HSPA4

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000774 adenyl-nucleotide exchange factor activity	IBA GO_REF:0000033	ACCEPT	Summary: adenyl-nucleotide exchange factor activity: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0005515 protein binding	IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b...	UNDECIDED	Summary: protein binding: The PMID:20029029 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:20029029 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:22990239 Metazoan Hsp70 machines use Hsp110 to power protein disaggre...	UNDECIDED	Summary: protein binding: The PMID:22990239 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:22990239 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ...	UNDECIDED	Summary: protein binding: The PMID:24658140 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:24658140 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	UNDECIDED	Summary: protein binding: The PMID:25416956 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:25416956 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	UNDECIDED	Summary: protein binding: The PMID:25416956 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:25416956 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive...	UNDECIDED	Summary: protein binding: The PMID:29568061 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:29568061 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	UNDECIDED	Summary: protein binding: The PMID:30021884 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:30021884 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	UNDECIDED	Summary: protein binding: The PMID:31980649 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:31980649 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	UNDECIDED	Summary: protein binding: The PMID:33961781 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:33961781 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	UNDECIDED	Summary: protein binding: The PMID:40205054 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:40205054 interaction annotation does not by itself identify a molecular role for HSPA4. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005524 ATP binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: ATP binding: Nucleotide engagement is compatible with the conserved Hsp110 nucleotide-binding region, but ATP binding alone does not describe HSPA4 biological specificity or prove robust intrinsic ATPase catalysis. Reason: Nucleotide engagement is compatible with the conserved Hsp110 nucleotide-binding region, but ATP binding alone does not describe HSPA4 biological specificity or prove robust intrinsic ATPase catalysis. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0005524 ATP binding	NAS PMID:8335910 Molecular cloning of a novel human hsp70 from a B cell line ...	KEEP AS NON CORE	Summary: ATP binding: Nucleotide engagement is compatible with the conserved Hsp110 nucleotide-binding region, but ATP binding alone does not describe HSPA4 biological specificity or prove robust intrinsic ATPase catalysis. Reason: Nucleotide engagement is compatible with the conserved Hsp110 nucleotide-binding region, but ATP binding alone does not describe HSPA4 biological specificity or prove robust intrinsic ATPase catalysis. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0005634 nucleus	IBA GO_REF:0000033	UNDECIDED	Summary: nucleus: The available evidence examined for HSPA4 does not resolve the exact claim of nucleus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for HSPA4 does not resolve the exact claim of nucleus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: cytoplasm: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: cytosol: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0005829 cytosol	IDA PMID:21231916 The diverse members of the mammalian HSP70 machine show dist...	ACCEPT	Summary: cytosol: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0006457 protein folding	IBA GO_REF:0000033	ACCEPT	Summary: protein folding: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0006986 response to unfolded protein	NAS PMID:8335910 Molecular cloning of a novel human hsp70 from a B cell line ...	UNDECIDED	Summary: response to unfolded protein: The available evidence examined for HSPA4 does not resolve the exact claim of response to unfolded protein. The specific experiment or traced orthology/phylogenetic inference behind PMID:8335910 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for HSPA4 does not resolve the exact claim of response to unfolded protein. The specific experiment or traced orthology/phylogenetic inference behind PMID:8335910 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000002	UNDECIDED	Summary: ATP hydrolysis activity: The primary Apg2 experiments show modulation of Hsc70 ATP hydrolysis, not necessarily substantial hydrolysis catalyzed by Apg2 itself. A direct HSPA4 ATPase assay is needed to separate the intrinsic catalytic claim from nucleotide-exchange regulation. Reason: The primary Apg2 experiments show modulation of Hsc70 ATP hydrolysis, not necessarily substantial hydrolysis catalyzed by Apg2 itself. A direct HSPA4 ATPase assay is needed to separate the intrinsic catalytic claim from nucleotide-exchange regulation. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0030150 protein import into mitochondrial matrix	IDA PMID:15644312 Dissection of the mitochondrial import and assembly pathway ...	UNDECIDED	Summary: protein import into mitochondrial matrix: The cached Tom40 import-paper abstract foregrounds Hsp90 and does not expose the HSPA4-specific experiment. This is not grounds for rejection or a wrong-gene claim; full text and the actual HSPA4 construct/assay are required. Reason: The cached Tom40 import-paper abstract foregrounds Hsp90 and does not expose the HSPA4-specific experiment. This is not grounds for rejection or a wrong-gene claim; full text and the actual HSPA4 construct/assay are required. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0043226 organelle	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: organelle: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Reason: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0051131 chaperone-mediated protein complex assembly	IDA PMID:15644312 Dissection of the mitochondrial import and assembly pathway ...	UNDECIDED	Summary: chaperone-mediated protein complex assembly: The cached Tom40 import-paper abstract foregrounds Hsp90 and does not expose the HSPA4-specific experiment. This is not grounds for rejection or a wrong-gene claim; full text and the actual HSPA4 construct/assay are required. Reason: The cached Tom40 import-paper abstract foregrounds Hsp90 and does not expose the HSPA4-specific experiment. This is not grounds for rejection or a wrong-gene claim; full text and the actual HSPA4 construct/assay are required. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	KEEP AS NON CORE	Summary: extracellular exosome: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Reason: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.
GO:0070062 extracellular exosome	IDA PMID:21276792 Morphologic and proteomic characterization of exosomes relea...	KEEP AS NON CORE	Summary: extracellular exosome: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Reason: The reported broad organelle/vesicle association does not establish the principal function of HSPA4. Retain the location as a contextual observation while using cytosolic chaperone regulation as the core biological description. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells.

Gene Description

Existing Annotations Review

Core Functions

HSPA4, also called Apg2, is an Hsp110-family chaperone that serves as a nucleotide-exchange factor for Hsc70.

References

Deep Research

Manual

📚 Additional Documentation

Notes

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