Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Combined Automated Annotation using Multiple IEA Methods

Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4.

DPH4 is a J-protein co-chaperone whose J-domain catalytically stimulates HSP70 ATPase activity; its CSL domain binds zinc or iron, and the iron-bound form is redox-active with electron-carrier activity, supporting moonlighting roles including diphthamide biosynthesis.

PMID:22509046

Immunotoxin resistance via reversible methylation of the DPH4 promoter is a unique survival strategy.

DPH4 is required for diphthamide biosynthesis on EEF2; silencing DPH4 (via promoter methylation) confers resistance to immunotoxins/diphtheria-toxin-like agents that ADP-ribosylate the diphthamide residue.

file:human/DNAJC24/DNAJC24-uniprot.txt

UniProt entry Q6P3W2 (DJC24_HUMAN), DnaJ homolog subfamily C member 24 (DPH4)

Stimulates the ATPase activity of HSP70-type chaperones (enhanced by iron binding); CSL domain binds zinc or iron; iron-bound form is redox-active; participates in diphthamide biosynthesis on EEF2; cytoplasmic.