Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
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BAG1 localizes to cytoplasm, nucleus, cytosol, and membrane
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BAG1 has adenyl-nucleotide exchange factor activity
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BAG1 binds protein-folding chaperones
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BAG1 involved in protein stabilization
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
BAG-1 modulates the chaperone activity of Hsp70/Hsc70
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BAG1 binds ATPase domain of Hsp70/Hsc70
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BAG1 forms heteromeric complexes with Hsp70/Hsc70
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BAG1 inhibits Hsp70-mediated protein refolding in vitro
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Hsp70 binding explains diverse BAG1 interactions (Raf-1, receptors)
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BAG1 binding to BCL2 is ATP-dependent (Hsp70 involvement)
HGF receptor associates with the anti-apoptotic protein BAG-1 and prevents cell death
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BAG1 associates with HGF receptor
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BAG1 enhances HGF and PDGF-mediated protection from apoptosis
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Historical characterization as anti-apoptotic
Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1
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BAG1 binds C-terminal lobe of Hsc70 ATPase domain
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Binding affinity KD = 22 nM for subdomain
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BAG1 acts as nucleotide exchange factor
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
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BAG1 stimulates CHIP-mediated degradation of glucocorticoid receptor
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BAG1 cooperates with CHIP in proteasomal sorting
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BAG1 UBL domain recruits Hsp70 complexes to proteasome
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BAG1 differs from BAG2 which inhibits CHIP
Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro
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BAG1 is a nucleotide exchange factor for Hsp70
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Affinity hierarchy BAG3 > BAG1 > Hsp105 > BAG2
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NEF affinity predicts potency in nucleotide release assays
Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines
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BAG-1L is nuclear, BAG-1M/S are cytosolic
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Alternative translation initiation generates isoforms
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BAG-1L has nuclear localization sequence
Proteomic characterization of the human sperm nucleus
HSP110s exchange ATP for ADP on HSP70s:ADP
An empirical framework for binary interactome mapping
Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways
A proteome-scale map of the human interactome network
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations
A reference map of the human binary protein interactome
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome
Multimodal cell maps as a foundation for structural and functional genomics