Publication for HNRNPL and ILF3

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
hsa HNRNPL heterogeneous nuclear ribonucleoprotein L 3191 [link]
hsa ILF3 interleukin enhancer binding factor 3 3609

Pubmed ID Priority Text
23976881 0.98 hnRNP L, DRBP76, and hnRNP A2/B1
0.98 hnRNP L, and DRBP76 were incubated with [32P]UTP-labeled VEGFA HSR, CARE, AUSL, AUSL-A, and AUSL-D RNA and subjected to UV crosslinking.
0.98 DRBP76 and hnRNP A2/B1, both were subjected to siRNA-mediated knock-down (hnRNP L knock-down served as positive control) (Figure 3A, top).
0.98 hnRNP L and HSR RNA were added, then a modest interaction between hnRNP A2/B1 and DRBP76 was detected.
0.98 hnRNP L as the "specificity factor," but likewise recruit DRBP76 to stabilize nearby stem-loop structures and drive formation of alternate regulatory conformers.
0.97 hnRNP L, DRBP76, and hnRNP A2/B1 to CARE.
0.97 hnRNP L interacted with VEGFA mRNA in control transfected cells; however, the interaction was substantially reduced following siRNA-mediated depletion of either hnRNP A2/B1 or DRBP76 (Figure 2B).
0.97 hnRNP L and DRBP76 directly bind the VEGFA HSR.
0.97 DRBP76 are essential for hnRNP L binding to VEGFA mRNA in vivo.
0.97 DRBP76-specific (or scrambled) siRNA, and lysates immunoprecipitated with anti-hnRNP L antibody.
0.97 DRBP76 or hnRNP A2/B1 dramatically impaired the hypoxia-driven RNA switch to an extent comparable to that of hnRNP L knockdown, and permitted GAIT complex-mediated translation inhibition by 24-h lysates (Figure 3A, bottom).
0.97 DRBP76, and hnRNP L, and scrambled (scramb.) control was determined by immunoblot analysis; beta-actin was probed as loading control (top).
0.97 hnRNP L, -VHL, -hnRNP A2/B1, and -DRBP76 antibodies.
0.97 hnRNP L, but not with hnRNP A2/B1 or DRBP76, in an IFN-gamma-dependent manner (Figure 4F).
0.97 DRBP76 did not affect hnRNP L stability (Figure S13).
0.97 hnRNP L (Y359D) was pre-incubated with DRBP76 and hnRNP A2/B1 as indicated (5 pmol each) for 0.5 h on ice.
0.97 DRBP76 and hnRNP A2/B1 is indirect and facilitated by hnRNP L and VEGFA HSR RNA (Figure 2F).
0.96 hnRNP L, hnRNP A2/B1, and DRBP76 in operating the RNA switch, we determined the regulatory activity of the purified proteins in vitro.
0.95 hnRNP L-DRBP76-hnRNP A2/B1) complex that coordinates a three-element RNA switch, enabling VEGFA mRNA translation during combined hypoxia and inflammation.
0.95 hnRNP L recruits DRBP76 (double-stranded RNA binding protein 76) to the 3'UTR, where it binds an adjacent AU-rich stem-loop (AUSL) element, "flipping" the RNA switch by disrupting the GAIT (interferon-gamma-activated inhibitor of translation) element, preventing GAIT complex binding, and driving robust VEGFA mRNA translation.
0.95 hnRNP L, DRBP76, and hnRNP A2/B1 detected by mass spectrometry.
0.95 hnRNP L was the binding site for DRBP76 (Figure 1G, right).
0.95 DRBP76 are required for hnRNP L binding to VEGFA mRNA, lysates from cells treated with IFN-gamma and hypoxia were subjected to ribonucleoprotein IP (RIP) using anti-hnRNP L antibody, coupled with RT-PCR.
0.95 hnRNP L and DRBP76.
0.95 DRBP76 and hnRNP A2/B1 by themselves did not bind, nor did the addition of either hnRNP L or HSR RNA restore their interaction significantly (Figure S15).
0.94 hnRNP L, hnRNP A2/B1, and DRBP76 was determined by immunoblot as input control (right panel).
0.94 hnRNP L directly interacted with recombinant hnRNP A2/B1 and DRBP76 (Figure 1F, left panel).
0.93 DRBP76 with VEGFA mRNA was abolished following hnRNP L depletion by siRNA-mediated gene silencing (Figure S2, right panels), suggesting that HILDA binding to VEGFA mRNA requires integrity of the entire complex.
0.91 hnRNP L, DRBP76, and hnRNP A2/B1 (HILDA) was shown to bind wild-type but not mutant antisense CARE RNA; substantially less binding of the three proteins to CARE RNA was observed in normoxic lysates (Figure 1D).
0.85 hnRNP L but not DRBP76 (Figure 1F, right panel).
0.80 hnRNP L binds the CARE, whereas DRBP76 binds the AU-rich stem loop (AUSL) (Figure 2C).
0.78 hnRNP L (Y359D) by itself or with either hnRNP A2/B1 or DRBP76, did not restore translation in the presence of lysates from cells treated with IFN-gamma for 24 h (Figure 6G).
0.73 hnRNP L and DRBP76, suggesting that the hnRNP L-DRBP76 complex is stabilized by RNA.
0.53 hnRNP L and DRBP76 were incubated with GST-hnRNP A2/B1 or GST immobilized to GSH-agarose beads (right).
0.50 hnRNP L antibody, and probed with hnRNP A2/B1- and DRBP76-specific antibodies (Figure 1E, left panel).
28520992 0.97 hnRNP L, but not DRBP76, suggesting that hnRNP L interaction with miR-574-3p does not require the HILDA complex (Figure 4B).
0.96 hnRNP L does not bind DRBP76 in hypoxia.
0.93 hnRNP L translocates out of the nucleus to interact with two other proteins to form the cytoplasmic HILDA (hypoxia-induced hnRNP L-DRBP76-hnRNP A2/B1) complex.
0.90 hnRNP L antibody and immunoblotted using anti-DRBP76, -hnRNP A2/B1 and -hnRNP L antibodies.
0.90 hnRNP L is joined by DRBP76 and hnRNP A2/B1 to form the HILDA complex that also binds the VEGFA mRNA HSR (Supplementary Figure S1A).
32206104 0.97 NF90/NF110, DExH-box helicase 9 (DHX9), Heterogeneous Nuclear Ribonucleoprotein L (HNRNPL), RNA-Binding Motif 20 (RBM20), Muscleblind protein (MBL)/vertebrate homolog Muscleblind-like protein 1 (MBNL1), Epithelial Splicing Regulatory Protein 1 (ESRP1), and serine/arginine (SR)-rich proteins.
0.96 NF90/NF110 and HNRNPL/SRs act in combinatorial and coordinated ways in circRNA biogenesis.
0.74 NF90/NF110, DHX9, HNRNPL, RBM20, ESRP1, and SR proteins, which all have been proposed to contain binding motifs for their corresponding circRNAs.
21747757 0.97 NF90, HuR, CUG-BP1, hnRNP A2, hnRNP L, and the iron-response proteins (IRP1, IRP2; Hamilton et al.,; Lopez de Silanes et al.,; Kim et al.,; Leipuviene and Theil,; Abdelmohsen et al.,).
25753659 0.96 hnRNP-L-DRBP76-hnRNP-A2/B1) complex has been shown to coordinate a three-element RNA switch, enabling VEGFA mRNA translation in hypoxia.
19583805 0.95 NF90, HuR, CUG-BP1, hnRNP A2, hnRNP L and the iron-response proteins (IRP1, IRP2).
26256788 0.92 heterogeneous nuclear ribonucleoprotein L (HNRNPL), insulin-like growth factor 2 binding protein 1 (IGF2BP1), interleukin enhancer binding factor 3 (ILF3, or NF90/NFAR-1), and U6 snRNA-associated Sm-like protein (LSM1-7), while synaptotagmin binding cytoplasmic RNA interacting protein (SYNCRIP, or NSAP1) binds to an RNA sequence immediately downstream of the 5'UTR.
29152905 0.90 hnRNP L in the HILDA (hypoxia-induced hnRNP L-DRBP76-hnRNP A2/B1) complex binds a CA-rich element directly adjacent to the GAIT element, and DRBP76 binds a downstream AU-rich stem loop thereby disrupting GAIT element formation, preventing GAIT complex binding, and enhancing VEGFA mRNA translation.
0.83 hnRNP L is phosphorylated at Tyr359 and accumulates in the cytoplasm in a complex with hnRNP A2/B1 and DRBP76 (double-stranded RNA-binding protein) (Fig. 6iii).
0.74 hnRNP L is phosphorylated at Tyr359 and joins hnRNP A2/B1 and double-stranded RNA binding protein, DRBP76, to form the active HILDA complex.
27165283 0.89 hnRNP L-DRBP76-hnRNP A2/B1) complex and the interferon gamma (IFN-gamma)-activated inhibitor of translation complex (GAIT).
27992500 0.88 hnRNP L-DRBP76-hnRNP A2/B1) complex that de-represses translation under stress was identified.
25951186 0.86 hnRNPL and DHX9), and transcription (PURA, CDK9, and ILF3).
29856133 0.84 NF90/NF110, heterogeneous nuclear ribonucleoprotein L (HNRNPL) and muscleblind (MBL/MBNL1).6, 7, 8, 9, 10, 11 Recently, based on RNA interference screening, Liang et al12 revealed that the expression ratio of linear to circular RNA is modulated by many core spliceosomal and transcription termination factors.
29593672 0.75 hnRNP L and NF90 have been demonstrated to stimulate HCV replication.
30216987 0.66 ILF3, HNRPL; B:EGR1, MYF5, TOPRS, NEIL2, TNR4, MYOD1, p53, MYF6, MYOG, IGF2, TERT, NEIL1, ACD, RECQ4, TINF2; C:NUCL, NPM, TOP1, EBNA1BP2, POTE1, CAMP, NDKB, DHX36, SF3B3, ILF2, NOA1, DHX30, DHX15, DPOE1, ERCC2, EFHD2, ERCC3, TERF1, SAFB1, SAFB2, DNM3B, FMR1, U2AF2, TERF2, DSRAD, SPAST, DNM3A, TE2IP, DNMT1, NEIL3, ADA10, IF16, PARP1, DDX21, POLH, BRCA1, NF2L2, ATRX, BLM, FANCJ, RFA2, RFA1, ELAV1) of proteins supported by approximately unbiased values (AU equal to or greater than 95 is considered to be statistically significant).
31671760 0.62 hnRNP L, hnRNP Q, NCL, RPL26, and Ku), there are also proteins RNPC1, Pdcd4, DAP5, TCP80, and RHA.



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