NONO_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NONO_RAT
• UniProt AC: Q5FVM4
• Protein Name: Non-POU domain-containing octamer-binding protein
• Gene Name: Nono
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 476
• Subcellular Localization: Nucleus. Nucleus, nucleolus. Nucleus speckle. Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles..
• Protein Description: 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..
• Protein Sequence: MQSNKTFNLEKQNHTPRKHHQHHHQQHHQQQQQQQQQQQQQPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPPGTPAPPGPAAMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRPAPGAEFAPNKRRRY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQSNKTFN -------CCCCCCCC	9.95	-
3	Phosphorylation	-----MQSNKTFNLE -----CCCCCCCCHH	38.71	23984901
5	Acetylation	---MQSNKTFNLEKQ ---CCCCCCCCHHHC	60.79	22902405
6	Phosphorylation	--MQSNKTFNLEKQN --CCCCCCCCHHHCC	23.23	23984901
11	Acetylation	NKTFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	-
73	Ubiquitination	NFRKPGEKTFTQRSR CCCCCCCCCEECCHH	55.65	-
152	Phosphorylation	RVRFACHSASLTVRN EEEEEECCCCCEECC	21.31	23984901
154	Phosphorylation	RFACHSASLTVRNLP EEEECCCCCEECCCC	27.82	23984901
156	Phosphorylation	ACHSASLTVRNLPQY EECCCCCEECCCCHH	18.22	23984901
203	Acetylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	25786129
214	Phosphorylation	RKALDRCSEGSFLLT HHHHHHHCCCCEEEE	45.98	27097102
217	Phosphorylation	LDRCSEGSFLLTTFP HHHHCCCCEEEEECC	14.52	27097102
221	Phosphorylation	SEGSFLLTTFPRPVT CCCCEEEEECCCCEE	28.65	27097102
267	Phosphorylation	PRFAQPGSFEYEYAM CCCCCCCCCHHHHHH	22.91	27097102
300	Acetylation	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	-
376	Acetylation	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	-
415	Phosphorylation	PAPVPPGTPAPPGPA CCCCCCCCCCCCCCC	23.27	28432305
429	Phosphorylation	AAMMPDGTLGLTPPT CCCCCCCCCCCCCCC	25.65	28432305
433	Phosphorylation	PDGTLGLTPPTTERF CCCCCCCCCCCCHHH	25.98	28432305
436	Phosphorylation	TLGLTPPTTERFGQA CCCCCCCCCHHHCCC	42.36	28432305
437	Phosphorylation	LGLTPPTTERFGQAA CCCCCCCCHHHCCCC	30.82	28432305
445	Phosphorylation	ERFGQAATMEGIGAI HHHCCCCCCCCCCCC	20.83	25575281
455	Phosphorylation	GIGAIGGTPPAFNRP CCCCCCCCCCCCCCC	22.38	27097102
461	Methylation	GTPPAFNRPAPGAEF CCCCCCCCCCCCCCC	23.46	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NONO_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NONO_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NONO_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of NONO_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.