Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.
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Hsp110 is highly efficient at preventing aggregation of heat-denatured proteins, functioning as a holdase chaperone that maintains substrates in a folding-competent state. It is significantly more efficient than Hsc70 at this holdase function.
"hsp110 is highly efficient in selectively recognizing denatured proteins and maintaining them in a soluble, folding-competent state and is significantly more efficient in performing this function than is hsc70"
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Hsp110 does not refold denatured proteins itself; refolding requires Hsc70 and Hdj-1. Hdj-1 does not function as a co-chaperone with Hsp110.
"hsp110-bound proteins can then be refolded by the addition of rabbit reticulocyte lysate or hsc70 and Hdj-1, whereas Hdj-1 does not itself function as a co-chaperone in folding with hsp110"
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Overexpression of Hsp110 confers substantial thermoresistance in vivo.
"the overexpression in vivo of hsp110 conferred substantial heat resistance to both Rat-1 and HeLa cells"
Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein.
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HSPH1 (Hsp110) was identified as a member of a significantly diverged subgroup of the Hsp70 protein family.
"Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein"
Deep research review of HSPH1 function
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HSPH1 operates as a NEF for cytosolic Hsp70s, catalyzing ADP-to-ATP exchange on the Hsp70 NBD to reset the chaperone for subsequent substrate cycles.
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HSPH1 participates in the Hsp70-DNAJ-HSPH1 disaggregase complex that can disaggregate heat-denatured luciferase and disease-associated amyloids.
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Constitutive cytoplasmic and nuclear localization is reported for Hsp105alpha (HSPH1) in mammalian tissues.