HSP90AA1 encodes HSP90alpha, the stress-inducible cytosolic isoform of the HSP90 molecular chaperone. It is a constitutive homodimer, joined through its C-terminal domain, with an N-terminal GHKL-type ATPase domain and a client-binding middle domain. ATP binding and hydrolysis drive a conformational clamp cycle: the N-domains dimerize into a closed state and reopen after hydrolysis. This cycle completes the late maturation, conformational activation and stabilization of a large set of metastable client proteins, including protein kinases (via CDC37), steroid hormone receptors (via HOP/STIP1, FKBP51/52 and p23/PTGES3), eNOS, telomerase and transcription factors such as HSF1. Co-chaperones control client selection and the ATPase cycle: CDC37, AHA1/AHSA1, TSC1, FNIP1/2 and the TPR-domain proteins that bind its C-terminal MEEVD motif. HSP90 also hands misfolded clients to CHIP/STUB1 for ubiquitin-dependent degradation. It acts mainly in the cytosol, with nuclear, mitochondria-associated and extracellular pools. It delivers preproteins to the mitochondrial import receptor TOM70, links TBK1/IRF3 to TOM70 in antiviral signalling, and its binding to HSF1 represses the heat shock response. For androgen-receptor complexes, co-chaperone effects on dimerization and chromatin engagement can be separated from nuclear import; an obligatory FKBP51-to-FKBP52 transport switch is not shared by all receptor systems.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001764 neuron migration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell-surface HSP90alpha contributes to neuronal migration in the mammalian source experiments. Reason: The primary rat explant study identifies the 4C5 antigen as HSP90alpha and inhibits migration with isoform-directed antibodies. This is participation by extracellular HSP90, not merely expression of a migration-associated client. Retain the existing mammalian inference as a peripheral role, while making clear that the cited experiment is rat rather than human. Supporting Evidence: PMID:15302889 Cell migration from cerebellar and sciatic nerve explants is inhibited by anti-HSP90alpha and anti-HSP90beta antibodies |
| GO:0002021 response to dietary excess | IEA GO_REF:0000107 | UNDECIDED | Summary: Diet-sensitive rat SCN expression does not resolve the corresponding human response claim. Reason: The donor study specifically measures diet-dependent circadian expression in rat suprachiasmatic nucleus. It supports a response at the donor expression level, but whether this tissue- and regimen-specific regulation is conserved in human HSP90AA1 remains unresolved; protein-sequence conservation alone does not determine that regulatory program. Supporting Evidence: PMID:26745660 The amplitude of Hsp90aa1 expression was lowest in CAF rats and highest in CR rats |
| GO:0002134 UTP binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: UTP binding is a supported peripheral biochemical capability. Reason: PMID:12755697 analyzed purified rat-liver Hsp90 by nucleotide-affinity cleavage and ATP-Sepharose competition. The full primary PDF reports binding of this nucleotide; most assays used beta-specific antibodies, while selected pan-isoform assays found no significant alpha/beta specificity difference (data not shown). This supports the existing conserved mammalian HSP90AA1 binding inference as non-core. It is not a direct measurement on purified human HSP90AA1, evidence of hydrolysis, or proof of physiological use of this nucleotide. ATP-driven chaperoning remains the established core activity. Supporting Evidence: url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf GTP and UTP are speciο¬c C-terminal nucleotides. url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf recognizes both Hsp90 isoforms, revealed no signiο¬cant differences between the nucleotide-bindingspeciο¬cities of Hsp90a and Hsp90b (data not shown). |
| GO:0002135 CTP binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CTP binding is a supported peripheral biochemical capability. Reason: PMID:12755697 analyzed purified rat-liver Hsp90 by nucleotide-affinity cleavage and ATP-Sepharose competition. The full primary PDF reports binding of this nucleotide; most assays used beta-specific antibodies, while selected pan-isoform assays found no significant alpha/beta specificity difference (data not shown). This supports the existing conserved mammalian HSP90AA1 binding inference as non-core. It is not a direct measurement on purified human HSP90AA1, evidence of hydrolysis, or proof of physiological use of this nucleotide. ATP-driven chaperoning remains the established core activity. Supporting Evidence: url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf The C-terminal domain allowed bindingof all kinds of nucleotides tested. url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf recognizes both Hsp90 isoforms, revealed no signiο¬cant differences between the nucleotide-bindingspeciο¬cities of Hsp90a and Hsp90b (data not shown). |
| GO:0002218 activation of innate immune response | IDA PMID:20628368 Tom70 mediates activation of interferon regulatory factor 3 ... | KEEP AS NON CORE | Summary: HSP90 bridges TBK1/IRF3 to mitochondrial Tom70 for antiviral signalling. Reason: Supported client/adaptor role; non-core. Supporting Evidence: PMID:20628368 Mechanistically, the clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thus recruiting TBK1/IRF3 to mitochondria. file:human/HSP90AA1/HSP90AA1-uniprot.txt Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response |
| GO:0002230 positive regulation of defense response to virus by host | IDA PMID:20628368 Tom70 mediates activation of interferon regulatory factor 3 ... | KEEP AS NON CORE | Summary: HSP90-Tom70 recruitment of TBK1/IRF3 promotes antiviral responses. Reason: Supported; non-core. Supporting Evidence: PMID:20628368 Mechanistically, the clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thus recruiting TBK1/IRF3 to mitochondria. |
| GO:0003009 skeletal muscle contraction | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Increased Hsp90 during muscle overload does not establish a role in contraction itself. Reason: The traced donor study measures Hsp90 abundance during compensatory hypertrophy after functional overload. The transferred term describes skeletal-muscle contraction, whereas the evidence concerns adaptation to increased loading. Chaperone involvement in adaptation does not by itself assign HSP90AA1 a step in the contraction machinery. This is a mismatch in biological scope, not a requirement to prove the annotation false. Supporting Evidence: PMID:20851858 Levels of Hsp72 and Hsp90 were higher in plantaris and soleus of FO than control mice and rats after 3 and 7 days of FO. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | KEEP AS NON CORE | Summary: Retain RNA association detected in independent human mRNA-interactome studies. Reason: The cited human studies use covalent UV crosslinking and mRNA purification, not expression correlation alone. The curated target-level HDA calls support a peripheral RNA-binding property; high-throughput scale is not a reason to reject it. A specific RNA-regulatory mechanism remains unresolved. Supporting Evidence: PMID:22658674 Employing two complementary protocols for covalent UV crosslinking of RBPs to RNA PMID:22681889 We developed a photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) purification approach to identify the mRNA-bound proteome |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | KEEP AS NON CORE | Summary: Retain RNA association detected in independent human mRNA-interactome studies. Reason: The cited human studies use covalent UV crosslinking and mRNA purification, not expression correlation alone. The curated target-level HDA calls support a peripheral RNA-binding property; high-throughput scale is not a reason to reject it. A specific RNA-regulatory mechanism remains unresolved. Supporting Evidence: PMID:22658674 Employing two complementary protocols for covalent UV crosslinking of RBPs to RNA PMID:22681889 We developed a photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) purification approach to identify the mRNA-bound proteome |
| GO:0003729 mRNA binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain RNA association detected in independent human mRNA-interactome studies. Reason: The cited human studies use covalent UV crosslinking and mRNA purification, not expression correlation alone. The curated target-level HDA calls support a peripheral RNA-binding property; high-throughput scale is not a reason to reject it. A specific RNA-regulatory mechanism remains unresolved. Supporting Evidence: PMID:22658674 Employing two complementary protocols for covalent UV crosslinking of RBPs to RNA PMID:22681889 We developed a photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) purification approach to identify the mRNA-bound proteome |
| GO:0005515 protein binding | IPI PMID:12176997 Akt forms an intracellular complex with heat shock protein 9... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:12604615 Aha1 binds to the middle domain of Hsp90, contributes to cli... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:12853476 Cofactor Tpr2 combines two TPR domains and a J domain to reg... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14638689 S100A1 is a novel molecular chaperone and a member of the Hs... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14676191 Comprehensive proteomic analysis of human Par protein comple... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14743216 A physical and functional map of the human TNF-alpha/NF-kapp... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14743216 A physical and functional map of the human TNF-alpha/NF-kapp... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14743216 A physical and functional map of the human TNF-alpha/NF-kapp... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:14743216 A physical and functional map of the human TNF-alpha/NF-kapp... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:15347682 Characterization of a novel interaction between the secretor... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:15708368 Small glutamine-rich tetratricopeptide repeat-containing pro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:15708368 Small glutamine-rich tetratricopeptide repeat-containing pro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16049941 A pilot proteomic study of amyloid precursor interactors in ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16169070 A human protein-protein interaction network: a resource for ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16275660 Identification of VCP/p97, carboxyl terminus of Hsp70-intera... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16307917 Chaperoned ubiquitylation--crystal structures of the CHIP U ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16307917 Chaperoned ubiquitylation--crystal structures of the CHIP U ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16844778 Hsp90 inhibition transiently activates Src kinase and promot... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:16888650 Glucocorticoids cause rapid dissociation of a T-cell-recepto... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:17024179 Hepatitis C virus RNA replication is regulated by FKBP8 and ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:18195352 HSP90 regulates cell survival via inositol hexakisphosphate ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19026643 HSP90 is required for TAK1 stability but not for its activat... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19740745 A truncated form of p23 down-regulates telomerase activity v... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:19875381 A proteomic investigation of ligand-dependent HSP90 complexe... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20133715 NudC-like protein 2 regulates the LIS1/dynein pathway by sta... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20133715 NudC-like protein 2 regulates the LIS1/dynein pathway by sta... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20188096 S100 proteins regulate the interaction of Hsp90 with Cycloph... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20188096 S100 proteins regulate the interaction of Hsp90 with Cycloph... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20353823 Stat1 mediates an auto-regulation of hsp90beta gene in heat ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20374249 The pathogenic E. coli type III effector EspZ interacts with... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20558745 Secreted heat shock protein 90alpha induces colorectal cance... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20628368 Tom70 mediates activation of interferon regulatory factor 3 ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20864032 CK2 phospho-dependent binding of R2TP complex to TEL2 is ess... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21871133 Apigenin inhibits proliferation and induces apoptosis in hum... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:22022502 An interaction network predicted from public data as a disco... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:22022502 An interaction network predicted from public data as a disco... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:22843495 Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23414517 A human skeletal muscle interactome centered on proteins inv... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23431407 Distinct roles of molecular chaperones HSP90Ξ± and HSP90Ξ² in ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23455922 Interlaboratory reproducibility of large-scale human protein... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23455922 Interlaboratory reproducibility of large-scale human protein... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:23995768 Paralog-selective Hsp90 inhibitors define tumor-specific reg... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24794838 Structural basis for phosphorylation-dependent recruitment o... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:24949977 Glucocorticoid receptor function regulated by coordinated ac... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25486457 Middle domain of human Hsp90 isoforms differentially binds A... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:25738358 C-terminal domain of SMYD3 serves as a unique HSP90-regulate... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:26517842 Client Proteins and Small Molecule Inhibitors Display Distin... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:26754925 IER5 generates a novel hypo-phosphorylated active form of HS... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27086506 HiQuant: Rapid Postquantification Analysis of Large-Scale MS... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:27880917 Phenotypic and Interaction Profiling of the Human Phosphatas... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:29079741 Combined x-ray crystallography and computational modeling ap... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:30833792 A protein-interaction network of interferon-stimulated genes... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31361762 The interaction between RE1-silencing transcription factor (... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:33990585 Crystal structure of SARS-CoV-2 Orf9b in complex with human ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:37045861 Interactome dynamics of RAF1-BRAF kinase monomers and dimers... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005515 protein binding | IPI PMID:9817749 In vivo function of Hsp90 is dependent on ATP binding and AT... | REMOVE | Summary: Generic protein binding (IPI) with ~195 partners, mostly clients, co-chaperones and high-throughput interactors. Reason: Uninformative term. HSP90 binds a very large set of clients and co-chaperones as part of its chaperone function, which is captured by the ATP-dependent chaperone, TPR domain binding and complex terms. Removal does not imply the reported interactions are false. |
| GO:0005524 ATP binding | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90 binds ATP in its N-terminal domain; FNIP co-chaperones modulate nucleotide cycling. Reason: Correct; inherent to the ATPase cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:27353360 FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
| GO:0005524 ATP binding | IDA PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | ACCEPT | Summary: HSP90 binds ATP in its N-terminal domain; FNIP co-chaperones modulate nucleotide cycling. Reason: Correct; inherent to the ATPase cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:27353360 FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: HSP90 binds ATP in its N-terminal domain; FNIP co-chaperones modulate nucleotide cycling. Reason: Correct; inherent to the ATPase cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:27353360 FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
| GO:0005525 GTP binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GTP binding is a supported peripheral biochemical capability. Reason: PMID:12755697 analyzed purified rat-liver Hsp90 by nucleotide-affinity cleavage and ATP-Sepharose competition. The full primary PDF reports binding of this nucleotide; most assays used beta-specific antibodies, while selected pan-isoform assays found no significant alpha/beta specificity difference (data not shown). This supports the existing conserved mammalian HSP90AA1 binding inference as non-core. It is not a direct measurement on purified human HSP90AA1, evidence of hydrolysis, or proof of physiological use of this nucleotide. ATP-driven chaperoning remains the established core activity. Supporting Evidence: url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf GTP and UTP are speciο¬c C-terminal nucleotides. url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf recognizes both Hsp90 isoforms, revealed no signiο¬cant differences between the nucleotide-bindingspeciο¬cities of Hsp90a and Hsp90b (data not shown). |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2247514 | KEEP AS NON CORE | Summary: Extracellular region (Reactome; neutrophil degranulation, secreted HSP90alpha). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6798748 | KEEP AS NON CORE | Summary: Extracellular region (Reactome; neutrophil degranulation, secreted HSP90alpha). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6800434 | KEEP AS NON CORE | Summary: Extracellular region (Reactome; neutrophil degranulation, secreted HSP90alpha). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | ACCEPT | Summary: A fraction of HSP90 is nuclear, where it acts on transcription factors and chromatin regulators. Reason: Supported location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: A fraction of HSP90 is nuclear, where it acts on transcription factors and chromatin regulators. Reason: Supported location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: A fraction of HSP90 is nuclear, where it acts on transcription factors and chromatin regulators. Reason: Supported location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: A fraction of HSP90 is nuclear, where it acts on transcription factors and chromatin regulators. Reason: Supported location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: A fraction of HSP90 is nuclear, where it acts on transcription factors and chromatin regulators. Reason: Supported location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5082356 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5082409 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5324617 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5618080 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5618093 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939203 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939204 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9032751 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9038161 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709547 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9716913 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9716947 | ACCEPT | Summary: Nucleoplasmic pool (Reactome; e.g. HSF1 and steroid receptor complexes). Reason: Consistent with nuclear role. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. |
| GO:0005737 cytoplasm | IDA PMID:10791971 Nucleolar localization of human methionyl-tRNA synthetase an... | MODIFY | Summary: Cytoplasmic localization. Reason: Refine the broad cytoplasm annotation to the directly supported cytosol location; separately documented nuclear and organelle-associated pools are retained independently. Proposed replacements: cytosol Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MODIFY | Summary: Cytoplasmic localization. Reason: Refine the broad cytoplasm annotation to the directly supported cytosol location; separately documented nuclear and organelle-associated pools are retained independently. Proposed replacements: cytosol Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | MODIFY | Summary: Cytoplasmic localization. Reason: Refine the broad cytoplasm annotation to the directly supported cytosol location; separately documented nuclear and organelle-associated pools are retained independently. Proposed replacements: cytosol Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | MODIFY | Summary: Cytoplasmic localization. Reason: Refine the broad cytoplasm annotation to the directly supported cytosol location; separately documented nuclear and organelle-associated pools are retained independently. Proposed replacements: cytosol Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005739 mitochondrion | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | KEEP AS NON CORE | Summary: A mitochondrial (outer membrane-associated) pool of HSP90 in Tom70/IRF3 complexes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. ORGANELLES check (2026-10-25). Both GO:0005739 rows rest on PMID:25609812 (full text cached): UniProt records Mitochondrion with ECO:0000269 from it, and GO_REF:0000044 maps that SL-0173 location, so the IEA row's feature is present and the organelle claim holds. The paper shows a recruited pool: the outer-membrane receptor Tom70 binds the Hsp90 C-terminal EEVD motif through its clamp domain and brings Hsp90/IRF3/Bax to mitochondria on Sendai virus infection. Stays at the root under rule 4, as for TRAF3 and BRAF: HSP90AA1 has no transit peptide or membrane anchor, and the association is binding to a TOM receptor, not an outer-membrane assay (no protease protection or sub-mitochondrial fractionation), so GO:0005741 is not added. Supporting Evidence: PMID:25609812 Here we report that a dynamic protein complex, Tom70/Hsp90/IRF3/Bax, mediates SeV-induced apoptosis. PMID:25609812 The clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thereby recruiting Hsp90/IRF3/Bax to mitochondria. file:human/HSP90AA1/HSP90AA1-uniprot.txt Mitochondrion {ECO:0000269|PubMed:25609812}. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A mitochondrial (outer membrane-associated) pool of HSP90 in Tom70/IRF3 complexes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. ORGANELLES check (2026-10-25). Both GO:0005739 rows rest on PMID:25609812 (full text cached): UniProt records Mitochondrion with ECO:0000269 from it, and GO_REF:0000044 maps that SL-0173 location, so the IEA row's feature is present and the organelle claim holds. The paper shows a recruited pool: the outer-membrane receptor Tom70 binds the Hsp90 C-terminal EEVD motif through its clamp domain and brings Hsp90/IRF3/Bax to mitochondria on Sendai virus infection. Stays at the root under rule 4, as for TRAF3 and BRAF: HSP90AA1 has no transit peptide or membrane anchor, and the association is binding to a TOM receptor, not an outer-membrane assay (no protease protection or sub-mitochondrial fractionation), so GO:0005741 is not added. Supporting Evidence: PMID:25609812 Here we report that a dynamic protein complex, Tom70/Hsp90/IRF3/Bax, mediates SeV-induced apoptosis. PMID:25609812 The clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thereby recruiting Hsp90/IRF3/Bax to mitochondria. file:human/HSP90AA1/HSP90AA1-uniprot.txt Mitochondrion {ECO:0000269|PubMed:25609812}. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | NAS PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1169421 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1218824 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1218833 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1220610 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1220611 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1220612 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1220613 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1220614 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225947 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225949 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225950 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225951 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225952 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225956 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225957 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225960 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1225961 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226012 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226014 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1226016 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1227964 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1247841 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1247842 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1247844 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1247999 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1248002 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1248655 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497784 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497796 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497810 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1918092 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1918095 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1963589 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202111 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202127 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202129 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574840 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574845 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000310 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000319 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3371503 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3371586 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380272 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380283 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380294 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380303 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380311 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380316 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380455 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380508 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-419644 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-419645 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218643 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218809 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218811 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218822 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218826 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218838 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218839 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5218851 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5324632 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617816 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618073 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618080 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618085 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618098 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618099 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618105 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618107 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618110 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626220 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626223 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626227 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626228 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626681 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626699 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637764 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637765 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637766 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637770 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637792 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637794 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637795 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637796 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637798 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637800 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637801 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637806 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5637808 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5638009 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5638137 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6790041 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8852362 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853405 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853419 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9018785 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9649393 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9652264 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9652277 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664567 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665121 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665232 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665278 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665280 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665284 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665286 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665304 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665311 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665315 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665388 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665405 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665412 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665696 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665697 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665702 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665703 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665708 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9665726 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9678925 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9688459 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9690534 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9698844 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705925 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705926 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9706837 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9709831 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9709852 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9725855 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9725885 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9726509 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9726580 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9726621 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9920829 | ACCEPT | Summary: HSP90alpha is a predominantly cytosolic chaperone. Reason: Core location. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm |
| GO:0005886 plasma membrane | EXP PMID:11276205 A CD14-independent LPS receptor cluster. | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202111 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202129 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202137 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202144 | KEEP AS NON CORE | Summary: Plasma membrane pool; HSP90 participates in an LPS receptor cluster at the cell surface. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes |
| GO:0005901 caveola | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Caveola (Ensembl transfer; eNOS-caveolin complex). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90 assists folding/maturation of client proteins. Reason: Core process (IBA and IEA consistent). Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. |
| GO:0006457 protein folding | IEA GO_REF:0000120 | ACCEPT | Summary: HSP90 assists folding/maturation of client proteins. Reason: Core process (IBA and IEA consistent). Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. |
| GO:0006839 mitochondrial transport | TAS PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | KEEP AS NON CORE | Summary: HSP90 delivers preproteins to the Tom70 import receptor. Reason: Supported; non-core. Supporting Evidence: PMID:12526792 Here, we show that in mammals, the cytosolic chaperones Hsp90 and Hsp70 dock onto a specialized TPR domain in the import receptor Tom70 at the outer mitochondrial membrane. file:human/HSP90AA1/HSP90AA1-uniprot.txt Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 |
| GO:0006986 response to unfolded protein | NAS PMID:2527334 Sequence and regulation of a gene encoding a human 89-kiloda... | ACCEPT | Summary: HSP90alpha is heat/stress-inducible and part of the response to unfolded proteins. Reason: Correct. Supporting Evidence: PMID:2527334 In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. |
| GO:0007004 telomere maintenance via telomerase | IDA PMID:10197982 Functional requirement of p23 and Hsp90 in telomerase comple... | KEEP AS NON CORE | Summary: HSP90 and p23 are required for assembly of active telomerase. Reason: Client-specific role (TERT); non-core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0007004 telomere maintenance via telomerase | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: HSP90 and p23 are required for assembly of active telomerase. Reason: Client-specific role (TERT); non-core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0009408 response to heat | ISS GO_REF:0000024 | ACCEPT | Summary: HSP90alpha synthesis increases in response to heat stress (ISS). Reason: Correct. Supporting Evidence: PMID:2527334 In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. |
| GO:0009409 response to cold | ISS GO_REF:0000024 | UNDECIDED | Summary: Cold-associated chicken-heart Hsp90 regulation has not resolved the human response claim. Reason: The native donor experiment reports reduced Hsp90 abundance during cold stress in chicken heart. This is real donor response evidence, but its temperature, tissue and avian physiological setting do not establish the same specific regulation in human HSP90AA1. The relevant human response remains unresolved. Supporting Evidence: PMID:23636703 the mRNA level and protein expression of Hsp90 decreased significantly |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: Chemotherapy-associated rat sperm HSP90AA1 expression leaves the human transfer unresolved. Reason: The donor paper reports persistent sperm HSP90AA1 overexpression after bleomycin/etoposide/cisplatin exposure. Its specific paternal treatment and germ-cell context supports a rat response, but does not determine whether the human gene participates in the same response. Generic drug sensitivity of HSP90 clients is not substituted for that missing context. Supporting Evidence: PMID:24478030 HSP90AA1, HSP90B1 and PDIA3, involved in spermatozoa-egg interactions, were overexpressed in BEP-exposed spermatozoa |
| GO:0009651 response to salt stress | IEA GO_REF:0000107 | UNDECIDED | Summary: Renal Hsp90 redistribution under sodium restriction requires a more precise transfer assessment. Reason: The donor study concerns low dietary sodium and renal redistribution, rather than necessarily hyperosmotic salt stress. Whether the broad salt-stress term captures that physiology and whether the same response is conserved in humans remain unresolved. This is a specific stimulus-scope and cross-species question. Supporting Evidence: PMID:15497505 Expression of Hsp9alpha and Hsp90beta was upregulated in the renal cortex during sodium restriction. |
| GO:0009986 cell surface | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell surface (Ensembl transfer); extracellular/surface HSP90alpha is documented. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0010592 positive regulation of lamellipodium assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell-surface HSP90 supports lamellipodium formation in migrating cells. Reason: Rat Schwann-cell antibody perturbations link cell-surface HSP90alpha/beta activity to actin organization required for lamellipodia. This provides a mechanism for the inherited peripheral annotation, without claiming that the experiment directly measured human HSP90AA1. Supporting Evidence: PMID:15302889 HSP90 activity is associated with actin cytoskeletal organization, necessary for lamellipodia formation. |
| GO:0010659 cardiac muscle cell apoptotic process | IEA GO_REF:0000107 | MODIFY | Summary: Refine apoptosis participation to the supported negative regulation of striated-muscle apoptosis. Reason: The traced donor context is cardioprotection, not Hsp90aa1 execution of apoptosis. Rat Hsp90aa1 gain/loss experiments in PMID:27076094 establish an anti-apoptotic regulatory role. Use the existing negative-regulation term rather than presenting HSP90AA1 as executing cardiac-cell death. Proposed replacements: negative regulation of striated muscle cell apoptotic process Supporting Evidence: PMID:27076094 over-expression of Hsp90aa1 could attenuate OGD-induced apoptosis of NRVCs |
| GO:0010664 negative regulation of striated muscle cell apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Hsp90aa1 protects striated muscle cells from stress-induced apoptosis. Reason: Full-text rat cardiomyocyte gain- and loss-of-function experiments show that Hsp90aa1 overexpression attenuates oxygen-glucose-deprivation apoptosis and Hsp90aa1 knockdown enhances it. This is a direct regulatory role, retained as a peripheral mammalian inference; the source is not a human cardiomyocyte experiment. Supporting Evidence: PMID:27076094 over-expression of Hsp90aa1 could attenuate OGD-induced apoptosis of NRVCs |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane (HDA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Basolateral plasma membrane (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Apical plasma membrane (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0016887 ATP hydrolysis activity | EXP PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0016887 ATP hydrolysis activity | IDA PMID:15937123 S-nitrosylation of Hsp90 promotes the inhibition of its ATPa... | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0016887 ATP hydrolysis activity | IDA PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0016887 ATP hydrolysis activity | TAS Reactome:R-HSA-8939203 | ACCEPT | Summary: HSP90 hydrolyses ATP; the ATPase is regulated by co-chaperones (CDC37, TSC1, FNIPs, AHSA1) and S-nitrosylation. Reason: Intrinsic ATPase activity is essential for chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. PMID:29127155 Here, we show that Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0017098 sulfonylurea receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ARBA/Ensembl: sulfonylurea receptor binding. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0019903 protein phosphatase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Binding to protein phosphatases (PP5/PPP5C via TPR domain). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0023026 MHC class II protein complex binding | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Retain experimentally observed association with exosomal MHC II as peripheral. Reason: The original study identifies HSP90 among proteins specifically co-immunoprecipitated with MHC II. This supports the curated binding annotation without establishing a primary antigen-presentation role or purified binary interaction. Supporting Evidence: PMID:20458337 a small subset of proteins that were specifically co-immunoprecipitated with MHC II from detergent-solubilized exosomes. These include HSC71, HSP90 |
| GO:0030150 protein import into mitochondrial matrix | IDA PMID:15644312 Dissection of the mitochondrial import and assembly pathway ... | KEEP AS NON CORE | Summary: HSP90 delivers Tom40 precursor to mitochondria in an ATP-dependent manner. Reason: Supported cytosolic chaperone step of import; non-core. Supporting Evidence: PMID:15644312 We identify that Hsp90 is involved in delivery of the Tom40 precursor to mitochondria in an ATP-dependent manner. |
| GO:0030235 nitric-oxide synthase regulator activity | EXP PMID:10781589 Reconstitution of an endothelial nitric-oxide synthase (eNOS... | KEEP AS NON CORE | Summary: HSP90 binds and activates eNOS; S-nitrosylation inhibits this effect. Reason: Well-established client-specific regulatory effect, but an instance of chaperone action on one client rather than a dedicated activity. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0030235 nitric-oxide synthase regulator activity | EXP PMID:9580552 Dynamic activation of endothelial nitric oxide synthase by H... | KEEP AS NON CORE | Summary: HSP90 binds and activates eNOS; S-nitrosylation inhibits this effect. Reason: Well-established client-specific regulatory effect, but an instance of chaperone action on one client rather than a dedicated activity. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0030235 nitric-oxide synthase regulator activity | IDA PMID:15937123 S-nitrosylation of Hsp90 promotes the inhibition of its ATPa... | KEEP AS NON CORE | Summary: HSP90 binds and activates eNOS; S-nitrosylation inhibits this effect. Reason: Well-established client-specific regulatory effect, but an instance of chaperone action on one client rather than a dedicated activity. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0030235 nitric-oxide synthase regulator activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: HSP90 binds and activates eNOS; S-nitrosylation inhibits this effect. Reason: Well-established client-specific regulatory effect, but an instance of chaperone action on one client rather than a dedicated activity. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. PMID:15937123 Hsp90 ATPase activity and its positive effect on eNOS activity are both inhibited by S-nitrosylation. |
| GO:0030911 TPR domain binding | IDA PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | ACCEPT | Summary: The C-terminal MEEVD motif binds TPR-domain co-chaperones (HOP, FKBP51/52, PP5, TOM34, TOM70, CHIP). Reason: Informative, well-established molecular property central to co-chaperone recruitment. Supporting Evidence: PMID:9660753 Using a yeast two-hybrid screen, the 12-kDa C-terminal domain of human hsp90alpha (C90) was found to mediate the interaction of hsp90 with TPR-containing sequences from the hsp90 cofactors FKBP51/54 and FKBP52. file:human/HSP90AA1/HSP90AA1-uniprot.txt The TPR repeat-binding motif mediates interaction with TPR |
| GO:0030911 TPR domain binding | TAS PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | ACCEPT | Summary: The C-terminal MEEVD motif binds TPR-domain co-chaperones (HOP, FKBP51/52, PP5, TOM34, TOM70, CHIP). Reason: Informative, well-established molecular property central to co-chaperone recruitment. Supporting Evidence: PMID:9660753 Using a yeast two-hybrid screen, the 12-kDa C-terminal domain of human hsp90alpha (C90) was found to mediate the interaction of hsp90 with TPR-containing sequences from the hsp90 cofactors FKBP51/54 and FKBP52. file:human/HSP90AA1/HSP90AA1-uniprot.txt The TPR repeat-binding motif mediates interaction with TPR |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Extracellular matrix (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0031396 regulation of protein ubiquitination | IDA PMID:16809764 Histone deacetylase 8 safeguards the human ever-shorter telo... | KEEP AS NON CORE | Summary: HSP90 complexes influence ubiquitination of clients (e.g. HDAC8/hEST1B; CHIP). Reason: Indirect, client-specific. |
| GO:0031396 regulation of protein ubiquitination | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: HSP90 complexes influence ubiquitination of clients (e.g. HDAC8/hEST1B; CHIP). Reason: Indirect, client-specific. |
| GO:0031526 brush border membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Brush border membrane (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Binding to ubiquitin ligases (CHIP/STUB1 and others). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:16207813 BAG-2 acts as an inhibitor of the chaperone-associated ubiqu... | KEEP AS NON CORE | Summary: Binding to ubiquitin ligases (CHIP/STUB1 and others). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0032212 positive regulation of telomere maintenance via telomerase | TAS PMID:19740745 A truncated form of p23 down-regulates telomerase activity v... | KEEP AS NON CORE | Summary: HSP90-p23 supports telomerase activity (truncated p23 disrupts it). Reason: Client-specific; non-core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0032273 positive regulation of protein polymerization | IDA PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and... | KEEP AS NON CORE | Summary: HSP90 binding to tau promotes tau conformational change and aggregation in vitro. Reason: Client-specific in vitro effect. Supporting Evidence: PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. |
| GO:0032354 response to follicle-stimulating hormone | IEA GO_REF:0000107 | UNDECIDED | Summary: FSH-associated expression in ovariectomized rats leaves human FSH-response participation unresolved. Reason: The donor comparison combines ovariectomy, FSH treatment and osteoporosis-associated protein changes. Hsp90alpha abundance correlates with the treatment and bone trabecular area, but the precise HSP90AA1 role and conservation of this response in humans are not resolved by that association. Supporting Evidence: PMID:32420764 In rats with high serum FSH, expression of Hsp90Ξ± protein was increased |
| GO:0032564 dATP binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: dATP binding is a supported peripheral biochemical capability. Reason: PMID:12755697 analyzed purified rat-liver Hsp90 by nucleotide-affinity cleavage and ATP-Sepharose competition. The full primary PDF reports binding of this nucleotide; most assays used beta-specific antibodies, while selected pan-isoform assays found no significant alpha/beta specificity difference (data not shown). This supports the existing conserved mammalian HSP90AA1 binding inference as non-core. It is not a direct measurement on purified human HSP90AA1, evidence of hydrolysis, or proof of physiological use of this nucleotide. ATP-driven chaperoning remains the established core activity. Supporting Evidence: url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf the N-terminal nucleotide bindingsite prefers adenine nucleotides (ATP and dATP). url:https://www.linkgroup.hu/docs/pcs/03ejb.pdf recognizes both Hsp90 isoforms, revealed no signiο¬cant differences between the nucleotide-bindingspeciο¬cities of Hsp90a and Hsp90b (data not shown). |
| GO:0032728 positive regulation of interferon-beta production | IDA PMID:20628368 Tom70 mediates activation of interferon regulatory factor 3 ... | KEEP AS NON CORE | Summary: HSP90-Tom70-TBK1/IRF3 axis promotes IFN-beta production. Reason: Supported; non-core. Supporting Evidence: PMID:20628368 Mechanistically, the clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thus recruiting TBK1/IRF3 to mitochondria. |
| GO:0032880 regulation of protein localization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: HSP90 regulates localization of client proteins (ISS/IEA). Reason: General consequence of chaperone action; non-core. |
| GO:0032880 regulation of protein localization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: HSP90 regulates localization of client proteins (ISS/IEA). Reason: General consequence of chaperone action; non-core. |
| GO:0032991 protein-containing complex | IBA GO_REF:0000033 | MODIFY | Summary: Refine to the supported specific function or location. Reason: Refine generic complex membership to the documented protein folding chaperone complex; the HSP90-CDC37 complex is an additional supported kinase-specific assembly. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163629 Β· PTN000163629 UNRESOLVED The broad inherited claim is biologically sound; refinement uses the better-resolved target function or complex. Original PAINT node provenance is retained; the complete ancestral topology and MSA were not independently reconstructed. Target self-support is not circularity. Proposed replacements: protein folding chaperone complex HSP90-CDC37 chaperone complex |
| GO:0032991 protein-containing complex | IDA PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | MODIFY | Summary: Refine to the supported specific function or location. Reason: Refine generic complex membership to the documented protein folding chaperone complex; the HSP90-CDC37 complex is an additional supported kinase-specific assembly. Proposed replacements: protein folding chaperone complex HSP90-CDC37 chaperone complex |
| GO:0032991 protein-containing complex | IEA GO_REF:0000120 | MODIFY | Summary: Refine to the supported specific function or location. Reason: Refine generic complex membership to the documented protein folding chaperone complex; the HSP90-CDC37 complex is an additional supported kinase-specific assembly. Proposed replacements: protein folding chaperone complex HSP90-CDC37 chaperone complex |
| GO:0034605 cellular response to heat | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90alpha is induced by heat and functions in the cellular heat response. Reason: Correct; IBA consistent. Supporting Evidence: PMID:2527334 In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. |
| GO:0034605 cellular response to heat | IEA GO_REF:0000120 | ACCEPT | Summary: HSP90alpha is induced by heat and functions in the cellular heat response. Reason: Correct; IBA consistent. Supporting Evidence: PMID:2527334 In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. |
| GO:0034774 secretory granule lumen | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Secretory granule lumen (Reactome neutrophil degranulation). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0034774 secretory granule lumen | TAS Reactome:R-HSA-6798748 | KEEP AS NON CORE | Summary: Secretory granule lumen (Reactome neutrophil degranulation). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0035651 AP-3 adaptor complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl transfer: AP-3 adaptor complex binding. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0035900 response to isolation stress | IEA GO_REF:0000107 | UNDECIDED | Summary: Isolation-dependent rat brain expression is a context-specific donor finding. Reason: The full source reports region-dependent Hsp90aa1 expression after prolonged social isolation in rats, within a study also manipulating ozone exposure. The evidence supports the donor response but does not establish conservation of that social-stress regulatory program in human HSP90AA1. Supporting Evidence: PMID:38001817 hippocampal HSP90aa1 increase in SI |
| GO:0036120 cellular response to platelet-derived growth factor stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: The PDGF-stimulated rat pulmonary-cell model supports an Hsp90aa1 role but leaves the human transfer unresolved. Reason: The paper uses PDGF-BB to stimulate rat pulmonary artery smooth-muscle cells and reports Hsp90aa1-dependent migration/ERK signaling. That is mechanistic donor evidence, not merely expression. The abstract does not resolve the exact contribution of human HSP90AA1 to PDGF signaling, and the full experiment-level source was unavailable; retain uncertainty about this specific transfer. Supporting Evidence: PMID:38909785 inhibition of Hsp90aa1 also reduced PASMCs migration and pERK/ERK protein level. |
| GO:0036126 sperm flagellum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Sperm flagellum (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0042026 protein refolding | TAS PMID:9660753 Specific binding of tetratricopeptide repeat proteins to the... | ACCEPT | Summary: HSP90 participates in refolding of non-native proteins with HSP70 and TPR co-chaperones. Reason: Consistent with chaperone function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. |
| GO:0042220 response to cocaine | IEA GO_REF:0000107 | UNDECIDED | Summary: Delayed rat hippocampal responses to cocaine withdrawal do not establish the human annotation. Reason: The full source reports increased HSP90AA1 transcript in dentate gyrus after prolonged cocaine withdrawal. This supports a precisely timed rat response rather than a direct cocaine-recognition activity. Conservation of the same temporal and tissue-specific response in humans remains unresolved. Supporting Evidence: PMID:22860061 increased MR and HSP90AA1 mRNA in DG |
| GO:0042307 positive regulation of protein import into nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: HSP90 complexes support nuclear import of clients such as steroid receptors (Ensembl transfer). Reason: Retain the client-dependent nuclear-import role as non-core. Do not extrapolate an obligatory AR-import step from GR-associated transport models: PMID:34057812 found AR nuclear translocation intact after FKBP51/FKBP52 depletion, despite reduced AR dimerization and chromatin binding. Supporting Evidence: PMID:34057812 depletion of either FKBP51 or FKBP52 reduced AR dimer formation, chromatin binding, and phosphorylation |
| GO:0042470 melanosome | EXP PMID:17081065 Proteomic and bioinformatic characterization of the biogenes... | KEEP AS NON CORE | Summary: Identified in melanosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0042470 melanosome | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Identified in melanosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0042802 identical protein binding | IDA PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IPI PMID:16169070 A human protein-protein interaction network: a resource for ... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IPI PMID:21360678 Label-free quantitative proteomics and SAINT analysis enable... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IPI PMID:21460846 The client protein p53 adopts a molten globule-like state in... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042802 identical protein binding | IPI PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required f... | ACCEPT | Summary: HSP90 forms constitutive C-terminally mediated homodimers. Reason: Dimerization is essential for the chaperone cycle. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation PMID:8289821 The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. |
| GO:0042803 protein homodimerization activity | IDA PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | ACCEPT | Summary: HSP90 is a homodimer. Reason: Correct and specific. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation |
| GO:0042826 histone deacetylase binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Binding to histone deacetylases (HDAC6 deacetylates HSP90; HDAC8 complex). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0042826 histone deacetylase binding | IPI PMID:16809764 Histone deacetylase 8 safeguards the human ever-shorter telo... | KEEP AS NON CORE | Summary: Binding to histone deacetylases (HDAC6 deacetylates HSP90; HDAC8 complex). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0042981 regulation of apoptotic process | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | KEEP AS NON CORE | Summary: Tom70/Hsp90/IRF3/Bax complex in virus-induced apoptosis. Reason: Supported; non-core. Supporting Evidence: PMID:25609812 Here we report that a dynamic protein complex, Tom70/Hsp90/IRF3/Bax, mediates SeV-induced apoptosis. |
| GO:0043025 neuronal cell body | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neuronal cell body (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0043025 neuronal cell body | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Neuronal cell body (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0043025 neuronal cell body | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Neuronal cell body (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0043202 lysosomal lumen | TAS PMID:25719862 Modulation of deregulated chaperone-mediated autophagy by a ... | KEEP AS NON CORE | Summary: Lysosomal lumen pool associated with chaperone-mediated autophagy. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. Supporting Evidence: PMID:25719862 We also show that P140, but not the unphosphorylated peptide, uses the clathrin-dependent endo-lysosomal pathway to enter into MRL/lpr B lymphocytes and accumulates in the lysosomal lumen where it may directly hamper lysosomal HSPA8 chaperoning functions, and also destabilize LAMP2A in lysosomes as a result of its effect on HSP90AA1. |
| GO:0043209 myelin sheath | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Myelin sheath (IBA/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0043209 myelin sheath | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Myelin sheath (IBA/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0043254 regulation of protein-containing complex assembly | NAS PMID:20176123 Chaperone-mediated autophagy: molecular mechanisms and physi... | KEEP AS NON CORE | Summary: HSP90 regulates LAMP2A translocation complex assembly in CMA (review, NAS). Reason: Supported in the CMA literature; non-core. |
| GO:0043335 protein unfolding | NAS PMID:20176123 Chaperone-mediated autophagy: molecular mechanisms and physi... | KEEP AS NON CORE | Summary: HSP90 is proposed to assist substrate unfolding for lysosomal translocation in CMA (review, NAS). Reason: Non-core. |
| GO:0043627 response to estrogen | IEA GO_REF:0000107 | UNDECIDED | Summary: Prenatal estrogen induces rat gonocyte Hsp90alpha; the corresponding human response is unresolved. Reason: Isoform-specific assays in the donor study establish expression changes after prenatal estrogen exposure in rat gonocytes. This is legitimate donor evidence. It does not determine whether the same developmental expression response is conserved in human HSP90AA1, and should not be conflated with the established chaperoning of estrogen receptors. Supporting Evidence: PMID:15229138 Hsp90alpha was primarily expressed in gonocytes, and that it was increased following estrogen exposure. |
| GO:0044183 protein folding chaperone | IEA GO_REF:0000120 | MODIFY | Summary: Refine to the supported specific function or location. Reason: The ATP-dependent HSP90 clamp cycle supports the more specific ATP-dependent protein folding chaperone activity already retained in this review. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. |
| GO:0044294 dendritic growth cone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Dendritic growth cone (ISS/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0044294 dendritic growth cone | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Dendritic growth cone (ISS/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0044295 axonal growth cone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Axonal growth cone (ISS/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0044295 axonal growth cone | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Axonal growth cone (ISS/IEA). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0044325 transmembrane transporter binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl transfer: transmembrane transporter binding (e.g. client ion channels). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0045429 positive regulation of nitric oxide biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: HSP90 activates eNOS, promoting NO production. Reason: Client-specific; non-core. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. |
| GO:0045429 positive regulation of nitric oxide biosynthetic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: HSP90 activates eNOS, promoting NO production. Reason: Client-specific; non-core. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. |
| GO:0045732 positive regulation of protein catabolic process | IGI PMID:18292230 Akt and CHIP coregulate tau degradation through coordinated ... | KEEP AS NON CORE | Summary: HSP90/CHIP complex promotes degradation of Akt and tau. Reason: Triage role with CHIP; non-core. Supporting Evidence: PMID:18292230 During stress, Akt is ubiquitinated and degraded by the tau ubiquitin ligase CHIP, and this largely depends on the Hsp90 complex. |
| GO:0045793 positive regulation of cell size | IEA GO_REF:0000107 | UNDECIDED | Summary: HSP90-dependent cardiac hypertrophy is supported, but human HSP90AA1-specific transfer remains unresolved. Reason: The source demonstrates a causal HSP90 chaperone contribution through IKK stabilization and includes knockdown, so the claim cannot be dismissed as an indirect generic client effect. The accessible report does not resolve the alpha-versus-beta isoform contribution and precise human transfer; those are the uncertainties requiring full experimental detail. Supporting Evidence: PMID:20980790 The small interfering RNA (siRNA)-mediated knockdown of HSP90 expression significantly inhibited angiotensin II-induced cell hypertrophy and NF-ΞΊB activation. |
| GO:0046209 nitric oxide metabolic process | TAS Reactome:R-HSA-203615 | KEEP AS NON CORE | Summary: Reactome: HSP90 in eNOS activation (NO metabolism). Reason: Client-specific; non-core. Supporting Evidence: PMID:9580552 Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. |
| GO:0046677 response to antibiotic | ISS GO_REF:0000024 | UNDECIDED | Summary: The donor experiment uses geldanamycin as an HSP90 inhibitor during heat stress. Reason: The cited chicken study uses an antibiotic as a pharmacological HSP90 perturbation to test heat-stress protection. A chaperone inhibitor being administered is not itself proof of an antibiotic-response function. It remains unresolved whether the detailed donor results support a regulated response rather than inhibition of the target, and whether that biological response transfers to human HSP90AA1. Supporting Evidence: PMID:25239533 the broilers in the GA group were injected intraperitoneally with GA |
| GO:0048156 tau protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Binding to tau (client). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. Supporting Evidence: PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. |
| GO:0048156 tau protein binding | IPI PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and... | KEEP AS NON CORE | Summary: Binding to tau (client). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. Supporting Evidence: PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. |
| GO:0048471 perinuclear region of cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0048471 perinuclear region of cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (IBA/IEA/ISS). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0050821 protein stabilization | IBA GO_REF:0000033 | ACCEPT | Summary: HSP90 stabilizes client proteins (e.g. FLCN with FNIP co-chaperones). Reason: Core outcome of HSP90 chaperoning. Supporting Evidence: PMID:27353360 FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
| GO:0050821 protein stabilization | IMP PMID:27353360 The FNIP co-chaperones decelerate the Hsp90 chaperone cycle ... | ACCEPT | Summary: HSP90 stabilizes client proteins (e.g. FLCN with FNIP co-chaperones). Reason: Core outcome of HSP90 chaperoning. Supporting Evidence: PMID:27353360 FNIPs decelerate the chaperone cycle, facilitating FLCN interaction with Hsp90, consequently ensuring FLCN stability. |
| GO:0051020 GTPase binding | IPI PMID:24337748 Guanylate binding protein 1-mediated interaction of T cell a... | KEEP AS NON CORE | Summary: Binding to GTPases (e.g. GBP1). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0051022 Rho GDP-dissociation inhibitor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl transfer: Rho GDP-dissociation inhibitor binding. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0051131 chaperone-mediated protein complex assembly | IDA PMID:15644312 Dissection of the mitochondrial import and assembly pathway ... | KEEP AS NON CORE | Summary: HSP90 assists assembly of client complexes (Tom40 import intermediate; telomerase). Reason: Supported; instance of chaperone function. Supporting Evidence: PMID:15644312 We identify that Hsp90 is involved in delivery of the Tom40 precursor to mitochondria in an ATP-dependent manner. |
| GO:0051131 chaperone-mediated protein complex assembly | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: HSP90 assists assembly of client complexes (Tom40 import intermediate; telomerase). Reason: Supported; instance of chaperone function. Supporting Evidence: PMID:15644312 We identify that Hsp90 is involved in delivery of the Tom40 precursor to mitochondria in an ATP-dependent manner. |
| GO:0051604 protein maturation | IDA PMID:27339980 Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 trap... | ACCEPT | Summary: Structure of HSP90-CDC37-CDK4 shows HSP90 trapping a partially unfolded kinase during maturation. Reason: Core; kinase client maturation. Supporting Evidence: PMID:27339980 Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. |
| GO:0060452 positive regulation of cardiac muscle contraction | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Cardioprotection and recovered ventricular pressure do not establish direct regulation of contraction. Reason: The isolated rat-heart preservation experiment links Hsp90 to anti-apoptotic protection and subsequent recovery of ventricular pressure. Positive regulation of the contraction process is more specific than the demonstrated protection of viable myocardium. Retain the independently supported apoptosis-regulatory role instead of assigning the downstream functional recovery to a contraction-regulatory step. Supporting Evidence: PMID:21620734 The Hsp90 inhibitor 17-allylamino-17-demethoxy-geldanamycin inhibited the diazoxide-induced decrease in cleavage of Bid, improvement of cardiac function, and decrease of apoptosis. |
| GO:0061684 chaperone-mediated autophagy | TAS PMID:25719862 Modulation of deregulated chaperone-mediated autophagy by a ... | KEEP AS NON CORE | Summary: HSP90 participates in chaperone-mediated autophagy at the lysosome. Reason: Non-core. Supporting Evidence: PMID:25719862 We also show that P140, but not the unphosphorylated peptide, uses the clathrin-dependent endo-lysosomal pathway to enter into MRL/lpr B lymphocytes and accumulates in the lysosomal lumen where it may directly hamper lysosomal HSPA8 chaperoning functions, and also destabilize LAMP2A in lysosomes as a result of its effect on HSP90AA1. |
| GO:0061771 response to caloric restriction | IEA GO_REF:0000107 | UNDECIDED | Summary: Calorie restriction changes rat SCN Hsp90aa1 expression; the human transfer remains unresolved. Reason: The donor experiment measures altered Hsp90aa1 expression rhythms under calorie restriction in rat SCN. It does not resolve conservation of this particular dietary/circadian regulatory response in humans. The uncertainty concerns the transferred regulatory context, not whether HSP90AA1 is a stress chaperone. Supporting Evidence: PMID:26745660 The amplitude of Hsp90aa1 expression was lowest in CAF rats and highest in CR rats |
| GO:0070062 extracellular exosome | HDA PMID:11487543 Intestinal epithelial cells secrete exosome-like vesicles. | KEEP AS NON CORE | Summary: Detected in exosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0070062 extracellular exosome | HDA PMID:12519789 Proteomic and biochemical analyses of human B cell-derived e... | KEEP AS NON CORE | Summary: Detected in exosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: Detected in exosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Detected in exosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: Detected in exosome proteomes. Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0070182 DNA polymerase binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Binding to TERT (DNA polymerase activity), required for telomerase assembly. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0070182 DNA polymerase binding | IPI PMID:10197982 Functional requirement of p23 and Hsp90 in telomerase comple... | KEEP AS NON CORE | Summary: Binding to TERT (DNA polymerase activity), required for telomerase assembly. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0070182 DNA polymerase binding | IPI PMID:19751963 Curcumin inhibits nuclear localization of telomerase by diss... | KEEP AS NON CORE | Summary: Binding to TERT (DNA polymerase activity), required for telomerase assembly. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:0070301 cellular response to hydrogen peroxide | IEA GO_REF:0000107 | UNDECIDED | Summary: The rat peroxide model supports an HSP90AA1βTFEB stress mechanism, with the human transfer unresolved. Reason: The source includes HSP90AA1 inhibition/silencing and TFEB interaction in hydrogen-peroxide-treated rat cortical neurons. This is mechanistic donor evidence. The unavailable full source and absence of a resolved corresponding human experiment leave the specific cellular peroxide-response annotation uncertain, rather than biologically disproven. Supporting Evidence: PMID:39855313 HSP90AA1 was shown to regulate Nrf2 expression by binding to TFEB in the cellular model. |
| GO:0071222 cellular response to lipopolysaccharide | IEA GO_REF:0000107 | UNDECIDED | Summary: HSP90AA1 modulates responses in LPS-treated mouse microglia; the exact human transfer is unresolved. Reason: The donor paper uses rat injury and mouse BV-2 microglial experiments, including HSP90AA1 overexpression under LPS stimulation. It supports a functional inflammatory context, not only expression. Whether the particular microgliaβastrocyte response is conserved for human HSP90AA1 remains unresolved from the accessible report. Supporting Evidence: PMID:39395636 these effects were offset by HSP90AA1 overexpression in lipopolysaccharide-induced BV-2 cells. |
| GO:0071260 cellular response to mechanical stimulus | IEA GO_REF:0000107 | UNDECIDED | Summary: Compression induces HSP90alpha in the donor fibroblast system; human transfer requires context-specific support. Reason: The source measures HSP90alpha expression and secretion after sustained compression of fibroblast-seeded collagen sponges. This is evidence of a donor cellular response. Conservation of that particular mechanical-response regulation in human HSP90AA1 is not established by protein homology alone, so the transferred claim remains unresolved. Supporting Evidence: PMID:25102054 HSP90Ξ±, CD44, HAS2, and COX2 expression was upregulated |
| GO:0071456 cellular response to hypoxia | IEA GO_REF:0000107 | UNDECIDED | Summary: The hypoxic pulmonary-hypertension model implicates Hsp90aa1 but leaves the specific human response unresolved. Reason: The study combines hypoxic rats, PDGF-stimulated rat pulmonary cells and human disease expression datasets. It supports Hsp90aa1-associated vascular remodeling, but the accessible abstract does not isolate an HSP90AA1-specific human cellular hypoxia-response mechanism. The full experimental context is required to settle that transfer. Supporting Evidence: PMID:38909785 inhibition of Hsp90aa1 also reduced PASMCs migration and pERK/ERK protein level. |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2247514 | KEEP AS NON CORE | Summary: Endocytic vesicle lumen (Reactome). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0097110 scaffold protein binding | IPI PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | KEEP AS NON CORE | Summary: Binding to scaffold proteins (KSR1). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0097226 sperm mitochondrial sheath | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Sperm mitochondrial sheath (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0097524 sperm plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Sperm plasma membrane (Ensembl transfer). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:0097718 disordered domain specific binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Binding of the HSP90 C-terminus to the partly disordered TPR domain of PP5. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0097718 disordered domain specific binding | IPI PMID:15713458 Molecular recognition via coupled folding and binding in a T... | KEEP AS NON CORE | Summary: Binding of the HSP90 C-terminus to the partly disordered TPR domain of PP5. Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
| GO:0098586 cellular response to virus | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | KEEP AS NON CORE | Summary: Tom70/Hsp90/IRF3/Bax complex mediates Sendai virus-induced apoptosis. Reason: Supported; non-core. Supporting Evidence: PMID:25609812 Here we report that a dynamic protein complex, Tom70/Hsp90/IRF3/Bax, mediates SeV-induced apoptosis. |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Regulation of postsynaptic receptor levels (Ensembl transfer). Reason: Client-specific neuronal role; non-core. |
| GO:0101031 protein folding chaperone complex | IDA PMID:25719862 Modulation of deregulated chaperone-mediated autophagy by a ... | ACCEPT | Summary: HSP90AA1 is in an HSPA8-HSP90AA1 chaperone complex involved in CMA. Reason: Correct; HSP90 is a core component of chaperone complexes. Supporting Evidence: PMID:25719862 We also show that P140, but not the unphosphorylated peptide, uses the clathrin-dependent endo-lysosomal pathway to enter into MRL/lpr B lymphocytes and accumulates in the lysosomal lumen where it may directly hamper lysosomal HSPA8 chaperoning functions, and also destabilize LAMP2A in lysosomes as a result of its effect on HSP90AA1. |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: HSP90 is an ATP-dependent chaperone whose ATPase cycle drives client maturation. Reason: Core molecular function. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. file:human/HSP90AA1/HSP90AA1-uniprot.txt Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. |
| GO:0140767 enzyme-substrate adaptor activity | EXP PMID:11988487 Domain mapping studies reveal that the M domain of hsp90 ser... | KEEP AS NON CORE | Summary: The HSP90 M domain scaffolds Akt-dependent eNOS phosphorylation. Reason: Supported client-specific scaffolding role; non-core. Supporting Evidence: PMID:11988487 Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. |
| GO:0140767 enzyme-substrate adaptor activity | EXP PMID:12799359 Synergistic activation of endothelial nitric-oxide synthase ... | KEEP AS NON CORE | Summary: The HSP90 M domain scaffolds Akt-dependent eNOS phosphorylation. Reason: Supported client-specific scaffolding role; non-core. Supporting Evidence: PMID:11988487 Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. |
| GO:0140767 enzyme-substrate adaptor activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The HSP90 M domain scaffolds Akt-dependent eNOS phosphorylation. Reason: Supported client-specific scaffolding role; non-core. Supporting Evidence: PMID:11988487 Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. |
| GO:1902988 neurofibrillary tangle assembly | IDA PMID:19363271 Binding of Hsp90 to tau promotes a conformational change and... | KEEP AS NON CORE | Summary: Retain the experimentally assigned tau-aggregation process as a pathological client-specific activity. Reason: The source reports direct HSP90 binding that alters tau conformation and promotes filamentous aggregation. HSP90 therefore does molecular work in this process; it is not merely a downstream phenotype. This pathological client context is peripheral to its general chaperone role. Supporting Evidence: PMID:19363271 binding of Hsp90 to tau facilitates a conformational change that could result in its phosphorylation by glycogen synthase kinase 3 and its aggregation into filamentous structures. |
| GO:1904813 ficolin-1-rich granule lumen | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Ficolin-1-rich granule lumen (Reactome neutrophil degranulation). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:1904813 ficolin-1-rich granule lumen | TAS Reactome:R-HSA-6800434 | KEEP AS NON CORE | Summary: Ficolin-1-rich granule lumen (Reactome neutrophil degranulation). Reason: HSP90 is an abundant, mainly cytosolic chaperone; this location reflects a minor or cell type-specific pool and is not core. |
| GO:1905323 telomerase holoenzyme complex assembly | IDA PMID:10197982 Functional requirement of p23 and Hsp90 in telomerase comple... | KEEP AS NON CORE | Summary: HSP90 is required for telomerase holoenzyme assembly. Reason: Client-specific; non-core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:1905323 telomerase holoenzyme complex assembly | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: HSP90 is required for telomerase holoenzyme assembly. Reason: Client-specific; non-core. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex |
| GO:1990565 HSP90-CDC37 chaperone complex | IEA GO_REF:0000117 | ACCEPT | Summary: HSP90 forms the HSP90-CDC37 kinase chaperone complex. Reason: Well-established complex. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity |
| GO:1990565 HSP90-CDC37 chaperone complex | IPI PMID:19073599 The human Cdc37.Hsp90 complex studied by heteronuclear NMR s... | ACCEPT | Summary: HSP90 forms the HSP90-CDC37 kinase chaperone complex. Reason: Well-established complex. Supporting Evidence: file:human/HSP90AA1/HSP90AA1-uniprot.txt Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity |
| GO:1990782 protein tyrosine kinase binding | IPI PMID:20353823 Stat1 mediates an auto-regulation of hsp90beta gene in heat ... | KEEP AS NON CORE | Summary: Binding to protein tyrosine kinases (e.g. JAK2, kinase clients). Reason: Binding of a client or co-chaperone; such interactions are how HSP90 exerts its chaperone function. Retained as non-core because the informative activity is the ATP-dependent chaperone function, of which this is one instance. |
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Download this section (compressed HTML)Q: Which client classes depend specifically on HSP90alpha (HSP90AA1) rather than the constitutive HSP90beta (HSP90AB1), and does this reflect isoform-specific co-chaperone affinities?
Q: Which of the many rodent physiology-based electronic annotations reflect HSP90alpha-specific functions versus indirect client effects?
Experiment: Quantitative client-interaction proteomics (e.g. LUMIER or AP-MS) in isogenic HSP90AA1-null and HSP90AB1-null human cells at basal and heat-shock conditions.
Hypothesis: HSP90alpha and HSP90beta differ in client spectrum under heat stress.
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