SSA3

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Cytosolic Hsp70-Ssa chaperones act largely in the cytosol but the proteostasis network they support spans the cytosol and nucleus, so a nuclear pool is plausible but peripheral to the core function. Kept as non-core. Reason: Falcon describes Ssa3 as predominantly cytosolic, functioning in the cytosol/nucleus proteostasis network. A nuclear localization is plausible but is not the primary site of action, so this is retained as a context-specific, non-core annotation. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Predominantly cytosolic; functions in the cytosol/nucleus proteostasis network
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: Ssa3 is a cytosolic Hsp70; cytoplasmic localization is well supported and consistent with the UniProt subcellular location (Cytoplasm). Reason: Falcon consistently treats SSA3 as a cytosolic Hsp70 of the Ssa family, consistent with UniProt (SUBCELLULAR LOCATION: Cytoplasm). Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a cytosolic Hsp70 of the Ssa family
GO:0005886 plasma membrane	IBA GO_REF:0000033	REMOVE	Summary: Plasma membrane is not a supported site of Ssa3 function. Ssa3 is the stress-inducible cytosolic Hsp70 paralog, and neither UniProt nor the SSA3-focused literature review supports a plasma-membrane pool. Reason: The pinned 2025 GOA row points to PAINT node PTN002500132, but the current local PTHR19375 PAINT snapshot retains nucleus and cytosol at that node and no longer carries GO:0005886. The stale inference also lacks target-specific corroboration: Ssa3 is independently supported as a cytosolic Hsp70. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN002500132 · PAINT Hsp70 family node SOURCE STALE OR MISSING The current PTHR19375 PAINT snapshot has nucleus and cytosol IBD rows at this node but no plasma-membrane IBD row; the pinned GOA transfer is stale. Supporting Evidence: file:yeast/SSA3/SSA3-hypotheses/existing-go-0005886-keep-as-non-core/openscientist.md The plasma-membrane assignment is a phylogenetic (IBA) inference only, carried on GO_REF:0000033, with no yeast-specific experimental support for Ssa3. file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a cytosolic Hsp70 of the Ssa family
GO:0016887 ATP hydrolysis activity	IBA GO_REF:0000033	ACCEPT	Summary: Ssa3 is an ATP-dependent Hsp70; ATP binding and hydrolysis by the N-terminal NBD drive the substrate-binding/release cycle. This is a core catalytic activity of the chaperone. Reason: Falcon establishes that Hsp70/Ssa chaperones are ATP-dependent and that ATP binding and hydrolysis drive the substrate-affinity cycle, supporting ATP hydrolysis activity as a core molecular function. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Hsp70/Ssa chaperones are ATP-dependent. They bind exposed hydrophobic segments of non-native proteins to prevent aggregation and promote productive folding/refolding and quality control. file:yeast/SSA3/SSA3-deep-research-falcon.md ATP binding and hydrolysis drive switching between low-affinity/high-exchange and high-affinity/slow-exchange substrate states; co-chaperones (notably J-domain proteins/Hsp40s) stimulate ATP hydrolysis and nucleotide-exchange factors reset the cycle.
GO:0031072 heat shock protein binding	IBA GO_REF:0000033	ACCEPT	Summary: Ssa3 functions within the Hsp70 chaperone network, interacting with Hsp40 (J-domain) co-chaperones and Hsp110 nucleotide-exchange factors, so heat-shock protein binding is consistent with its biology. Reason: Falcon states that Ssa proteins function with Hsp40 J-proteins and Hsp110 NEFs, supporting heat shock protein binding. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins function with Hsp40 J-proteins and Hsp110 NEFs
GO:0044183 protein folding chaperone	IBA GO_REF:0000033	MODIFY	Summary: Ssa3 is a cytosolic ATP-dependent protein chaperone that assists folding and refolding and limits aggregation of non-native proteins. The more precise molecular function is GO:0140662. Reason: The family-level chaperone term is biologically correct but less precise than the ATP-dependent Hsp70 mechanism supported for Ssa3; replace it with GO:0140662. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER The family transfer correctly identifies chaperone activity in Ssa3, but GO:0140662 captures its ATP-dependent mechanism more precisely. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 encodes a cytosolic ATP-dependent protein chaperone that participates in proteostasis by assisting folding/refolding and limiting aggregation of stress-denatured proteins.
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: The cytosol is the primary site of Ssa3 chaperone activity. Strongly supported and also annotated by direct assay (IDA below). Reason: Falcon consistently treats SSA3 as a cytosolic Hsp70, supporting cytosol as the core cellular component. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a cytosolic Hsp70 of the Ssa family
GO:0042026 protein refolding	IBA GO_REF:0000033	ACCEPT	Summary: Ssa3 promotes refolding of denatured/non-native proteins as part of the cytosolic Hsp70 system, a core biological process for a stress-inducible chaperone. Reason: Falcon states Hsp70-Ssa proteins assist folding/refolding and that Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates, supporting protein refolding as a core process. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates
GO:0000166 nucleotide binding	IEA GO_REF:0000043	MODIFY	Summary: Nucleotide binding is a generic parent of the more informative ATP binding activity; Ssa3 has an N-terminal nucleotide-binding (ATPase) domain. Reason: Nucleotide binding is correct but too broad for the Hsp70 nucleotide-binding domain; replace it with the existing, mechanistically specific ATP-binding term. Proposed replacements: ATP binding Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Hsp70 proteins consist of an N-terminal nucleotide-binding/ATPase domain (NBD) and a substrate-binding domain (SBD) with a helical
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: Ssa3 binds ATP via its N-terminal NBD; ATP binding is required for the Hsp70 chaperone cycle. Core molecular function. Reason: Falcon describes the N-terminal nucleotide-binding/ATPase domain and the ATP-driven substrate-affinity cycle, supporting ATP binding. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Hsp70 proteins consist of an N-terminal nucleotide-binding/ATPase domain (NBD) and a substrate-binding domain (SBD) with a helical
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: Cytoplasmic localization, consistent with UniProt and with the cytosolic assignment of Ssa3. Same conclusion as the IBA cytoplasm annotation above. Reason: Falcon treats SSA3 as a cytosolic Hsp70, consistent with cytoplasm. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a cytosolic Hsp70 of the Ssa family
GO:0006457 protein folding	IEA GO_REF:0000117	ACCEPT	Summary: Ssa3 assists de novo and stress-induced protein folding as a cytosolic Hsp70. Core biological process. Same conclusion as the IGI protein folding annotation below. Reason: Falcon describes Hsp70-Ssa proteins binding non-native proteins to assist folding/refolding, supporting protein folding as a core process. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Hsp70-Ssa proteins bind exposed hydrophobic regions on unfolded proteins, assist folding/refolding, and support proteostasis
GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation	IEA GO_REF:0000117	MODIFY	Summary: Cytosolic Hsp70-Ssa proteins assist precursor translocation, but the available evidence supports post-translational import of selected ER precursors, not SRP-dependent cotranslational targeting. Reason: The broad translocation role is supported, but the electronic annotation is over-specific about SRP dependence. Replace it with the corresponding post-translational targeting/translocation term. Proposed replacements: post-translational protein targeting to membrane, translocation Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000120	ACCEPT	Summary: ATP hydrolysis by the Hsp70 NBD; core catalytic activity. Same conclusion as the IBA and IGI ATP hydrolysis annotations. Reason: Falcon establishes ATP-dependent operation with ATP binding and hydrolysis driving the substrate-affinity cycle. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md ATP binding and hydrolysis drive switching between low-affinity/high-exchange and high-affinity/slow-exchange substrate states; co-chaperones (notably J-domain proteins/Hsp40s) stimulate ATP hydrolysis and nucleotide-exchange factors reset the cycle.
GO:0006457 protein folding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	ACCEPT	Summary: This separate genetic-interaction row is linked to SSA4 (WITH/FROM SGD:S000000905). Kim et al. support SSA-class cytosolic Hsp70 function in folding newly translated proteins; the partner records the tested genetic context rather than an isoform-specific mechanism. Reason: Protein folding is a core Ssa3 process supported at the SSA-family level; retain this partner-specific IGI row. Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0005515 protein binding	IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MTC5 association (WITH/FROM UniProtKB:Q03897) from a high-throughput protein-complex mass-spectrometry study. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–HEM13 association (WITH/FROM UniProtKB:P11353) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RAD50 association (WITH/FROM UniProtKB:P12753) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–YCR043C association (WITH/FROM UniProtKB:P25361) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RAD23 association (WITH/FROM UniProtKB:P32628) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–PMT1 association (WITH/FROM UniProtKB:P33775) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–SIS2 association (WITH/FROM UniProtKB:P36024) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–ENP1 association (WITH/FROM UniProtKB:P38333) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MSB3 association (WITH/FROM UniProtKB:P48566) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RPL38 association (WITH/FROM UniProtKB:P49167) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–PKR1 association (WITH/FROM UniProtKB:Q03880) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MTC5 association (WITH/FROM UniProtKB:Q03897) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MMS22 association (WITH/FROM UniProtKB:Q06164) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–GTT2 association (WITH/FROM UniProtKB:Q12390) from a global affinity-purification protein-complex map. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–HEM13 association (WITH/FROM UniProtKB:P11353) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RAD50 association (WITH/FROM UniProtKB:P12753) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MODIFY	Summary: This separate GOA row records a dataset-level Ssa3–SSA4 association (WITH/FROM UniProtKB:P22202) from the TAP-tag chaperone-interaction atlas. Because SSA4 is another Hsp70 paralog, the partner class supports a more informative Hsp70-protein-binding replacement; the dataset does not by itself establish direct binary contact. Reason: Replace generic protein binding with GO:0030544 Hsp70 protein binding. The curator-supplied partner identity establishes that the bound partner is an Hsp70, which licenses the partner-class refinement even though the affinity-capture dataset does not establish direct binary contact. Proposed replacements: Hsp70 protein binding
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–YCR043C association (WITH/FROM UniProtKB:P25361) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RAD23 association (WITH/FROM UniProtKB:P32628) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–PMT1 association (WITH/FROM UniProtKB:P33775) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–SIS2 association (WITH/FROM UniProtKB:P36024) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–ENP1 association (WITH/FROM UniProtKB:P38333) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MSB3 association (WITH/FROM UniProtKB:P48566) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–RPL38 association (WITH/FROM UniProtKB:P49167) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–PKR1 association (WITH/FROM UniProtKB:Q03880) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MTC5 association (WITH/FROM UniProtKB:Q03897) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–MMS22 association (WITH/FROM UniProtKB:Q06164) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–GTT2 association (WITH/FROM UniProtKB:Q12390) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:27107014 An inter-species protein-protein interaction network across ...	MARK AS OVER ANNOTATED	Summary: This separate GOA row records a dataset-level Ssa3–human HSPBP1 association (WITH/FROM UniProtKB:Q9NZL4) from an inter-species interaction network. The generic term does not identify an enabled molecular function and the dataset does not by itself establish direct binary contact. Reason: Protein binding is uninformative; retain the partner provenance in the review but do not use this generic term as a functional assertion.
GO:0005515 protein binding	IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i...	MODIFY	Summary: This separate GOA row records a dataset-level Ssa3–SSA4 association (WITH/FROM UniProtKB:P22202) from a paralog-heteromer retention study. Because SSA4 is another Hsp70 paralog, the partner class supports a more informative Hsp70-protein-binding replacement; the dataset does not by itself establish direct binary contact. Reason: Replace generic protein binding with GO:0030544 Hsp70 protein binding. The curator-supplied partner identity establishes that the bound partner is an Hsp70, which licenses the partner-class refinement even though the study does not establish direct binary contact for this pair. Proposed replacements: Hsp70 protein binding
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins	IMP PMID:24855027 Life-span extension by a metacaspase in the yeast Saccharomy...	KEEP AS NON CORE	Summary: Ssa3, as a cytosolic Hsp70, contributes to protein quality control of misfolded/non-native proteins. The cached PMID:24855027 record is abstract-only and Mca1-focused and does not expose the SSA3-specific IMP experiment, so this curator annotation is retained by deference as a genuine but non-core proteostasis process. Reason: Falcon supports the general role of cytosolic Hsp70-Ssa proteins in proteostasis and quality control (degradation/refolding of non-native substrates). Because the cached paper is abstract-only and does not show the SSA3-specific experiment available to the curator, retain the IMP by deference and keep the process annotation non-core. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates
GO:0005829 cytosol	IDA PMID:10745074 Cytosolic Hsp70s are involved in the transport of aminopepti...	ACCEPT	Summary: Cytosol is the established primary compartment of Ssa3. The cached abstract discusses cytoplasmic Ssa-family Hsp70s and focuses its detailed localization results on Ssa1/2, so it does not by itself establish an SSA3-specific direct assay; the curator annotation is retained because the localization is independently well supported. Reason: Cytosol is biologically correct for Ssa3 and consistent with UniProt and the SSA3-focused literature review. The cached abstract is incomplete for the SSA3-specific experimental detail, so this ACCEPT defers to the curator rather than overclaiming what the abstract shows. Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins. file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a cytosolic Hsp70 of the Ssa family
GO:0006457 protein folding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	ACCEPT	Summary: This separate genetic-interaction row is linked to SSA1 (WITH/FROM SGD:S000000004). Kim et al. support SSA-class cytosolic Hsp70 function in folding newly translated proteins; the partner records the tested genetic context rather than an isoform-specific mechanism. Reason: Protein folding is a core Ssa3 process supported at the SSA-family level; retain this partner-specific IGI row. Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0051082 unfolded protein binding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	MODIFY	Summary: This separate genetic-interaction row is linked to SSA1 (WITH/FROM SGD:S000000004). Binding non-native clients is real, but the productive, ATP-coupled chaperone activity is more precisely represented by GO:0140662. Reason: Replace generic unfolded-protein binding with ATP-dependent protein folding chaperone activity while retaining this partner-specific IGI provenance. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0051082 unfolded protein binding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	MODIFY	Summary: This separate genetic-interaction row is linked to SSA4 (WITH/FROM SGD:S000000905). Binding non-native clients is real, but the productive, ATP-coupled chaperone activity is more precisely represented by GO:0140662. Reason: Replace generic unfolded-protein binding with ATP-dependent protein folding chaperone activity while retaining this partner-specific IGI provenance. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0051082 unfolded protein binding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	MODIFY	Summary: This separate genetic-interaction row is linked to SSA2 (WITH/FROM SGD:S000003947). Binding non-native clients is real, but the productive, ATP-coupled chaperone activity is more precisely represented by GO:0140662. Reason: Replace generic unfolded-protein binding with ATP-dependent protein folding chaperone activity while retaining this partner-specific IGI provenance. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0006457 protein folding	IGI PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme...	ACCEPT	Summary: This separate genetic-interaction row is linked to SSA2 (WITH/FROM SGD:S000003947). Kim et al. support SSA-class cytosolic Hsp70 function in folding newly translated proteins; the partner records the tested genetic context rather than an isoform-specific mechanism. Reason: Protein folding is a core Ssa3 process supported at the SSA-family level; retain this partner-specific IGI row. Supporting Evidence: PMID:9789005 yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins.
GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation	IMP PMID:8754838 Functional interaction of cytosolic hsp70 and a DnaJ-related...	MODIFY	Summary: Cytosolic Hsp70-Ssa, together with Ydj1, supports precursor protein translocation in vivo. The strongest direct result is rapid inhibition of post-translational ER import of prepro-alpha-factor; this is not an SRP-dependent cotranslational process. Reason: The essence of the annotation is supported, but the term is over-specific. Replace it with post-translational protein targeting to membrane, translocation (GO:0031204). The paper also reports a mitochondrial precursor phenotype, but that broader effect is not encoded by this ER-scoped replacement. Proposed replacements: post-translational protein targeting to membrane, translocation Supporting Evidence: PMID:8754838 prepro-alpha-factor was inhibited within 2 min of the shift to 37 degrees C, suggesting a direct effect of the hsp70 defect on translocation. More than 50% of radiolabeled alpha-factor accumulated in the precursor form file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates
GO:0016887 ATP hydrolysis activity	IGI PMID:3302682 Complex interactions among members of an essential subfamily...	ACCEPT	Summary: The GOA row records an SSA3–SSA1 genetic interaction (WITH/FROM SGD:S000000004). Genetic interactions within the essential SSA subfamily are consistent with ATP-dependent Hsp70 chaperone activity; the ATPase claim is accepted on established Hsp70 family mechanism rather than as a direct biochemical assay in this paper. Reason: Falcon establishes ATP-dependent operation of the Ssa chaperones with ATP hydrolysis driving the substrate-affinity cycle. PMID:3302682 supplies the SSA1 genetic-interaction context, while the biochemical ATPase conclusion rests on the independently established Hsp70 family mechanism. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Hsp70/Ssa chaperones are ATP-dependent. They bind exposed hydrophobic segments of non-native proteins to prevent aggregation and promote productive folding/refolding and quality control.
GO:0051082 unfolded protein binding	IEA GO_REF:0000117	MODIFY	Summary: Ssa3 binds non-native/unfolded proteins, but as an ATP-dependent Hsp70 the more precise molecular function is ATP-dependent protein folding chaperone activity (GO:0140662), which is also the term InterPro assigns in UniProt. Reason: Falcon emphasizes ATP-dependent, ATPase-cycle-coupled substrate binding; GO:0140662 (ATP-dependent protein folding chaperone) captures this more precisely than the generic unfolded protein binding, and matches the InterPro IEA annotation in UniProt. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md ATP binding and hydrolysis drive switching between low-affinity/high-exchange and high-affinity/slow-exchange substrate states; co-chaperones (notably J-domain proteins/Hsp40s) stimulate ATP hydrolysis and nucleotide-exchange factors reset the cycle.

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

OpenScientist

📚 Additional Documentation

Notes

📄 View Raw YAML