Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB Subcellular Location vocabulary mapping
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex.
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Human MPP11 (DNAJC2) forms a stable heterodimeric ribosome-associated complex (RAC) with Hsp70L1 (HSPA14), the mammalian counterpart of yeast Ssz1p/zuotin, functioning in co-translational folding at the ribosome.
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HSPA14/RAC is cytosolic and associates with ribosomes, consistent with action at the ribosomal exit tunnel.
Defining the membrane proteome of NK cells.
The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Multimodal cell maps as a foundation for structural and functional genomics.
UniProt entry Q0VDF9 (HSP7E_HUMAN), Heat shock 70 kDa protein 14 / HSP70L1
The chaperone network connected to human ribosome-associated complex.
Intracellular HSP70L1 inhibits human dendritic cell maturation by promoting suppressive H3K27me3 and H2AK119Ub1 histone modifications.
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Intracellular HSP70L1 can enter the nucleus in differentiating human monocyte-derived dendritic cells and is implicated in Ash1l/H3K27me3/H2AK119Ub1 chromatin control.
"Mechanistically, intracellular HSP70L1 inhibits the recruitment of Ash1l to and maintains the repressive H3K27me3 and H2AK119Ub1 modifications on the promoter regions of costimulatory, MHC and STAT3 genes."
OpenScientist SSZ1 ATPase adjudication (comparative scope)
OpenScientist focused review of HSPA14 ATPase, refolding and secondary compartments, 2026-09-21
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The report argued that HSPA14 is a cytosolic ribosome-associated atypical Hsp70 whose established activity is ATP binding rather than direct ATP hydrolysis.
"HSPA14's experimentally supported identity is a **cytosolic, ribosome-associated, ATP-*binding* (not hydrolysis-driven) atypical Hsp70**"
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The report distinguished inherited refolding from HSPA14's established cotranslational nascent-chain folding role.
"GO:0042026 (protein refolding) is **IBA only** (ECO:0000318, node PTN000452648)"
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The report found no endogenous plasma-membrane evidence behind the stale IBA.
"The plasma-membrane claim is the weakest: it is absent from the current GO_Central path for Q0VDF9 and is supported only by a generic membrane-fraction proteome and by recombinant extracellular immunology"
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The report identified HSPA14 sequence divergence from canonical HSP70 catalytic and substrate-handling motifs.
"the invariant Hsp70 catalytic/phosphate-binding signature (IDLGTTxS) is degenerate in HSPA14 (GVHLGCTSA), and the protein lacks the C-terminal EEVD and GGMP substrate-handling elements"