Search Results

Overview

Uniprot IDQ15233
Protein NameNon-POU domain-containing octamer-binding protein
Gene NameNONO
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
107 AGEVFIHKDKGFGFI
109 EVFIHKDKGFGFIRL
11 NKTFNLEKQNHTPRK
198 GIVEFSGKPAARKAL
243 LPEKLVIKNQQFHKE
249 IKNQQFHKEREQPPR
272 YEYAMRWKALIEMEK
295 NIKEAREKLEMEMEA
336 LHNQEVQKRKQLELR
338 NQEVQKRKQLELRQE
371 RRQQEGFKGTFPDAR
467 GAEFAPNKRRRY***
5 ***MQSNKTFNLEKQ
68 NFRKPGEKTFTQRSR
96 EMRKLFEKYGKAGEV

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)

Protein Sequence

10 MQSNKTFNLE 20 KQNHTPRKHH 30 QHHHQQQHHQ 40 QQQQQPPPPP 50 IPANGQQASS 60 QNEGLTIDLK 70 NFRKPGEKTF 80 TQRSRLFVGN 90 LPPDITEEEM 100 RKLFEKYGKA 110 GEVFIHKDKG 120 FGFIRLETRT 130 LAEIAKVELD 140 NMPLRGKQLR 150 VRFACHSASL 160 TVRNLPQYVS 170 NELLEEAFSV 180 FGQVERAVVI 190 VDDRGRPSGK 200 GIVEFSGKPA 210 ARKALDRCSE 220 GSFLLTTFPR 230 PVTVEPMDQL 240 DDEEGLPEKL 250 VIKNQQFHKE 260 REQPPRFAQP 270 GSFEYEYAMR 280 WKALIEMEKQ 290 QQDQVDRNIK 300 EAREKLEMEM 310 EAARHEHQVM 320 LMRQDLMRRQ 330 EELRRMEELH 340 NQEVQKRKQL 350 ELRQEEERRR 360 REEEMRRQQE 370 EMMRRQQEGF 380 KGTFPDAREQ 390 EIRMGQMAMG 400 GAMGINNRGA 410 MPPAPVPAGT 420 PAPPGPATMM 430 PDGTLGLTPP 440 TTERFGQAAT 450 MEGIGAIGGT 460 PPAFNRAAPG 470 AEFAPNKRRR Y

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0016020 membrane
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0042382 paraspeckles
Cellular Component GO:0090575 RNA polymerase II transcription regulator complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0106222 lncRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:1904385 cellular response to angiotensin
Biological Process GO:0071456 cellular response to hypoxia
Biological Process GO:0007623 circadian rhythm
Biological Process GO:0006310 DNA recombination
Biological Process GO:0006281 DNA repair
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045087 innate immune response
Biological Process GO:0006397 mRNA processing
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:1903377 negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
Biological Process GO:0042752 regulation of circadian rhythm
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0008380 RNA splicing

Reference

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[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[10] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[11] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[12] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[13] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.