CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019880
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Non-POU domain-containing octamer-binding protein 
Protein Synonyms/Alias
 NonO protein 
Gene Name
 Nono 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
101KLFEKYGKAGEVFIHubiquitination[1]
111EVFIHKDKGFGFIRLacetylation[2]
111EVFIHKDKGFGFIRLubiquitination[1]
128RTLAEIAKVELDNMPacetylation[3]
128RTLAEIAKVELDNMPubiquitination[1]
192DRGRPSGKGIVEFSGacetylation[3]
200GIVEFSGKPAARKALacetylation[2, 3, 4]
200GIVEFSGKPAARKALubiquitination[1]
245LPEKLVIKNQQFHKEubiquitination[1]
281KALIEMEKQQQDQVDubiquitination[1]
297NIKEAREKLEMEMEAacetylation[4]
373RRQQEGFKGTFPDARacetylation[3, 4]
469GAEFAPNKRRRY***acetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional 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 nonhomologous 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 avtivity (By similarity). NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. 
Sequence Annotation
 DOMAIN 76 143 RRM 1.
 DOMAIN 150 231 RRM 2.
 REGION 56 375 DBHS (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 5 5 N6-acetyllysine (By similarity).
 MOD_RES 11 11 N6-acetyllysine (By similarity).
 MOD_RES 149 149 Phosphoserine (By similarity).
 MOD_RES 200 200 N6-acetyllysine (By similarity).
 MOD_RES 430 430 Phosphothreonine (By similarity).
 MOD_RES 442 442 Phosphothreonine (By similarity).
 MOD_RES 452 452 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil; Complete proteome; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 473 AA 
Protein Sequence
MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA SSQNEGLTID 60
LKNFRKPGEK TFTQRSRLFV GNLPPDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET 120
RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY VSNELLEEAF SVFGQVERAV 180
VIVDDRGRPS GKGIVEFSGK PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE 240
KLVIKNQQFH KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM 300
EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER RRREEEMRRQ 360
QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR GAMPPAPVPP GTPAPPGPAT 420
MMPDGTLGLT PPTTERFGQA ATMEGIGAIG GTPPAFNRPA PGAEFAPNKR RRY 473 
Gene Ontology
 GO:0016363; C:nuclear matrix; IEA:Compara.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0042382; C:paraspeckles; ISO:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012975; NOPS.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF08075; NOPS
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS