Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization.
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The human NatC complex contains the catalytic subunit hMak3 (NAA30) and auxiliary subunits hMak10 (NAA35) and hMak31 (NAA38); it associates with ribosomes and hMak3 acetylates Met-Leu protein N-termini in vitro.
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Knockdown of NatC subunits results in p53-dependent cell death and aberrant ARL8B localization, indicating ARL8B is a NatC substrate in vivo.
An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.
Multimodal cell maps as a foundation for structural and functional genomics.
Falcon deep research report for NAA30
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NAA30 is the catalytic GNAT-fold subunit of the heterotrimeric NatC complex (NAA30 catalytic, NAA35 large auxiliary/ribosome-anchoring, NAA38 small auxiliary) that co-translationally acetylates the alpha-amino group of N-terminal methionines retained in front of hydrophobic/amphipathic residues (Met-Leu, Met-Ile, Met-Phe, Met-Trp).
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NatC-mediated N-terminal acetylation shields hydrophobic Met-starting N-termini from recognition as N-degrons by the Arg/N-degron pathway E3 ligases (UBR1, UBR2, UBR4-KCMF1), protecting substrates from proteasomal degradation; validated human NatC substrates include the trafficking GTPase ARL8B.