PFDN2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for cytoplasm localization. Prefoldin is a cytosolic chaperone complex; PFDN2 functions primarily in the cytoplasm where it captures nascent actin and tubulin and delivers them to TRiC/CCT (PMID:9630229). Experimental evidence from PMID:16876117 and PMID:17936702 confirms cytoplasmic localization by immunofluorescence. Reason: Core localization. The IBA annotation is phylogenetically supported and confirmed by multiple experimental studies showing cytoplasmic localization of PFDN2. Supporting Evidence: PMID:9630229 We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin. PMID:16876117 Prefoldin 2 is a subunit of a hexameric molecular chaperone complex, named prefoldin, which delivers nascent actin and tubulin proteins to the eukaryotic cytosolic chaperonin for facilitated folding.
GO:0006457 protein folding	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for protein folding. Prefoldin is a co-chaperone that participates in protein folding by capturing unfolded substrates and delivering them to TRiC/CCT (PMID:9630229, PMID:30955883). Well-established core function. Reason: Core biological process for prefoldin. The IBA is phylogenetically well-supported and consistent with extensive biochemical evidence for prefoldin's role in protein folding. Supporting Evidence: PMID:9630229 prefoldin promotes folding in an environment in which there are many competing pathways for nonnative proteins. PMID:30955883 The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis. file:human/PFDN2/PFDN2-deep-research-falcon.md PFDN2 is a structural subunit of the canonical eukaryotic prefoldin holdase. It contributes to the capture of nascent or non-native polypeptides, principally cytoskeletal actins and tubulins, and their targeted delivery to TRiC/CCT.
GO:0044183 protein folding chaperone	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for protein folding chaperone molecular function. GO:0044183 is defined as "Binding to a protein or a protein-containing complex to assist the protein folding process." This precisely describes prefoldin's holdase function - binding unfolded substrates and transferring them to TRiC/CCT (PMID:9630229, PMID:30955883). Reason: This is the correct and most appropriate MF term for prefoldin subunits. Prefoldin acts as a holdase/transfer chaperone, binding unfolded actin and tubulin and delivering them to TRiC/CCT. The IBA is well-supported phylogenetically. Supporting Evidence: PMID:9630229 Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it. PMID:30955883 PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation for nuclear localization based on UniProt subcellular location mapping. Nuclear localization of PFDN2 is supported by UniProt's curated subcellular location statement and by functional studies showing prefoldin subunits on transcribed chromatin supporting RNAPII CTD phosphorylation and co-transcriptional splicing. Reason: Although IEA, this is consistent with UniProt's curated localization and functional evidence for nuclear roles in transcription/splicing. Supporting Evidence: file:human/PFDN2/PFDN2-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269\|PubMed:17936702}. Cytoplasm {ECO:0000269\|PubMed:17936702}. Mitochondrion {ECO:0000269\|PubMed:17936702}.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation for cytoplasm based on UniProt subcellular location mapping. Redundant with the IBA annotation for the same term but from a different source. Cytoplasmic localization is well-established experimentally. Reason: Duplicates the IBA annotation but from IEA source. Both are valid. Cytoplasmic localization is well-supported.
GO:0005739 mitochondrion	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: IEA annotation for mitochondrial localization based on UniProt subcellular location mapping. UniProt curates PFDN2 to mitochondrion from PMID:17936702. This localization is non-core relative to canonical cytosolic prefoldin function. Reason: Mitochondrial localization is curated by UniProt from PMID:17936702 but is not the core location for canonical prefoldin chaperone function. Not a core localization for prefoldin function. Supporting Evidence: file:human/PFDN2/PFDN2-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269\|PubMed:17936702}. Cytoplasm {ECO:0000269\|PubMed:17936702}. Mitochondrion {ECO:0000269\|PubMed:17936702}.
GO:0006457 protein folding	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation for protein folding based on InterPro domain mapping. Consistent with the IBA and IDA annotations for the same term. Prefoldin's role in protein folding is well-established. Reason: Redundant with IBA and IDA annotations for the same term. The InterPro-based mapping is correct and consistent with the known function of prefoldin.
GO:0016272 prefoldin complex	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation for prefoldin complex based on InterPro domain mapping. PFDN2 is a well-established component of the canonical prefoldin heterohexameric complex, confirmed by cryo-EM structures (PDB:6NR8, 7WU7) and biochemical studies (PMID:9630229, PMID:30955883). Reason: Core cellular component. PFDN2 is a structural subunit of the prefoldin complex, confirmed by multiple structures and biochemical characterization. Supporting Evidence: PMID:9630229 We describe the discovery of a heterohexameric chaperone protein, prefoldin
GO:0032991 protein-containing complex	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: IEA annotation from ARBA machine learning for generic protein-containing complex. This is technically correct but too general - PFDN2 is specifically part of the prefoldin complex (GO:0016272) which is already annotated. Reason: Too generic. The more specific term GO:0016272 (prefoldin complex) is already annotated and better describes the actual complex membership. This parent term adds no information.
GO:0051082 unfolded protein binding	IEA GO_REF:0000002	MODIFY	Summary: IEA annotation for unfolded protein binding based on InterPro mapping. While prefoldin does bind unfolded proteins, the more informative and accurate MF term is GO:0044183 (protein folding chaperone), which captures the functional role of binding unfolded substrates to assist folding, not merely binding them. Reason: GO:0051082 "unfolded protein binding" describes only the binding aspect. The correct MF term for prefoldin is GO:0044183 "protein folding chaperone" which captures the complete holdase/transfer chaperone function. The IBA already uses GO:0044183. Proposed replacements: protein folding chaperone
GO:0005515 protein binding	IPI PMID:15923622 The HRPT2 tumor suppressor gene product parafibromin associa...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from PMID:15923622 (Yart et al., 2005). This paper is about parafibromin (HRPT2) associating with PAF1 and RNAPII. The interaction with PFDN2 may have been detected as part of a larger interactome study. The generic protein binding term is uninformative. Reason: Generic protein binding from a study focused on parafibromin/PAF1/RNAPII. Does not provide specific functional information about PFDN2. The term "protein binding" is uninformative per curation guidelines.
GO:0005515 protein binding	IPI PMID:16876117 Interaction of hepatitis C virus F protein with prefoldin 2 ...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from PMID:16876117 (Tsao et al., 2006). This study demonstrated that HCV F protein interacts with PFDN2 via yeast two-hybrid and co-immunoprecipitation. The interaction impedes PFDN1-PFDN2 interaction and perturbs tubulin cytoskeleton. While a genuine interaction, the generic term is uninformative. Reason: Generic protein binding. The actual functional annotation from this paper (protein folding chaperone activity, positive regulation of cytoskeleton organization) is captured by other annotations from the same reference. Supporting Evidence: PMID:16876117 hepatitis C virus (HCV) F protein was found to interact with a cellular protein named prefoldin 2
GO:0005515 protein binding	IPI PMID:17353931 Large-scale mapping of human protein-protein interactions by...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from large-scale mass spectrometry interactome study (Ewing et al., 2007). High-throughput interactome data. Generic protein binding is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative per curation guidelines.
GO:0005515 protein binding	IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from quantitative chaperone interaction network study (Taipale et al., 2014). While this study provides valuable context about PFDN2's position in the chaperone network, the generic protein binding term is uninformative. Reason: Generic protein binding from chaperone interactome study. The actual functional annotations from prefoldin studies are better captured by GO:0044183.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from large-scale interactome architecture study (Huttlin et al., 2017). High-throughput study. Generic term is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: IPI protein binding from binary protein interactome reference map (Luck et al., 2020). High-throughput study. Generic term is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from neurodegenerative disease protein interactome mapping study (Haenig et al., 2020). High-throughput study. Generic term is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from dual proteome-scale network study. High-throughput study. Generic term is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from multimodal cell maps study. High-throughput study. Generic term is uninformative. Reason: Generic protein binding from high-throughput interactome study. Uninformative.
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: IDA annotation for nucleoplasm based on immunofluorescence data curation (HPA). Consistent with known nuclear roles of prefoldin subunits in transcription elongation and co-transcriptional splicing. Reason: Supported by immunofluorescence data from HPA and consistent with nuclear functions of prefoldin in transcription/splicing regulation.
GO:0005739 mitochondrion	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: IDA annotation for mitochondrion based on immunofluorescence data curation (HPA). Consistent with PMID:17936702 showing PFDN2 association with URI1 at mitochondria. Reason: Mitochondrial localization is experimentally supported but is a non-core localization relating to URI/PAQosome function rather than canonical prefoldin chaperone activity.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: IDA annotation for cytosol based on immunofluorescence data curation (HPA). Cytosol is the primary site of prefoldin's canonical co-chaperone function. Reason: Core localization. Cytosol is where prefoldin performs its primary function of capturing nascent actin/tubulin and delivering to TRiC/CCT.
GO:0050821 protein stabilization	NAS PMID:31738558 Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subuni...	KEEP AS NON CORE	Summary: NAS annotation for protein stabilization from PMID:31738558 (Cloutier et al., 2020). This paper describes ASDURF as a novel prefoldin-like subunit of the PAQosome, which includes PFDN2. The PAQosome is involved in biogenesis of protein complexes, which involves stabilization. Prefoldin's holdase activity does stabilize unfolded proteins against aggregation. Reason: Protein stabilization is a secondary consequence of prefoldin's holdase function. The primary function is better captured as protein folding chaperone. Stabilization is not incorrect but is a secondary effect rather than core function.
GO:0006457 protein folding	NAS PMID:32699605 The functions and mechanisms of prefoldin complex and prefol...	ACCEPT	Summary: NAS annotation for protein folding from the review by Liang et al. (2020) covering prefoldin functions and mechanisms. Consistent with core function. Reason: Redundant with IBA and IDA annotations but from a review source. Protein folding is a core function of prefoldin.
GO:0006457 protein folding	NAS PMID:34761191 A comprehensive analysis of prefoldins and their implication...	ACCEPT	Summary: NAS annotation for protein folding from Herranz-Montoya et al. (2021) comprehensive analysis of prefoldins. Consistent with core function. Reason: Redundant with other protein folding annotations. Consistent with the well-established core function of the prefoldin complex.
GO:0050821 protein stabilization	NAS PMID:34761191 A comprehensive analysis of prefoldins and their implication...	KEEP AS NON CORE	Summary: NAS annotation for protein stabilization from Herranz-Montoya et al. (2021). Prefoldin stabilizes client proteins (e.g., VHL) against aggregation. Reason: Protein stabilization is a secondary consequence of prefoldin's holdase function, not the primary molecular activity. Core function is better captured as protein folding chaperone.
GO:0050821 protein stabilization	NAS PMID:29662061 RPAP3 provides a flexible scaffold for coupling HSP90 to the...	KEEP AS NON CORE	Summary: NAS annotation for protein stabilization from PMID:29662061 (Martino et al., 2018). This paper is about RPAP3 providing a scaffold for coupling HSP90 to the R2TP co-chaperone complex. Relevant to the PAQosome context of PFDN2. Reason: Relates to the R2TP/PAQosome complex stabilization function. Not a core function of PFDN2 in the canonical prefoldin complex.
GO:0006457 protein folding	IDA PMID:30955883 The Chaperonin TRiC/CCT Associates with Prefoldin through a ...	ACCEPT	Summary: IDA annotation for protein folding from Gestaut et al. (2019) Cell paper. This landmark study used cryo-EM, crosslinking-MS, and biochemical approaches to show that prefoldin associates with TRiC/CCT through a conserved electrostatic interface, with PFD enhancing folding rate and yield while suppressing non-productive cycles. Reason: Strong experimental evidence from a landmark Cell paper demonstrating the structural and functional basis for prefoldin-TRiC cooperation in protein folding. Supporting Evidence: PMID:30955883 PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles.
GO:0016272 prefoldin complex	IDA PMID:30955883 The Chaperonin TRiC/CCT Associates with Prefoldin through a ...	ACCEPT	Summary: IDA annotation for prefoldin complex from Gestaut et al. (2019). Cryo-EM structures of the prefoldin-TRiC complex were resolved, directly demonstrating prefoldin complex architecture. Reason: Strong structural evidence from cryo-EM demonstrating prefoldin complex structure in association with TRiC/CCT. Supporting Evidence: PMID:30955883 we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD.
GO:0051082 unfolded protein binding	IDA PMID:30955883 The Chaperonin TRiC/CCT Associates with Prefoldin through a ...	MODIFY	Summary: IDA annotation for unfolded protein binding from Gestaut et al. (2019). While prefoldin does bind unfolded proteins, the more accurate MF term is GO:0044183 (protein folding chaperone) which captures the complete functional role. Reason: GO:0051082 describes only the binding aspect. GO:0044183 "protein folding chaperone" better captures prefoldin's complete holdase/transfer function. The binding is in service of assisted folding, not binding per se. Proposed replacements: protein folding chaperone Supporting Evidence: PMID:30955883 PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers.
GO:0001540 amyloid-beta binding	IDA PMID:23614719 Human prefoldin inhibits amyloid-β (Aβ) fibrillation and con...	KEEP AS NON CORE	Summary: IDA annotation for amyloid-beta binding from Sorgjerd et al. (2013). The study demonstrated that recombinant human prefoldin (hPFD) inhibits Abeta fibrillation and induces formation of less toxic Abeta oligomers. This is a property of the intact hexameric complex, not specific to PFDN2. Reason: The study demonstrated Abeta binding as a property of the intact prefoldin complex. This is consistent with prefoldin's general holdase function against misfolded proteins. However, this is not a core physiological function but rather reflects the general anti-aggregation capacity of the complex. Supporting Evidence: PMID:23614719 we investigated the effect of recombinant human PFD (hPFD) on Abeta(1-42) aggregation in vitro and found that hPFD inhibited Abeta fibrillation and induced formation of soluble Abeta oligomers.
GO:0016272 prefoldin complex	IDA PMID:23614719 Human prefoldin inhibits amyloid-β (Aβ) fibrillation and con...	ACCEPT	Summary: IDA annotation for prefoldin complex from Sorgjerd et al. (2013). The study used recombinant human prefoldin complex to study Abeta interactions, confirming the hexameric complex assembly. Reason: Confirms prefoldin complex formation with recombinant human subunits.
GO:1905907 negative regulation of amyloid fibril formation	IDA PMID:23614719 Human prefoldin inhibits amyloid-β (Aβ) fibrillation and con...	KEEP AS NON CORE	Summary: IDA annotation for negative regulation of amyloid fibril formation from Sorgjerd et al. (2013). The study showed hPFD inhibits Abeta fibrillation in vitro. This is a property of the intact complex and reflects the general anti-aggregation holdase function. Reason: This reflects in vitro anti-aggregation activity of the prefoldin complex rather than a primary physiological function. It is a secondary consequence of the holdase activity. The annotation is not wrong but represents a non-core function. Supporting Evidence: PMID:23614719 hPFD inhibited Abeta fibrillation and induced formation of soluble Abeta oligomers. Interestingly, cell viability measurements...showed that Abeta oligomers formed by hPFD were 30-40% less toxic
GO:0005634 nucleus	IDA PMID:16876117 Interaction of hepatitis C virus F protein with prefoldin 2 ...	ACCEPT	Summary: IDA annotation for nuclear localization from Tsao et al. (2006). The study used confocal immunofluorescence microscopy and showed PFDN2 in both nucleus and cytoplasm. Reason: Experimental evidence (immunofluorescence) supports nuclear localization. Consistent with known nuclear roles of prefoldin in transcription and splicing regulation. Supporting Evidence: PMID:16876117 The interaction was confirmed by confocal immunofluorescence microscopy as well as coimmunoprecipitation experiments.
GO:0005737 cytoplasm	IDA PMID:16876117 Interaction of hepatitis C virus F protein with prefoldin 2 ...	ACCEPT	Summary: IDA annotation for cytoplasm from Tsao et al. (2006). Immunofluorescence confirms cytoplasmic localization. Reason: Core localization confirmed by experimental immunofluorescence data. Consistent with canonical cytosolic chaperone function.
GO:0044183 protein folding chaperone	IPI PMID:16876117 Interaction of hepatitis C virus F protein with prefoldin 2 ...	ACCEPT	Summary: IPI annotation for protein folding chaperone from Tsao et al. (2006). The study showed PFDN2 interacts with HCV F protein, and that this interaction impedes PFDN1-PFDN2 interaction and perturbs tubulin cytoskeleton. This demonstrates PFDN2's role as a chaperone for tubulin folding. Reason: Demonstrates PFDN2's chaperone function via perturbation - HCV F protein interaction with PFDN2 disrupts prefoldin complex assembly and impairs tubulin folding, confirming PFDN2's role as a protein folding chaperone. Supporting Evidence: PMID:16876117 expression of HCV F protein impeded the interaction between prefoldin 1 and 2...expression of HCV F protein resulted in aberrant organization of tubulin cytoskeleton.
GO:0051495 positive regulation of cytoskeleton organization	IDA PMID:16876117 Interaction of hepatitis C virus F protein with prefoldin 2 ...	KEEP AS NON CORE	Summary: IDA annotation for positive regulation of cytoskeleton organization from Tsao et al. (2006). The study showed that disruption of PFDN2 function (by HCV F protein) leads to aberrant tubulin cytoskeleton organization, implying PFDN2 normally promotes proper cytoskeleton organization through its chaperone activity. Reason: While the study demonstrates that PFDN2 is required for proper cytoskeleton organization, this is a downstream consequence of its chaperone function (folding actin and tubulin) rather than a direct regulatory role. The annotation captures a true biological effect but the mechanism is indirect through protein folding. Supporting Evidence: PMID:16876117 expression of HCV F protein resulted in aberrant organization of tubulin cytoskeleton
GO:0005515 protein binding	IPI PMID:17936702 S6K1-mediated disassembly of mitochondrial URI/PP1gamma comp...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from Djouder et al. (2007). UniProt curates PFDN2 interaction with URI1 and subsequent work places PFDN2 in the PAQosome/R2TP prefoldin-like complex. Generic protein binding is uninformative for this context. Reason: Generic protein binding is a true but low-information interaction annotation. The specific URI1/PFDL context is better represented as a separate cellular component annotation to the RPAP3/R2TP/prefoldin-like complex. Supporting Evidence: file:human/PFDN2/PFDN2-uniprot.txt Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. PMID:29662061 This PFDL module includes prefoldin and prefoldin-like proteins PFDN2, PFDN6, URI1, UXT, PDRG1, and it associates with two additional components, the RNA polymerase subunit POLR2E/RPB5 and WDR92/Monad5.
GO:1990062 RPAP3/R2TP/prefoldin-like complex	IPI PMID:29662061 RPAP3 provides a flexible scaffold for coupling HSP90 to the...	NEW	Summary: PFDN2 is a component of the PAQosome/R2TP prefoldin-like module together with PFDN6, URI1, UXT, and PDRG1. This cellular component annotation captures the specific complex membership underlying the generic URI1 protein-binding evidence. Reason: GO:1990062 specifically represents the RPAP3/R2TP/prefoldin-like complex curated for PAQosome/PFDL membership. It is more informative than generic protein binding and does not conflate this PAQosome context with the canonical prefoldin complex. Supporting Evidence: file:human/PFDN2/PFDN2-uniprot.txt Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. PMID:29662061 This PFDL module includes prefoldin and prefoldin-like proteins PFDN2, PFDN6, URI1, UXT, PDRG1, and it associates with two additional components, the RNA polymerase subunit POLR2E/RPB5 and WDR92/Monad5.
GO:0005634 nucleus	IDA PMID:17936702 S6K1-mediated disassembly of mitochondrial URI/PP1gamma comp...	ACCEPT	Summary: IDA annotation for nuclear localization from Djouder et al. (2007). The study showed PFDN2 localizes to nucleus, cytoplasm, and mitochondria through immunofluorescence. Reason: Experimental evidence for nuclear localization by immunofluorescence.
GO:0005737 cytoplasm	IDA PMID:17936702 S6K1-mediated disassembly of mitochondrial URI/PP1gamma comp...	ACCEPT	Summary: IDA annotation for cytoplasm from Djouder et al. (2007). Confirmed by immunofluorescence. Reason: Core localization confirmed experimentally.
GO:0005739 mitochondrion	IDA PMID:17936702 S6K1-mediated disassembly of mitochondrial URI/PP1gamma comp...	KEEP AS NON CORE	Summary: IDA annotation for mitochondrial localization from Djouder et al. (2007), represented in UniProt's curated subcellular-location statement. Reason: Experimentally supported mitochondrial localization, but not the core location for canonical prefoldin chaperone function. Supporting Evidence: file:human/PFDN2/PFDN2-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269\|PubMed:17936702}. Cytoplasm {ECO:0000269\|PubMed:17936702}. Mitochondrion {ECO:0000269\|PubMed:17936702}.
GO:0051082 unfolded protein binding	NAS PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy...	MODIFY	Summary: NAS annotation for unfolded protein binding from Vainberg et al. (1998), the original prefoldin discovery paper. While accurate that prefoldin binds unfolded proteins, GO:0044183 is the more appropriate MF term. Reason: GO:0051082 describes only the binding aspect. GO:0044183 "protein folding chaperone" better captures the complete holdase/transfer function described in this paper. Proposed replacements: protein folding chaperone Supporting Evidence: PMID:9630229 Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it.
GO:0016272 prefoldin complex	NAS PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy...	ACCEPT	Summary: NAS annotation for prefoldin complex from the original prefoldin discovery paper (Vainberg et al., 1998). Describes the heterohexameric complex architecture. Reason: The foundational paper establishing the prefoldin complex. Core annotation. Supporting Evidence: PMID:9630229 We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin.
GO:0006457 protein folding	NAS PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy...	ACCEPT	Summary: NAS annotation for protein folding from Vainberg et al. (1998). This paper established that prefoldin promotes protein folding by delivering substrates to c-CPN (TRiC/CCT). Reason: Core function established in the original prefoldin paper. Supporting Evidence: PMID:9630229 prefoldin promotes folding in an environment in which there are many competing pathways for nonnative proteins.

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

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