plausible developmental role in animals; non-core. |
| GO:0003015 heart process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Heart process (IEA): a circulatory process carried out by the heart, such as contraction. Reason: YAP controls cardiomyocyte proliferation and heart growth/regeneration, not cardiac physiological processes; those roles are captured by the cardiac proliferation and regeneration rows. |
| GO:0003682 chromatin binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Chromatin binding (IEA). YAP1 associates with chromatin at TEAD/AP-1 enhancers, but indirectly through its DNA-binding partners. Reason: Not wrong as a statement of chromatin association, but YAP has no chromatin-binding domain and the association depends on TEAD [PMID:20368466, PMID:18579750]. The coactivator term captures the function better. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0003712 transcription coregulator activity | IDA PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | ACCEPT | Summary: Transcription coregulator activity; correct parent of the coactivator activity that is YAP1's core function. Reason: LATS1 phosphorylation suppresses YAP's regulation of target genes by cytoplasmic sequestration [PMID:18158288]. This is the term used for YAP1 in the Reactome-derived Hippo GO-CAMs; the more specific GO:0003713 is also annotated. Supporting Evidence: PMID:18158288 LATS1 inactivates YAP oncogenic function by suppressing its transcription regulation of cellular genes via sequestration of YAP in the cytoplasm after phosphorylation of YAP |
| GO:0003713 transcription coactivator activity | IBA GO_REF:0000033 | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:16772533 WW domain binding protein-2, an E6-associated protein intera... | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:16772533 YAP's coactivation function is absolutely dependent on WBP-2 PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:18158288 LATS1 inactivates YAP oncogenic function by suppressing its transcription regulation of cellular genes via sequestration of YAP in the cytoplasm after phosphorylation of YAP PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:20368466 Structural and functional analysis of the YAP-binding domain... | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:25796446 Aerobic glycolysis tunes YAP/TAZ transcriptional activity. | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:25796446 binds the YAP/TAZ transcriptional cofactors TEADs and promotes their functional and biochemical cooperation with YAP/TAZ PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IDA PMID:27380321 ZDHHC7-mediated S-palmitoylation of Scribble regulates cell ... | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:27380321 Knockout of ZDHHC7 led to SCRIB mislocalization and YAP activation PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IEA GO_REF:0000120 | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003713 transcription coactivator activity | IMP PMID:20123905 Structural insights into the YAP and TEAD complex. | ACCEPT | Summary: YAP1 is a transcriptional coactivator: it has a transactivation domain but no DNA-binding domain and is recruited to target genes by DNA-binding partners, chiefly TEAD1-4 (also p73, RUNX, SMADs). Reason: Core molecular function, supported by structural, biochemical and reporter evidence [PMID:20368466, PMID:18579750, PMID:20123905]. The coactivator/TEAD partnership is ancestral: Capsaspora coYki binds Capsaspora Sd/TEAD and activates a Hippo-responsive reporter [PMID:22832104]. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression PMID:22832104 co-expression of Co-Sd and Co-Yki stimulated the transcription of the HRE-luciferase reporter in Drosophila S2R+ cells |
| GO:0003714 transcription corepressor activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Transcription corepressor activity. YAP-TEAD complexes also repress some target genes, but repression is a secondary, context-dependent output of a protein that is mainly a coactivator. Reason: Kept as non-core. The IBA reflects a PAINT judgment on the YAP/TAZ/Yorkie clade and the IDA was made by curators from the full text of PMID:18158288 (abstract only cached; the abstract reports genes both up- and down-regulated by YAP). Not core: the primary activity is coactivation. Supporting Evidence: PMID:18158288 LATS1 inactivates YAP oncogenic function by suppressing its transcription regulation of cellular genes via sequestration of YAP in the cytoplasm after phosphorylation of YAP |
| GO:0003714 transcription corepressor activity | IDA PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | KEEP AS NON CORE | Summary: Transcription corepressor activity. YAP-TEAD complexes also repress some target genes, but repression is a secondary, context-dependent output of a protein that is mainly a coactivator. Reason: Kept as non-core. The IBA reflects a PAINT judgment on the YAP/TAZ/Yorkie clade and the IDA was made by curators from the full text of PMID:18158288 (abstract only cached; the abstract reports genes both up- and down-regulated by YAP). Not core: the primary activity is coactivation. Supporting Evidence: PMID:18158288 LATS1 inactivates YAP oncogenic function by suppressing its transcription regulation of cellular genes via sequestration of YAP in the cytoplasm after phosphorylation of YAP |
| GO:0005515 protein binding | IPI PMID:11278422 Yes-associated protein and p53-binding protein-2 interact th... | REMOVE | Summary: Protein binding (IPI) with TP53BP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:11278685 Physical interaction with Yes-associated protein enhances p7... | MODIFY | Summary: Protein binding (IPI) with TP73, TP63, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:11278685 The WW domain of YAP and the PPPPY motif of p73 are directly involved in the association |
| GO:0005515 protein binding | IPI PMID:11278685 Physical interaction with Yes-associated protein enhances p7... | MODIFY | Summary: Protein binding (IPI) with TP73, TP63, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:11278685 The WW domain of YAP and the PPPPY motif of p73 are directly involved in the association |
| GO:0005515 protein binding | IPI PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 1... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAZ), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:16166090 NHERF2/SIP-1 interacts with mouse SRY via a different mechan... | REMOVE | Summary: Protein binding (IPI) with NHERF2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:17502622 Proline-rich Gla protein 2 is a cell-surface vitamin K-depen... | REMOVE | Summary: Protein binding (IPI) with PRRG2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:17974916 Inactivation of YAP oncoprotein by the Hippo pathway is invo... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB), from a targeted study. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | REMOVE | Summary: Protein binding (IPI) with LATS1, LATS2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | REMOVE | Summary: Protein binding (IPI) with LATS1, LATS2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | MODIFY | Summary: Protein binding (IPI) with TP73, RUNX1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes |
| GO:0005515 protein binding | IPI PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | MODIFY | Summary: Protein binding (IPI) with TP73, RUNX1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes |
| GO:0005515 protein binding | IPI PMID:18579750 TEAD mediates YAP-dependent gene induction and growth contro... | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD4, TEAD2, TEAD3, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression |
| GO:0005515 protein binding | IPI PMID:18579750 TEAD mediates YAP-dependent gene induction and growth contro... | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD4, TEAD2, TEAD3, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression |
| GO:0005515 protein binding | IPI PMID:18579750 TEAD mediates YAP-dependent gene induction and growth contro... | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD4, TEAD2, TEAD3, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression |
| GO:0005515 protein binding | IPI PMID:18579750 TEAD mediates YAP-dependent gene induction and growth contro... | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD4, TEAD2, TEAD3, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression |
| GO:0005515 protein binding | IPI PMID:19439659 Scribble participates in Hippo signaling and is required for... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB), from a targeted study. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:19914168 Nuclear CDKs drive Smad transcriptional activation and turno... | MODIFY | Summary: Protein binding (IPI) with SMAD1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:19914168 Smad1 is mediated by the recruitment of YAP to the phosphorylated linker sites |
| GO:0005515 protein binding | IPI PMID:20048001 A coordinated phosphorylation by Lats and CK1 regulates YAP ... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB), from a targeted study. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:20368466 Structural and functional analysis of the YAP-binding domain... | MODIFY | Summary: Protein binding (IPI) with TEAD2, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:21187284 Angiomotin-like proteins associate with and negatively regul... | REMOVE | Summary: Protein binding (IPI) with AMOT, AMOTL1, AMOTL2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0005515 protein binding | IPI PMID:21187284 Angiomotin-like proteins associate with and negatively regul... | REMOVE | Summary: Protein binding (IPI) with AMOT, AMOTL1, AMOTL2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0005515 protein binding | IPI PMID:21187284 Angiomotin-like proteins associate with and negatively regul... | REMOVE | Summary: Protein binding (IPI) with AMOT, AMOTL1, AMOTL2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0005515 protein binding | IPI PMID:21205866 Angiomotin is a novel Hippo pathway component that inhibits ... | REMOVE | Summary: Protein binding (IPI) with AMOT, AMOTL2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:21205866 Angiomotin is a novel Hippo pathway component that inhibits ... | REMOVE | Summary: Protein binding (IPI) with AMOT, AMOTL2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:21376238 Yap1 acts downstream of Ξ±-catenin to control epidermal proli... | REMOVE | Summary: Protein binding (IPI) with CTNNB1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: Protein binding (IPI) with BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:22234184 A molecular mechanism that links Hippo signalling to the inh... | REMOVE | Summary: Protein binding (IPI) with CTNNB1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:22525271 PTPN14 interacts with and negatively regulates the oncogenic... | REMOVE | Summary: Protein binding (IPI) with PTPN14, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. Supporting Evidence: PMID:22525271 through the WW domain of YAP and the PPxY domain of PTPN14 |
| GO:0005515 protein binding | IPI PMID:22863277 Regulation of the Hippo-YAP pathway by G-protein-coupled rec... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:22863277 Regulation of the Hippo-YAP pathway by G-protein-coupled rec... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:22921829 Structural basis for the versatile interactions of Smad7 wit... | REMOVE | Summary: Protein binding (IPI) with SMAD7, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:22948661 PTPN14 is required for the density-dependent control of YAP1... | REMOVE | Summary: Protein binding (IPI) with PTPN14, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:23245941 Ξ²-Catenin-driven cancers require a YAP1 transcriptional comp... | REMOVE | Summary: Protein binding (IPI) with CTNNB1, TBX5, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:23245941 Ξ²-Catenin-driven cancers require a YAP1 transcriptional comp... | REMOVE | Summary: Protein binding (IPI) with CTNNB1, TBX5, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:23873930 Cellular localization and characterization of cytosolic bind... | REMOVE | Summary: Protein binding (IPI) with PRRG4, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24211253 MEK1 promotes YAP and their interaction is critical for tumo... | REMOVE | Summary: Protein binding (IPI) with MAP2K1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24255178 Protein interaction network of the mammalian Hippo pathway r... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, TEAD1, YWHAB, YWHAE, YWHAZ, NHERF2, PTPN14, PATJ, PARD3, WBP2, LIN7C, TJP2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Protein binding (IPI) with MPDZ, LATS1, YWHAB, YWHAE, PTPN14, PATJ, RAPGEF6, WBP2, LIN7C, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24525233 A peptide mimicking VGLL4 function acts as a YAP antagonist ... | MODIFY | Summary: Protein binding (IPI) with TEAD4, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:24581491 Hippo signaling regulates microprocessor and links cell-dens... | REMOVE | Summary: Protein binding (IPI) with TEAD1, DDX17, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24581491 Hippo signaling regulates microprocessor and links cell-dens... | REMOVE | Summary: Protein binding (IPI) with TEAD1, DDX17, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:24882516 Mutant Gq/11 promote uveal melanoma tumorigenesis by activat... | MODIFY | Summary: Protein binding (IPI) with TEAD1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:24976009 YAP/TAZ incorporation in the Ξ²-catenin destruction complex o... | REMOVE | Summary: Protein binding (IPI) with AXIN1, mouse Axin1, CTNNB1, BTRC, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24976009 YAP/TAZ incorporation in the Ξ²-catenin destruction complex o... | REMOVE | Summary: Protein binding (IPI) with AXIN1, mouse Axin1, CTNNB1, BTRC, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24976009 YAP/TAZ incorporation in the Ξ²-catenin destruction complex o... | REMOVE | Summary: Protein binding (IPI) with AXIN1, mouse Axin1, CTNNB1, BTRC, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:24976009 YAP/TAZ incorporation in the Ξ²-catenin destruction complex o... | REMOVE | Summary: Protein binding (IPI) with AXIN1, mouse Axin1, CTNNB1, BTRC, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:25180228 Opposing activities of the Ras and Hippo pathways converge o... | REMOVE | Summary: Protein binding (IPI) with SOCS6, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25283809 Ligand binding to WW tandem domains of YAP2 transcriptional ... | REMOVE | Summary: Protein binding (IPI) with PRRG2, SMAD7, TP73, LATS1, RUNX1, PTCH1, ERBB4, PTPN14, WBP2, WBP1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25670079 14-3-3ΞΆ turns TGF-Ξ²'s function from tumor suppressor to meta... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAZ), from a targeted study. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:25731159 A gp130-Src-YAP module links inflammation to epithelial rege... | REMOVE | Summary: Protein binding (IPI) with SRC, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751139 AMPK modulates Hippo pathway activity to regulate energy hom... | REMOVE | Summary: Protein binding (IPI) with LATS1, TEAD1, YWHAE, PRKAA1, TEAD4, TEAD2, PTPN14, mouse Prkaa1, WBP2, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751140 Cellular energy stress induces AMPK-mediated regulation of Y... | REMOVE | Summary: Protein binding (IPI) with TEAD1, PRKAA1, TEAD4, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751140 Cellular energy stress induces AMPK-mediated regulation of Y... | REMOVE | Summary: Protein binding (IPI) with TEAD1, PRKAA1, TEAD4, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25751140 Cellular energy stress induces AMPK-mediated regulation of Y... | REMOVE | Summary: Protein binding (IPI) with TEAD1, PRKAA1, TEAD4, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:25796446 Aerobic glycolysis tunes YAP/TAZ transcriptional activity. | MODIFY | Summary: Protein binding (IPI) with PFKM, TEAD1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:25796446 binds the YAP/TAZ transcriptional cofactors TEADs and promotes their functional and biochemical cooperation with YAP/TAZ |
| GO:0005515 protein binding | IPI PMID:26258633 Genome-wide association between YAP/TAZ/TEAD andΒ AP-1 at enh... | MODIFY | Summary: Protein binding (IPI) with TEAD1, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:26592798 Targeting the Central Pocket in Human Transcription Factor T... | MODIFY | Summary: Protein binding (IPI) with TEAD4, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Protein binding (IPI) with NHERF2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:28468127 Rab11a promotes proliferation and invasion through regulatio... | REMOVE | Summary: Protein binding (IPI) with RAB11A, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAZ), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | REMOVE | Summary: Protein binding (IPI) with SCRIB, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | REMOVE | Summary: Protein binding (IPI) with SCRIB, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:30865227 Citron kinase interacts with LATS2 and inhibits its activity... | REMOVE | Summary: Protein binding (IPI) with CIT, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:31835537 Evidence for the Desmosomal Cadherin Desmoglein-3 in Regulat... | REMOVE | Summary: Protein binding (IPI) with DSG3, YWHAG, PKP1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. Supporting Evidence: PMID:31835537 Dsg3 formed a complex with phospho-YAP and sequestered it to the plasma membrane |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: Protein binding (IPI) with TEAD2, from a high-throughput/proteome-scale screen. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with MPDZ, YWHAB, YWHAZ, TEAD4, TEAD2, NHERF2, PTPN14, PRRG4, BTRC, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: Protein binding (IPI) with TP73, LATS1, TMEM139, WBP1, TRERF1, PRRG4, TP63, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:35140242 Human transcription factor protein interaction networks. | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD2, from a high-throughput/proteome-scale screen. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:35140242 Human transcription factor protein interaction networks. | MODIFY | Summary: Protein binding (IPI) with TEAD1, TEAD2, from a high-throughput/proteome-scale screen. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB, YWHAE), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB, YWHAE), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: Protein binding (IPI) with GRID2IP, MPDZ, DLG4, APBA1, DLG1, IL16, SCRIB, NHERF2, DLG2, PDZK1, FRMPD2, MAGI2, NHERF4, LNX2, PATJ, LNX1, RAPGEF6, PARD3, DLG3, APBA2, GRIP2, LIN7C, WHRN, TJP2, GRIP1, SHANK1, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB, YWHAE, YWHAZ), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB, YWHAE, YWHAZ), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | MODIFY | Summary: Protein binding (IPI) with 14-3-3 protein(s) (YWHAB, YWHAE, YWHAZ), from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative. Binding of 14-3-3 to LATS-phosphorylated S127 retains YAP1 in the cytoplasm and is a central Hippo-pathway inhibitory mechanism [PMID:20048001]. Replace with 14-3-3 protein binding. Proposed replacements: 14-3-3 protein binding Supporting Evidence: PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005515 protein binding | IPI PMID:36959122 YAP and Ξ²-catenin cooperate to drive H. pylori-induced gastr... | REMOVE | Summary: Protein binding (IPI) with CTNNB1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:37100772 Large-scale phage-based screening reveals extensive pan-vira... | REMOVE | Summary: Protein binding (IPI) with rabies virus M, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: Protein binding (IPI) with TP73, TRERF1, PRRG4, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: Protein binding (IPI) with TP73, TRERF1, PRRG4, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: Protein binding (IPI) with TP73, TRERF1, PRRG4, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: Protein binding (IPI) with TP73, TRERF1, PRRG4, UVRAG, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding (IPI) with YWHAB, TEAD4, NHERF2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding (IPI) with YWHAB, TEAD4, NHERF2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding (IPI) with YWHAB, TEAD4, NHERF2, from a high-throughput/proteome-scale screen. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. TEAD or other transcription-factor partners reported in this paper are covered by GO:0140297. |
| GO:0005515 protein binding | IPI PMID:7644498 The WW domain of Yes-associated protein binds a proline-rich... | REMOVE | Summary: Protein binding (IPI) with mouse Wbp1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:9202023 Characterization of the WW domain of human yes-associated pr... | REMOVE | Summary: Protein binding (IPI) with mouse Wbp1, from a targeted study. Reason: Generic protein binding is uninformative, so the row is removed. This does not mean the interaction is false. Many of these partners (LATS kinases, angiomotins, PTPN14, WBP proteins, PDZ and junction proteins, beta-catenin, SMAD7) bind YAP1 through its WW domains or C-terminal PDZ-binding motif and regulate YAP1 localization or stability. Those binding modes are captured by GO:0070064 proline-rich region binding, and the regulatory outcome by the hippo signaling and localization rows. |
| GO:0005515 protein binding | IPI PMID:9305852 Interaction of WW domains with hematopoietic transcription f... | MODIFY | Summary: Protein binding (IPI) with NFE2, from a targeted study. The partners are DNA-binding transcription factors that recruit YAP1 as a coactivator. Reason: Generic protein binding is uninformative. These interactions are YAP1's core mechanism: as a coactivator without a DNA-binding domain it binds sequence-specific transcription factors (TEADs via its TEAD-binding domain; p73/p63/NF-E2/SMAD1 via its WW domains) [PMID:20368466, PMID:11278685]. Replace with DNA-binding transcription factor binding. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005634 nucleus | EXP PMID:20048001 A coordinated phosphorylation by Lats and CK1 regulates YAP ... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:22525271 PTPN14 interacts with and negatively regulates the oncogenic... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:26598551 Role of Angiomotin-like 2 mono-ubiquitination on YAP inhibit... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:29695716 Regulation of Yki/Yap subcellular localization and Hpo signa... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:30447097 Identification of genes involved in the regulation of TERT i... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:34404733 AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibiti... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | EXP PMID:38512451 The alanyl-tRNA synthetase AARS1 moonlights as a lactyltrans... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:17974916 Inactivation of YAP oncoprotein by the Hippo pathway is invo... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:20868367 Functional complexes between YAP2 and ZO-2 are PDZ domain-de... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:21145499 The Crumbs complex couples cell density sensing to Hippo-dep... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:21205866 Angiomotin is a novel Hippo pathway component that inhibits ... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:25796446 Aerobic glycolysis tunes YAP/TAZ transcriptional activity. | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:25849865 Actin remodelling factors control ciliogenesis by regulating... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:28169360 Loss of DLG5 promotes breast cancer malignancy by inhibiting... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:29400695 Claudin-18-mediated YAP activity regulates lung stem and pro... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:30865227 Citron kinase interacts with LATS2 and inhibits its activity... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:31835537 Evidence for the Desmosomal Cadherin Desmoglein-3 in Regulat... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:35429439 WWC proteins mediate LATS1/2 activation by Hippo kinases and... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IDA PMID:41511042 Keratin 15 promotes a progenitor cell state in basal keratin... | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Nucleus. Unphosphorylated YAP1 enters the nucleus to coactivate TEAD and other factors; nuclear/cytoplasmic partitioning is the main way the Hippo pathway regulates it. Reason: Localization is supported by many independent studies [PMID:17974916, PMID:20868367, PMID:21145499]. Nuclear entry of a Yorkie ortholog when its upstream kinases are lost is also seen in Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20868367 The endogenous ZO-2 and YAP2 proteins co-localize in the nucleus |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1254248 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2032770 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2032775 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2064406 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8871260 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8871265 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8871266 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8951676 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8951695 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956639 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956649 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956659 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956676 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9618559 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9865176 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9909654 | ACCEPT | Summary: Nucleoplasm, where YAP1 acts with TEADs (HPA immunofluorescence and Reactome). Reason: Consistent with YAP1 function as a nuclear transcriptional coactivator. |
| GO:0005667 transcription regulator complex | IEA GO_REF:0000107 | ACCEPT | Summary: Transcription regulator complex; parent of the TEAD-YAP complex. Reason: Consistent with YAP1 forming heterodimeric transcription factors with TEADs [PMID:20368466]. Supporting Evidence: PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0005730 nucleolus | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Nucleolus, from Human Protein Atlas immunofluorescence. Reason: No functional link between YAP1 and the nucleolus is established in the literature I reviewed; kept as an experimental observation, not core. |
| GO:0005737 cytoplasm | EXP PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | EXP PMID:20048001 A coordinated phosphorylation by Lats and CK1 regulates YAP ... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | EXP PMID:22525271 PTPN14 interacts with and negatively regulates the oncogenic... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | EXP PMID:26598551 Role of Angiomotin-like 2 mono-ubiquitination on YAP inhibit... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | EXP PMID:29695716 Regulation of Yki/Yap subcellular localization and Hpo signa... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | EXP PMID:34404733 AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibiti... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:17974916 Inactivation of YAP oncoprotein by the Hippo pathway is invo... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:21205866 Angiomotin is a novel Hippo pathway component that inhibits ... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:25849865 Actin remodelling factors control ciliogenesis by regulating... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:29400695 Claudin-18-mediated YAP activity regulates lung stem and pro... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:31835537 Evidence for the Desmosomal Cadherin Desmoglein-3 in Regulat... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IDA PMID:41511042 Keratin 15 promotes a progenitor cell state in basal keratin... | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasm. LATS-phosphorylated YAP1 is held in the cytoplasm by 14-3-3, angiomotins and other partners. Reason: Cytoplasmic sequestration is the main inhibitory mechanism [PMID:17974916, PMID:18158288, PMID:20048001]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | IDA PMID:30865227 Citron kinase interacts with LATS2 and inhibits its activity... | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1254248 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1254251 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2028583 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2028598 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2028644 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2028724 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2032770 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2064406 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2064421 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9865176 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9865196 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9865226 | ACCEPT | Summary: Cytosol; the soluble cytoplasmic pool of phosphorylated YAP1 (HPA, Reactome, IDA). Reason: Consistent with cytoplasmic retention after LATS phosphorylation [PMID:17974916]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein |
| GO:0005886 plasma membrane | IDA PMID:31835537 Evidence for the Desmosomal Cadherin Desmoglein-3 in Regulat... | KEEP AS NON CORE | Summary: Plasma membrane. A fraction of phospho-YAP is held at the plasma membrane by junctional partners such as desmoglein-3. Reason: Supported by PMID:31835537; a site of inhibition rather than of function. Supporting Evidence: PMID:31835537 Dsg3 formed a complex with phospho-YAP and sequestered it to the plasma membrane |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Plasma membrane. A fraction of phospho-YAP is held at the plasma membrane by junctional partners such as desmoglein-3. Reason: Supported by PMID:31835537; a site of inhibition rather than of function. Supporting Evidence: PMID:31835537 Dsg3 formed a complex with phospho-YAP and sequestered it to the plasma membrane |
| GO:0005911 cell-cell junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell-cell junction. YAP1 is recruited to junctions by angiomotins, alpha-catenin and ZO-2. Reason: Junctional sequestration is an inhibitory mechanism, part of how cell density is sensed [PMID:21187284, PMID:21145499]. Non-core. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0005911 cell-cell junction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cell-cell junction. YAP1 is recruited to junctions by angiomotins, alpha-catenin and ZO-2. Reason: Junctional sequestration is an inhibitory mechanism, part of how cell density is sensed [PMID:21187284, PMID:21145499]. Non-core. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0005923 bicellular tight junction | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Bicellular tight junction (UniProt subcellular location mapping). Reason: Reflects recruitment by tight-junction partners such as ZO-2 and angiomotins [PMID:20868367, PMID:21187284]. Non-core. Supporting Evidence: PMID:21187284 We demonstrate that AMOTL1 and AMOTL2 can regulate YAP1 cytoplasm-to-nucleus translocation through direct protein-protein interaction |
| GO:0006974 DNA damage response | IDA PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | KEEP AS NON CORE | Summary: DNA damage response: after DNA damage, c-Abl phosphorylates YAP1 Y357, and YAP1 coactivates p73 proapoptotic genes. Reason: Supported by PMID:18280240; a context-specific use of the coactivator, not core. Supporting Evidence: PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes |
| GO:0010628 positive regulation of gene expression | IMP PMID:29403552 Downregulation of YAP inhibits proliferation and induces apo... | KEEP AS NON CORE | Summary: Positive regulation of gene expression (IMP) from YAP knockdown in an esophageal cancer line. Reason: Correct but generic, and from a single cancer cell line; the specific coactivation process is covered by GO:0045944. Supporting Evidence: PMID:29403552 YAP gene inhibition suppresses the proliferation and induces apoptosis in ECA-109 cells |
| GO:0010629 negative regulation of gene expression | IMP PMID:29403552 Downregulation of YAP inhibits proliferation and induces apo... | MARK AS OVER ANNOTATED | Summary: Negative regulation of gene expression (IMP): YAP knockdown raised p53 and caspase-3 levels in Eca-109 cells. Reason: An indirect consequence of knockdown in one cancer line, not a demonstrated repressive activity of YAP1. Supporting Evidence: PMID:29403552 YAP gene inhibition suppresses the proliferation and induces apoptosis in ECA-109 cells |
| GO:0010838 positive regulation of keratinocyte proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of keratinocyte proliferation (transferred from mouse). Reason: Yap1 controls epidermal stem/progenitor proliferation through TEAD in mouse skin [PMID:21376238]; also modelled in the KRT14/KRT15 GO-CAMs. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0010838 positive regulation of keratinocyte proliferation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of keratinocyte proliferation (transferred from mouse). Reason: Yap1 controls epidermal stem/progenitor proliferation through TEAD in mouse skin [PMID:21376238]; also modelled in the KRT14/KRT15 GO-CAMs. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0016020 membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Membrane (IEA). Uninformative, but consistent with the junction- and membrane-bound pools of YAP1. Reason: Kept as non-core; see the plasma membrane and cell-cell junction rows [PMID:31835537]. Supporting Evidence: PMID:31835537 Dsg3 formed a complex with phospho-YAP and sequestered it to the plasma membrane |
| GO:0030307 positive regulation of cell growth | IDA PMID:17974916 Inactivation of YAP oncoprotein by the Hippo pathway is invo... | KEEP AS NON CORE | Summary: Positive regulation of cell growth. In these papers 'growth' means proliferation, anchorage-independent growth and transformation, not cell size. Reason: Experimentally supported [PMID:17974916, PMID:18579750] and kept, but a downstream outcome of TEAD coactivation, and the 'cell growth' wording slightly misstates it. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:18579750 TEAD is also required for YAP-induced cell growth, oncogenic transformation, and epithelial-mesenchymal transition PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0030307 positive regulation of cell growth | IDA PMID:18579750 TEAD mediates YAP-dependent gene induction and growth contro... | KEEP AS NON CORE | Summary: Positive regulation of cell growth. In these papers 'growth' means proliferation, anchorage-independent growth and transformation, not cell size. Reason: Experimentally supported [PMID:17974916, PMID:18579750] and kept, but a downstream outcome of TEAD coactivation, and the 'cell growth' wording slightly misstates it. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:18579750 TEAD is also required for YAP-induced cell growth, oncogenic transformation, and epithelial-mesenchymal transition PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0030859 polarized epithelial cell differentiation | IC PMID:27380321 ZDHHC7-mediated S-palmitoylation of Scribble regulates cell ... | KEEP AS NON CORE | Summary: Polarized epithelial cell differentiation (IC). In PMID:27380321, SCRIB palmitoylation controls polarity and SCRIB mislocalization activates YAP; YAP coactivator activity is part of the curator's GO-CAM model 62900b6400001749 for this process. Reason: YAP1 is a downstream read-out of polarity in this work, not a demonstrated effector of polarized differentiation. Kept as non-core in deference to the curated model. Supporting Evidence: PMID:27380321 Knockout of ZDHHC7 led to SCRIB mislocalization and YAP activation |
| GO:0032570 response to progesterone | IDA PMID:16772533 WW domain binding protein-2, an E6-associated protein intera... | KEEP AS NON CORE | Summary: Response to progesterone: YAP enhances progesterone-receptor transactivation, dependent on WBP2. Reason: Supported by PMID:16772533 (abstract); a peripheral coactivator role. Supporting Evidence: PMID:16772533 YAP's coactivation function is absolutely dependent on WBP-2 |
| GO:0035265 organ growth | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Organ growth (transferred from mouse). YAP drives organ growth, e.g. liver and heart, as the Hippo effector. Reason: Well established in animals [PMID:21808241]. YAP regulates organ growth rather than performing it; GO:0046620 regulation of organ growth would be more precise. Organ-size control is an animal-specific role: the Capsaspora ortholog does not control proliferation [PMID:35659869, PMID:38729842]. Supporting Evidence: PMID:21808241 Extensive research led to the identification of the Hippo tumour-suppressor pathway as a key regulator of organ size in Drosophila and mammals PMID:38729842 We describe new evidence indicating that the ancestral function of this pathway was not regulation of proliferation, but of cytoskeletal dynamics, and that this pathway function predated the emergence of animals |
| GO:0035265 organ growth | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Organ growth (transferred from mouse). YAP drives organ growth, e.g. liver and heart, as the Hippo effector. Reason: Well established in animals [PMID:21808241]. YAP regulates organ growth rather than performing it; GO:0046620 regulation of organ growth would be more precise. Organ-size control is an animal-specific role: the Capsaspora ortholog does not control proliferation [PMID:35659869, PMID:38729842]. Supporting Evidence: PMID:21808241 Extensive research led to the identification of the Hippo tumour-suppressor pathway as a key regulator of organ size in Drosophila and mammals PMID:38729842 We describe new evidence indicating that the ancestral function of this pathway was not regulation of proliferation, but of cytoskeletal dynamics, and that this pathway function predated the emergence of animals |
| GO:0035329 hippo signaling | IBA GO_REF:0000033 | ACCEPT | Summary: YAP1 is the terminal transcriptional effector of hippo signaling; the GO definition names YAP1 phosphorylation by LATS1/2 as part of the pathway. Reason: Phosphorylation by LATS1/2 on HXRXXS motifs causes 14-3-3 binding and cytoplasmic retention, and later degradation [PMID:17974916, PMID:20048001, PMID:18158288]. Kinase-cascade regulation of a Yorkie ortholog by cytoplasmic sequestration is shared with Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0035329 hippo signaling | IDA PMID:35429439 WWC proteins mediate LATS1/2 activation by Hippo kinases and... | ACCEPT | Summary: YAP1 is the terminal transcriptional effector of hippo signaling; the GO definition names YAP1 phosphorylation by LATS1/2 as part of the pathway. Reason: Phosphorylation by LATS1/2 on HXRXXS motifs causes 14-3-3 binding and cytoplasmic retention, and later degradation [PMID:17974916, PMID:20048001, PMID:18158288]. Kinase-cascade regulation of a Yorkie ortholog by cytoplasmic sequestration is shared with Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0035329 hippo signaling | IEA GO_REF:0000117 | ACCEPT | Summary: YAP1 is the terminal transcriptional effector of hippo signaling; the GO definition names YAP1 phosphorylation by LATS1/2 as part of the pathway. Reason: Phosphorylation by LATS1/2 on HXRXXS motifs causes 14-3-3 binding and cytoplasmic retention, and later degradation [PMID:17974916, PMID:20048001, PMID:18158288]. Kinase-cascade regulation of a Yorkie ortholog by cytoplasmic sequestration is shared with Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0035329 hippo signaling | NAS PMID:21808241 The Hippo pathway in organ size control, tissue regeneration... | ACCEPT | Summary: YAP1 is the terminal transcriptional effector of hippo signaling; the GO definition names YAP1 phosphorylation by LATS1/2 as part of the pathway. Reason: Phosphorylation by LATS1/2 on HXRXXS motifs causes 14-3-3 binding and cytoplasmic retention, and later degradation [PMID:17974916, PMID:20048001, PMID:18158288]. Kinase-cascade regulation of a Yorkie ortholog by cytoplasmic sequestration is shared with Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0035329 hippo signaling | TAS PMID:18158288 Tumor suppressor LATS1 is a negative regulator of oncogene Y... | ACCEPT | Summary: YAP1 is the terminal transcriptional effector of hippo signaling; the GO definition names YAP1 phosphorylation by LATS1/2 as part of the pathway. Reason: Phosphorylation by LATS1/2 on HXRXXS motifs causes 14-3-3 binding and cytoplasmic retention, and later degradation [PMID:17974916, PMID:20048001, PMID:18158288]. Kinase-cascade regulation of a Yorkie ortholog by cytoplasmic sequestration is shared with Capsaspora [PMID:38517944]. Supporting Evidence: PMID:17974916 Phosphorylation by the Lats tumor suppressor kinase leads to cytoplasmic translocation and inactivation of the YAP oncoprotein PMID:20048001 which results in YAP 14-3-3 binding and cytoplasmic retention |
| GO:0035331 negative regulation of hippo signaling | IDA PMID:35429439 WWC proteins mediate LATS1/2 activation by Hippo kinases and... | UNDECIDED | Summary: Negative regulation of hippo signaling (IDA, PMID:35429439). The paper concerns WWC proteins organizing MST1/2-SAV1-LATS1/2 activation; YAP/TAZ are the read-out. Reason: Only the abstract is cached, and it presents YAP/TAZ as the effectors repressed by LATS1/2, not as regulators of the cascade. YAP-TEAD does feed back on the pathway (e.g. by inducing pathway components), but I cannot see which experiment the curator used, so I neither accept nor remove. Supporting Evidence: PMID:35429439 The activity of YAP/TAZ is strictly repressed upon phosphorylation by LATS1/2 tumor suppressors |
| GO:0042060 wound healing | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Wound healing (IEA). Reason: gp130-Src-YAP signalling promotes mucosal healing [PMID:25731159]; non-core. Supporting Evidence: PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation |
| GO:0045599 negative regulation of fat cell differentiation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Negative regulation of fat cell differentiation. Kindlin-2 controls MSC fate through YAP1/TAZ; YAP1/TAZ loss favours adipogenesis. Reason: Supported by PMID:29496737 (YAP1 and TAZ studied together); a cell-fate output of mechanotransduction, not core. Supporting Evidence: PMID:29496737 kindlin-2 regulates MSC differentiation through controlling YAP1/TAZ at both the transcript and protein levels |
| GO:0045599 negative regulation of fat cell differentiation | IMP PMID:29496737 Kindlin-2 regulates mesenchymal stem cell differentiation th... | KEEP AS NON CORE | Summary: Negative regulation of fat cell differentiation. Kindlin-2 controls MSC fate through YAP1/TAZ; YAP1/TAZ loss favours adipogenesis. Reason: Supported by PMID:29496737 (YAP1 and TAZ studied together); a cell-fate output of mechanotransduction, not core. Supporting Evidence: PMID:29496737 kindlin-2 regulates MSC differentiation through controlling YAP1/TAZ at both the transcript and protein levels |
| GO:0045669 positive regulation of osteoblast differentiation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Positive regulation of osteoblast differentiation, from the same kindlin-2/YAP1-TAZ study. Reason: As for GO:0045599 [PMID:29496737]. Supporting Evidence: PMID:29496737 kindlin-2 regulates MSC differentiation through controlling YAP1/TAZ at both the transcript and protein levels |
| GO:0045669 positive regulation of osteoblast differentiation | IMP PMID:29496737 Kindlin-2 regulates mesenchymal stem cell differentiation th... | KEEP AS NON CORE | Summary: Positive regulation of osteoblast differentiation, from the same kindlin-2/YAP1-TAZ study. Reason: As for GO:0045599 [PMID:29496737]. Supporting Evidence: PMID:29496737 kindlin-2 regulates MSC differentiation through controlling YAP1/TAZ at both the transcript and protein levels |
| GO:0045747 positive regulation of Notch signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of Notch signaling (IEA). Reason: YAP and Notch act together downstream of gp130 in intestinal regeneration [PMID:25731159]; non-core. Supporting Evidence: PMID:25731159 gp130, a co-receptor for IL-6 cytokines, triggers activation of YAP and Notch |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:20368466 Structural and functional analysis of the YAP-binding domain... | ACCEPT | Summary: Positive regulation of DNA-templated transcription; correct, slightly less specific than GO:0045944. Reason: Supported by the YAP-TEAD structural and functional studies [PMID:20368466, PMID:20123905]. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0045893 positive regulation of DNA-templated transcription | IEA GO_REF:0000107 | ACCEPT | Summary: Positive regulation of DNA-templated transcription; correct, slightly less specific than GO:0045944. Reason: Supported by the YAP-TEAD structural and functional studies [PMID:20368466, PMID:20123905]. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0045893 positive regulation of DNA-templated transcription | IMP PMID:20123905 Structural insights into the YAP and TEAD complex. | ACCEPT | Summary: Positive regulation of DNA-templated transcription; correct, slightly less specific than GO:0045944. Reason: Supported by the YAP-TEAD structural and functional studies [PMID:20368466, PMID:20123905]. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: Positive regulation of transcription by RNA polymerase II through TEAD- and other factor-dependent coactivation (e.g. CTGF). Reason: TEADs are essential for YAP-dependent gene expression, and CTGF is a direct target [PMID:18579750]. This is the process directly enabled by the core coactivator activity. Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:20123905 Structural insights into the YAP and TEAD complex. | ACCEPT | Summary: Positive regulation of transcription by RNA polymerase II through TEAD- and other factor-dependent coactivation (e.g. CTGF). Reason: TEADs are essential for YAP-dependent gene expression, and CTGF is a direct target [PMID:18579750]. This is the process directly enabled by the core coactivator activity. Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:25796446 Aerobic glycolysis tunes YAP/TAZ transcriptional activity. | ACCEPT | Summary: Positive regulation of transcription by RNA polymerase II through TEAD- and other factor-dependent coactivation (e.g. CTGF). Reason: TEADs are essential for YAP-dependent gene expression, and CTGF is a direct target [PMID:18579750]. This is the process directly enabled by the core coactivator activity. Supporting Evidence: PMID:18579750 Here we demonstrate that the TEAD family transcription factors are essential in mediating YAP-dependent gene expression PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0050673 epithelial cell proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Epithelial cell proliferation (transferred from mouse). Reason: YAP regulates, rather than executes, proliferation; see GO:0050679. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0050673 epithelial cell proliferation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Epithelial cell proliferation (transferred from mouse). Reason: YAP regulates, rather than executes, proliferation; see GO:0050679. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0050679 positive regulation of epithelial cell proliferation | IBA GO_REF:0000033 | ACCEPT | Summary: Positive regulation of epithelial cell proliferation; the best-known output of YAP-TEAD coactivation in animal epithelia. Reason: Supported in mouse skin and intestine [PMID:21376238, PMID:25731159] and by knockdown in cancer cells [PMID:29403552]; the IBA places it in the animal YAP/TAZ/Yorkie clade. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0050679 positive regulation of epithelial cell proliferation | IEA GO_REF:0000117 | ACCEPT | Summary: Positive regulation of epithelial cell proliferation; the best-known output of YAP-TEAD coactivation in animal epithelia. Reason: Supported in mouse skin and intestine [PMID:21376238, PMID:25731159] and by knockdown in cancer cells [PMID:29403552]; the IBA places it in the animal YAP/TAZ/Yorkie clade. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0050679 positive regulation of epithelial cell proliferation | IMP PMID:29403552 Downregulation of YAP inhibits proliferation and induces apo... | ACCEPT | Summary: Positive regulation of epithelial cell proliferation; the best-known output of YAP-TEAD coactivation in animal epithelia. Reason: Supported in mouse skin and intestine [PMID:21376238, PMID:25731159] and by knockdown in cancer cells [PMID:29403552]; the IBA places it in the animal YAP/TAZ/Yorkie clade. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation PMID:35659869 we demonstrate that coYki regulates cytoskeletal dynamics at the cell cortex but is dispensable for the proliferation of Capsaspora cells |
| GO:0050767 regulation of neurogenesis | IDA PMID:25433207 Nf2-Yap signaling controls the expansion of DRG progenitors ... | KEEP AS NON CORE | Summary: Regulation of neurogenesis (acts upstream of or within). Nf2-Yap signaling controls expansion of DRG progenitors and glia. Reason: Supported by PMID:25433207; a developmental, non-core role. Supporting Evidence: PMID:25433207 Aberrant YAP activation leads to overexpansion of DRG progenitor and glial populations |
| GO:0060045 positive regulation of cardiac muscle cell proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of cardiac muscle cell proliferation (transferred from mouse). Reason: A well-documented role of YAP in heart growth; animal-specific, non-core. |
| GO:0060576 intestinal epithelial cell development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Intestinal epithelial cell development (transferred from mouse). Reason: YAP affects intestinal epithelial proliferation and differentiation [PMID:25731159]; non-core. Supporting Evidence: PMID:25731159 Through YAP and Notch, intestinal gp130 signalling stimulates epithelial cell proliferation |
| GO:0061026 cardiac muscle tissue regeneration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cardiac muscle tissue regeneration (transferred from mouse). Reason: Part of YAP's role in regeneration [PMID:21808241]; non-core. Supporting Evidence: PMID:21808241 Extensive research led to the identification of the Hippo tumour-suppressor pathway as a key regulator of organ size in Drosophila and mammals |
| GO:0065003 protein-containing complex assembly | IDA PMID:20368466 Structural and functional analysis of the YAP-binding domain... | MARK AS OVER ANNOTATED | Summary: Protein-containing complex assembly, from the YAP-TEAD structural studies. Reason: YAP is a subunit of the TEAD-YAP complex, already captured by GO:0140552 and GO:0140297. Calling its binding 'complex assembly' adds no information. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0065003 protein-containing complex assembly | IMP PMID:20123905 Structural insights into the YAP and TEAD complex. | MARK AS OVER ANNOTATED | Summary: Protein-containing complex assembly, from the YAP-TEAD structural studies. Reason: YAP is a subunit of the TEAD-YAP complex, already captured by GO:0140552 and GO:0140297. Calling its binding 'complex assembly' adds no information. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0070064 proline-rich region binding | IEA GO_REF:0000107 | ACCEPT | Summary: Proline-rich region binding through the WW domains, which bind PPxY motifs in partners such as p73, PTPN14, angiomotins, LATS1/2 and WBP2. Reason: WW domain-PPxY binding is the mechanism of many YAP1 interactions [PMID:11278685, PMID:22525271, PMID:21187284]. The two WW domains are conserved in Capsaspora coYki [PMID:38729842], so this binding mode is ancestral. Supporting Evidence: PMID:11278685 The WW domain of YAP and the PPPPY motif of p73 are directly involved in the association PMID:22525271 through the WW domain of YAP and the PPxY domain of PTPN14 |
| GO:0070102 interleukin-6-mediated signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Interleukin-6-mediated signaling pathway (IEA). Reason: gp130, the IL-6 family co-receptor, activates YAP through Src/Yes phosphorylation [PMID:25731159]. YAP is a downstream effector; non-core. Supporting Evidence: PMID:25731159 gp130, a co-receptor for IL-6 cytokines, triggers activation of YAP and Notch |
| GO:0071480 cellular response to gamma radiation | IDA PMID:18280240 Yap1 phosphorylation by c-Abl is a critical step in selectiv... | KEEP AS NON CORE | Summary: Cellular response to gamma radiation, from the same c-Abl/p73 study. Reason: Kept as non-core, as for GO:0006974 [PMID:18280240]. Supporting Evidence: PMID:18280240 Tyrosine-phosphorylated Yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes |
| GO:0072091 regulation of stem cell proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Regulation of stem cell proliferation. Reason: YAP regulates epidermal stem cell and DRG progenitor proliferation [PMID:21376238, PMID:25433207]; animal-specific, non-core. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25433207 Aberrant YAP activation leads to overexpansion of DRG progenitor and glial populations |
| GO:0072091 regulation of stem cell proliferation | IDA PMID:25433207 Nf2-Yap signaling controls the expansion of DRG progenitors ... | KEEP AS NON CORE | Summary: Regulation of stem cell proliferation. Reason: YAP regulates epidermal stem cell and DRG progenitor proliferation [PMID:21376238, PMID:25433207]; animal-specific, non-core. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25433207 Aberrant YAP activation leads to overexpansion of DRG progenitor and glial populations |
| GO:0072091 regulation of stem cell proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Regulation of stem cell proliferation. Reason: YAP regulates epidermal stem cell and DRG progenitor proliferation [PMID:21376238, PMID:25433207]; animal-specific, non-core. In the unicellular filasterean Capsaspora the Yorkie/YAP ortholog coYki is dispensable for proliferation [PMID:35659869], so YAP-driven proliferative growth control is regarded as an animal-specific recruitment of an ancestral TEAD-coactivator module [PMID:38729842]. Supporting Evidence: PMID:21376238 Yap1 is a critical modulator of epidermal stem cell proliferation and tissue expansion PMID:25433207 Aberrant YAP activation leads to overexpansion of DRG progenitor and glial populations |
| GO:0140297 DNA-binding transcription factor binding | IPI PMID:20123905 Structural insights into the YAP and TEAD complex. | ACCEPT | Summary: Binding to DNA-binding transcription factors, above all TEAD1-4, via the N-terminal TEAD-binding domain (residues ~50-171). Reason: The YAP-TEAD1 crystal structure shows direct binding through three interfaces [PMID:20123905]. Binding to the TEAD ortholog is ancestral (Capsaspora coYki-coSd [PMID:22832104]). Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression |
| GO:0140552 TEAD-YAP complex | IDA PMID:20123905 Structural insights into the YAP and TEAD complex. | ACCEPT | Summary: YAP1 is the coactivator subunit of the TEAD-YAP complex. Reason: Structural and binding studies of YAP with TEAD1 and TEAD2 [PMID:20123905, PMID:20368466]; peptide disruption of the YAP-TEAD interface [PMID:25384421]. The GO term itself is defined around YAP. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0140552 TEAD-YAP complex | IDA PMID:20368466 Structural and functional analysis of the YAP-binding domain... | ACCEPT | Summary: YAP1 is the coactivator subunit of the TEAD-YAP complex. Reason: Structural and binding studies of YAP with TEAD1 and TEAD2 [PMID:20123905, PMID:20368466]; peptide disruption of the YAP-TEAD interface [PMID:25384421]. The GO term itself is defined around YAP. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0140552 TEAD-YAP complex | IEA GO_REF:0000120 | ACCEPT | Summary: YAP1 is the coactivator subunit of the TEAD-YAP complex. Reason: Structural and binding studies of YAP with TEAD1 and TEAD2 [PMID:20123905, PMID:20368466]; peptide disruption of the YAP-TEAD interface [PMID:25384421]. The GO term itself is defined around YAP. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:0140552 TEAD-YAP complex | IPI PMID:25384421 Targeting Hippo pathway by specific interruption of YAP-TEAD... | ACCEPT | Summary: YAP1 is the coactivator subunit of the TEAD-YAP complex. Reason: Structural and binding studies of YAP with TEAD1 and TEAD2 [PMID:20123905, PMID:20368466]; peptide disruption of the YAP-TEAD interface [PMID:25384421]. The GO term itself is defined around YAP. Supporting Evidence: PMID:20123905 The TEAD family of transcription factors binds directly to and mediates YAP-induced gene expression PMID:20368466 interact with YAP (which lacks a DNA-binding domain but contains an activation domain) to form functional heterodimeric transcription factors |
| GO:1900182 positive regulation of protein localization to nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Positive regulation of protein localization to nucleus. YAP/TAZ control nuclear accumulation of SMAD complexes. Reason: Supported in principle by PMID:21145499; non-core. Supporting Evidence: PMID:21145499 TAZ/YAP dictate the localization of active SMAD complexes |
| GO:1900182 positive regulation of protein localization to nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of protein localization to nucleus. YAP/TAZ control nuclear accumulation of SMAD complexes. Reason: Supported in principle by PMID:21145499; non-core. Supporting Evidence: PMID:21145499 TAZ/YAP dictate the localization of active SMAD complexes |
| GO:1902018 negative regulation of cilium assembly | IMP PMID:25849865 Actin remodelling factors control ciliogenesis by regulating... | KEEP AS NON CORE | Summary: Negative regulation of cilium assembly: YAP/TAZ knockdown induces ciliogenesis and hyperactivation suppresses it. Reason: Supported by PMID:25849865 (abstract); an indirect, non-core output. Supporting Evidence: PMID:25849865 knockdown of YAP/TAZ is sufficient to induce ciliogenesis |
| GO:1904036 negative regulation of epithelial cell apoptotic process | IMP PMID:29403552 Downregulation of YAP inhibits proliferation and induces apo... | KEEP AS NON CORE | Summary: Negative regulation of epithelial cell apoptotic process (IMP, Eca-109 cells). Reason: YAP knockdown induced apoptosis in one ESCC line [PMID:29403552]; non-core. Supporting Evidence: PMID:29403552 YAP gene inhibition suppresses the proliferation and induces apoptosis in ECA-109 cells |
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Download this section (compressed HTML)Q: Proliferation and organ-size control by YAP/Yorkie appear absent in Capsaspora, where coYki regulates cortical actomyosin and aggregate shape. At which node on the lineage leading to animals did YAP/Yorkie-TEAD acquire proliferative target genes, and does this coincide with the origin of TEAD-bound distal enhancers?
Q: Does human YAP1 keep an ancestral, proliferation-independent role in cortical cytoskeleton and blebbing, analogous to coYki? Could some YAP1 mechanotransduction phenotypes in epithelia reflect that older function rather than growth control?
Q: The S. rosetta Yorkie candidate (PTSG_06057) lacks a recognizable TEAD-binding motif. Did the choanoflagellate lineage lose YAP-TEAD coupling, or does it bind TEAD through a divergent interface? And should GO propagation of TEAD-YAP complex membership to choanoflagellates be restricted?
Q: Many GOA annotations for 'YAP' come from studies that knocked down or assayed YAP1 and WWTR1 (TAZ) together. Which of the developmental and differentiation terms (e.g. osteoblast vs adipocyte differentiation, ciliogenesis) are specific to YAP1 rather than shared or TAZ-dominant?
Experiment: Express human YAP1, YAP1 S94A (TEAD-binding-dead) and WWTR1 in Capsaspora coYki-/- cells and score blebbing and aggregate morphology. This tests whether the ancestral cytoskeletal output is retained in the human protein and whether it depends on TEAD.
Hypothesis: Human YAP1 can substitute for coYki in Capsaspora, restoring normal cortical behaviour.
Type: cross-species complementation
Experiment: Compare YAP1-TEAD ChIP-seq/CUT&RUN targets in human epithelial cells with orthologs of coYki-dependent genes. Test whether the shared set is enriched for actin-cytoskeleton and adhesion genes rather than cell-cycle genes.
Hypothesis: TEAD-YAP target genes that are shared with Capsaspora coYki targets define an ancestral, non-proliferative core program.
Type: comparative genomics / chromatin profiling
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