Zinc-regulated GTPase metalloprotein activator

Definition

This family of proteins functions as zinc chaperones, facilitating the transfer of zinc ions to target metalloproteins, which results in their activation. The proteins possess a GTPase domain with a CXCC motif that binds zinc and, upon GTP hydrolysis, transfers the zinc to specific binding sites on metalloproteins. This process is essential for the proper function of metalloenzymes such as methionine aminopeptidase METAP1, which cleaves initiator methionine from nascent polypeptides. The activity of these GTPases is regulated by metal binding; zinc inhibits while other metals like Co(II) and Ni(II) decrease the GTPase activity. These proteins are part of the SIMIBI class G3E GTPase family within the ZNG1 subfamily.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• ZNG1A
• ZNG1B
• ZNG1C
• ZNG1E
• ZNG1F