Annotation inferences using phylogenetic trees
Gene Ontology annotation through association of InterPro records with GO terms
The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress.
Biallelic Mutations in DNAJC12 Cause Hyperphenylalaninemia, Dystonia, and Intellectual Disability.
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DNAJC12 is an HSP70-family co-chaperone that interacts with phenylalanine hydroxylase (PAH), tyrosine hydroxylase and tryptophan hydroxylase; biallelic loss-of-function causes non-BH4-deficient hyperphenylalaninemia with dopamine/serotonin deficiency, dystonia and intellectual disability.
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PAH enzyme activity is reduced in the presence of DNAJC12 mutations; the J domain (HPD motif) stimulates HSP70 ATPase activity.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
UniProt entry Q9UKB3 (DJC12_HUMAN), DnaJ homolog subfamily C member 12 / JDP1
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Probable co-chaperone participating in proper folding of biopterin-dependent aromatic amino acid hydroxylases (PAH, TH, TPH1, TPH2); interacts with HSPA8/Hsc70; cytoplasmic; loss-of-function causes non-BH4-deficient hyperphenylalaninemia.