Annotation inferences using phylogenetic trees
Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation.
UniProt entry Q9NX36 (DJC28_HUMAN), DnaJ homolog subfamily C member 28
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J-domain (HSP40) protein with a predicted coiled-coil; function annotated only as a possible role in protein folding or as a chaperone; expressed in brain, testis, uterus, spleen and liver; phosphorylated at Thr-347.
OpenScientist hypothesis run: DNAJC28 J-domain HPD-motif check
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Structurally supports a functional J-domain co-chaperone - DNAJC28 has an intact HPD tripeptide (H79-P80-D81) in a canonically folded J-domain, sub-2 A RMSD to DNAJA1's Hsp70-interaction surface, and the HPD is conserved in 18/20 vertebrate orthologs; it is not a degenerate pseudo-co-chaperone. Caveat - no direct Hsp70 ATPase-stimulation assay has been published.
"DNAJC28 is a structurally competent Hsp70 co-chaperone, not a degenerate J-domain protein."
Manual DNAJC28 curation notes
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Records the core unresolved experimental gap for DNAJC28: no direct assay has established co-chaperone activity, substrate, or compartment of action.
"No experimental characterization of co-chaperone (HSP70 ATPase-stimulating) activity, substrate, or compartment of action."
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Records that the mitochondrial localization hypothesis is sequence-based and has not been experimentally confirmed.
"this is a prediction, not experimentally confirmed in the UniProt record."
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Records that the phylogenetically transferred temperature-homeostasis process annotation has no reliable DNAJC28-specific evidence.
"No reliable evidence for "temperature homeostasis" as a specific function."