Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation of UniProtKB entries based on the manual curation of subcellular locations
Stch encodes the 'ATPase core' of a microsomal stress 70 protein.
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STCH/HSPA13 is a microsome-associated HSP70-family member with a hydrophobic leader sequence, a ~50-residue insertion in the ATP-binding domain and a truncated C-terminal peptide-binding region; it has peptide-independent ATPase activity, is constitutively expressed, and is induced by calcium ionophore but not by heat shock.
A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.
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STCH binding to Chap1/Chap2 does not require their ubiquitin-like domains.
"While the N-terminal UbL domains were not essential for Stch binding"
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Chap1 instead requires a Sti1-like repeat for this interaction.
"Chap1/Dsk2 contains a Sti1-like repeat sequence that is required for binding to
Stch"
Towards a proteome-scale map of the human protein-protein interaction network.
A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Toward an understanding of the protein interaction network of the human liver.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Chr21 protein-protein interactions: enrichment in proteins involved in intellectual disability, autism, and late-onset Alzheimer's disease.
GOA annotation export for HSPA13
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GOA currently carries GO:0044183 protein folding chaperone for HSPA13 as an IBA propagated through GO_REF:0000033 with PANTHER:PTN000452648 among the source entities.
"UniProtKB P48723 HSPA13 enables GO:0044183 protein folding chaperone molecular_function ECO:0000318 IBA GO_REF:0000033 FB:FBgn0266599|MGI:MGI:95835|MGI:MGI:96244|MGI:MGI:99517|PANTHER:PTN000452648|UniProtKB:P0A6Y8|UniProtKB:P0DMV8|UniProtKB:P0DMV9 9606 Homo sapiens GO_Central Heat shock 70 kDa protein 13 20250903"
OpenScientist hypothesis investigation - HSPA13 protein folding chaperone
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The provider documents canonical substrate-binding-domain loss, but explicitly lacks a direct target chaperone assay.
"**No direct in vitro chaperone assay for HSPA13**"
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The report could not access the full PAINT tree topology.
"could not access full tree topology"
UniProt entry P48723 (HSP13_HUMAN), Heat shock 70 kDa protein 13 (STCH)
Heat shock protein Hspa13 regulates endoplasmic reticulum and cytosolic proteostasis through modulation of protein translocation.
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Human-cell HSPA13 binds translocon components and ER chaperones and alters secretory-protein import/maturation.
"Hspa13 specifically binds a majority of translocon subunits"
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Proximity labeling supports principal ER localization.
"ER resident proteins BiP and Hspa13 are preferentially labeled by ERHRP"
Differential Effects of STCH and Stress-Inducible Hsp70 on the Stability and Maturation of NKCC2.