SSA1 encodes the major constitutively expressed cytosolic Ssa-family Hsp70 chaperone in Saccharomyces cerevisiae. Ssa1 binds non-native polypeptides and uses an ATP-driven substrate-binding cycle to promote folding and refolding, prevent aggregation, and support proteostasis. J-domain cochaperones such as Ydj1 and Sis1 stimulate its ATPase cycle, while nucleotide-exchange factors including Sse1/Sse2 and Fes1 promote ADP release. Ssa1 also cooperates with Hsp104 and Hsp40 in recovery of aggregated proteins and applies this core chaperone mechanism to protein targeting, degradation, and stress responses.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: SSA1 has been detected in the nucleus by multiple methods. It is involved in protein import into the nucleus (PMID:10347213) and in tRNA import (PMID:25853343). IBA annotation is consistent with IDA evidence from PMID:10347213 and HDA from PMID:11914276. Reason: Correct and well-supported by experimental localization and nuclear-import studies, but nuclear localization is secondary to Ssa1's predominant cytosolic chaperone function. Supporting Evidence: file:yeast/SSA1/SSA1-deep-research-falcon.md Ssa1 is primarily **cytosolic** but also functions in the **nucleus** |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: SSA1 is the major cytoplasmic Hsp70 chaperone. IBA is consistent with extensive experimental evidence (IDA from PMID:8755907, HDA from PMID:11914276). Reason: Core localization. SSA1 is constitutively expressed and highly abundant in the cytoplasm. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | REMOVE | Summary: The pinned GOA row carries a plasma-membrane IBA, but the current local PTHR19375 PAINT snapshot no longer places GO:0005886 at the cited PTN002500132 node. This stale propagation is removed independently of the separate experimental HDA row, which is retained conservatively as non-core. Reason: The pinned 2025 GOA row points to PAINT node PTN002500132, whereas the current PTHR19375 snapshot has nucleus and cytosol IBD rows at that node and no plasma-membrane IBD row. The source state is therefore stale or missing; this conclusion is based on current node content, not donor count. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN002500132 · PAINT Hsp70 family node SOURCE STALE OR MISSING Current PTHR19375 data retain GO:0005634 and GO:0005829 at this node but not GO:0005886. |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: SSA1 has well-characterized ATPase activity, demonstrated directly by IDA in PMID:7737974 and PMID:18706386. The ATPase cycle is central to its chaperone mechanism. IBA is consistent. Reason: Core molecular function. The ATPase activity of SSA1 is well established and drives the chaperone cycle. Supporting Evidence: PMID:7737974 The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. PMID:18706386 Ssa1(L483W) ATPase activity was elevated 10-fold and was least stimulated by substrates or Hsp40 co-chaperones. file:yeast/SSA1/SSA1-deep-research-falcon.md ATP binding/hydrolysis in the NBD drives conformational switching in the SBD that controls client affinity |
| GO:0031072 heat shock protein binding | IBA GO_REF:0000033 | ACCEPT | Summary: SSA1 interacts with numerous heat shock proteins including Hsp90 (HSP82, HSC82), Hsp110 (SSE1, SSE2), and Hsp40s (Ydj1, Sis1). These interactions are well documented by co-purification and two-hybrid studies. Reason: The PAINT assertion is supported at Hsp70 family node PTN000452648. Targeted biochemical and structural studies further establish the Ssa1-Sse1 Hsp70-Hsp110 complex (PMID:16688211; PMID:18555782). Bulk interaction-screen rows are only corroborating context and are not used to infer this molecular function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000452648 · PAINT Hsp70 family node SUPPORTS TRANSFER The current PAINT node carries the GO:0031072 IBD assertion and supports transfer to Ssa1. Supporting Evidence: PMID:16688211 that the yeast homologue, Sse1p, acts as an efficient nucleotide exchange factor PMID:18555782 Here we present the crystal structure of the yeast NEF Sse1p (Hsp110) in complex with the nucleotide-binding domain (NBD) of Hsp70. file:yeast/SSA1/SSA1-deep-research-falcon.md A 2024 NMR study mapped how the **Ssa1 C-terminal EEVD motif** binds **Sis1** at multiple sites, refining the physical basis of Hsp70–JDP coordination |
| GO:0044183 protein folding chaperone | IBA GO_REF:0000033 | MODIFY | Summary: SSA1 is a bona fide protein folding chaperone. It assists de novo folding of newly translated proteins (PMID:9789005) and refolding of denatured proteins (PMID:8947547, PMID:18706386). The IBA annotation correctly captures the core molecular function. Reason: The family-level chaperone term is correct but less precise than the directly supported ATP-dependent Hsp70 mechanism. 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 Ssa1, but GO:0140662 captures its ATP-dependent mechanism more precisely. 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 PMID:8947547 These results demonstrate, for the first time, the refolding activity of Ssa1/2p in the context of the yeast cytosol, and define refolding activity as a chaperone function specific to Ssa1/2p file:yeast/SSA1/SSA1-deep-research-falcon.md SSA1 encodes **Ssa1**, an **ATP-dependent Hsp70 “foldase”/chaperone hub** that binds non-native protein segments (typically exposed hydrophobic stretches) |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: SSA1 is primarily a cytosolic protein. IBA is consistent with HDA evidence (PMID:26928762). Reason: Core localization. SSA1 is the major cytosolic Hsp70. |
| GO:0042026 protein refolding | IBA GO_REF:0000033 | ACCEPT | Summary: SSA1 is directly involved in protein refolding, both alone and in collaboration with Hsp104 and Hsp40. IBA is consistent with IDA evidence from PMID:18706386, PMID:9674429, and PMID:8947547. Reason: Well-supported core function. Refolding of denatured proteins is a central activity of SSA1. Supporting Evidence: PMID:9674429 in concert with Hsp40 and Hsp70, Hsp104 can reactivate proteins that have been denatured and allowed to aggregate PMID:8947547 Depletion of Ssa1/2p had no effect on the ability of the yeast lysate to synthesize enzymatically active luciferase, but had a dramatic effect on the ability of the lysate to refold chemically denatured luciferase. file:yeast/SSA1/SSA1-deep-research-falcon.md refolding of stress-denatured proteins, |
| GO:0000049 tRNA binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: IEA annotation for tRNA binding. Consistent with IDA evidence from PMID:25853343 which demonstrates that SSA1 binds tRNA as part of a tRNA nuclear import system. Reason: Correct but non-core. The IEA is supported by direct experimental evidence (IDA from PMID:25853343) showing SSA1 binds tRNA to facilitate its nuclear import. However, tRNA binding is a specialized/moonlighting activity, not part of SSA1's core chaperone function. |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | MARK AS OVER ANNOTATED | Summary: SSA1 binds ATP and ADP as part of its chaperone cycle. This is a parent term of ATP binding and is correct but overly general. Reason: The annotation is not false, but it is redundant and substantially less informative than the existing ATP-binding and ATP-hydrolysis annotations. |
| GO:0000329 fungal-type vacuole membrane | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: SSA1 localization to the vacuole membrane is supported by IDA evidence from PMID:10745074, which showed SSA1 involvement in aminopeptidase I transport to the vacuole. Reason: Direct experiments localize Ssa1/2 to the vacuolar membrane during Ape1 transport, but this is a specialized localization rather than the core site of Ssa1 chaperone activity. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: SSA1 is an ATPase and binds ATP through its nucleotide-binding domain (NBD). This is core to its function. Reason: Correct and fundamental. ATP binding is essential for the SSA1 chaperone cycle. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Duplicate of the IBA and IDA annotations for cytoplasm. Correct. Reason: Correct. Redundant with IBA and IDA annotations but acceptable. |
| GO:0006457 protein folding | IEA GO_REF:0000117 | ACCEPT | Summary: SSA1 is directly involved in protein folding as demonstrated experimentally (IDA from PMID:8947547). IEA is consistent. Reason: Correct. Consistent with direct experimental evidence. |
| GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation | IEA GO_REF:0000117 | MODIFY | Summary: SSA1 has been implicated in protein translocation to the ER membrane (IDA from PMID:8754838). However, PMID:8947547 found that depletion of Ssa1/2p had no effect on translocation efficiency in vitro. The role may be more indirect. Reason: The cited SSA/Ydj1 evidence concerns post-translational precursor translocation rather than the SRP-dependent cotranslational route. The replacement captures the supported mechanism without making it core. Proposed replacements: post-translational protein targeting to membrane, translocation |
| GO:0009277 fungal-type cell wall | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: SSA1 has been detected in the cell wall by IDA (PMID:8755907). IEA is consistent. Reason: Direct cell-wall immunoblot, intact-cell immunofluorescence, and surface biotinylation support the localization, but it is secondary to the core cytosolic chaperone function. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: Duplicate of IBA and IDA annotations. Correct InterPro-based annotation. Reason: Correct. Redundant with IBA and IDA annotations but acceptable. |
| GO:0033554 cellular response to stress | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: SSA1 is a heat shock protein involved in stress response. The more specific term GO:0034605 (cellular response to heat) is annotated with IDA evidence (PMID:24291094). This broader term is acceptable. Reason: Correct but broad and secondary to Ssa1's direct folding/refolding mechanism; retain alongside the experimentally supported heat-response annotation without treating it as a separate core function. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: SSA1 participates in ubiquitin-dependent protein degradation as demonstrated by IMP/IGI evidence from PMID:27178214. IEA is consistent. Reason: Correct but non-core. SSA1 assists in presenting misfolded substrates to the ubiquitin-proteasome system, which is part of its broader protein quality control role but not its primary chaperone function. |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000117 | MODIFY | Summary: GO:0051082 (obsolete unfolded protein binding) was obsoleted on 2026-07-25. SSA1 does bind unfolded proteins, but this is part of its chaperone activity, not a standalone binding function. The appropriate replacement is GO:0044183 (protein folding chaperone) or more specifically GO:0140662 (ATP-dependent protein folding chaperone). Reason: GO:0051082 is obsolete. SSA1 binds unfolded proteins as part of its ATP-dependent chaperone cycle, not as a passive binding activity. The correct annotation is the already-present GO:0044183 (protein folding chaperone) or its child GO:0140662 (ATP-dependent protein folding chaperone). Since GO:0044183 is already annotated via IBA, this IEA annotation should be replaced. Proposed replacements: ATP-dependent protein folding chaperone |
| GO:0051170 import into nucleus | IEA GO_REF:0000117 | ACCEPT | Summary: SSA1 is involved in nuclear import. This is a parent of GO:0006606 (protein import into nucleus), which has IDA/IGI evidence from PMID:10347213. IEA is consistent but less specific. Reason: Correct but general. Consistent with the more specific experimental annotation for protein import into nucleus. |
| GO:0005515 protein binding | IPI PMID:14729968 The ctf13-30/CTF13 genomic haploinsufficiency modifier scree... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32832) from a proteasome-interaction affinity-capture study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:14729968 The ctf13-30/CTF13 genomic haploinsufficiency modifier scree... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P43609) from a proteasome-interaction affinity-capture study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:14729968 The ctf13-30/CTF13 genomic haploinsufficiency modifier scree... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q06639) from a proteasome-interaction affinity-capture study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:15102838 A novel mode of chaperone action: heme activation of Hap1 by... | MARK AS OVER ANNOTATED | Summary: IPI evidence for SSA1 binding HAP1 (UniProtKB:P0CS82). SSA1 is part of the HAP1 transcriptional repressor complex (CPX-1882 in ComplexPortal) where it represses HAP1 activity in the absence of heme. This is a specific and well-characterized chaperone-client interaction. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P02829) from a large-scale affinity-purification protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P15108) from a large-scale affinity-purification protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16284124 An integrated mass spectrometry-based proteomic approach: qu... | MARK AS OVER ANNOTATED | Summary: IPI evidence for SSA1 binding RPT6 (UniProtKB:Q01939; proteasome subunit) from a proteasome interactome study. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P04806) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P05453) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P06785) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P07259) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P07991) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10592) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10964) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P12688) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P14680) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P19454) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25343) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P27697) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P28273) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P29547) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32454) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32589) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32861) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P33416) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P34241) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P35207) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P36102) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38260) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38798) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38996) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P39102) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P39677) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P52488) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53276) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53855) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q04217) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q04947) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05022) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q06697) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q08972) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12033) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12118) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12125) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12234) from the Gavin et al. TAP-MS protein-complex survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:16688211 Chaperone network in the yeast cytosol: Hsp110 is revealed a... | MODIFY | Summary: IPI evidence for SSA1 binding SSE1 (UniProtKB:P32589; Hsp110). This study revealed Sse1 as an Hsp70 nucleotide exchange factor. The Ssa1-Sse1 interaction is functionally critical. Reason: Protein binding is uninformative. This targeted biochemical study identifies a stable Ssa1-Sse1 Hsp70-Hsp110 complex and establishes Sse1 as an Ssa1 nucleotide-exchange factor, licensing the partner-class refinement to GO:0031072. Partner identity alone, as reported by bulk interaction screens, is not sufficient for this refinement. Proposed replacements: heat shock protein binding |
| GO:0005515 protein binding | IPI PMID:17441508 SGT2 and MDY2 interact with molecular chaperone YDJ1 in Sacc... | MARK AS OVER ANNOTATED | Summary: IPI evidence for SSA1 binding SGT2 (UniProtKB:Q12118) via Ydj1. SGT2 is involved in the GET pathway for tail-anchored protein targeting. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:17892321 Structure-templated predictions of novel protein interaction... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25294) from a genome-scale structure-templated interaction-prediction study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:17892321 Structure-templated predictions of novel protein interaction... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53940) from a genome-scale structure-templated interaction-prediction study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:18555782 Structural basis for the cooperation of Hsp70 and Hsp110 cha... | MODIFY | Summary: IPI evidence for SSA1 binding SSE1 (UniProtKB:P32589). Structural basis for Hsp70-Hsp110 cooperation. The Ssa1-Sse1 complex structure was determined. Reason: Protein binding is uninformative. This targeted structural study resolves a yeast Sse1-Hsp70 complex, licensing the partner-class refinement to GO:0031072. Partner identity alone, as reported by bulk interaction screens, is not sufficient for this refinement, and the interaction is not reinterpreted as a separate catalytic reaction. Proposed replacements: heat shock protein binding |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | MARK AS OVER ANNOTATED | Summary: High-quality binary protein interaction map (Yu et al. 2008) with pinned partner UniProtKB:P38260. Large-scale Y2H study. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P00546) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P00942) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P02829) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P04806) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P05453) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P06785) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P07259) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P07991) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P0CS82) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10592) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10659) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10964) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P11484) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P12688) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P13365) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P14680) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P15108) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P16861) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P17157) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P19454) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P22137) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25294) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25343) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25491) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P27697) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P28273) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P29547) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32324) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32454) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32565) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32589) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32590) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32598) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32832) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32861) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P33416) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P34241) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P35177) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P35207) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P36016) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P36102) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38129) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38260) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38798) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38821) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38922) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38996) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P39102) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P39677) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P41277) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P43558) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P43609) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P47103) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P50102) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P52488) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53276) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53855) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01454) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01476) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01939) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q02336) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q03761) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q03921) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q04217) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q04947) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05022) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05027) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05788) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q06639) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q06697) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q08972) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12004) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12033) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12118) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12125) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12176) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12234) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12449) from the TAP-tag chaperone-interaction atlas. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P35177) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38129) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P50102) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q02336) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q03761) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21734642 Combinatorial depletion analysis to assemble the network arc... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05027) from a combinatorial SAGA/ADA complex analysis. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:21876155 Control of the function of the transcription and repair fact... | MARK AS OVER ANNOTATED | Summary: IPI evidence for SSA1 binding TFB4 (UniProtKB:Q12004; TFIIH subunit). Study showed cochaperone Ydj1 controls TFIIH function via SSA1. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P00546) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P00942) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P02829) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P05453) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P07259) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10659) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P10964) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P11484) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P12688) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P13365) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P14680) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P15108) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P16861) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P17157) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P22137) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25294) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25343) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25491) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P25693) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P29547) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32324) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32565) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32589) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32590) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32598) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32832) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P32861) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P33416) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P35190) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P36016) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38260) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38821) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38922) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P38996) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P41277) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P43558) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P43609) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P53276) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01454) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01476) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q01939) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q03921) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q04947) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05022) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q05788) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q08972) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12118) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12125) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12176) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:Q12449) from a phosphoregulated Hsp70 interaction survey. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:24239293 Rrp5 binding at multiple sites coordinates pre-rRNA processi... | MARK AS OVER ANNOTATED | Summary: IPI evidence for SSA1 binding RRP5 (UniProtKB:Q05022). Rrp5 is involved in pre-rRNA processing. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:37070168 RNA-dependent interactome allows network-based assignment of... | MARK AS OVER ANNOTATED | Summary: RNA-dependent interactome study. SSA1 interacts with GLC7 (UniProtKB:P32598) in an RNA-dependent manner. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | MARK AS OVER ANNOTATED | Summary: Social and structural architecture of the yeast protein interactome with pinned partner UniProtKB:P00942. Large-scale study. Reason: Protein binding is uninformative. Preserve the targeted partner and study context in the row, but do not convert an interaction observation into a protein-folding-chaperone reaction without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P02829) from an Hsp70/Hsp90 chaperone-network study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | MARK AS OVER ANNOTATED | Summary: This separate pinned GOA row records a dataset-level Ssa1 association (WITH/FROM UniProtKB:P47103) from an Hsp70/Hsp90 chaperone-network study. The generic term does not identify an enabled molecular function, and the dataset-level association does not by itself establish a direct binary contact or a specific chaperone reaction. Reason: Protein binding is uninformative. Preserve the exact partner provenance in this row, but do not convert an interaction observation into a chaperone activity assertion without reaction-specific evidence. |
| GO:0005634 nucleus | NAS PMID:15102838 A novel mode of chaperone action: heme activation of Hap1 by... | KEEP AS NON CORE | Summary: NAS annotation from ComplexPortal for SSA1 nuclear localization in context of the HAP1 repressor complex. Consistent with IDA evidence from PMID:10347213. Reason: Correct, but this nuclear client-specific role is secondary to Ssa1's core cytosolic chaperone function. |
| GO:0045892 negative regulation of DNA-templated transcription | NAS PMID:15102838 A novel mode of chaperone action: heme activation of Hap1 by... | KEEP AS NON CORE | Summary: SSA1 is part of the HAP1 transcriptional repressor complex (ComplexPortal CPX-1882) where it represses HAP1-dependent transcription in the absence of heme. This is a well-characterized indirect regulatory role. Reason: This is a genuine but secondary function of SSA1. It acts as a repressive chaperone holdase for HAP1, preventing transcriptional activation. This is not a core molecular function of SSA1 but rather a consequence of its chaperone activity on a specific client (HAP1). |
| GO:0070482 response to oxygen levels | NAS PMID:15102838 A novel mode of chaperone action: heme activation of Hap1 by... | KEEP AS NON CORE | Summary: SSA1 is part of the HAP1 complex that responds to heme/oxygen levels. The Hsp90 chaperone cycle regulates HAP1 activation in response to heme. Reason: This is a secondary consequence of SSA1's role in the HAP1 repressor complex, not a core function. SSA1 participates in oxygen sensing through its chaperone role on HAP1 but is not itself a sensor. |
| GO:0070482 response to oxygen levels | NAS PMID:9632766 Molecular mechanism governing heme signaling in yeast: a hig... | KEEP AS NON CORE | Summary: Same process annotation from a different reference. PMID:9632766 describes the higher-order HAP1 complex mechanism. Reason: Duplicate process annotation for the same indirect role. SSA1 participates in oxygen/heme signaling through the HAP1 complex but this is not its core function. |
| GO:0034605 cellular response to heat | IDA PMID:24291094 Coordination of translational control and protein homeostasi... | KEEP AS NON CORE | Summary: SSA1 is directly involved in the cellular response to heat. PMID:24291094 showed SSA1 coordinates translational control and protein homeostasis during severe heat stress, including stress granule disassembly. Reason: This is a well-supported physiological role, but it is an application of SSA1's core ATP-dependent chaperone mechanism rather than a separate core molecular function. During heat stress, Ssa1 supports proteostasis and stress granule disassembly; Hsp70 binding also restrains Hsf1 until accumulating misfolded proteins titrate Hsp70 away and free Hsf1 activity. Supporting Evidence: file:yeast/SSA1/SSA1-deep-research-falcon.md Hsp70 binding restrains Hsf1, and misfolded proteins titrate Hsp70 away under heat shock, freeing Hsf1 activity |
| GO:0072671 mitochondria-associated ubiquitin-dependent protein catabolic process | IMP PMID:32118579 A protein quality control pathway at the mitochondrial outer... | KEEP AS NON CORE | Summary: PMID:32118579 described a protein quality control pathway at the mitochondrial outer membrane (mitoRQC) requiring SSA1. SSA1 assists in degradation of proteins that fail to import into mitochondria. Reason: Genuine but secondary function. SSA1 participates in mitochondrial protein quality control as part of its broader role in ubiquitin-dependent protein degradation, but this is not its primary function. |
| GO:0006606 protein import into nucleus | IDA PMID:10347213 A nuclear export signal prevents Saccharomyces cerevisiae Hs... | KEEP AS NON CORE | Summary: PMID:10347213 demonstrated that SSA1 is involved in nuclear protein import using direct assay. SSA1 was shown to stimulate nuclear localization signal-directed nuclear transport. Reason: Genuine but secondary function. SSA1 facilitates nuclear import by maintaining substrates in import-competent conformations, which is a consequence of its chaperone activity rather than a specialized nuclear import function. |
| GO:0006606 protein import into nucleus | IGI PMID:10347213 A nuclear export signal prevents Saccharomyces cerevisiae Hs... | KEEP AS NON CORE | Summary: IGI evidence from the same study, with genetic interaction with SSB1 (SGD:S000004571). Reason: Same function as above, supported by genetic interaction data. Secondary function. |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: HDA evidence from SWAp-Tag strategy for yeast library creation. Consistent with SSA1 being a cytosolic protein. Reason: Correct core localization. SSA1 is predominantly cytosolic. Supporting Evidence: file:yeast/SSA1/SSA1-deep-research-falcon.md Ssa1 is primarily **cytosolic** but also functions in the **nucleus** |
| GO:0005634 nucleus | HDA PMID:11914276 Subcellular localization of the yeast proteome. | KEEP AS NON CORE | Summary: HDA evidence from the Huh et al. global GFP-tagged protein localization study. SSA1-GFP was detected in the nucleus. Reason: Correct and experimentally supported, but secondary to the predominant cytosolic localization. |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: HDA evidence from the global localization study. SSA1 is cytoplasmic. Reason: Correct core localization. |
| GO:0005886 plasma membrane | HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and... | KEEP AS NON CORE | Summary: HDA evidence from plasma membrane proteome study. SSA1 was detected in the plasma membrane fraction. Reason: Retain conservatively as a non-core high-throughput fractionation result; the abstract does not establish a stable or functional plasma-membrane pool. Supporting Evidence: file:yeast/SSA1/SSA1-hypotheses/existing-go-0005886-keep-as-non-core/openscientist.md Because the annotation reflects bulk co-purification rather than a demonstrated functional site, treating plasma membrane as **non-core is the correct handling of the evidence weight** |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IMP PMID:27178214 The requirements of yeast Hsp70 of SSA family for the ubiqui... | KEEP AS NON CORE | Summary: PMID:27178214 demonstrated SSA1's requirement for ubiquitin-dependent degradation of short-lived and abnormal proteins via mutant phenotype analysis. Reason: Genuine but secondary function. SSA1 assists in presenting misfolded substrates to the ubiquitin-proteasome system. This is part of its broader protein quality control role. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IGI PMID:27178214 The requirements of yeast Hsp70 of SSA family for the ubiqui... | KEEP AS NON CORE | Summary: IGI evidence from the same study showing genetic interaction with SSE1 (SGD:S000003947) in proteasomal degradation. Reason: Same function as above, supported by genetic interaction. Secondary function. |
| GO:0000209 protein polyubiquitination | IDA PMID:20462952 Ubr1 and Ubr2 function in a quality control pathway for degr... | KEEP AS NON CORE | Summary: PMID:20462952 showed SSA1 functions in a quality control pathway for degradation of unfolded cytosolic proteins. SSA1 delivers misfolded substrates to E3 ubiquitin ligases Ubr1/Ubr2 for polyubiquitination. Reason: Genuine but secondary function. SSA1 participates in ubiquitin-mediated protein quality control by delivering substrates for ubiquitination, but this is downstream of its core chaperone function. Falcon corroborates that in the San1/Ubr1 quality control pathways Ssa1/Ssa2 are required both outside and inside the nucleus. Supporting Evidence: file:yeast/SSA1/SSA1-deep-research-falcon.md In San1/Ubr1 QC pathways, **Ssa1/Ssa2 are required both outside and inside the nucleus**, while Ydj1 and Sse1 contribute to trafficking/import and Sis1 is required inside the nucleus |
| GO:0000049 tRNA binding | IDA PMID:25853343 Cytosolic Hsp70 and co-chaperones constitute a novel system ... | KEEP AS NON CORE | Summary: PMID:25853343 demonstrated that cytosolic Hsp70 (SSA1) and co-chaperones constitute a novel system for tRNA import into the nucleus. SSA1 directly binds tRNA. Reason: Genuine but specialized function. tRNA binding is a moonlighting activity of SSA1 related to its role in tRNA nuclear import. It is not the core chaperone function. |
| GO:0035617 stress granule disassembly | IDA PMID:24291094 Coordination of translational control and protein homeostasi... | KEEP AS NON CORE | Summary: PMID:24291094 showed SSA1 promotes stress granule disassembly during recovery from heat stress. Reason: Genuine but secondary function. Stress granule disassembly is a specific consequence of SSA1's chaperone/disaggregase activity during stress recovery. |
| GO:0072318 clathrin coat disassembly | IDA PMID:23913685 Clathrin coat disassembly by the yeast Hsc70/Ssa1p and auxil... | KEEP AS NON CORE | Summary: PMID:23913685 demonstrated SSA1 participates in ATP-dependent disassembly of clathrin coats, functioning analogously to mammalian Hsc70/HSPA8 with auxilin/Swa2p. Reason: Genuine but specialized function. Clathrin uncoating is a well-characterized Hsp70 function conserved from yeast to mammals, but it is a specific application of the general chaperone/ATPase activity rather than a core function per se. |
| GO:0016887 ATP hydrolysis activity | IDA PMID:7737974 The dissociation of ATP from hsp70 of Saccharomyces cerevisi... | ACCEPT | Summary: PMID:7737974 directly demonstrated that ATP dissociation from SSA1 is stimulated by both Ydj1p and peptide substrates. This establishes SSA1's intrinsic ATPase activity. Reason: Core molecular function with direct experimental evidence. Supporting Evidence: PMID:7737974 The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. |
| GO:0000329 fungal-type vacuole membrane | IDA PMID:10745074 Cytosolic Hsp70s are involved in the transport of aminopepti... | KEEP AS NON CORE | Summary: PMID:10745074 showed cytosolic Hsp70s are involved in transport of aminopeptidase I from cytoplasm into the vacuole, and SSA1 localizes to the vacuole membrane. Reason: Direct experiments support transient vacuolar-membrane localization in Ape1 transport, but this is a specialized application of Ssa1 function. |
| GO:0002181 cytoplasmic translation | IMP PMID:11279042 The yeast hsp70 homologue Ssa is required for translation an... | KEEP AS NON CORE | Summary: PMID:11279042 showed SSA1 is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. SSA-deficient strains show reduced translation. Reason: Genuine but secondary function. SSA1 associates with translating ribosomes and supports translation, likely through co-translational chaperone activity, but this is a downstream consequence of its chaperone function. Supporting Evidence: PMID:11279042 The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. |
| GO:0005634 nucleus | IDA PMID:10347213 A nuclear export signal prevents Saccharomyces cerevisiae Hs... | KEEP AS NON CORE | Summary: Direct demonstration of SSA1 nuclear localization from the nuclear import study. Reason: Correct and directly supported, but secondary to the predominant cytosolic localization. |
| GO:0005737 cytoplasm | IDA PMID:8755907 Members of the Hsp70 family of proteins in the cell wall of ... | ACCEPT | Summary: PMID:8755907 identified Hsp70 family members in the cell wall but also confirmed cytoplasmic localization of SSA1. Reason: Correct core localization with direct experimental evidence. |
| GO:0006457 protein folding | IDA PMID:8947547 The refolding activity of the yeast heat shock proteins Ssa1... | ACCEPT | Summary: PMID:8947547 demonstrated SSA1/SSA2 refolding activity using denatured luciferase as a substrate. Depletion of Ssa1/2p dramatically reduced refolding capacity of yeast cytosol. Reason: Core biological process. Direct experimental demonstration of SSA1's role in protein folding. Supporting Evidence: PMID:8947547 Depletion of Ssa1/2p had no effect on the ability of the yeast lysate to synthesize enzymatically active luciferase, but had a dramatic effect on the ability of the lysate to refold chemically denatured luciferase. |
| GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation | IDA PMID:8754838 Functional interaction of cytosolic hsp70 and a DnaJ-related... | MODIFY | Summary: PMID:8754838 showed functional interaction of cytosolic hsp70 and Ydj1p in protein translocation in vivo. However, PMID:8947547 later found depletion of Ssa1/2p had no effect on translocation efficiency in vitro. The in vivo role may be indirect. Reason: PMID:8754838 supports an in-vivo SSA/Ydj1 role in post-translational precursor import, not SRP-dependent cotranslational targeting. PMID:8947547 further shows that Ssa1/2 depletion did not reduce translocation in its cell-free assay, so this remains a non-core class-level role. Proposed replacements: post-translational protein targeting to membrane, translocation Supporting Evidence: PMID:8947547 Depletion of Ssa1/2p had no effect on the efficiency of translocation in this in vitro assay. |
| GO:0009277 fungal-type cell wall | IDA PMID:8755907 Members of the Hsp70 family of proteins in the cell wall of ... | KEEP AS NON CORE | Summary: PMID:8755907 directly identified SSA1 as a cell wall protein in S. cerevisiae. Reason: Direct immunoblotting, intact-cell immunofluorescence, and extracellular biotinylation support cell-wall exposure, but this is not the core site of Ssa1 chaperone activity. |
| GO:0016887 ATP hydrolysis activity | IDA PMID:18706386 Prion-impairing mutations in Hsp70 chaperone Ssa1: effects o... | ACCEPT | Summary: PMID:18706386 characterized ATPase activity of SSA1 wild-type and mutants. Demonstrated effects of prion-impairing mutations on ATPase and chaperone activities. Reason: Core molecular function with direct biochemical characterization. Supporting Evidence: PMID:18706386 Ssa1(L483W) ATPase activity was elevated 10-fold and was least stimulated by substrates or Hsp40 co-chaperones. |
| GO:0042026 protein refolding | IDA PMID:18706386 Prion-impairing mutations in Hsp70 chaperone Ssa1: effects o... | ACCEPT | Summary: PMID:18706386 measured reactivation of denatured luciferase by SSA1 wild-type and mutants, directly demonstrating protein refolding activity. Reason: Core function. Direct biochemical demonstration of protein refolding activity. Supporting Evidence: PMID:18706386 Peptide binding and reactivation of denatured luciferase were enhanced in Ssa1(A17V) and Ssa1(R34K) but compromised in Ssa1(L483W). |
| GO:0042026 protein refolding | IDA PMID:9674429 Hsp104, Hsp70, and Hsp40: a novel chaperone system that resc... | ACCEPT | Summary: PMID:9674429 (Glover & Lindquist 1998) demonstrated that Hsp104, Hsp70, and Hsp40 form a disaggregation/refolding system. SSA1 (as the Hsp70 component) cooperates with Hsp104 and Ydj1 to reactivate aggregated proteins. Reason: Core function. Landmark study demonstrating the Hsp104-Hsp70-Hsp40 disaggregation and refolding system. Supporting Evidence: PMID:9674429 in concert with Hsp40 and Hsp70, Hsp104 can reactivate proteins that have been denatured and allowed to aggregate, substrates refractory to the action of other chaperones. |
| GO:0051082 unfolded protein binding | IDA PMID:9789005 Folding in vivo of a newly translated yeast cytosolic enzyme... | MODIFY | Summary: PMID:9789005 showed that the SSA class of Hsp70 proteins assists folding of newly translated cytosolic enzymes in vivo. The study demonstrated SSA-dependent folding of ornithine transcarbamoylase (OTC). GO:0051082 was obsoleted because it confounds binding with chaperone activity. Reason: GO:0051082 (obsolete unfolded protein binding) is obsolete. PMID:9789005 actually demonstrates that SSA1 functions as a protein folding chaperone for newly translated proteins, not merely as an unfolded protein binder. The correct term is GO:0044183 (protein folding chaperone) or more specifically GO:0140662 (ATP-dependent protein folding chaperone). SSA1 binds unfolded proteins as part of its ATP-dependent chaperone cycle to assist folding. 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 PMID:9789005 These findings indicate that, in vivo, the Hsp70 system assists in folding at least some newly translated cytosolic enzymes |
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)