Anti-NAA38 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

NAA38 also referred to as N-alpha-acetyltransferase 38 or NAT10 is a component of the N-alpha-acetyltransferase complex. It plays a role in protein acetylation a significant post-translational modification. NAA38 a relatively small protein with an approximate mass of 14 kDa participates in protein modifications by catalyzing the transfer of an acetyl group to the N-terminal of proteins. This protein finds expression in a variety of tissues especially abundant in the liver and brain suggesting roles in key physiological processes in these regions.

Biological function summary

NAA38 functions within the NatC complex where it catalyzes N-terminal acetylation of a subset of proteins. This modification can regulate protein stability localization and interactions. NAA38 activity influences numerous cellular processes such as cell cycle regulation and apoptosis highlighting its role in maintaining cellular homeostasis. As part of the NatC complex NAA38 works synergistically with other complex components like NAA35 and NAA15 to achieve its biological functions.

Pathways

The acetylation process involving NAA38 integrates into the broader protein modification pathway influencing key cellular mechanisms. It directly interacts through acetylation with proteins in the cell cycle and apoptosis pathways controlling cellular proliferation and programmed cell death. This complex modulation assists in regulating cellular responses to external signals and the protein interacts with pathway components such as Cyclin-Dependent Kinase (CDK) and Bcl-xL playing a regulatory role in these pathways.

Associated diseases and disorders

NAA38 connections to aberrant N-terminal acetylation have implications for cancer and neurodegenerative diseases. Dysregulation in its activity may contribute to unchecked cellular proliferation leading to oncogenesis where altered protein acetylation states can disrupt cellular control. Additionally its role in the brain links it to neurodegenerative diseases; an imbalance in acetylation affects neuronal viability and synaptic functions. NAA38's interactions with proteins like p53 in cancer and α-synuclein in neurodegeneration highlight its involvement in these pathological conditions.