HSP70-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: HSC70-1 is predominantly localized to the cytoplasm under non-stress conditions, where it maintains HSF transcription factors in their inactive state and performs housekeeping protein folding functions. Reason: Well-supported by IBA phylogenetic inference and experimental evidence. PMID:32573848 demonstrates cytoplasmic localization and shows HSC70-1 sequesters HsfA1d and HsfA1e in the cytosol under non-heat stress conditions. PMID:18065690 confirms cytoplasmic distribution. This is a core cellular localization for HSC70-1's primary functions. Supporting Evidence: PMID:32573848 Hsc70-1 showed physical interaction with HsfA1d and HsfA1e protein in the cytosol under non-HS conditions. PMID:18065690 Arabidopsis SGT1a and SGT1b proteins associate with HSC70 in vivo and distribute with HSC70 in the cytosol and nucleus.
GO:0016887 ATP hydrolysis activity	IBA GO_REF:0000033	ACCEPT	Summary: HSC70-1 possesses ATP hydrolysis activity that is essential for its chaperone function, driving conformational changes between ATP-bound (low substrate affinity) and ADP-bound (high substrate affinity) states. Reason: Core molecular function of all Hsp70 family members. ATP hydrolysis is the central enzymatic activity that powers the protein folding cycle. Deep research confirms ATP-dependent conformational cycles are fundamental to HSC70-1 function. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md In its ATP-bound conformation, HSC70-1 adopts an open state with substantially reduced affinity for protein substrates... Upon binding of a J-domain protein cochaperone... the ATPase activity of HSC70-1 is stimulated approximately 20-100 fold, accelerating the hydrolysis of ATP to ADP.
GO:0031072 heat shock protein binding	IBA GO_REF:0000033	MODIFY	Summary: HSC70-1 binds to other heat shock proteins, particularly through interactions with HSF transcription factors and potentially other Hsps in chaperone complexes. Reason: The local experimental support is physical interaction with HsfA1d and HsfA1e, which are DNA-binding heat shock transcription factors rather than unfolded protein substrates. The more specific replacement captures the supported HSF-client interaction without converting it to unfolded protein binding. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000452648 · HSP70 family node SUPPORTS TRANSFER Hsp70 co-chaperone and HSP-HSP interactions across the seeds support the node-level term. UniProtKB:P11142 · human HSPA8 (HSC70) SUPPORTS TRANSFER Well-characterized co-chaperone interactions ground the IBD; the target-specific supported interaction is with HsfA1d/HsfA1e transcription factors, hence the more specific replacement. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:32573848 Hsc70-1 showed physical interaction with HsfA1d and HsfA1e protein in the cytosol under non-HS conditions.
GO:0044183 protein folding chaperone	IBA GO_REF:0000033	ACCEPT	Summary: HSC70-1 functions as a protein folding chaperone, facilitating ATP-dependent folding of nascent and misfolded proteins. Reason: Core molecular function well-supported by IBA and literature. HSC70-1 is a canonical member of the Hsp70 chaperone family with established protein folding activity. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md HSC70-1 functions as a molecular chaperone through an ATP-driven cycle that enables rapid, reversible binding to client protein substrates while maintaining extremely low intrinsic ATP hydrolysis rates that must be stimulated by cochaperones.
GO:0042026 protein refolding	IBA GO_REF:0000033	ACCEPT	Summary: HSC70-1 participates in protein refolding through ATP-dependent cycles of substrate binding and release, particularly during stress recovery. Reason: Well-supported by IBA phylogenetic evidence. Protein refolding is a core Hsp70 family function, particularly important during recovery from heat stress when aggregated proteins must be resolubilized. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md HSC70-1 possesses the capacity to actively unfold and disaggregate stable, pre-formed protein aggregates through a mechanism termed entropic pulling.
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: HSC70-1 binds ATP and ADP nucleotides as part of its chaperone cycle. Reason: Accurate but generic IEA annotation. Nucleotide binding is essential for HSC70-1 function, though 'ATP binding' is more specific and already annotated.
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: HSC70-1 binds ATP in its nucleotide-binding domain, with ATP hydrolysis driving conformational changes. Reason: Core molecular function supported by IEA and extensive literature. ATP binding is fundamental to all Hsp70 chaperone activity.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: HSC70-1 can translocate to the nucleus, particularly during heat stress when it co-localizes with HSF1. Reason: Accurate IEA annotation supported by experimental evidence. HSC70-1 contains nuclear localization signals and undergoes stress-induced nuclear translocation. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md Upon exposure to elevated temperatures, HSC70-1 undergoes rapid translocation to the nucleus in a process that is dependent on simultaneous nuclear import of heat shock factor 1 (HSF1). PMID:18065690 Arabidopsis SGT1a and SGT1b proteins associate with HSC70 in vivo and distribute with HSC70 in the cytosol and nucleus. PMID:32573848 AtHsc70-1 negatively regulates the basal heat tolerance in Arabidopsis thaliana through affecting the activity of HsfAs and Hsp101.
GO:0006952 defense response	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: HSC70-1 contributes to defense response through its role in maintaining NB-LRR immune receptor stability and function. Reason: HSC70-1 does participate in immune responses (PMID:18065690), but this is a pleiotropic function rather than core molecular activity. Overexpression actually impairs immunity, suggesting a complex regulatory role. Supporting Evidence: PMID:18065690 HSC70-1 overexpression disables resistance to virulent and avirulent pathogens.
GO:0009408 response to heat	IEA GO_REF:0000117	ACCEPT	Summary: HSC70-1 responds to heat stress through nuclear translocation and regulation of HSF activity, though paradoxically its loss enhances basal thermotolerance. Reason: The term 'response to heat' is appropriate but doesn't fully capture HSC70-1's NEGATIVE regulatory role. However, there isn't a perfect replacement term. The annotation is accurate as HSC70-1 does respond to and participate in heat stress responses, even though it paradoxically acts as a negative regulator of basal thermotolerance. Accept with this caveat. Supporting Evidence: PMID:32573848 Arabidopsis hsc70-1 mutant seedlings show elevated basal heat tolerance compared with wild-type.
GO:0009615 response to virus	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: HSC70-1 is induced by viral infection as part of general protein stress response. Reason: While HSC70-1 is upregulated during viral infection, this represents a general stress response rather than a specific antiviral function. The primary role is managing protein folding stress caused by viral protein accumulation.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000002	ACCEPT	Summary: Duplicate annotation - ATP hydrolysis activity already covered by IBA annotation. Reason: Duplicate of IBA annotation for same term. Both IBA and IEA evidence support this core molecular function.
GO:0005515 protein binding	IPI PMID:18065690 Interaction between SGT1 and cytosolic/nuclear HSC70 chapero...	KEEP AS NON CORE	Summary: HSC70-1 binds to SGT1B protein through direct physical interaction. Reason: The SGT1B interaction is experimentally supported, but SGT1 is a co-chaperone/adaptor in immune receptor complex assembly rather than a canonical protein-folding chaperone. Retain the existing protein-binding annotation as context-specific, non-core evidence rather than replacing it with protein-folding chaperone binding. Supporting Evidence: PMID:18065690 We affinity-purified SGT1-interacting proteins from Arabidopsis thaliana leaf extracts and identified by mass spectrometry cytosolic heat shock cognate 70 (HSC70) chaperones as the major stable SGT1 interactors.
GO:0010494 cytoplasmic stress granule	IDA PMID:30664249 Protein and metabolite composition of Arabidopsis stress gra...	ACCEPT	Summary: HSC70-1 localizes to cytoplasmic stress granules under stress conditions. Reason: Supported by IDA experimental evidence from PMID:30664249. Stress granule localization is consistent with HSC70-1's role in managing protein aggregation during stress. Supporting Evidence: PMID:30664249 Protein and metabolite composition of Arabidopsis stress granules.
GO:0000325 plant-type vacuole	HDA PMID:17151019 A proteomics dissection of Arabidopsis thaliana vacuoles iso...	MARK AS OVER ANNOTATED	Summary: HSC70-1 detected in plant-type vacuole by proteomics. Reason: HDA (high-throughput direct assay) from proteomics. Likely represents minor contaminant or transient localization rather than functional compartment. Primary localization is cytosol/nucleus. Supporting Evidence: PMID:17151019 Epub 2006 Dec 6. A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture.
GO:0005794 Golgi apparatus	HDA PMID:22430844 Isolation and proteomic characterization of the Arabidopsis ...	MARK AS OVER ANNOTATED	Summary: HSC70-1 detected in Golgi apparatus by proteomics. Reason: HDA proteomics annotation. Likely over-annotation as Golgi is not a known functional compartment for cytosolic Hsp70s. May represent transient association or contamination. Supporting Evidence: PMID:22430844 Mar 19. Isolation and proteomic characterization of the Arabidopsis Golgi defines functional and novel components involved in plant cell wall biosynthesis.
GO:0009505 plant-type cell wall	HDA PMID:16287169 Arabidopsis cell wall proteome defined using multidimensiona...	MARK AS OVER ANNOTATED	Summary: HSC70-1 detected in plant-type cell wall by proteomics. Reason: HDA proteomics annotation. HSC70-1 lacks secretion signals and functions as cytosolic chaperone. Cell wall detection likely represents contamination in cell wall preparations. Supporting Evidence: PMID:16287169 Arabidopsis cell wall proteome defined using multidimensional protein identification technology.
GO:0005730 nucleolus	HDA PMID:15496452 Proteomic analysis of the Arabidopsis nucleolus suggests nov...	KEEP AS NON CORE	Summary: HSC70-1 detected in nucleolus by proteomics. Reason: HDA proteomics evidence. While HSC70-1 does translocate to nucleus during stress, nucleolus localization is not a primary function. May represent legitimate but minor localization. Supporting Evidence: PMID:15496452 Oct 20. Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions.
GO:0048046 apoplast	HDA PMID:18538804 Hydroponic isotope labelling of entire plants (HILEP) for qu...	MARK AS OVER ANNOTATED	Summary: HSC70-1 detected in apoplast by proteomics. Reason: HDA proteomics annotation. Apoplast is extracellular space - HSC70-1 lacks secretion signals and this likely represents contamination. Supporting Evidence: PMID:18538804 Epub 2008 Jun 5. Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study.
GO:0005634 nucleus	HDA PMID:14617066 Analysis of the Arabidopsis nuclear proteome and its respons...	ACCEPT	Summary: HSC70-1 detected in nucleus by proteomics (HDA evidence). Reason: HDA evidence supports the well-established nuclear localization. This complements the IEA and IDA annotations for nuclear localization. Supporting Evidence: PMID:14617066 Analysis of the Arabidopsis nuclear proteome and its response to cold stress.
GO:0022626 cytosolic ribosome	HDA PMID:15821981 High heterogeneity within the ribosomal proteins of the Arab...	KEEP AS NON CORE	Summary: HSC70-1 detected in cytosolic ribosome by proteomics. Reason: HDA proteomics evidence. Ribosome association is consistent with co-translational folding function mentioned in deep research, but this is not a stable localization. Represents transient functional association. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md HSC70-1 participates in the co-translational folding of nascent polypeptides through association with actively translating ribosomes. PMID:15821981 High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome.
GO:0005886 plasma membrane	HDA PMID:17644812 A high content in lipid-modified peripheral proteins and int...	KEEP AS NON CORE	Summary: HSC70-1 detected at plasma membrane by proteomics. Reason: HDA proteomics evidence supports retaining the plasma membrane localization as a non-core, low-specificity localization call. No AT5G02500-specific clathrin-uncoating mechanism is asserted from this annotation. Supporting Evidence: PMID:17644812 Epub 2007 Jul 20. A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome.
GO:0009506 plasmodesma	HDA PMID:21533090 Arabidopsis plasmodesmal proteome.	MARK AS OVER ANNOTATED	Summary: HSC70-1 detected in plasmodesma by proteomics. Reason: HDA proteomics annotation. Plasmodesma localization is not supported by functional studies. Likely represents contamination or very transient association. Supporting Evidence: PMID:21533090 Arabidopsis plasmodesmal proteome.
GO:0009507 chloroplast	HDA PMID:18431481 Sorting signals, N-terminal modifications and abundance of t...	REMOVE	Summary: HSC70-1 detected in chloroplast by proteomics (HDA). Reason: HSC70-1 is a CYTOSOLIC Hsp70, not a chloroplast protein. Chloroplasts have their own cpHsc70 proteins (At4g24280, At5g49910). This HDA annotation represents contamination or mislabeling. UniProt does NOT indicate chloroplast localization. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md cpHsc70-1 and cpHsc70-2 are two putative stromal Hsp70s in Arabidopsis [referring to At4g24280 and At5g49910]... HSC70-1 at AT5G02500 is the CYTOSOLIC one PMID:18431481 Sorting signals, N-terminal modifications and abundance of the chloroplast proteome.
GO:0005515 protein binding	IPI PMID:32573848 AtHsc70-1 negatively regulates the basal heat tolerance in A...	MODIFY	Summary: HSC70-1 physically interacts with HsfA1d (AT1G32330) and HsfA1e (AT3G02990) transcription factors. Reason: Generic 'protein binding' term is uninformative. The cited evidence is physical interaction with HsfA1d and HsfA1e, so DNA-binding transcription factor binding is the supported, more specific replacement. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:32573848 Hsc70-1 showed physical interaction with HsfA1d and HsfA1e protein in the cytosol under non-HS conditions.
GO:0005634 nucleus	IDA PMID:32573848 AtHsc70-1 negatively regulates the basal heat tolerance in A...	ACCEPT	Summary: HSC70-1 localizes to nucleus as demonstrated by IDA in PMID:32573848. Reason: Experimental IDA evidence supporting nuclear localization. Complements other evidence (IEA, HDA) for nuclear presence. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-goa.tsv The GOA source records an IDA located_in nucleus annotation for HSP70-1 from PMID:32573848. file:ARATH/AT5G02500/AT5G02500-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
GO:0005829 cytosol	IDA PMID:32573848 AtHsc70-1 negatively regulates the basal heat tolerance in A...	ACCEPT	Summary: HSC70-1 localizes to cytosol as demonstrated by IDA in PMID:32573848. Reason: Experimental IDA evidence for cytosolic localization, which is the primary compartment for HSC70-1 function. Supporting Evidence: PMID:32573848 Hsc70-1 showed physical interaction with HsfA1d and HsfA1e protein in the cytosol under non-HS conditions.
GO:0010286 heat acclimation	IMP PMID:32573848 AtHsc70-1 negatively regulates the basal heat tolerance in A...	ACCEPT	Summary: HSC70-1 participates in heat acclimation process. Reason: The heat acclimation annotation is reasonable but HSC70-1's role is complex - it NEGATIVELY regulates basal heat tolerance. However, the IMP evidence from PMID:32573848 is valid. Accept with the understanding that HSC70-1 modulates (rather than directly promotes) heat acclimation. Supporting Evidence: PMID:32573848 Arabidopsis hsc70-1 mutant seedlings show elevated basal heat tolerance compared with wild-type. Over-expression of Hsc70-1 resulted in increased heat sensitivity.
GO:0003729 mRNA binding	IDA PMID:32344669 Discovering the RNA-Binding Proteome of Plant Leaves with an...	ACCEPT	Summary: HSC70-1 binds mRNA as demonstrated by RNA interactome capture. Reason: Experimental IDA evidence from PMID:32344669 using RNA interactome capture method. mRNA binding is consistent with ribosome-associated protein folding and potential roles in mRNA quality control. Supporting Evidence: PMID:32344669 Discovering the RNA-Binding Proteome of Plant Leaves with an Improved RNA Interactome Capture Method.
GO:0005829 cytosol	HDA PMID:25293756 A proteomic strategy for global analysis of plant protein co...	ACCEPT	Summary: HSC70-1 detected in cytosol by proteomics (HDA). Reason: HDA proteomics evidence supporting cytosolic localization, which is the primary functional compartment. Supporting Evidence: PMID:25293756 Oct 7. A proteomic strategy for global analysis of plant protein complexes.
GO:0005737 cytoplasm	ISM GO_REF:0000122	ACCEPT	Summary: Cytoplasm localization based on sequence analysis (ISM). Reason: ISM computational evidence from AtSubP analysis. Consistent with experimental evidence for cytoplasmic localization.
GO:0009507 chloroplast	ISM GO_REF:0000122	REMOVE	Summary: Chloroplast localization predicted by sequence analysis (ISM). Reason: Incorrect ISM prediction. HSC70-1 is a cytosolic protein lacking chloroplast transit peptide. Contradicts all experimental evidence and UniProt annotation. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md HSC70-1 at AT5G02500 is the CYTOSOLIC one [not chloroplast]. The presence of the C-terminal GPKIEEVD sequence, rather than organellar targeting peptides, ensures that HSC70-1 is directed to and retained within the cytoplasmic compartment.
GO:0098542 defense response to other organism	IMP PMID:26408532 Opposing Effects on Two Phases of Defense Responses from Con...	KEEP AS NON CORE	Summary: HSC70-1 involved in defense response to other organism as shown by IMP in PMID:26408532. Reason: Valid IMP evidence for role in immunity, but this is not a core function. HSC70-1's role in immunity is through chaperone support of immune receptors, and overexpression actually impairs defense (PMID:18065690). Supporting Evidence: PMID:18065690 HSC70-1 overexpression disables resistance to virulent and avirulent pathogens. PMID:26408532 Sep 25. Opposing Effects on Two Phases of Defense Responses from Concerted Actions of HEAT SHOCK COGNATE70 and BONZAI1 in Arabidopsis.
GO:0009408 response to heat	IEP PMID:15805473 Virus induction of heat shock protein 70 reflects a general ...	ACCEPT	Summary: HSC70-1 expression pattern changes in response to heat (IEP evidence). Reason: Valid IEP (expression pattern) evidence. While HSC70-1 is constitutively expressed, it does show modest induction by heat stress. Supporting Evidence: PMID:15805473 Apr 1. Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol.
GO:0010187 negative regulation of seed germination	IMP PMID:21586649 The cytosolic/nuclear HSC70 and HSP90 molecular chaperones a...	KEEP AS NON CORE	Summary: HSC70-1 negatively regulates seed germination as shown by IMP in PMID:21586649, consistent with its negative regulation of ABA responses. Reason: IMP evidence supports HSC70-1's role in ABA-mediated germination control. This is retained as a non-core, ABA-linked physiological effect rather than as the central molecular function of this Hsp70 chaperone. Supporting Evidence: PMID:21586649 Plants overexpressing HSC70-1 or with reduced HSP90.2 activity are hypersensitive to ABA in seed germination assays
GO:0090332 stomatal closure	IMP PMID:21586649 The cytosolic/nuclear HSC70 and HSP90 molecular chaperones a...	KEEP AS NON CORE	Summary: HSC70-1 negatively regulates stomatal closure as shown by IMP in PMID:21586649. Reason: The stomatal closure annotation is valid IMP evidence but HSC70-1 acts as a NEGATIVE regulator - overexpression compromises closure. The term is retained as a non-core physiological process because it reflects stress and ABA signaling context rather than the primary chaperone activity. Supporting Evidence: PMID:21586649 Plants overexpressing HSC70-1 or with reduced HSP90.2 activity are compromised in the dark-, CO(2)-, flagellin 22 peptide-, and abscisic acid (ABA)-induced stomatal closure.
GO:0005829 cytosol	RCA NOT PMID:21166475 Analysis of the Arabidopsis cytosolic proteome highlights su...	REMOVE	Summary: Negated cytosol localization based on RCA conflicts with positive cytosol evidence for HSC70-1. Reason: The NOT qualifier means the annotation asserts that HSC70-1 is not located in the cytosol, not merely that it is not exclusively cytosolic. That interpretation conflicts with positive cytosol annotations, UniProt cytosolic localization, and the PMID:21166475 cytosolic proteome context. Supporting Evidence: PMID:21166475 The cytosolic protein fraction from cell suspensions of Arabidopsis thaliana was isolated and analyzed using offline strong cation exchange liquid chromatography and LC-MS/MS.
GO:0005634 nucleus	IDA PMID:21418353 AtHsp70-15-deficient Arabidopsis plants are characterized by...	ACCEPT	Summary: Nuclear localization demonstrated by IDA in PMID:21418353. Reason: Experimental IDA evidence for nuclear presence. Consistent with dynamic nucleo-cytoplasmic shuttling. Supporting Evidence: PMID:21418353 2011 Apr 28. AtHsp70-15-deficient Arabidopsis plants are characterized by reduced growth, a constitutive cytosolic protein response and enhanced resistance to TuMV.
GO:0005829 cytosol	IDA PMID:21418353 AtHsp70-15-deficient Arabidopsis plants are characterized by...	ACCEPT	Summary: Cytosol localization demonstrated by IDA in PMID:21418353. Reason: Experimental IDA evidence for primary cytosolic localization. Supporting Evidence: PMID:21418353 2011 Apr 28. AtHsp70-15-deficient Arabidopsis plants are characterized by reduced growth, a constitutive cytosolic protein response and enhanced resistance to TuMV.
GO:0005737 cytoplasm	IDA PMID:18065690 Interaction between SGT1 and cytosolic/nuclear HSC70 chapero...	ACCEPT	Summary: Cytoplasm localization demonstrated by IDA in PMID:18065690. Reason: Experimental IDA evidence for cytoplasmic localization. Supporting Evidence: PMID:18065690 Dec 7. Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses.
GO:0009408 response to heat	IMP PMID:18065690 Interaction between SGT1 and cytosolic/nuclear HSC70 chapero...	ACCEPT	Summary: HSC70-1 affects response to heat as shown by IMP in PMID:18065690. Reason: Valid IMP evidence for HSC70 involvement in heat-stress tolerance context. The cited paper supports SGT1/HSC70 complex roles in environmental responses and notes that deregulation of HSC70-1 affects heat-shock tolerance; the HSF/Hsp101 mechanism is supported by PMID:32573848, not this annotation's original paper. Supporting Evidence: PMID:18065690 We conclude that an HSC70-SGT1 chaperone complex is important for multiple plant environmental responses.
GO:0042742 defense response to bacterium	IMP PMID:18065690 Interaction between SGT1 and cytosolic/nuclear HSC70 chapero...	KEEP AS NON CORE	Summary: HSC70-1 modulates defense responses to bacterial pathogens as shown by IMP evidence in PMID:18065690, consistent with its immune receptor chaperone role. Reason: IMP evidence demonstrates HSC70-1 is required for proper defense against bacterial pathogens via the HSC70-SGT1-HSP90 immune chaperone network, but this is a context-specific outcome of chaperone function rather than the core molecular role of HSP70-1. Supporting Evidence: PMID:18065690 HSC70-1 overexpression disables resistance to virulent and avirulent pathogens.
GO:0050832 defense response to fungus	IMP PMID:18065690 Interaction between SGT1 and cytosolic/nuclear HSC70 chapero...	KEEP AS NON CORE	Summary: HSC70-1 modulates defense responses to fungal pathogens as shown by IMP evidence in PMID:18065690, consistent with its immune chaperone function. Reason: IMP evidence supports HSC70-1's role in defense against fungal pathogens via the HSC70-SGT1-HSP90 complex, but this is retained as a non-core immune consequence of chaperone biology rather than a primary function. Supporting Evidence: PMID:18065690 HSC70-1 overexpression disables resistance to virulent and avirulent pathogens.
GO:0002020 protease binding	IPI PMID:20543027 The deubiquitinating enzyme AMSH3 is required for intracellu...	ACCEPT	Summary: HSC70-1 binds to AMSH3 deubiquitinating enzyme (protease). Reason: Valid IPI evidence from PMID:20543027. Protease binding represents a specific interaction relevant to HSC70-1's role in protein quality control and trafficking. Supporting Evidence: file:ARATH/AT5G02500/AT5G02500-deep-research-perplexity.md Binds to the deubiquitinating enzyme AMSH3. PMID:20543027 The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana.
GO:0009615 response to virus	IEP PMID:15805473 Virus induction of heat shock protein 70 reflects a general ...	KEEP AS NON CORE	Summary: HSC70-1 expression responds to virus infection (IEP evidence). Reason: Valid IEP expression evidence. HSC70-1 is induced by viral infection but this reflects general protein stress response rather than specific antiviral function. Supporting Evidence: PMID:15805473 Apr 1. Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol.
GO:0009408 response to heat	IEP PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis...	ACCEPT	Summary: HSC70-1 expression responds to heat (IEP evidence from PMID:11402207). Reason: Valid IEP expression evidence showing heat responsiveness. Supporting Evidence: PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.
GO:0005829 cytosol	TAS PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis...	ACCEPT	Summary: Cytosol localization based on TAS (traceable author statement) from PMID:11402207. Reason: TAS evidence from authoritative publication confirming cytosolic localization. Supporting Evidence: PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.
GO:0006457 protein folding	TAS PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis...	ACCEPT	Summary: HSC70-1 involved in protein folding based on TAS from PMID:11402207. Reason: TAS evidence for core protein folding function. Well-established role for all Hsp70 family members. Supporting Evidence: PMID:11402207 Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.

Gene Description

Existing Annotations Review

Core Functions

ATP-dependent Hsp70-family chaperone activity supporting protein folding, refolding, and proteostasis in the cytosol and nucleus.

Negative regulation of basal thermotolerance through interaction with HsfA transcription factors and control of Hsp101 expression.

References

Deep Research

Falcon

Perplexity

📚 Additional Documentation

Notes

Annotation Review Summary

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