Literature summary for 2.3.1.258 extracted from

Van Damme, P.; Hole, K.; Gevaert, K.; Arnesen, T.
N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases (2015), Proteomics, 15, 2436-2446.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Saccharomyces cerevisiae lacking endogenous Naa50	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	ectopically expressed hNaa50 results, predominantly, in the N-terminal-acetylation of N-terminal Met (iMet) starting N-termini, including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr N-termini. Presence of a kinetic competition between Naa50 and Met-aminopeptidases	Homo sapiens	?	-	?
additional information	potential substrates that are less acetylated in strains lacking isoform Naa50 are: vacuolar morphogenesis protein 7, nuclear cap-binding protein subunit 2, 60S ribosomal protein L16-A, aromatic amino acid aminotransferase 1, tRNA guanosine-2'-O-methyltransferase TRM3, low specificity L-threonine aldolase	Saccharomyces cerevisiae	?	-	?

Synonyms

Synonyms	Comment	Organism
Naa50	-	Homo sapiens
Naa50	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)