RNA guanine quadruplexes (rG4s) are non-canonical nucleic acid structures essential for various cellular functions and disease pathways. Characterizing rG4-interacting proteins (rG4IPs) is crucial for deciphering biological roles of rG4s. Building upon the RNA-protein interaction detection (RaPID) method, we introduced G4-RaPID – a tailored strategy for robustly profiling rG4IPs in living cells. Using G4-RaPID with three distinct rG4 sequences in live cells, we identified 105 candidate rG4IPs with diverse biological functions. We also validated the direct binding of recombinant hnRNPA0, CHD4, and IGF2BP1 proteins with rG4 structures in vitro. Additionally, our CLIP-Seq data revealed an enrichment of hnRNPA0 at rG4 loci. Moreover, luciferase reporter assay results showed that hnRNPA0 interacts with the rG4 in the 5UTR of NRAS mRNA to negatively regulate its translation. Together, we developed an rG4-RaPID method for characterizing rG4-protein interactions in living cells, and documented the functions of hnRNPA0-rG4 interaction in modulating the translation of NRAS mRNA.