Falcon deep research report for BAG6
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Falcon research supports BAG6 as a cytosolic BAG6/UBL4A/TRC35 holdase and adaptor linking tail-anchored protein targeting with ERAD/proteasome quality control.
"BAG6 is embedded in this pathway as both a substrate-holding factor and a quality-control adaptor"
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data from the Human Protein Atlas
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
A ribosome-associating factor chaperones tail-anchored membrane proteins.
A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.
Protein targeting and degradation are coupled for elimination of mislocalized proteins.
SGTA antagonizes BAG6-mediated protein triage.
A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation.
USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation.
Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6.
Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain.
Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis.
Structural basis for regulation of the nucleo-cytoplasmic distribution of Bag6 by TRC35.
HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53.
Human leukocyte antigen-B-associated transcript 3 is released from tumor cells and engages the NKp30 receptor on natural killer cells.
Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function.
Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.
Ricin triggers apoptotic morphological changes through caspase-3 cleavage of BAT3.
Towards a proteome-scale map of the human protein-protein interaction network.
BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4 histone dimethylation and gene expression.
Defining the membrane proteome of NK cells.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors.
The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding.
SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
A proteome-scale map of the human interactome network.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.
UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Definition of the human mitochondrial TOM interactome reveals TRABD as a new interacting protein.
Pre-emptive Quality Control Protects the ER from Protein Overload via the Proximity of ERAD Components and SRP.