NONO_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NONO_MOUSE
• UniProt AC: Q99K48
• Protein Name: Non-POU domain-containing octamer-binding protein
• Gene Name: Nono
• Organism: Mus musculus (Mouse).
• Sequence Length: 473
• 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. [PubMed: 26571461Plays 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: MQSNKAFNLEKQNHTPRKHHQHHHQQHHQQQQQQQQQQPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPPGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRPAPGAEFAPNKRRRY

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	-------MQSNKAFN -------CCCCCCCC	9.95	23806337
3	Phosphorylation	-----MQSNKAFNLE -----CCCCCCCCHH	38.71	29514104
5	Acetylation	---MQSNKAFNLEKQ ---CCCCCCCCHHHC	60.65	23806337
11	Acetylation	NKAFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	23806337
11	Malonylation	NKAFNLEKQNHTPRK CCCCCHHHCCCCCCH	60.61	26320211
15	Phosphorylation	NLEKQNHTPRKHHQH CHHHCCCCCCHHHHH	32.13	25266776
101	Ubiquitination	KLFEKYGKAGEVFIH HHHHHHCCCCCEEEE	50.56	-
111	Ubiquitination	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	-
111	Acetylation	EVFIHKDKGFGFIRL CEEEECCCCCCEEEE	62.03	23236377
128	Acetylation	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	22826441
128	Ubiquitination	RTLAEIAKVELDNMP CCHHHHHCEEHHCCC	41.73	-
147	S-nitrosylation	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	20925432
147	Glutathionylation	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	24333276
147	S-nitrosocysteine	QLRVRFACHSASLTV EEEEEEEECCCCCEE	2.10	-
149	Phosphorylation	RVRFACHSASLTVRN EEEEEECCCCCEECC	21.31	25266776
151	Phosphorylation	RFACHSASLTVRNLP EEEECCCCCEECCCC	27.82	25266776
153	Phosphorylation	ACHSASLTVRNLPQY EECCCCCEECCCCHH	18.22	28066266
160	Phosphorylation	TVRNLPQYVSNELLE EECCCCHHHCHHHHH	12.14	26643407
162	Phosphorylation	RNLPQYVSNELLEEA CCCCHHHCHHHHHHH	21.47	26643407
192	Acetylation	DRGRPSGKGIVEFSG CCCCCCCCCEEEECC	50.21	22826441
200	Acetylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	23806337
200	Ubiquitination	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	-
200	Malonylation	GIVEFSGKPAARKAL CEEEECCCHHHHHHH	30.22	26320211
245	Ubiquitination	LPEKLVIKNQQFHKE CCHHHEEECHHHHCC	41.02	-
258	Methylation	KEREQPPRFAQPGSF CCCCCCCCCCCCCCC	46.33	18601079
264	Phosphorylation	PRFAQPGSFEYEYAM CCCCCCCCCHHHHHH	22.91	26643407
267	Phosphorylation	AQPGSFEYEYAMRWK CCCCCCHHHHHHHHH	16.54	26643407
281	Ubiquitination	KALIEMEKQQQDQVD HHHHHHHHHHHHHHH	52.69	-
297	Acetylation	NIKEAREKLEMEMEA HHHHHHHHHHHHHHH	44.16	23806337
373	Acetylation	RRQQEGFKGTFPDAR HHHHHCCCCCCCCHH	68.82	23806337
412	Phosphorylation	PAPVPPGTPAPPGPA CCCCCCCCCCCCCCC	23.27	25159016
420	Phosphorylation	PAPPGPATMMPDGTL CCCCCCCCCCCCCCC	19.69	25159016
426	Phosphorylation	ATMMPDGTLGLTPPT CCCCCCCCCCCCCCC	25.65	25159016
430	Phosphorylation	PDGTLGLTPPTTERF CCCCCCCCCCCCHHH	25.98	22942356
433	Phosphorylation	TLGLTPPTTERFGQA CCCCCCCCCHHHCCC	42.36	26643407
434	Phosphorylation	LGLTPPTTERFGQAA CCCCCCCCHHHCCCC	30.82	25159016
442	Phosphorylation	ERFGQAATMEGIGAI HHHCCCCCCCCCCCC	20.83	25619855
452	Phosphorylation	GIGAIGGTPPAFNRP CCCCCCCCCCCCCCC	22.38	25521595
458	Methylation	GTPPAFNRPAPGAEF CCCCCCCCCCCCCCC	23.46	-
469	Acetylation	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	23236377
469	Ubiquitination	GAEFAPNKRRRY--- CCCCCCCCCCCC---	46.34	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
15	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

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

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPNE1_HUMAN	CPNE1	physical	12522145
CPNE4_HUMAN	CPNE4	physical	12522145
SFPQ_HUMAN	SFPQ	physical	11259580

Drug and Disease Associations

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