DNA- and RNA binding protein, involved in several nuclearprocesses. Bindsthe conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably bybinding to a purine-rich sequence located on the 3' side of U5 snRNAstem 1b. Together with PSPC1, required for theformation of nuclear paraspeckles. The SFPQ-NONOheteromer associated with MATR3 may play a role in nuclear retention ofdefective RNAs. The SFPQ-NONO heteromer may beinvolved in DNA unwinding by modulating the function of topoisomeraseI/TOP1. The SFPQ-NONO heteromer may be involved inDNA non-homologous end joining (NHEJ) required for double-strand breakrepair and V (D) J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA endjoining, binds directly to the DNA substrates and cooperates with theKu70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligationcomplex. NONO is involved in transcriptionalregulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter andregulates basal and cAMP-dependent transcriptional activity. NONO binds to an enhancer element in long terminalrepeats of endogenous intracisternal A particles (IAPs) and activatestranscription. Regulates the circadian clock byrepressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the functionalorganization of GABAergic synapses. Plays a specificand important role in the regulation of synaptic RNAs and GPHN/gephyrinscaffold structure, through the regulation of GABRA2 transcript. Plays a key role during neuronal differentiation byrecruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels. Plays a role in theregulation of DNA virus-mediated innate immune response by assemblinginto the HDP-RNP complex, a complex that serves as a platform for IRF3phosphorylation and subsequent innate immune response activationthrough the cGAS-STING pathway. Promotes activation of the cGAS-STING pathway in response to HIV-2infection: acts by interacting with HIV-2 Capsid protein p24, therebypromoting detection of viral DNA by CGAS, leading to CGAS-mediatedinmmune activation. In contrast, the weak interactionwith HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway. [1-3]

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