LLPS-Ran-0025
Nono

▼ OVERVIEW

Status: Reviewed
Protein Name: Non-POU domain-containing octamer-binding protein
Gene Name: Nono
Ensembl Gene: ENSRNOG00000003689.6
Ensembl Protein: ENSRNOP00000068383.1
Organism: Rattus norvegicus
Taxa ID: 10116
LLPS Type: LLPS regulator


▼ PROPERTY


——— Disorder propensity (calculated by IUPred2A)

▼ Classification

Condensates:
CondensateDescriptionTissue/CellPMIDs
Neuronal granule
"...Intriguingly, we found that JNK interacted with neuronal transport granule proteins such as Sfpq and Nono upon NGF treatment."
PC12 cells25326457
Neuronal granule
"...RNP granule containing HERMES, NonO, and G3BP1 is not a stress granule but rather is a type of neuronal granule."
RGC–5 cells25651939
Others
"...The presence of paraspeckles in GH4C1 cells was anatomically evidenced by confocal microscopy on the basis of the overlap of their protein components using antibodies directed against SFPQ, NONO, PSPC1 and RBM14. SFPQ, NONO, PSPC1 and RBM14 staining appeared as punctate clusters located exclusively within the boundaries of the nucleus as delimitated by Hoechst labeling."
GH4C1 cells27441387
Nuclear speckle, Nucleolus, Paraspeckle, Perinucleolar compartment, P-body, Stress granule, Postsynaptic densityPredicted from orthologsN/A(View)

▼ 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. 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. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the functional organization of GABAergic synapses. Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript. 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.

▼ SEQUENCE

Protein Sequence (FASTA)
1     MQSNKTFNLE  KQNHTPRKHH  QHHHQQHHQQ  QQQQQQQQQQ  QPPPPIPANG  QQASSQNEGL  60
61    TIDLKNFRKP  GEKTFTQRSR  LFVGNLPPDI  TEEEMRKLFE  KYGKAGEVFI  HKDKGFGFIR  120
121   LETRTLAEIA  KVELDNMPLR  GKQLRVRFAC  HSASLTVRNL  PQYVSNELLE  EAFSVFGQVE  180
181   RAVVIVDDRG  RPSGKGIVEF  SGKPAARKAL  DRCSEGSFLL  TTFPRPVTVE  PMDQLDDEEG  240
241   LPEKLVIKNQ  QFHKEREQPP  RFAQPGSFEY  EYAMRWKALI  EMEKQQQDQV  DRNIKEAREK  300
301   LEMEMEAARH  EHQVMLMRQD  LMRRQEELRR  MEELHNQEVQ  KRKQLELRQE  EERRRREEEM  360
361   RRQQEEMMRR  QQEGFKGTFP  DAREQEIRMG  QMAMGGAMGI  NNRGAMPPAP  VPPGTPAPPG  420
421   PAAMMPDGTL  GLTPPTTERF  GQAATMEGIG  AIGGTPPAFN  RPAPGAEFAP  NKRRRY  476
Nucleotide CDS Sequence (FASTA)
1     ATGCAGAGCA  ATAAAACCTT  TAACTTGGAG  AAGCAGAATC  ATACTCCAAG  GAAGCACCAT  60
61    CAGCATCACC  ACCAGCAGCA  CCATCAGCAA  CAGCAGCAGC  AGCAGCAGCA  GCAGCAGCAG  120
121   CAGCCACCCC  CACCAATACC  TGCAAATGGA  CAGCAGGCCA  GCAGCCAGAA  TGAAGGCTTG  180
181   ACTATTGACC  TGAAGAATTT  TAGGAAACCA  GGAGAGAAGA  CCTTTACCCA  ACGTAGCCGT  240
241   CTCTTTGTGG  GCAATCTTCC  CCCTGACATC  ACTGAGGAGG  AAATGAGGAA  ACTTTTTGAG  300
301   AAATATGGGA  AAGCAGGCGA  AGTTTTCATT  CATAAGGATA  AAGGCTTTGG  CTTTATTCGC  360
361   TTGGAAACAC  GAACCCTAGC  GGAAATTGCC  AAAGTGGAGC  TGGACAACAT  GCCACTCCGT  420
421   GGAAAGCAGC  TGCGAGTGCG  CTTTGCTTGT  CATAGTGCAT  CCCTTACGGT  TCGCAACCTT  480
481   CCTCAGTACG  TGTCCAACGA  ACTGCTGGAA  GAAGCCTTTT  CTGTGTTTGG  CCAGGTGGAG  540
541   AGGGCTGTAG  TCATTGTGGA  TGACCGAGGA  AGGCCCTCGG  GGAAAGGCAT  TGTTGAGTTC  600
601   TCAGGGAAGC  CAGCTGCTCG  GAAAGCTCTG  GACAGATGCA  GTGAAGGCTC  CTTCTTGCTA  660
661   ACCACATTTC  CTCGGCCTGT  GACTGTGGAG  CCTATGGACC  AGTTAGATGA  TGAAGAGGGA  720
721   CTTCCGGAGA  AGTTGGTTAT  AAAAAACCAG  CAATTTCACA  AGGAGAGAGA  ACAGCCACCC  780
781   AGATTTGCAC  AGCCTGGGTC  CTTTGAGTAT  GAGTATGCCA  TGCGCTGGAA  GGCTCTCATT  840
841   GAGATGGAGA  AGCAACAGCA  GGATCAAGTG  GACCGAAACA  TCAAGGAGGC  TCGTGAGAAG  900
901   CTGGAGATGG  AGATGGAGGC  AGCACGCCAT  GAGCACCAGG  TTATGCTAAT  GAGGCAGGAT  960
961   TTGATGAGAC  GTCAAGAAGA  GCTTCGAAGA  ATGGAGGAGC  TGCATAACCA  AGAGGTTCAG  1020
1021  AAACGAAAGC  AGTTAGAACT  CAGGCAGGAA  GAGGAACGCA  GGCGCCGTGA  GGAAGAGATG  1080
1081  CGGCGACAGC  AAGAAGAAAT  GATGCGACGG  CAGCAGGAAG  GATTCAAGGG  AACCTTCCCT  1140
1141  GATGCGAGAG  AACAAGAGAT  ACGGATGGGC  CAAATGGCTA  TGGGAGGTGC  CATGGGCATA  1200
1201  AACAATAGAG  GCGCCATGCC  CCCTGCTCCT  GTGCCACCTG  GTACTCCAGC  TCCTCCAGGA  1260
1261  CCTGCTGCTA  TGATGCCAGA  TGGAACCCTT  GGATTGACTC  CACCAACAAC  TGAACGTTTT  1320
1321  GGCCAAGCTG  CTACAATGGA  AGGAATTGGA  GCAATTGGTG  GAACTCCTCC  TGCATTCAAC  1380
1381  CGTCCAGCTC  CTGGAGCTGA  ATTTGCTCCA  AATAAACGCC  GCCGATATTA  G  1431

▼ KEYWORD

ID
Family
Acetylation
Activator
Biological rhythms
Coiled coil
Complete proteome
DNA damage
DNA recombination
DNA repair
DNA-binding
Immunity
Innate immunity
Isopeptide bond
Methylation
mRNA processing
mRNA splicing
Nucleus
Phosphoprotein
Reference proteome
Repeat
Repressor
RNA-binding
Transcription
Transcription regulation
Ubl conjugation

▼ GENE ONTOLOGY

ID
Classification
Description
Cellular Component
Nuclear matrix
Cellular Component
Nuclear speck
Cellular Component
Nucleolus
Cellular Component
Nucleus
Cellular Component
Paraspeckles
Cellular Component
RNA polymerase II transcription factor complex
Molecular Function
Chromatin binding
Molecular Function
E-box binding
Molecular Function
Identical protein binding
Molecular Function
RNA binding
Molecular Function
RNA polymerase II distal enhancer sequence-specific DNA binding
Molecular Function
Transcription regulatory region sequence-specific DNA binding
Biological Process
Activation of innate immune response
Biological Process
Circadian rhythm
Biological Process
DNA recombination
Biological Process
DNA repair
Biological Process
Innate immune response
Biological Process
MRNA processing
Biological Process
Negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
Biological Process
Negative regulation of transcription, DNA-templated
Biological Process
Regulation of circadian rhythm
Biological Process
RNA splicing

▼ KEGG


▼ ORTHOLOGY

DrLLPS IDOrganismIdentityE-valueScore
LLPS-Mam-0629Macaca mulatta99.210.0 534
LLPS-Rhb-1136Rhinopithecus bieti99.182e-174 502
LLPS-Mum-2291Mus musculus98.950.0 668
LLPS-Mea-2707Mesocricetus auratus98.950.0 667
LLPS-Loa-1487Loxodonta africana97.90.0 662
LLPS-Chs-1435Chlorocebus sabaeus97.671e-86 273
LLPS-Cas-0455Carlito syrichta97.441e-1583.2
LLPS-Ict-1823Ictidomys tridecemlineatus97.060.0 656
LLPS-Caf-3557Canis familiaris97.060.0 656
LLPS-Eqc-2268Equus caballus97.060.0 656
LLPS-Urm-3013Ursus maritimus97.060.0 656
LLPS-Fec-0219Felis catus97.060.0 656
LLPS-Aim-0480Ailuropoda melanoleuca97.060.0 656
LLPS-Mup-1765Mustela putorius furo97.060.0 656
LLPS-Tut-2333Tursiops truncatus97.060.0 656
LLPS-Sus-0568Sus scrofa97.060.0 656
LLPS-Orc-1832Oryctolagus cuniculus97.020.0 617
LLPS-Meg-0633Meleagris gallopavo96.950.0 531
LLPS-Anp-0358Anas platyrhynchos96.950.0 529
LLPS-Gog-3033Gorilla gorilla96.890.0 598
LLPS-Hos-0189Homo sapiens96.850.0 655
LLPS-Pat-2706Pan troglodytes96.850.0 655
LLPS-Pap-1531Pan paniscus96.850.0 655
LLPS-Man-1250Macaca nemestrina96.850.0 655
LLPS-Mal-2399Mandrillus leucophaeus96.850.0 655
LLPS-Bot-0244Bos taurus96.850.0 654
LLPS-Caj-0860Callithrix jacchus96.850.0 655
LLPS-Maf-1489Macaca fascicularis96.850.0 655
LLPS-Aon-2578Aotus nancymaae96.850.0 655
LLPS-Myl-2107Myotis lucifugus96.640.0 652
LLPS-Ova-1576Ovis aries96.640.0 653
LLPS-Fud-2496Fukomys damarensis96.640.0 654
LLPS-Poa-3070Pongo abelii96.430.0 656
LLPS-Cap-1546Cavia porcellus96.060.0 650
LLPS-Ere-0554Erinaceus europaeus95.80.0 655
LLPS-Paa-2392Papio anubis95.40.0 588
LLPS-Dio-0005Dipodomys ordii95.380.0 654
LLPS-Nol-0550Nomascus leucogenys93.910.0 642
LLPS-Mod-0490Monodelphis domestica91.940.0 616
LLPS-Tag-0062Taeniopygia guttata91.150.0 575
LLPS-Pes-0998Pelodiscus sinensis91.150.0 573
LLPS-Fia-1755Ficedula albicollis89.910.0 566
LLPS-Gaga-2715Gallus gallus88.80.0 557
LLPS-Cea-0816Cercocebus atys87.820.0 540
LLPS-Anc-1590Anolis carolinensis87.240.0 561
LLPS-Sah-0203Sarcophilus harrisii84.580.0 555
LLPS-Lac-0907Latimeria chalumnae79.022e-164 478
LLPS-Scf-1620Scleropages formosus78.781e-155 457
LLPS-Orn-2914Oreochromis niloticus77.624e-153 451
LLPS-Asm-0881Astyanax mexicanus77.15e-151 445
LLPS-Tar-0181Takifugu rubripes76.51e-153 452
LLPS-Icp-1524Ictalurus punctatus76.499e-152 447
LLPS-Xim-4053Xiphophorus maculatus76.163e-149 441
LLPS-Dar-0715Danio rerio75.839e-151 444
LLPS-Leo-1881Lepisosteus oculatus75.581e-137 413
LLPS-Gaa-1863Gasterosteus aculeatus74.791e-149 441
LLPS-Xet-2207Xenopus tropicalis74.420.0 547
LLPS-Ora-1184Ornithorhynchus anatinus74.133e-85 273
LLPS-Orl-0775Oryzias latipes74.071e-145 431
LLPS-Scm-0235Scophthalmus maximus73.683e-76 245
LLPS-Otg-0242Otolemur garnettii72.284e-128 389
LLPS-Ten-0597Tetraodon nigroviridis71.388e-120 370
LLPS-Pof-0316Poecilia formosa70.547e-124 378
LLPS-Cis-0223Ciona savignyi59.21e-92 298
LLPS-Cii-0299Ciona intestinalis55.432e-94 302
LLPS-Drm-2087Drosophila melanogaster46.158e-66 231
LLPS-Cae-0445Caenorhabditis elegans45.121e-64 225
LLPS-Sem-0631Selaginella moellendorffii35.379e-1577.4
LLPS-Map-0047Magnaporthe poae33.768e-1374.3
LLPS-Gag-0271Gaeumannomyces graminis33.768e-1374.3
LLPS-Nec-1122Neurospora crassa33.333e-1272.4
LLPS-Nef-0476Neosartorya fischeri32.911e-1170.9
LLPS-Cogr-0174Colletotrichum graminicola32.692e-1170.1
LLPS-Cog-0774Colletotrichum gloeosporioides32.692e-1169.7
LLPS-Coo-0139Colletotrichum orbiculare32.692e-1170.1
LLPS-Scj-1180Schizosaccharomyces japonicus31.688e-1374.7
LLPS-Mao-1001Magnaporthe oryzae31.322e-1170.1
LLPS-Miv-0375Microbotryum violaceum30.34e-1375.9
LLPS-Arl-2034Arabidopsis lyrata29.764e-1066.2
LLPS-Bro-1641Brassica oleracea29.597e-0962.4
LLPS-Brr-2213Brassica rapa29.591e-0964.7
LLPS-Brn-0839Brassica napus29.597e-0962.4
LLPS-Art-0966Arabidopsis thaliana29.176e-1065.5
LLPS-Sol-1541Solanum lycopersicum27.921e-1274.3
LLPS-Hea-2651Helianthus annuus27.333e-0860.1
LLPS-Coc-1626Corchorus capsularis27.12e-0860.8
LLPS-Dac-0276Daucus carota27.17e-0756.2
LLPS-Mae-0690Manihot esculenta26.831e-0655.1
LLPS-Nia-0029Nicotiana attenuata26.834e-0653.5
LLPS-Sot-0545Solanum tuberosum26.839e-0755.5
LLPS-Met-1781Medicago truncatula26.096e-0652.8
LLPS-Thc-2063Theobroma cacao25.332e-1170.5
LLPS-Viv-1699Vitis vinifera25.322e-1170.9