Anti-SMG1

SMG1 is a PIKK (phosphoinositide 3-kinase related kinases) protein kinase that plays a key role in RNA surveillance via nonsense-mediated mRNA decay (NMD). SMG1 phosphorylates Upf1, a factor that possesses RNA helicase activity and is also central to NMD. SMG1 and UPF-1 have been shown to exist in a complex with the translation termination release factors eRF3, and eRF1. This complex has been termed SURF and associates with the exon junction complex (EJC) to function in the recognition of premature termination codons in aberrant RNAs to trigger NMD. Protein function: Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense- mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. [The UniProt Consortium]