SSB2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Ssb2 functions on cytosolic translating ribosomes; a nuclear pool is at most transient/peripheral (e.g., association with pre-ribosomes during ribosome biogenesis). Not a core localization. Reason: PMID:20368619 directly supports a specialized nuclear RAC-Ssb role in ribosome biogenesis, while direct localization and biochemical studies place the principal Ssb pool in the cytosol and on translating ribosomes. Nucleus is therefore retained as a non-core site of action. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002500132 · PAINT Hsp70 family node SUPPORTS TRANSFER The family inference is compatible with Ssb2 participation in nuclear ribosome biogenesis, but nucleus is not its predominant site. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md Ssb proteins (Ssb1/Ssb2) are cytosolic and ribosome-associated, positioned at the 60S tunnel exit
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: The cytoplasm is a principal location of Ssb2 and its ribosome-associated folding activity. Reason: The translating-ribosome association characterized in PMID:1394434 and PMID:9670014 establishes Ssb cytoplasmic function, consistent with the localization survey. A cellular component can be a core property; the broader cytoplasm term remains accurate alongside cytosol and ribosome annotations. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md Ssb proteins (Ssb1/Ssb2) are cytosolic and ribosome-associated, positioned at the 60S tunnel exit
GO:0005886 plasma membrane	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: A secondary plasma-membrane-associated Ssb2 pool is compatible with the curated fractionation result. Reason: The HDA annotation from PMID:16622836 records Ssb2 in a stripped plasma-membrane proteome. Its main soluble/ribosomal location does not exclude peripheral membrane association, and lack of a dedicated membrane function is not negative localization evidence. Retain as non-core without claiming membrane integration. For the IBA, GOA names PTN002500132; the current snapshot lacks the membrane assertion, a version discrepancy that does not erase the independent experimental annotation. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002500132 · PTN002500132 SOURCE STALE OR MISSING Current PAINT differs from the pinned GOA row; target experimental fractionation supports retaining a contextual membrane association. Supporting Evidence: PMID:16622836 Proteins from a stripped plasma membrane fraction were solubilized
GO:0016887 ATP hydrolysis activity	IBA GO_REF:0000033	ACCEPT	Summary: Ssb2 is an Hsp70 ATPase (EC 3.6.4.10); ATP hydrolysis powers its chaperone cycle and is stimulated by the Zuo1 J-domain of RAC. Reason: Directly supported. The Ssb ATPase activity is experimentally characterized and the ATP-driven conformational cycle is central to its function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER The conserved Hsp70-family ATPase inference agrees with direct Ssb biochemistry from PMID:9860955. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md J-domain protein Zuo1 stimulates ATP hydrolysis of Ssb1/2, driving this high-affinity substrate engagement on nascent chains
GO:0031072 heat shock protein binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Ssb2 interacts with co-chaperone partners of the Hsp70 system, notably the RAC J-protein Zuo1/Ssz1 and the Hsp110 nucleotide exchange factor Sse1. Reason: Consistent with documented Ssb-RAC and Ssb-Sse1 interactions, but this binding term is ancillary to Ssb2's direct ATP-dependent folding activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER Conserved Hsp70-network interactions support the transfer, while heat-shock-protein binding remains non-core for Ssb2. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md RAC is an obligate Zuo1–Ssz1 heterodimer attached to the ribosome (via Zuo1)
GO:0044183 protein folding chaperone	IBA GO_REF:0000033	ACCEPT	Summary: Ssb2 is a protein folding chaperone whose ATP-dependent cycle supports cotranslational folding. Reason: The broad GO:0044183 assertion at PTN000452648 is supported by nascent-chain binding, ATPase activity and folding studies (PMID:9670014, PMID:9860955, PMID:23332755). The ATP-dependent child term used in core_functions adds precision without invalidating the existing parent term. The existing SSB1/SSB2 OpenScientist investigation supports a shared folding mechanism and finds no demonstrated paralog-specific substrate distinction; its scope does not adjudicate protein refolding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PTN000452648 SUPPORTS TRANSFER The ancestral chaperone function is retained and experimentally supported in the nearly identical Ssb pair. Supporting Evidence: PMID:23332755 SSB binds to a subset of nascent polypeptides file:yeast/SSB1/SSB1-hypotheses/core-function-the-four-amino-acid-differences-between-ssb1-and-ssb2-confer-a-demonstrated-paralo/openscientist.md absence of evidence for divergence is not the same as proof of perfect functional identity
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: Ssb2 is a cytosolic chaperone; ~50% is ribosome-associated and the remainder is free cytosolic Ssb. This is the core localization. Reason: Strongly supported. The cytosol (and specifically cytosolic translating ribosomes) is where Ssb2 carries out its function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002500132 · PAINT Hsp70 family node SUPPORTS TRANSFER The ancestral cytosol inference agrees with Ssb2's direct localization and ribosome-associated folding function. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md only about ~50% of total cellular Ssb is ribosome-associated at steady state
GO:0042026 protein refolding	IBA GO_REF:0000033	MODIFY	Summary: The current PAINT fungal revision supports broad protein folding in place of the older protein-refolding assertion. Reason: The pinned GOA row descends from PTN000452648. Current PAINT explicitly places NOT/IRD for GO:0042026 at fungal node PTN001065099 (2026-06-16), with PTN000452648 as its source, and carries the broader GO:0006457 protein-folding assertion through that same node. Current target leaf records retain that broader descent. Follow this node-specific generalization rather than replacing refolding with the sibling cotranslational-folding term merely because it is the best-studied role. The revision and primary folding evidence support MODIFY; they do not demonstrate zero refolding capacity under every biochemical condition. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN000452648 · PTN000452648 SOURCE STALE OR MISSING The ancestral refolding IBD remains, but descendant fungal PTN001065099 explicitly carries its NOT/IRD and generalized protein-folding assertion; the pinned leaf annotation predates this revision. Proposed replacements: protein folding
GO:0000054 ribosomal subunit export from nucleus	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Ssb/RAC participates in a ribosome-anchored chaperone network linked to ribosome biogenesis; a role in ribosomal subunit export was reported by genetic interaction. This is downstream/ancillary to the core folding role. Reason: Supported by genetic interaction (PMID:20368619) but ancillary to the core cotranslational chaperone function. Kept as non-core.
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: ATP binding by the Ssb2 nucleotide-binding domain satisfies the broader nucleotide-binding term. Reason: PMID:9860955 characterizes the Ssb Hsp70 ATPase cycle. The existing broad molecular-function term is chemically correct and core; overlap with a more specific ATP term is not over-annotation.
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: Ssb2's N-terminal nucleotide-binding domain binds ATP, the basis of its ATP-driven Hsp70 chaperone cycle. Reason: Directly supported by domain architecture and the ATP-driven conformational cycle of the chaperone. Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md core biochemistry is an ATP-driven conformational cycle
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: The cytoplasm is a principal location of Ssb2 and its ribosome-associated folding activity. Reason: The translating-ribosome association characterized in PMID:1394434 and PMID:9670014 establishes Ssb cytoplasmic function, consistent with the localization survey. A cellular component can be a core property; the broader cytoplasm term remains accurate alongside cytosol and ribosome annotations.
GO:0006364 rRNA processing	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Ssb/RAC is part of a ribosome-anchored chaperone network implicated in ribosome biogenesis (rRNA processing reported by genetic interaction). This is ancillary to the core cotranslational folding role. Reason: Indirect/ancillary role via the ribosome-anchored chaperone network (PMID:20368619); not the core function.
GO:0006412 translation	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Ssb contributes to protein synthesis through the folding and quality control of nascent polypeptides on translating ribosomes. Reason: PMID:1394434 and PMID:9670014 establish the direct ribosome/nascent-chain role. Translation is broader than the defining cotranslational chaperone activity, but it is not rendered incorrect by that breadth. Retain the process as non-core, consistently with the existing cytoplasmic-translation IMP and IPI rows.
GO:0006450 regulation of translational fidelity	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Loss of Ssb1/2 (or RAC) impairs translational fidelity, primarily at translation termination. A genuine, experimentally supported downstream role. Reason: Supported experimentally (PMID:15456889), but translational fidelity is a downstream consequence of the RAC-Ssb system rather than the chaperone's direct core molecular activity.
GO:0006452 translational frameshifting	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Deletion of Ssb1/2 (or RAC) specifically inhibits -1 programmed ribosomal frameshifting and impairs Killer virus maintenance. Reason: Supported experimentally (PMID:16607023). Note the effect is specific to -1 PRF (no effect on +1 PRF), a downstream consequence of Ssb's role at the translating ribosome.
GO:0016787 hydrolase activity	IEA GO_REF:0000043	ACCEPT	Summary: ATP hydrolysis by Ssb2 satisfies the broader hydrolase-activity term. Reason: PMID:9860955 characterizes the Ssb Hsp70 ATPase cycle. The existing broad molecular-function term is chemically correct and core; overlap with a more specific ATP term is not over-annotation.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000120	ACCEPT	Summary: Ssb2 hydrolyzes ATP as part of its Hsp70 chaperone cycle (EC 3.6.4.10), stimulated by the RAC J-protein Zuo1. Reason: Directly supported; duplicate of the IBA/IDA ATP hydrolysis annotations.
GO:0051082 unfolded protein binding	IEA GO_REF:0000117	MODIFY	Summary: GO:0051082 is obsolete. OLS records protein folding chaperone (GO:0044183) as a term to consider; for the ATP-dependent Ssb2 Hsp70, the more specific GO:0140662 captures the supported activity. Reason: Modify because GO:0051082 is obsolete, not because substrate binding lacks support. OLS directs curators to consider GO:0044183; Ssb2's ATP-dependent Hsp70 mechanism supports its child GO:0140662. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md J-domain protein Zuo1 stimulates ATP hydrolysis of Ssb1/2, driving this high-affinity substrate engagement on nascent chains
GO:0051083 'de novo' cotranslational protein folding	IEA GO_REF:0000117	ACCEPT	Summary: This is the core biological process of Ssb2: direct binding to nascent chains at the ribosomal tunnel exit to promote de novo cotranslational folding, activated by RAC. Reason: Core function, strongly supported by both the falcon report and primary literature (PMID:9670014, PMID:23332755). Supporting Evidence: file:yeast/SSB2/SSB2-deep-research-falcon.md Ssb1/2 (including Ssb2) act as the direct nascent-chain binders during co-translational folding in yeast
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	REMOVE	Summary: Generic protein-binding from a high-throughput proteome survey; provides no specific functional information. Reason: The generic protein binding term supplies no informative molecular function beyond the established chaperone role. Remove the uninformative annotation while retaining the interaction observations; do not interpret this as a rejection of the physical interaction or infer an unsupported specific function from a proteomic association.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	REMOVE	Summary: Generic protein-binding from a high-throughput complex landscape study; no specific functional information. Reason: The generic protein binding term supplies no informative molecular function beyond the established chaperone role. Remove the uninformative annotation while retaining the interaction observations; do not interpret this as a rejection of the physical interaction or infer an unsupported specific function from a proteomic association.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	REMOVE	Summary: Generic protein-binding from a chaperone-interaction atlas; no specific functional information beyond the chaperone network role. Reason: The generic protein binding term supplies no informative molecular function beyond the established chaperone role. Remove the uninformative annotation while retaining the interaction observations; do not interpret this as a rejection of the physical interaction or infer an unsupported specific function from a proteomic association.
GO:0005515 protein binding	IPI PMID:23332755 The cotranslational function of ribosome-associated Hsp70 in...	MODIFY	Summary: The substrate-interaction study establishes cotranslational Ssb chaperoning, not merely generic protein binding. Reason: PMID:23332755 maps nascent-polypeptide clients and links Ssb loss to aggregation of newly synthesized proteins. Together with the established Ssb ATPase cycle, this supports an informative ATP-dependent protein folding chaperone replacement. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:23332755 SSB binds to a subset of nascent polypeptides PMID:23332755 Deletion of SSB leads to widespread aggregation of newly synthesized polypeptides.
GO:0005515 protein binding	IPI PMID:37070168 RNA-dependent interactome allows network-based assignment of...	REMOVE	Summary: Generic protein-binding from an RNA-dependent interactome study; no specific functional information. Reason: The generic protein binding term supplies no informative molecular function beyond the established chaperone role. Remove the uninformative annotation while retaining the interaction observations; do not interpret this as a rejection of the physical interaction or infer an unsupported specific function from a proteomic association.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Generic protein-binding from a global interactome architecture study; no specific functional information. Reason: The generic protein binding term supplies no informative molecular function beyond the established chaperone role. Remove the uninformative annotation while retaining the interaction observations; do not interpret this as a rejection of the physical interaction or infer an unsupported specific function from a proteomic association.
GO:0010494 cytoplasmic stress granule	HDA PMID:26777405 ATPase-Modulated Stress Granules Contain a Diverse Proteome ...	KEEP AS NON CORE	Summary: As an abundant cytosolic Hsp70, Ssb2 is detected in stress granules; this is a stress-condition localization, not the core function. Reason: Plausible stress-condition localization detected by high-throughput proteomics; peripheral to the core cotranslational folding function.
GO:0005737 cytoplasm	HDA PMID:11914276 Subcellular localization of the yeast proteome.	ACCEPT	Summary: The cytoplasm is a principal location of Ssb2 and its ribosome-associated folding activity. Reason: The translating-ribosome association characterized in PMID:1394434 and PMID:9670014 establishes Ssb cytoplasmic function, consistent with the localization survey. A cellular component can be a core property; the broader cytoplasm term remains accurate alongside cytosol and ribosome annotations.
GO:0005886 plasma membrane	HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and...	KEEP AS NON CORE	Summary: A secondary plasma-membrane-associated Ssb2 pool is compatible with the curated fractionation result. Reason: The HDA annotation from PMID:16622836 records Ssb2 in a stripped plasma-membrane proteome. Its main soluble/ribosomal location does not exclude peripheral membrane association, and lack of a dedicated membrane function is not negative localization evidence. Retain as non-core without claiming membrane integration. For the IBA, GOA names PTN002500132; the current snapshot lacks the membrane assertion, a version discrepancy that does not erase the independent experimental annotation. Supporting Evidence: PMID:16622836 Proteins from a stripped plasma membrane fraction were solubilized
GO:0006452 translational frameshifting	IMP PMID:16607023 Specific effects of ribosome-tethered molecular chaperones o...	KEEP AS NON CORE	Summary: Deletion of Ssb1p/Ssb2p (or RAC) specifically inhibits -1 programmed ribosomal frameshifting and impairs Killer virus maintenance, with no effect on +1 PRF. Reason: Strong direct IMP evidence (PMID:16607023). A genuine, specific downstream consequence of Ssb function at the translating ribosome. Supporting Evidence: PMID:16607023 deletion of Ssb1p/Ssb2p or of Ssz1p/Zuo1p resulted in specific inhibition of -1
GO:0000054 ribosomal subunit export from nucleus	IGI PMID:20368619 A ribosome-anchored chaperone network that facilitates eukar...	KEEP AS NON CORE	Summary: Genetic interaction evidence places Ssb/RAC in a ribosome-anchored chaperone network facilitating ribosome biogenesis, including subunit export. Ancillary to the core cotranslational folding role. Reason: Supported by genetic interaction (PMID:20368619) but ancillary; kept as non-core.
GO:0002181 cytoplasmic translation	IMP PMID:1394434 The translation machinery and 70 kd heat shock protein coope...	KEEP AS NON CORE	Summary: Ssb1/2 are associated with translating ribosomes; ssb1 ssb2 mutants grow slowly, have fewer translating ribosomes, and are hypersensitive to protein synthesis inhibitors, linking Ssb to cytoplasmic translation. Reason: Supported by IMP (PMID:1394434), but cytoplasmic translation is the context for Ssb2's nascent-chain folding activity rather than a separate core activity of the chaperone. Supporting Evidence: PMID:1394434 Mutant ssb1 ssb2 file:yeast/SSB2/SSB2-deep-research-falcon.md Single-gene loss has little obvious phenotype, whereas combined ssb1/2Δ causes broad defects
GO:0002181 cytoplasmic translation	IPI PMID:1394434 The translation machinery and 70 kd heat shock protein coope...	KEEP AS NON CORE	Summary: Ssb1/2p associate with translating ribosomes and the association is disrupted by puromycin, suggesting direct binding to the nascent polypeptide during cytoplasmic translation. Reason: Supported (PMID:1394434). The interaction places Ssb2 in cytoplasmic translation, but this is the context for its core cotranslational folding role rather than a distinct core process. Supporting Evidence: PMID:1394434 The SSB hsp70s (Ssb1/2p) are associated with
GO:0006364 rRNA processing	IGI PMID:20368619 A ribosome-anchored chaperone network that facilitates eukar...	KEEP AS NON CORE	Summary: Genetic interaction places Ssb/RAC in a ribosome-anchored chaperone network facilitating ribosome biogenesis (rRNA processing). Ancillary to the core cotranslational folding role. Reason: Indirect/ancillary role via the ribosome-anchored chaperone network (PMID:20368619); not the core function.
GO:0006450 regulation of translational fidelity	IMP PMID:15456889 The ribosome-bound chaperones RAC and Ssb1/2p are required f...	KEEP AS NON CORE	Summary: Absence of RAC or Ssb1/2p impairs translational fidelity in vivo and in vitro, primarily through a defect in translation termination, enhanced by paromomycin. Reason: Strong direct IMP evidence (PMID:15456889), retained as a genuine secondary consequence beyond Ssb2's core nascent-chain chaperone role. Supporting Evidence: PMID:15456889 Translational fidelity was impaired in the absence of functional RAC or Ssb1/2p
GO:0016887 ATP hydrolysis activity	IDA PMID:9860955 The biochemical properties of the ATPase activity of a 70-kD...	ACCEPT	Summary: Ssb has direct, biochemically characterized ATPase activity with unusual kinetics (low steady-state affinity for ATP, higher Vmax, K+-independent) governed by its C-terminal domains. Reason: Strong direct IDA biochemical evidence (PMID:9860955) for the Ssb ATPase activity underlying its Hsp70 chaperone cycle. Supporting Evidence: PMID:9860955 Ssb, however, has an unusually low steady-state affinity for ATP but a file:yeast/SSB2/SSB2-deep-research-falcon.md core biochemistry is an ATP-driven conformational cycle
GO:0042149 cellular response to glucose starvation	IGI PMID:19723765 The Hsp70 homolog Ssb is essential for glucose sensing via t...	KEEP AS NON CORE	Summary: Ssb is required for glucose sensing via the SNF1 kinase network: the chaperone keeps SNF1 in the nonphosphorylated state in the presence of glucose, and Deltassb1 Deltassb2 cells resemble glucose-repression mutants. Reason: Supported by genetic interaction (PMID:19723765). A genuine downstream physiological role connecting Ssb chaperone function to glucose/SNF1 signaling. Supporting Evidence: PMID:19723765 the chaperone Ssb is required to keep SNF1 in the
GO:0051082 unfolded protein binding	IDA PMID:9670014 The molecular chaperone Ssb from Saccharomyces cerevisiae is...	MODIFY	Summary: Ssb can be cross-linked to nascent chains and is released with nascent chains upon puromycin treatment, demonstrating direct binding to unfolded/nascent polypeptides. GO:0051082 is obsolete; for this ATP-dependent Hsp70, GO:0140662 captures the supported activity. Reason: Modify because GO:0051082 is obsolete, not because the IDA evidence is deficient. OLS directs curators to consider GO:0044183; Ssb2's ATP-dependent Hsp70 mechanism supports its child GO:0140662. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:9670014 Ssb could be cross-linked to nascent chains file:yeast/SSB2/SSB2-deep-research-falcon.md J-domain protein Zuo1 stimulates ATP hydrolysis of Ssb1/2, driving this high-affinity substrate engagement on nascent chains
GO:0051083 'de novo' cotranslational protein folding	IDA PMID:9670014 The molecular chaperone Ssb from Saccharomyces cerevisiae is...	ACCEPT	Summary: Ssb is a core component of the translating ribosome that interacts with both the nascent polypeptide and the ribosome, functioning as a chaperone to prevent misfolding of newly synthesized proteins. This is the core process. Reason: Core function with direct IDA evidence (PMID:9670014). The defining biological role of Ssb2. Supporting Evidence: PMID:9670014 Ssb to function as a chaperone on the ribosome, preventing the misfolding of file:yeast/SSB2/SSB2-deep-research-falcon.md Ssb2 belongs to an Hsp70 triad at the exit tunnel
GO:0043022 ribosome binding	IDA PMID:9670014 The molecular chaperone Ssb from Saccharomyces cerevisiae is...	NEW	Summary: Proposed new annotation for Ssb2's directly characterized physical association with translating ribosomes. Reason: PMID:9670014 used puromycin release, salt resistance, and nascent-chain cross-linking to characterize the Ssb-ribosome interaction; the current SSB2 GOA set lacks ribosome-binding molecular function. Supporting Evidence: PMID:9670014 We propose that Ssb is a core component of the translating ribosome which interacts with both the nascent polypeptide chain and the ribosome.
GO:0022626 cytosolic ribosome	IDA PMID:9670014 The molecular chaperone Ssb from Saccharomyces cerevisiae is...	NEW	Summary: Proposed new annotation for the cytosolic translating ribosome where Ssb2 performs its cotranslational chaperone cycle. Reason: PMID:9670014 directly demonstrates stable Ssb association with translating ribosomes, while PMID:1394434 identifies the SSB proteins as cytosolic Hsp70s associated with translating ribosomes. Supporting Evidence: PMID:9670014 The Ssbs of Saccharomyces cerevisiae are an abundant type of Hsp70 found associated with translating ribosomes. PMID:1394434 We suggest that cytosolic hsp70 aids in the passage of the nascent polypeptide chain through the ribosome in a manner analogous to the role played by organelle-localized hsp70 in the transport of proteins across membranes.

Gene Description

Existing Annotations Review

Core Functions

ATP-dependent Hsp70 molecular chaperone that binds short, largely hydrophobic segments of nascent polypeptides emerging from the ribosomal tunnel exit, using an ATP-driven NBD/SBD conformational cycle (stimulated by the RAC J-protein Zuo1) to promote de novo cotranslational protein folding.

References

Deep Research

Falcon

📚 Additional Documentation

Notes

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