Annotation inferences using phylogenetic trees
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DAP1 ribosome binding and ribosome hibernation functions are inferred from phylogenetic analysis
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Negative regulation of autophagy is conserved across the DAP family
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Apoptotic signaling pathway involvement is phylogenetically conserved
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
DAP1, a novel substrate of mTOR, negatively regulates autophagy.
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DAP1 is a direct substrate of mTOR
"Here we identify death-associated protein 1 (DAP1) as a novel substrate of mTOR that negatively regulates autophagy."
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Phosphorylation at Ser3 and Ser51 by mTOR inactivates DAP1 autophagy suppression
"DAP1 is functionally silenced in growing cells through mTOR-dependent phosphorylations on Ser3 and Ser51."
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DAP1 knockdown enhances autophagic flux
"The link of DAP1 to autophagy was first apparent in that its knockdown enhanced autophagic flux"
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Dephosphorylated DAP1 actively suppresses autophagy during starvation
"Inactivation of mTOR during starvation caused a rapid reduction in these phosphorylation sites and converted the protein into an active suppressor of autophagy."
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DAP1 acts as a "brake" to prevent autophagy overactivation
"These results are consistent with a "Gas and Brake" model in which mTOR inhibition also controls a buffering mechanism that counterbalances the autophagic flux and prevents its overactivation under nutrient deprivation."
Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death.
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DAP1 originally identified through functional cloning screen for IFN-gamma-induced cell death mediators
"In this system we have identified two novel genes whose expression was indispensable for the execution of this type of cell death."
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DAP1 is a basic, proline-rich 15 kDa protein
"One of those genes (DAP-1) is expressed as a single 2.4-kb mRNA that codes for a basic, proline-rich, 15-kD protein."
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Antisense RNA knockdown of DAP1 protected cells from IFN-gamma-induced programmed cell death
"The antisense RNA-mediated inactivation of the two novel genes protected the cells from the IFN-gamma-induced cell death"
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DAP1 involvement is specific to programmed cell death, not necrosis or cytostatic effects
"protected the cells from the IFN-gamma-induced cell death but not from the cytostatic effects of the cytokine or from a necrotic type of cell death"
UniProt entry for human DAP1
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DAP1 is an intrinsically disordered protein (entire 102 AA region)
"Ribosome-binding protein involved in ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation"
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Associates with ribosomes via eIF5A interaction at polypeptide exit tunnel
"Acts via its association with eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the ribosome, preventing mRNA translation (By similarity)."
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Involved in ribosome hibernation, particularly in oocytes
"Involved in ribosome hibernation in the mature oocyte by preventing mRNA translation, leading to ribosome inactivation (By similarity)."
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Phosphorylation by mTOR at Ser3 and Ser51 inhibits autophagy suppression activity
"Phosphorylated. Phosphorylation by MTOR inhibits the suppressive activity of DAP toward autophagy."
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Additional phosphorylation sites at Ser49 and Ser91 identified by mass spectrometry
"Also acts as a negative regulator of autophagy"
Deep research review of DAP1 gene function
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DAP1 is an mTORC1-phosphoregulated intrinsically disordered cytoplasmic protein that suppresses autophagy when dephosphorylated
"Human DAP1 (UniProt P51397) is an mTORC1-phosphoregulated, intrinsically disordered cytoplasmic protein that suppresses autophagy when dephosphorylated."
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Key regulatory sites Ser3 and Ser51 link nutrient signaling to autophagy control
"Key regulatory sites (Ser3, Ser51) link nutrient signaling to autophagy control."
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DAP1 behaves as an intrinsically disordered protein with limited secondary structure propensity
"Nearly complete 1H/13C/15N NMR chemical-shift assignments show limited spectral dispersion and minimal secondary-structure propensity (0% alpha-helix by shift-derived analysis), supporting a disordered state"