NONO report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006281Biological processDNA repair
GO_0006397Biological processmRNA processing
GO_1903377Biological processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
GO_0045087Biological processinnate immune response
GO_0007623Biological processcircadian rhythm
GO_0042752Biological processregulation of circadian rhythm
GO_0008380Biological processRNA splicing
GO_0006355Biological processregulation of DNA-templated transcription
GO_0002218Biological processactivation of innate immune response
GO_0006310Biological processDNA recombination
GO_0045892Biological processnegative regulation of DNA-templated transcription
GO_0016020Cellular componentmembrane
GO_0016607Cellular componentnuclear speck
GO_0005654Cellular componentnucleoplasm
GO_0001650Cellular componentfibrillar center
GO_0016363Cellular componentnuclear matrix
GO_0090575Cellular componentRNA polymerase II transcription regulator complex
GO_0042382Cellular componentparaspeckles
GO_0005694Cellular componentchromosome
GO_0005634Cellular componentnucleus
GO_0003677Molecular functionDNA binding
GO_0003682Molecular functionchromatin binding
GO_0042802Molecular functionidentical protein binding
GO_0003723Molecular functionRNA binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameNONO
Protein nameNon-POU domain-containing octamer-binding protein
Non-POU domain containing octamer binding
Non-POU domain containing octamer-binding isoform 1
Non-POU domain containing octamer-binding isoform 2
Non-POU domain-containing octamer-binding protein (NonO protein) (54 kDa nuclear RNA- and DNA-binding protein) (p54(nrb)) (p54nrb) (55 kDa nuclear protein) (NMT55) (DNA-binding p52/p100 complex, 52 kDa subunit)
SynonymsNRB54
DescriptionFUNCTION: 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 . 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 . Together with PSPC1, required for the formation of nuclear paraspeckles . 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 non-homologous 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 activity . NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer (By similarity). Important for the functional organization of GABAergic synapses (By similarity). Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript (By similarity). Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By similarity). 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 . Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation . In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway . .

AccessionsENST00000677014.1
ENST00000677245.1
ENST00000678335.1
ENST00000450092.6 [Q15233-1]
ENST00000678231.1 [Q15233-1]
ENST00000450092
ENST00000677879.1
ENST00000677446.1 [Q15233-1]
ENST00000676797.1 [Q15233-2]
ENST00000678830.1
ENST00000276079.13 [Q15233-1]
C9IZL7
ENST00000420903
C9JYS8
ENST00000454976
C9J4X2
A0A7I2V5Y7
Q15233
ENST00000679029.1
A0A7I2V4N2
C9JJ13
ENST00000678660.1
ENST00000413858.5
A0A0S2Z4Z9
A0A7I2V464
ENST00000677274.1 [Q15233-1]
A0A0S2Z4E7
A0A7I2V447
H7C367
ENST00000677612.1 [Q15233-1]
ENST00000535149.5 [Q15233-2]
ENST00000418921.1
ENST00000373856.8
A0A7P0MRW0
ENST00000420903.6 [Q15233-1]
ENST00000373841.5 [Q15233-1]
A0A7I2V535
A0A7I2YQK8
ENST00000454976.2 [Q15233-1]
A0A7I2V4K9
A0A7I2V4J2
ENST00000678437.1