BAG2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000774 adenyl-nucleotide exchange factor activity	IBA GO_REF:0000033	ACCEPT	Summary: BAG2 is a nucleotide-exchange factor (NEF) for HSP70/HSC70, promoting ADP release via its BAG domain. This is the core molecular function and is well supported experimentally. Reason: NEF activity toward HSP70/HSC70 is the defining, experimentally validated molecular function of BAG2 and is consistent with the phylogenetic inference. Supporting Evidence: file:human/BAG2/BAG2-uniprot.txt a nucleotide-exchange factor (NEF) promoting the release of ADP from PMID:24318877 Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70).
GO:0050821 protein stabilization	IBA GO_REF:0000033	ACCEPT	Summary: BAG2 stabilizes specific chaperone clients (CFTR, PINK1, ataxin-3) by reducing their ubiquitination, so protein stabilization is a supported core process. Reason: BAG2 lowers ubiquitination of clients such as PINK1 and pathogenic ataxin-3, stabilizing them, and stabilizes immature CFTR conformations. This is a well-supported outcome of BAG2 co-chaperone/CHIP-inhibitory activity. Supporting Evidence: PMID:24383081 which directly binds with and stabilises PINK1 by decreasing its ubiquitination PMID:25006867 stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination
GO:0000774 adenyl-nucleotide exchange factor activity	IEA GO_REF:0000002	ACCEPT	Summary: NEF activity for HSP70/HSC70 is the defining molecular function of BAG2, well supported experimentally and consistent with the InterPro/BAG-domain inference. Reason: The BAG domain confers nucleotide-exchange activity on HSP70/HSC70; this IEA annotation agrees with direct biochemical evidence. Supporting Evidence: file:human/BAG2/BAG2-uniprot.txt a nucleotide-exchange factor (NEF) promoting the release of ADP from PMID:24318877 Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70).
GO:0006457 protein folding	IEA GO_REF:0000117	ACCEPT	Summary: As an HSP70/HSC70 co-chaperone that regulates the chaperone cycle and can display intrinsic client-stabilizing activity, BAG2 participates in protein folding/refolding. Reason: BAG2 modulates HSP70/HSC70 chaperone activity and contributes to chaperone-assisted folding/maturation of clients (e.g., CFTR), supporting the protein folding process. Supporting Evidence: PMID:16207813 stimulates the chaperone-assisted maturation of CFTR
GO:0051087 protein-folding chaperone binding	IEA GO_REF:0000002	ACCEPT	Summary: BAG2 binds the ATPase domain of HSP70/HSC70 chaperones; chaperone binding is a core molecular feature underlying its co-chaperone/NEF role. Reason: Direct binding of BAG2 to the HSP/HSC70 ATPase domain is well established and is the basis of its NEF activity. Supporting Evidence: file:human/BAG2/BAG2-uniprot.txt Binds to the ATPase domain of HSP/HSC70 chaperones PMID:9873016 bind with high affinity (KD congruent with 1-10
GO:0051247 positive regulation of protein metabolic process	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: This is an over-broad parent process term. BAG2's effects on protein metabolism are better captured by specific terms (protein stabilization, protein folding, negative regulation of ubiquitination). Reason: positive regulation of protein metabolic process is too general to convey BAG2 function and duplicates more specific accepted terms.
GO:0005515 protein binding	IPI PMID:18457437 Identification of intracellular proteins associated with the...	MARK AS OVER ANNOTATED	Summary: Generic high-throughput interactome/affinity-purification protein-binding annotation (EBNA5 TAP-MS); uninformative for BAG2 function. Reason: Bare protein binding from a proteomic screen does not identify a physiologically interpretable BAG2 molecular function.
GO:0005515 protein binding	IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a spliceosome interaction-mapping study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:22810586 Interpreting cancer genomes using systematic host network pe...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a tumour-virus host network perturbation screen; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:24510904 Unbiased screen for interactors of leucine-rich repeat kinas...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from an LRRK2 interactor screen; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a chromatin protein-interaction study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc...	MARK AS OVER ANNOTATED	Summary: From a quantitative chaperone interaction network; the relevant BAG2 biology (HSP70 co-chaperone binding) is captured by specific chaperone-binding terms, so bare protein binding is uninformative here. Reason: Bare protein binding is too general; chaperone-network membership is better represented by protein-folding chaperone binding/complex terms.
GO:0005515 protein binding	IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a TRAIL apoptosis kinase-network study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:25959826 Quantitative interaction proteomics of neurodegenerative dis...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a neurodegenerative-disease interaction proteomics study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a quantitative interactome study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:29513927 Comparative Protein Interaction Network Analysis Identifies ...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a ROCO-protein interaction-network study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a MAC-tag AP-MS/BioID mapping study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a histone crosslinking-MS study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from an EGFR-network rewiring study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from the binary interactome reference map; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a neurodegenerative-disease interactome study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a dual proteome-scale network study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:35167623 DNAJB1-PRKACA in HEK293T cells induces LINC00473 overexpress...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a DNAJB1-PRKACA signaling study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:35266954 The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its loc...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a TRIM1/LRRK2 study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from the OpenCell endogenous-tagging study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:37045861 Interactome dynamics of RAF1-BRAF kinase monomers and dimers...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a RAF1-BRAF interactome study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: Generic protein-binding annotation from a multimodal cell-map study; uninformative for BAG2 function. Reason: Bare protein binding from a high-throughput interactome is not informative.
GO:0042802 identical protein binding	IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli...	KEEP AS NON CORE	Summary: BAG2 self-association (homodimer) is a real biochemical property, but this particular annotation derives from a high-throughput spliceosome interaction map. Reason: BAG2 forms homodimers, so identical protein binding is plausible, but the supporting study is a generic interactome screen; retain as non-core.
GO:0042802 identical protein binding	IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc...	KEEP AS NON CORE	Summary: BAG2 homodimerization is consistent with biochemistry; annotation from a chaperone interaction-network screen. Reason: Self-association is a genuine BAG2 property; retain as non-core given the high-throughput source.
GO:0042802 identical protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	KEEP AS NON CORE	Summary: BAG2 homodimerization is consistent with biochemistry; annotation from the proteome-scale interactome map. Reason: Self-association is a genuine BAG2 property; retain as non-core given the high-throughput source.
GO:0005874 microtubule	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: The BAG2/HSP70 complex is tethered to the microtubule in neurons; microtubule colocalization is supported but is a context-specific (neuronal) localization. Reason: Microtubule tethering is demonstrated for the tau-triage function but is a neuronal-context localization rather than the universal BAG2 site of action. Supporting Evidence: PMID:19228967 The BAG2/Hsp70 complex is tethered to the microtubule
GO:0030424 axon	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Neuronal compartment localization inferred from the tau-triage microtubule work; context-specific. Reason: Axonal localization is a neuronal-context inference, not a core universal localization of BAG2.
GO:0030425 dendrite	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Neuronal compartment localization inferred from the tau-triage microtubule work; context-specific. Reason: Dendritic localization is a neuronal-context inference, not a core universal localization of BAG2.
GO:0031072 heat shock protein binding	IEA GO_REF:0000107	ACCEPT	Summary: BAG2 binds the HSP70/HSC70 chaperone ATPase domain; heat shock protein binding is a core molecular feature. Reason: Direct binding of BAG2 to HSP/HSC70 is well established and underlies its co-chaperone/NEF activity. Supporting Evidence: file:human/BAG2/BAG2-uniprot.txt Binds to the ATPase domain of HSP/HSC70 chaperones
GO:0031397 negative regulation of protein ubiquitination	IEA GO_REF:0000120	ACCEPT	Summary: BAG2 inhibits CHIP-mediated ubiquitination of chaperone clients; negative regulation of protein ubiquitination is a core process. Reason: BAG2 abrogates CHIP/E2 cooperation and decreases ubiquitination of clients such as CFTR, PINK1, and ataxin-3. Supporting Evidence: PMID:16207813 BAG-2 inhibits the ubiquitin ligase activity of CHIP by abrogating the CHIP/E2 cooperation
GO:0031625 ubiquitin protein ligase binding	IEA GO_REF:0000107	ACCEPT	Summary: BAG2 binds and inhibits the E3 ubiquitin ligase CHIP (STUB1); ubiquitin protein ligase binding is supported and mechanistically central. Reason: BAG2 is a main component of CHIP complexes and binds CHIP to inhibit its ligase activity. Supporting Evidence: PMID:16207813 We identified the Hsc70 cochaperone
GO:0048156 tau protein binding	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: BAG2 (via the BAG2/HSP70 complex) captures misfolded/insoluble tau; tau binding is supported in the neuronal protein-triage context. Reason: Tau binding/capture is well documented but is a client-specific, neuronal-context activity rather than the universal BAG2 molecular function. Supporting Evidence: PMID:19228967 this complex can capture and deliver Tau to the
GO:1901588 dendritic microtubule	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Neuronal dendritic-microtubule colocalization inferred from the tau-triage microtubule work; context-specific. Reason: Highly specific neuronal localization inference; retain as non-core.
GO:1901800 positive regulation of proteasomal protein catabolic process	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: In neurons BAG2/HSP70 delivers tau to the proteasome for ubiquitin-independent degradation, promoting proteasomal catabolism of this client. Reason: Supported by the tau-triage mechanism (ubiquitin-independent proteasomal degradation), but it is a client/context-specific role rather than a general one. Supporting Evidence: PMID:19228967 deliver Tau to the
GO:0048156 tau protein binding	NAS PMID:28386764 Roles of tau protein in health and disease.	KEEP AS NON CORE	Summary: Review-based assertion of BAG2-tau binding; consistent with the primary tau-triage data but context-specific (neuronal). Reason: Tau binding is real but client/context-specific; retain as non-core.
GO:0005874 microtubule	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	KEEP AS NON CORE	Summary: BAG2 associates with microtubules (even without tau) in the neuronal tau-triage work; supported but context-specific. Reason: Microtubule association is demonstrated but is a neuronal-context localization. Supporting Evidence: PMID:19228967 The BAG2/Hsp70 complex is tethered to the microtubule
GO:0030424 axon	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	KEEP AS NON CORE	Summary: Neuronal axonal localization inferred from the tau-triage study; context-specific. Reason: Axonal localization is a neuronal-context inference, not a core localization.
GO:0030425 dendrite	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	KEEP AS NON CORE	Summary: Neuronal dendritic localization inferred from the tau-triage study; context-specific. Reason: Dendritic localization is a neuronal-context inference, not a core localization.
GO:0031397 negative regulation of protein ubiquitination	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	ACCEPT	Summary: By inhibiting CHIP, BAG2 directs the HSP70-tau complex away from ubiquitination; negative regulation of protein ubiquitination is core. Reason: Consistent with BAG2's established CHIP-inhibitory, anti-ubiquitination role. Supporting Evidence: PMID:19228967 BAG2 directs the Hsp70-Tau complex away from ubiquitination
GO:0031397 negative regulation of protein ubiquitination	IDA PMID:24383081 The BAG2 protein stabilises PINK1 by decreasing its ubiquiti...	ACCEPT	Summary: BAG2 stabilizes PINK1 by decreasing its ubiquitination; direct support for negative regulation of protein ubiquitination. Reason: Direct experimental demonstration that BAG2 reduces client ubiquitination. Supporting Evidence: PMID:24383081 stabilises PINK1 by decreasing its ubiquitination
GO:0031397 negative regulation of protein ubiquitination	IDA PMID:25006867 The BAG2 and BAG5 proteins inhibit the ubiquitination of pat...	ACCEPT	Summary: BAG2 inhibits ubiquitination of pathogenic ataxin-3; direct support for negative regulation of protein ubiquitination. Reason: Direct experimental demonstration that BAG2 reduces client ubiquitination. Supporting Evidence: PMID:25006867 stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination
GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process	ISS NOT PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	ACCEPT	Summary: The NOT annotation is well justified - BAG2 routes tau to a ubiquitin-INDEPENDENT proteasomal pathway while inhibiting CHIP, so it does not promote ubiquitin-dependent proteasomal catabolism. Reason: BAG2 mediates ubiquitin-independent proteasomal degradation of tau and inhibits the ubiquitin-dependent CHIP route, supporting the negation. Supporting Evidence: PMID:19228967 BAG2 mediates ubiquitin independent degradation of Tau through the proteasome
GO:0050821 protein stabilization	IDA PMID:24383081 The BAG2 protein stabilises PINK1 by decreasing its ubiquiti...	ACCEPT	Summary: BAG2 directly stabilizes PINK1 by decreasing its ubiquitination; core process. Reason: Direct experimental demonstration of BAG2-mediated client stabilization. Supporting Evidence: PMID:24383081 directly binds with and stabilises PINK1 by decreasing its ubiquitination
GO:0050821 protein stabilization	IDA PMID:25006867 The BAG2 and BAG5 proteins inhibit the ubiquitination of pat...	ACCEPT	Summary: BAG2 stabilizes pathogenic ataxin-3 by inhibiting its ubiquitination; core process. Reason: Direct experimental demonstration of BAG2-mediated client stabilization. Supporting Evidence: PMID:25006867 stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination
GO:1901588 dendritic microtubule	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	KEEP AS NON CORE	Summary: Neuronal dendritic-microtubule colocalization from the tau-triage study; context-specific. Reason: Highly specific neuronal localization; retain as non-core.
GO:1901800 positive regulation of proteasomal protein catabolic process	ISS PMID:19228967 The cochaperone BAG2 sweeps paired helical filament- insolub...	KEEP AS NON CORE	Summary: BAG2/HSP70 promotes ubiquitin-independent proteasomal degradation of tau; supported but client/context-specific. Reason: Supported by the tau-triage mechanism but context-specific to neuronal tau handling. Supporting Evidence: PMID:19228967 deliver Tau to the
GO:0005515 protein binding	IPI PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	MARK AS OVER ANNOTATED	Summary: The underlying interaction is BAG2 with CHIP (and HSC70); bare protein binding is too generic and is better captured by the specific chaperone/E3-ligase binding terms. Reason: protein binding is uninformative; the specific BAG2-CHIP and BAG2-HSC70 interactions are represented by other terms in this review.
GO:0010954 positive regulation of protein processing	IMP PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	KEEP AS NON CORE	Summary: BAG2 stimulates chaperone-assisted maturation of CFTR; this is better captured as client stabilization/folding and negative regulation of ubiquitination. The generic "protein processing" term is a loose fit. Reason: Supported for CFTR maturation but client/context-specific, and the term is a somewhat imprecise description of BAG2's CHIP-inhibition/stabilization mechanism. Supporting Evidence: PMID:16207813 stimulates the chaperone-assisted maturation of CFTR
GO:0044325 transmembrane transporter binding	IPI PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	KEEP AS NON CORE	Summary: BAG2 recognizes CFTR (a transmembrane transporter) NBD1 peptides and stabilizes immature CFTR; transmembrane transporter binding is supported but client-specific. Reason: CFTR is one client of BAG2; the binding is supported but not the universal core molecular function. Supporting Evidence: PMID:16207813 also to stabilize immature CFTR conformations
GO:0050821 protein stabilization	IDA PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	ACCEPT	Summary: BAG2 stabilizes immature CFTR conformations in addition to inhibiting CHIP; protein stabilization is a core BAG2 process. Reason: Direct evidence that BAG2 stabilizes a chaperone client (CFTR). Supporting Evidence: PMID:16207813 also to stabilize immature CFTR conformations
GO:0051087 protein-folding chaperone binding	IPI PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	ACCEPT	Summary: BAG2 binds HSC70 (a protein-folding chaperone) within CHIP complexes; chaperone binding is core. Reason: Direct evidence of BAG2 association with HSC70 chaperone complexes underlies its co-chaperone function. Supporting Evidence: PMID:16207813 the Hsc70 cochaperone
GO:0101031 protein folding chaperone complex	IPI PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu...	ACCEPT	Summary: BAG2 is a component of HSC70/CHIP chaperone complexes; membership in a protein-folding chaperone complex is core. Reason: BAG2 is a main component of CHIP/HSC70 chaperone complexes, consistent with its co-chaperone role. Supporting Evidence: PMID:16207813 We identified the Hsc70 cochaperone
GO:0000774 adenyl-nucleotide exchange factor activity	IDA PMID:24318877 Binding of human nucleotide exchange factors to heat shock p...	ACCEPT	Summary: Direct biochemical demonstration of BAG2 NEF activity toward HSP70 (HSPA1A); this is the core molecular function. Reason: BAG2 binds Hsp72 and functions in nucleotide/peptide release assays as a NEF, directly validating this molecular function. Supporting Evidence: PMID:24318877 Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). PMID:24318877 their relative affinity values
GO:0005515 protein binding	IPI PMID:24318877 Binding of human nucleotide exchange factors to heat shock p...	MARK AS OVER ANNOTATED	Summary: The underlying interaction is BAG2 with HSP70 (HSPA1A); generic protein binding is uninformative and is captured by specific chaperone-binding/NEF terms. Reason: Bare protein binding is too general; the BAG2-HSP70 interaction is represented by heat shock protein binding and NEF activity.
GO:0005829 cytosol	TAS Reactome:R-HSA-5252079	ACCEPT	Summary: BAG2 is a cytosolic co-chaperone; cytosolic localization is the core compartment for its HSP70 NEF/CHIP-regulatory activity. Reason: Consistent with BAG2 acting on cytosolic HSP70/HSC70 and CHIP complexes. Supporting Evidence: file:human/BAG2/BAG2-uniprot.txt Co-chaperone for HSP70 and HSC70 chaperone proteins
GO:0019538 protein metabolic process	IDA PMID:9873015 Control of glycogen synthesis in cultured human muscle cells...	REMOVE	Summary: The cited reference (PMID:9873015) is about glycogen synthesis in muscle cells and does not concern BAG2; this is a wrong-reference curation error rather than a genuine (if over-broad) annotation. Reason: The cited reference (PMID:9873015, "Control of glycogen synthesis in cultured human muscle cells") contains no evidence for any BAG2 role - it is a database mis-attribution. The annotation is unlikely to be correct based on the combined evidence and should be removed at source rather than merely downgraded.
GO:0006457 protein folding	TAS PMID:9873016 An evolutionarily conserved family of Hsp70/Hsc70 molecular ...	ACCEPT	Summary: As an HSP70/HSC70 chaperone regulator, BAG2 participates in protein folding; supported by the foundational BAG-family chaperone-regulator study. Reason: BAG2 modulates HSP70/HSC70 chaperone activity, consistent with a protein folding role. Supporting Evidence: PMID:9873016 modulating their

Gene Description

Existing Annotations Review

Core Functions

BAG2 acts as a nucleotide-exchange factor (NEF) for the HSP70/HSC70 molecular chaperones, binding the chaperone ATPase domain via its BAG domain and promoting ADP release to regulate the chaperone cycle and client release.

BAG2 inhibits the chaperone-associated E3 ubiquitin ligase CHIP (STUB1) by abrogating CHIP/E2 cooperation, thereby negatively regulating ubiquitination of chaperone clients and shifting protein triage away from degradation.

BAG2 stabilizes specific chaperone clients (e.g., immature CFTR, PINK1, polyglutamine-expanded ataxin-3) by decreasing their ubiquitination, contributing to chaperone-assisted protein quality control.

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