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Degradation signals (degrons) that are targeted by the N\u2010end rule pathway include a set called <jats:italic>N<\/jats:italic>\u2010degrons. The main determinant of an <jats:italic>N<\/jats:italic>\u2010degron is a destabilizing N\u2010terminal residue of a protein. In eukaryotes, the N\u2010end rule pathway is a part of the ubiquitin system and consists of two branches, the Ac\/N\u2010end rule and the Arg\/N\u2010end rule pathways. The Ac\/N\u2010end rule pathway targets proteins containing N<jats:sup>\u03b1<\/jats:sup>\u2010terminally acetylated (Nt\u2010acetylated) residues. The Arg\/N\u2010end rule pathway recognizes unacetylated N\u2010terminal residues and involves N\u2010terminal arginylation. Together, these branches target for degradation a majority of cellular proteins. For example, more than 80% of human proteins are cotranslationally Nt\u2010acetylated. Thus, most proteins harbor a specific degradation signal, termed <jats:sup>Ac<\/jats:sup><jats:italic>N<\/jats:italic>\u2010degron, from the moment of their birth. Specific N\u2010end rule pathways are also present in prokaryotes and in mitochondria. Enzymes that produce <jats:italic>N<\/jats:italic>\u2010degrons include methionine\u2010aminopeptidases, caspases, calpains, Nt\u2010acetylases, Nt\u2010amidases, arginyl\u2010transferases, and leucyl\u2010transferases. Regulated degradation of specific proteins by the N\u2010end rule pathway mediates a legion of physiological functions, including the sensing of heme, oxygen, and nitric oxide; selective elimination of misfolded proteins; the regulation of DNA repair, segregation, and condensation; the signaling by G proteins; the regulation of peptide import, fat metabolism, viral and bacterial infections, apoptosis, meiosis, spermatogenesis, neurogenesis, and cardiovascular development; and the functioning of adult organs, including the pancreas and the brain. 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