Human Gene NONO (uc004dzp.3) Description and Page Index
Description: Homo sapiens non-POU domain containing, octamer-binding (NONO), transcript variant 3, mRNA. RefSeq Summary (NM_001145409): This gene encodes an RNA-binding protein which plays various roles in the nucleus, including transcriptional regulation and RNA splicing. A rearrangement between this gene and the transcription factor E3 gene has been observed in papillary renal cell carcinoma. Alternatively spliced transcript variants have been described. Pseudogenes exist on Chromosomes 2 and 16. [provided by RefSeq, Feb 2009]. Transcript (Including UTRs) Position: hg19 chrX:70,503,042-70,521,018 Size: 17,977 Total Exon Count: 11 Strand: + Coding Region Position: hg19 chrX:70,510,488-70,519,926 Size: 9,439 Coding Exon Count: 10
ID:NONO_HUMAN DESCRIPTION: RecName: Full=Non-POU domain-containing octamer-binding protein; Short=NonO protein; AltName: Full=54 kDa nuclear RNA- and DNA-binding protein; AltName: Full=55 kDa nuclear protein; AltName: Full=DNA-binding p52/p100 complex, 52 kDa subunit; AltName: Full=NMT55; AltName: Full=p54(nrb); Short=p54nrb; FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double stranded DNA. 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. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. 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. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity). Together with PSPC1, required for the formation of nuclear paraspeckles. SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1 (By similarity). Interacts with RNF43. Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins. INTERACTION: Self; NbExp=3; IntAct=EBI-350527, EBI-350527; Q8WXF1:PSPC1; NbExp=6; IntAct=EBI-350527, EBI-1392258; SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus speckle. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines. PTM: The N-terminus is blocked. DISEASE: Note=A chromosomal aberration involving NONO may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;X)(p11.2;q13.1) with TFE3. SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/NONOID168.html";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q15233
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.