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Side-chain 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 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.
Gene Name: | N-terminal asparagine amidase |
Synonyms: | NTAN1, N-terminal asparagine amidase, PNAA, PNAD, Protein NTN-amidase, Protein N-terminal Asn amidase |
Target Sequences: | NP_775745.1 Q96AB6 |
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