Function | N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn. |
Protein Name | Protein N-Terminal Asparagine AmidohydrolaseProtein Nh2-Terminal Asparagine AmidohydrolasePnaaProtein Nh2-Terminal Asparagine DeamidasePnadProtein N-Terminal Asn AmidaseProtein N-Terminal Asparagine AmidaseProtein Ntn-Amidase |
Cellular Localisation | Cytoplasm |
Alternative Antibody Names | Anti-Protein N-Terminal Asparagine Amidohydrolase antibodyAnti-Protein Nh2-Terminal Asparagine Amidohydrolase antibodyAnti-Pnaa antibodyAnti-Protein Nh2-Terminal Asparagine Deamidase antibodyAnti-Pnad antibodyAnti-Protein N-Terminal Asn Amidase antibodyAnti-Protein N-Terminal Asparagine Amidase antibodyAnti-Protein Ntn-Amidase antibodyAnti-NTAN1 antibody |
Information sourced from Uniprot.org