CPLM-012520

Genbank Nucleotide ID

Non-POU domain-containing octamer-binding protein

Protein Synonyms/Alias

NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; 55 kDa nuclear protein; DNA-binding p52/p100 complex, 52 kDa subunit; NMT55; p54(nrb); p54nrb

Homo sapiens (Human)

Position	Peptide	Type	References
5	***MQSNKTFNLEKQ	acetylation	[1]
5	***MQSNKTFNLEKQ	ubiquitination	[2, 3, 4, 5, 6]
11	NKTFNLEKQNHTPRK	acetylation	[1]
11	NKTFNLEKQNHTPRK	ubiquitination	[5, 6]
64	IDLKNFRKPGEKTFT	acetylation	[1]
64	IDLKNFRKPGEKTFT	ubiquitination	[7]
68	NFRKPGEKTFTQRSR	ubiquitination	[4, 6, 8]
96	EMRKLFEKYGKAGEV	acetylation	[1]
96	EMRKLFEKYGKAGEV	ubiquitination	[4, 6]
99	KLFEKYGKAGEVFIH	ubiquitination	[4, 5, 6, 7, 8, 9]
107	AGEVFIHKDKGFGFI	acetylation	[1]
107	AGEVFIHKDKGFGFI	ubiquitination	[4, 6, 7]
109	EVFIHKDKGFGFIRL	ubiquitination	[2, 3, 4, 5, 6, 7, 9]
126	RTLAEIAKVELDNMP	ubiquitination	[3, 4, 6, 7, 9, 10, 11]
190	DRGRPSGKGIVEFSG	ubiquitination	[4, 5, 6, 7, 8]
198	GIVEFSGKPAARKAL	acetylation	[1]
198	GIVEFSGKPAARKAL	ubiquitination	[3, 4, 5, 6, 7, 8, 9]
239	DEEGLPEKLVIKNQQ	ubiquitination	[9]
243	LPEKLVIKNQQFHKE	ubiquitination	[5, 6, 7, 8]
249	IKNQQFHKEREQPPR	ubiquitination	[4, 6, 7]
272	YEYAMRWKALIEMEK	ubiquitination	[4, 5, 6]
279	KALIEMEKQQQDQVD	ubiquitination	[3, 4, 6, 7, 8, 9]
290	DQVDRNIKEAREKLE	ubiquitination	[6]
295	NIKEAREKLEMEMEA	ubiquitination	[4, 6]
336	LHNQEVQKRKQLELR	ubiquitination	[6, 7, 8]
338	NQEVQKRKQLELRQE	ubiquitination	[6]
371	RRQQEGFKGTFPDAR	acetylation	[12]
371	RRQQEGFKGTFPDAR	ubiquitination	[3, 4, 5, 6, 7, 8, 9, 10, 12]
467	GAEFAPNKRRRY***	acetylation	[1, 12, 13]
467	GAEFAPNKRRRY***	ubiquitination	[5, 6, 10, 11, 12]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[11] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[12] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[13] 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]

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 (By similarity). 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. 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. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription (By similarity). Together with PSPC1, required for the formation of nuclear paraspeckles.

DOMAIN 74 141 RRM 1.
DOMAIN 148 229 RRM 2.
REGION 54 373 DBHS.
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 5 5 N6-acetyllysine.
MOD_RES 11 11 N6-acetyllysine.
MOD_RES 147 147 Phosphoserine.
MOD_RES 198 198 N6-acetyllysine.
MOD_RES 428 428 Phosphothreonine.
MOD_RES 440 440 Phosphothreonine.
MOD_RES 450 450 Phosphothreonine.

3D-structure; Acetylation; Activator; Alternative splicing; Chromosomal rearrangement; 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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0042382; C:paraspeckles; IDA: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; TAS:ProtInc.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0008380; P:RNA splicing; TAS:ProtInc.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR012975; NOPS.
IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.

PF08075; NOPS
PF00076; RRM_1