Based on limited published evidence, ZNG1A encodes a zinc chaperone that activates metalloproteins by transferring zinc cofactors to their active sites. Structurally, ZNG1A's N-terminal psi-PxLVp motif docks with the zinc finger domain of methionine aminopeptidase METAP1, facilitating zinc transfer from ZNG1A's CXCC motif via GTP hydrolysis, followed by GTP/GDP exchange for METAP1 release. METAP1 activation enables removal of initiator methionines from nascent polypeptides. ZNG1A localizes to nucleus and cytoplasm and exhibits zinc ion binding activity. Recent whole-genome sequencing identified ZNG1A among 24 critical genes for 9p deletion syndrome, with potential involvement in mitochondrial function 1.