HSC82 is annotated to GO:0140662 ATP-dependent protein folding chaperone via InterPro-to-GO mapping reflecting Hsp90 family membership.

PANTHER phylogenetic-tree annotation propagates conserved Hsp90 chaperone functions (ATP binding, ATP hydrolysis, protein folding, cellular response to heat, protein stabilization, identical protein binding, cytosol localization) to S. cerevisiae HSC82.

UniProtKB keyword 'Nucleotide-binding' maps to GO:0000166 nucleotide binding for HSC82 based on its conserved Hsp90 ATPase domain.

HSC82 UniProt subcellular location annotations (cytoplasm, mitochondrion) are mapped to corresponding cellular component GO terms.

ARBA machine-learning model assigns HSC82 to box C/D snoRNP assembly and proteasome assembly based on Hsp90 family signatures and chaperone client patterns.

Combined automated IEA pipelines annotate HSC82 with ATP binding, ATP hydrolysis activity, protein folding, and unfolded protein binding from UniProt features.

HSC82 was identified in multi-protein complexes by systematic functional organization of the yeast proteome.

HSC82 was identified in multi-protein complexes by systematic affinity-purification mass spectrometry.

HSC82/Hsp90 is required for assembly and maintenance of the 26S proteasome in vivo, supporting GO:0043248 proteasome assembly as a client-dependent secondary function.

Genome-wide GFP localization study assigns HSC82 to the cytoplasm in S. cerevisiae.

HSC82 was detected in the yeast mitochondrial proteome, supporting a minor mitochondrial pool.

HSC82 appears in polyubiquitin conjugate analysis as a Rpn10-relevant proteasome substrate context, consistent with chaperone roles in client triage.

Integrative map of HSC82/Hsp90 physical and genetic interactions defines its central position in the yeast chaperone network.

Proteome survey of yeast cellular machinery places HSC82 within multi-protein modules consistent with its chaperone hub status.

HSC82 is part of the global landscape of yeast protein complexes mapped by tandem affinity purification.

HSC82 was detected in the plasma membrane proteome of S. cerevisiae, supporting a minor membrane-associated pool.

HSC82 was detected in extended yeast mitochondrial proteomics datasets, consistent with a minor mitochondrial pool.

HSC82/Hsp90 modulates multiple telomerase activities, supporting its role in telomere maintenance regulation as a client-dependent function.

HSC82/Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation, providing IMP evidence for box C/D snoRNP assembly involvement.

Direct biochemical measurement of ATPase activity showing intra- and intermonomer cooperation

HSC82 is captured in a high-quality binary interaction map of the yeast interactome.

Yeast atlas of chaperone-protein interactions defines HSC82's extensive chaperone-client and chaperone-cochaperone interaction network.

HSC82 likely appeared as a background chaperone interactor in affinity-purification proteomics of SAGA/ADA; HSC82-specific information appears to be in supplementary data rather than the cached main text. This reference underlies the IPI protein-binding annotation and supports the MARK_AS_OVER_ANNOTATED decision rather than implying genuine SAGA/ADA membership.

The paper studies CDK-dependent T36 phosphorylation of the yeast Hsp70 Ssa1 (and the homologous T38 site of mammalian Hsc70) controlling G1 cyclin (Cln3/Cyclin D1) binding and degradation; HSC82 is not the subject of this paper. The IPI annotation likely reflects HSC82 being captured in Ssa1 interactome MS as part of the broader Hsp70/Hsp90 chaperone network, hence the over-annotation classification of the protein binding term.

HSC82 was detected as an interactor in molecular architecture studies of the SEA complex, a TORC1 pathway modulator.

Both HSP82 and HSC82 are required for growth at elevated temperatures

Structural pleiotropy and regulatory evolution maintain HSP82-HSC82 paralog heteromers, supporting identical protein binding (homo- and heterodimerization).

HSC82 appeared as a prey protein in a quantitative proteomics study mapping RNA-dependent interactions for 40 yeast RBPs; specific RDI vs PPI classification for HSC82 is in supplementary data not reproduced in the cached text. This reference underlies the IPI protein-binding annotation and supports the MARK_AS_OVER_ANNOTATED decision.

HSC82 is part of the social/structural architecture of the yeast protein interactome captured by integrative network analysis.

Hsp90 is required for protein folding in vivo

HSC82 binds unfolded proteins

The paper identifies Hsp82, not HSC82, in the purified HAP1 complex; its use for HSC82 is a family-level paralog extrapolation based on their shared client repertoire.

CNS1 encodes an essential p60/Sti1 homolog that suppresses cyclophilin 40 mutations and interacts with HSC82/Hsp90, supporting the cochaperone-network annotations.

HSC82 stabilizes and regulates calcineurin (CNA2) under salt stress conditions

Falcon deep research synthesis covering the core HSC82 functions (ATP-dependent Hsp90 chaperone cycle, cytosolic localization, client/ co-chaperone complexes, calcineurin/CNA2 stabilization) and adjudicating non-core or questionable annotations (plasma membrane, perinuclear region, mitochondrion, generic protein-containing complex/nucleotide binding, unfolded protein binding vs. ATP-dependent protein folding chaperone, box C/D snoRNP/R2TP, kinetochore/SGT1, broad stress-response terms), with explicit distinction from the inducible HSP82 paralog.

Reviewed Swiss-Prot entry describing HSC82 as the constitutive cytosolic Hsp90 isoform "ATP-dependent molecular chaperone HSC82" (705 aa). Source of UniProt-curated cross-references and the IEA mappings (GO_REF:0000043, GO_REF:0000044, GO_REF:0000117) used in the GOA file.