Ontology highlight
ABSTRACT:
SUBMITTER: Arnesen T
PROVIDER: S-EPMC1475586 | biostudies-literature | 2006 Apr
REPOSITORIES: biostudies-literature
Arnesen Thomas T Betts Matthew J MJ Pendino Frédéric F Liberles David A DA Anderson Dave D Caro Jaime J Kong Xianguo X Varhaug Jan E JE Lillehaug Johan R JR
BMC biochemistry 20060425
<h4>Background</h4>Protein acetylation is increasingly recognized as an important mechanism regulating a variety of cellular functions. Several human protein acetyltransferases have been characterized, most of them catalyzing epsilon-acetylation of histones and transcription factors. We recently described the human protein acetyltransferase hARD1 (human Arrest Defective 1). hARD1 interacts with NATH (N-Acetyl Transferase Human) forming a complex expressing protein N-terminal alpha-acetylation ac ...[more]