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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Non-POU domain-containing octamer-binding protein

UniprotKB/SwissProt ID: Q99K48 (Q99K48)

Gene Name: Nono

Organism: Mus musculus (Mouse)

Function: DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA (PubMed:8355702). Also binds single-stranded DNA and RNA at a site independent of the duplex site (By similarity). Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (By similarity). Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (By similarity). Together with PSPC1, required for the formation of nuclear paraspeckles (By similarity). The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (By similarity). The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (By similarity). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends (By similarity). In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex (By similarity). NONO is involved in transcriptional regulation (By similarity). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (By similarity). NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (PubMed:9001221). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (PubMed:22966205). Important for the functional organization of GABAergic synapses (PubMed:26571461). Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (PubMed:26571461). Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (PubMed:32286661). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus, nucleolus. Nucleus speckle. Chromosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR012975 NOPS
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034552 p54nrb_RRM1
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

The S-nitrosylation sites of Q99K48

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 147 RGKQLRVRFA C HSASLTVRNL  CCCCCCCCHH H CCCCCCHHHH  2.1% 20925432
21278135