SSA3 (YBL075C) encodes Ssa3, one of the four cytosolic Hsp70-Ssa molecular chaperones of budding yeast. It is an ATP-dependent chaperone of the Hsp70 family with an N-terminal nucleotide-binding/ATPase domain and a C-terminal substrate-binding domain that binds exposed hydrophobic segments of non-native polypeptides to prevent aggregation and promote folding/refolding and protein quality control. Unlike constitutively expressed Ssa1/Ssa2, Ssa3 and Ssa4 are stress/heat-inducible: Ssa3 has very low basal expression and is strongly induced by heat shock and other proteotoxic stress through Hsf1/heat shock element promoter architecture, and SSA3-HSE reporters are widely used as readouts of Hsf1 activity. Ssa3 functions predominantly in the cytosol, with a context-dependent nuclear pool, works with Hsp40 co-chaperones and Hsp110 nucleotide-exchange factors, and contributes to cotranslational folding, post-translational protein translocation, refolding of denatured substrates, and prion propagation. Although the Ssa paralogs are partly redundant, Ssa3 shows measurable functional specialization. SSA3 has a paralog, SSA4, that arose from whole-genome duplication.
| 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. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002500132 · cytosolic/nuclear Hsp70 ancestral node SUPPORTS TRANSFER Current PTHR19375 PAINT places the nucleus IBD on PTN002500132, the opisthokont cytosolic/nuclear Hsp70 node inherited by budding-yeast SSA3. SGD:S000000004 · S. cerevisiae SSA1 SUPPORTS TRANSFER Budding-yeast SSA1 supplies fungal cytosolic-Hsp70 support for stress-linked nuclear localization. UniProtKB:P11142 · human HSPA8 SUPPORTS TRANSFER Human HSPA8 contributes metazoan evidence for nuclear/nucleolar shuttling in this Hsp70 branch. WB:WBGene00002005 · C. elegans hsp-1 SUPPORTS TRANSFER The nematode hsp-1 seed extends support for the secondary nuclear location across opisthokont cytosolic Hsp70s. 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). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002321897 · eukaryotic Hsp70 cytoplasm node SUPPORTS TRANSFER Current PTHR19375 PAINT places the broad cytoplasm IBD on PTN002321897, a eukaryotic Hsp70 node that includes budding-yeast SSA3. SGD:S000000171 · S. cerevisiae SSA3 SUPPORTS TRANSFER The budding-yeast SSA3 self-seed records cytoplasmic localization evidence and is expected in its own inherited IBA. PomBase:SPCC1739.13 · S. pombe ssa2 SUPPORTS TRANSFER The fission-yeast Ssa2 donor is present in the current PTN002321897 seed set and supports broad cytoplasmic localization in the fungal Ssa branch. UniProtKB:P11142 · human HSPA8 SUPPORTS TRANSFER Human HSPA8 contributes metazoan support for this conserved cytoplasmic chaperone compartment. 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 refreshed live GOA no longer carries the GO:0005886 IBA row for Ssa3. That retirement agrees with the current local PTHR19375 PAINT snapshot: node PTN002500132 retains nucleus and cytosol but 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. CGD:CAL0000184706 · pinned Candida plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. CGD:CAL0000184853 · pinned Candida plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. CGD:CAL0000194973 · pinned Candida plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. MGI:MGI:105384 · pinned mouse plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. MGI:MGI:96243 · pinned mouse plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. RGD:1593284 · pinned rat plasma-membrane donor SOURCE STALE OR MISSING This extant donor appears in the pinned GOA WITH/FROM list, but the current PTHR19375 snapshot has no GO:0005886 row. 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. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER Current PTHR19375 PAINT places the ATP hydrolysis IBD on PTN000452648, the deeply conserved Hsp70 ATPase node inherited by budding-yeast SSA3. SGD:S000000171 · S. cerevisiae SSA3 SUPPORTS TRANSFER The budding-yeast SSA3 self-seed is valid Hsp70-family ATPase support and is expected in its own inherited IBA. UniProtKB:P0DMV8 · human HSPA1A SUPPORTS TRANSFER Human HSPA1A supports conservation of ATP hydrolysis in cytosolic Hsp70s. UniProtKB:P38646 · human HSPA9 SUPPORTS TRANSFER Human mitochondrial HSPA9 supports family-wide conservation of the Hsp70 nucleotide-binding ATPase. 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. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER Current PTHR19375 PAINT places the heat-shock-protein-binding IBD on PTN000452648, the Hsp70-family node inherited by SSA3. UniProtKB:P0DMV8 · human HSPA1A SUPPORTS TRANSFER Human HSPA1A is one of the current PTN000452648 seeds for heat-shock-protein binding. UniProtKB:P0DMV9 · human HSPA1B SUPPORTS TRANSFER Human HSPA1B supplies independent cytosolic-Hsp70 support for the same Hsp70-network binding assertion. UniProtKB:P11142 · human HSPA8 SUPPORTS TRANSFER Human HSPA8 is a constitutive cytosolic-Hsp70 donor that supports the conserved heat-shock-protein binding activity. 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 Current PTHR19375 PAINT places the broad chaperone IBD on PTN000452648 and supports transfer to Ssa3, but GO:0140662 captures its ATP-dependent mechanism more precisely. UniProtKB:P0A6Y8 · E. coli DnaK SUPPORTS TRANSFER Bacterial DnaK is one of the current Hsp70-family seeds supporting a deeply conserved ATP-dependent folding chaperone activity. UniProtKB:P0DMV8 · human HSPA1A SUPPORTS TRANSFER Human HSPA1A supports the conserved cytosolic-Hsp70 foldase activity captured by the broad parent term. MGI:MGI:95835 · mouse Hspa5 SUPPORTS TRANSFER The BiP/Grp78 seed supports conservation of ATP-dependent Hsp70 protein-folding chaperone activity outside the cytosolic branch. 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. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002500132 · cytosolic/nuclear Hsp70 ancestral node SUPPORTS TRANSFER Current PTHR19375 PAINT places the cytosol IBD on PTN002500132, the same opisthokont node inherited by budding-yeast SSA3. SGD:S000000171 · S. cerevisiae SSA3 SUPPORTS TRANSFER The budding-yeast SSA3 self-seed reflects direct evidence for cytosolic localization and is expected in its own inherited IBA. PomBase:SPBC1709.05 · S. pombe sks2/hsc1 SUPPORTS TRANSFER The fission-yeast ribosome-associated Hsp70 Sks2/Hsc1 is a current PTN002500132 cytosol donor; it supports cytosolic Hsp70 localization without delimiting the fungal Ssa branch. UniProtKB:P11142 · human HSPA8 SUPPORTS TRANSFER Human HSPA8 contributes metazoan support for cytosolic residence of constitutive Hsp70s. 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. Current PAINT places an IRD (NOT) for this term at PTN001065099 (2026-06-16), a fungal node spanning the SSA, SSB and SSZ1 branches, so this IBA is no longer propagated by PAINT and remains only in the cached GOA file. The PTHR19375 family review judges that IRD too broad (LOSS_TOO_BROAD): the loss fits the ribosome-associated SSB and SSZ1 branches, and the SSA subfamilies, including SF385 with SSA3 and SSA4, should again inherit protein refolding. An IBA asserts inheritance, so SSA-subfamily inheritance is the basis of this ACCEPT; no study found here assays refolding by Ssa3 on its own. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER Current PTHR19375 PAINT still places the protein-refolding IBD on PTN000452648. The same snapshot records a descendant 2026 fungal NOT/IRD at PTN001065099, but the pinned SSA3 row still descends from PTN000452648 and has no GO:0006457 replacement IBA, consistent with SSA3 sitting outside the fungal loss node. SGD:S000000004 · S. cerevisiae SSA1 SUPPORTS TRANSFER Budding-yeast SSA1 is a same-organism donor for the Ssa-family refolding evidence. UniProtKB:P11142 · human HSPA8 SUPPORTS TRANSFER Human HSPA8 supports conservation of Hsp70-mediated protein refolding in the cytosolic branch. UniProtKB:P54652 · human HSPA2 SUPPORTS TRANSFER Human HSPA2 is another current PTN000452648 cytosolic-Hsp70 refolding seed. 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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 ... | REMOVE | 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: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). 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. 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. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: Ssa3 binds ATP through its conserved Hsp70 nucleotide-binding domain; ATP binding is a distinct core activity that gates Hsp70 substrate affinity. Reason: InterPro IPR013126 correctly identifies Ssa3 as an Hsp70, and ATP binding by the N-terminal nucleotide-binding domain is a core step in the Hsp70 chaperone cycle rather than a less-specific substitute for ATP hydrolysis. 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:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: Ssa3 has the conserved Hsp70 ATPase domain and hydrolyzes ATP to drive cycles of client binding and release; this duplicates the current IBA ATPase row but is correct. Reason: InterPro IPR013126 supports ATP hydrolysis activity for Hsp70-family chaperones. ATP hydrolysis, like ATP binding, is a core biochemical step in the Ssa3 chaperone mechanism. 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 |
| GO:0030163 protein catabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Ssa-family Hsp70s can triage misfolded clients toward protein degradation, but protein catabolism is secondary to Ssa3's ATP-dependent folding/refolding chaperone activity. Reason: The broad ARBA protein-catabolic-process mapping is consistent with the role of Ssa Hsp70s in protein quality control and degradation of damaged clients, but it is contextual and less direct than Ssa3's core ATP-dependent chaperone activity. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md Ssa proteins promote folding, translocation, degradation, and refolding of denatured substrates |
| 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: Ssa3 is a cytosolic Hsp70, so the refreshed 2026 PTN002321897 cytoplasm PAINT row remains a correct inherited core localization. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002321897 · eukaryotic Hsp70 cytoplasm node SUPPORTS TRANSFER The current PTHR19375 snapshot retains the broad cytoplasm IBD on PTN002321897, a eukaryotic Hsp70 node that includes budding-yeast SSA3. SGD:S000000171 · S. cerevisiae SSA3 SUPPORTS TRANSFER The refreshed row still carries SSA3 itself as a descendant evidence source, which is expected for a self-supported inherited IBA. Supporting Evidence: file:yeast/SSA3/SSA3-deep-research-falcon.md SSA3 is consistently treated as a **cytosolic** Hsp70 of the Ssa family |
| GO:0006515 protein quality control | 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, including degradation or 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 Hsp70-Ssa proteins bind exposed hydrophobic regions on unfolded proteins, assist folding/refolding, and support proteostasis |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: ATP hydrolysis is a conserved, core Hsp70 molecular function, and the refreshed PTN000452648 IBA continues to place this activity on the broad Hsp70-family node inherited by Ssa3. Reason: The current PTHR19375 PAINT table retains the GO:0016887 IBD assertion at PTN000452648 with fungal, metazoan, plant, and bacterial seeds; ATP hydrolysis is central to Ssa3's Hsp70 chaperone cycle. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · Hsp70 ATPase ancestral node SUPPORTS TRANSFER Current PAINT places the ATP hydrolysis IBD on PTN000452648, the broad Hsp70-family node inherited by budding-yeast SSA3. SGD:S000000171 · S. cerevisiae SSA3 SUPPORTS TRANSFER SSA3 itself is still a descendant evidence source for this row, as expected for an inherited IBA grounded in target-family evidence. 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 |
| GO:0044183 protein folding chaperone | IBA GO_REF:0000033 | MODIFY | Summary: GO:0044183 correctly captures inherited Hsp70 chaperone activity, but GO:0140662 is the more precise ATP-dependent Hsp70 molecular-function term. Reason: The refreshed PTN000452648 transfer remains biologically sound for Ssa3, but the family-level protein-folding-chaperone term should be narrowed to the child term GO:0140662 to capture the ATP-dependent Hsp70 cycle. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000452648 · Hsp70 chaperone ancestral node SUPPORTS TRANSFER PTN000452648 continues to support inherited Hsp70 chaperone activity, but GO:0140662 is the more precise term for Ssa3's ATP-dependent mechanism. 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 |
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Download this section (compressed HTML)ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication
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