NONO
entrez
4841
canonical
uniprot
Q15233
canonical
ensembl
ENSG00000147140
resolver
ensp
ENSP00000276079
resolver
ensp
ENSP00000362947
resolver
ensp
ENSP00000410299
resolver
ensp
ENSP00000441364
resolver
genesymbol
NONO
resolver
genesymbol_syn
NRB54
resolver
hgnc
HGNC:7871
resolver
uniprot
A0A0S2Z4Z9
resolver
uniprot
B7Z4C2
resolver
uniprot
D3DVV4
resolver
uniprot
F5GYZ3
resolver
uniprot
O00201
resolver
uniprot
P30807
resolver
uniprot
Q12786
resolver
uniprot
Q9BQC5
resolver
uniprot_entry
A0A0S2Z4Z9_HUMAN
resolver
uniprot_entry
NONO_HUMAN
resolver
uniprot_sec
B7Z4C2
resolver
uniprot_sec
D3DVV4
resolver
uniprot_sec
F5GYZ3
resolver
uniprot_sec
O00201
resolver
uniprot_sec
P30807
resolver
uniprot_sec
Q12786
resolver
uniprot_sec
Q9BQC5
resolver
amino_acid_sequence
MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:9393982}.; DISEASE: Intellectual developmental disorder, X-linked, syndromic 34 (MRXS34) [MIM:300967]: A syndrome characterized by intellectual deficit, delayed psychomotor development, poor speech, and dysmorphic features. {ECO:0000269|PubMed:26571461}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes (PubMed:11525732, PubMed:12403470, PubMed:26571461). Binds the conventional octamer sequence in double-stranded DNA (PubMed:11525732, PubMed:12403470, PubMed:26571461). Also binds single-stranded DNA and RNA at a site independent of the duplex site (PubMed:11525732, PubMed:12403470, PubMed:26571461). Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, PubMed:12403470, PubMed:26571461). Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b (PubMed:12403470). Together with PSPC1, required for the formation of nuclear paraspeckles (PubMed:22416126). The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs (PubMed:11525732). The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1 (PubMed:10858305). 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 (PubMed:15590677). 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 (PubMed:15590677). NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity (PubMed:11897684). 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 (PubMed:28712728, PubMed:30270045). 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 (PubMed:30270045). In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway (PubMed:30270045). {ECO:0000250|UniProtKB:Q99K48, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:26571461, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:30270045}.
uniprot
proteins
mass_dalton
54232
uniprot
proteins
mutagenesis
MUTAGEN 267; /note="Y->A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271."; /evidence="ECO:0000269|PubMed:22416126"; MUTAGEN 271; /note="W->A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267."; /evidence="ECO:0000269|PubMed:22416126
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked.
uniprot
proteins
pubmed
10858305
uniprot
proteins
pubmed
11525732
uniprot
proteins
pubmed
11897684
uniprot
proteins
pubmed
12403470
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15590677
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16148043
uniprot
proteins
pubmed
16767080
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17693683
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18655028
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22002106
uniprot
proteins
pubmed
22416126
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
26571461
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28712728
uniprot
proteins
pubmed
30270045
uniprot
proteins
pubmed
8371983
uniprot
proteins
pubmed
8439294
uniprot
proteins
pubmed
9341872
uniprot
proteins
pubmed
9360842
uniprot
proteins
pubmed
9393982
uniprot
proteins
pubmed
9756848
uniprot
proteins
sequence_length
471
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:28712728}. Nucleus, nucleolus. Nucleus speckle {ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:28712728}. Chromosome {ECO:0000250|UniProtKB:Q99K48}. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. {ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:28712728}.
uniprot
proteins