Fig 2: Knockdown of KIN17 by lentiviral recombinant vector-mediated siRNA transfection inhibited the invasiveness of A549 cells. (A) Morphological features and fluorescence-indicated transfection of A549Mock, A549NC and A549KIN17 KD cells (×100). (B) mRNA and (C) protein levels of KIN17 in A549NC and A549KIN17 KD cells were decreased following KIN17 knockdown, identified by reverse transcription-quantitative polymerase chain reaction analysis and western blotting, respectively. Scratch assay (D) representative images (×100) and (E) quantification. Matrigel assay (F) representative images (×100) and (G) quantification. KIN17, KIN17 DNA and RNA binding protein; A549KIN17 KD, A549 cells transfected with recombinant lentiviral vectors carrying the KD4 siRNA sequence targeting KIN17 gene; A549NC, A549 cells transfected with the control vector; A549MOCK, A549 cells without transfection of vector.

Fig 3: KIN protein methylation assay. (A) Monomethylation at arginine on position 36; (B) In vitro methylation assay with tritium-labeled S-(methyl-3H)-Adenosyl-L-methionine, PRMT7 enzyme, and KIN-His wild type and KIN-His mutated R36K. (C). In vitro methylation assay with tritium-labeled S-(methyl-3H)-Adenosyl-L-methionine, GST-PRMT family of proteins, and KIN-His. The protein KIN demonstrated strongest affinity with PRMT7.

Fig 4: KIN protein immunolocalization. (A) Immunofluorescence of HeLa cells shows KIN present at the nucleolus, as well as in other parts of the nucleus. Scale bar: 32 µm. (B) Predicted nucleolar localization signal by NOD.

Fig 5: Identification of KIN-related prognostic genes in cervical cancer. (a) graphical summaries of IPA pathway analysis. (b) univariate Cox regression analysis of intersecting genes. ((c)-(d)) LASSO analysis revealing the minimal lambda. ((e)-(f)) time-dependent ROC curve.