Publication for HNRNPA1 and HNRNPL

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	HNRNPA1	heterogeneous nuclear ribonucleoprotein A1	3178			[link]
hsa	HNRNPL	heterogeneous nuclear ribonucleoprotein L	3191

Pubmed ID	Priority	Text
31085639	0.98	hnRNPA1, hnRNPL, and PCBP1 are required for transcription inhibition-induced dissociation of MALAT1 from nuclear speckles.
	0.95	hnRNPA1 and hnRNPL are freed from nascent mRNA transcripts to allow their binding to other RNA species.
	0.75	hnRNPA1, hnRNPL, and PCBP1, transcription inhibition fails to dissociate MALAT1 from nuclear speckles.
	0.71	hnRNPA1 and hnRNPL could bind to MALAT1, which may compete with factors that recruit MALAT1 to nuclear speckles, thereby preventing the nuclear speckle localization of MALAT1 under transcription inhibition.
30658689	0.98	HNRNPA1 (sc32301), PSF (sc101137), from Santa Cruz; beta-Actin (622102) from Biolegend or HNRNPL (A303-895A) from Bethyl Laboratories.
	0.97	hnRNP A1, hnRNP U, hnRNP L, HuR, PSF and NONO.
23394998	0.97	hnRNP L recruits hnRNP A1 and is required for exon repression
	0.97	hnRNP L and hnRNP A1 we turned to an MS2-tethering system in which the ESS1 of exon 4 minigene is replaced by a MS2 binding sequence and hnRNP L is expressed as an MS2 fusion protein (Figure S5).
	0.97	hnRNP A1 with the 3' end of exon 4 is required for ESS1-and hnRNP L-dependent exon repression
	0.96	hnRNP A1 and U1 association with the 3' end of exon 4 is that hnRNP L promotes the recruitment of these components to otherwise weak binding sites.
	0.96	hnRNP A1 to RNA by hnRNP L is required for MS2-hnRNP L-mediated exon repression (Figure 5D).
	0.96	hnRNP L to interact with hnRNP A1 correlates with the ability of hnRNP L to promote exon repression, although we have not determined whether this interaction is direct or indirect.
	0.96	hnRNP A1 and the U1 snRNA to the 3' end of CD45 exon 4 even in the absence of hnRNP L (e.g. in the Derepressed constructs).
	0.95	hnRNP L (L), hnRNP A1 (A1) or GFP as control.
	0.94	hnRNP L to co-precipitate hnRNP A1 depends on a proline-rich linker sequence within hnRNP L (Figure 5B,C).
	0.94	hnRNP L is dependent on both the integrity of the 3' end of exon 4 and on hnRNP A1, indicating that MS2-hnRNP L causes repression by the same mechanism as does hnRNP L bound to the ESS1 (Figure S5B,C).
	0.94	hnRNP A1 and U1 recruitment by hnRNP L is sufficient to predict regulatory effect of hnRNP L on multiple exons
	0.92	hnRNP L, together with hnRNP A1, effectively holds the U1 snRNA in an extended basepaired conformation that precludes the normal exchange of U1 for U6 at the 5' splice site.
	0.88	hnRNP L that are not required for repression activity in the MS2-tethering assay, do not reduce co-precipitation of hnRNP A1 with hnRNP L (Figure 5B-D).
	0.85	hnRNP A1 with the U1 snRNP at the 3' end of exon 4 (Figure 3), the observed recruitment of hnRNP A1 by hnRNP L is sufficient to explain the requirement for hnRNP L/ESS1 for the C-15 crosslink of U1; although we cannot rule out additional direct contacts between hnRNP L and U1.
	0.81	hnRNP L efficiently precipitates hnRNP A1 (Figure 5B).
	0.77	hnRNP A1, while the 65 kD protein is hnRNP L (Figure 3B, S3A).
	0.75	hnRNP A1 and U1 with the 3' end of exon 4 are required for both hnRNP L and ESS1-dependent exon repression.
	0.66	hnRNP L function, the 3' end of the exon contains a UGCU sequence (similar to the sequence surrounding the C-15 crosslink) within 20 nts upstream of the 5' splice site, as well as an upstream AG dinucleotide which could serve as a binding site for hnRNP A1 (Figure 7B, S7A).
	0.57	HnRNP L interacts with hnRNP A1 through linker domain and recruits hnRNP A1 to exon 4 to achieve repression
	0.54	hnRNP A1 results in a reduction in exon 4 skipping from the minigene, although knockdown of hnRNP L has a more prominent effect consistent with hnRNP L functioning as the driving factor in repression (Figure 4D, S4D).
	0.54	hnRNP L to recruit hnRNP A1, and the ability of hnRNP A1 and U1 snRNA to interact with the 3' end of exon 4, are all required for repression of exon 4.
	0.51	hnRNP A1 and the U1 snRNA are present in at least several exons we have previously shown to be regulated by hnRNP L. Moreover, the predicted free-energy of potential basepairing of these exons with U1 snRNA is sufficient to explain the functional effect of hnRNP L on splicing.
26110767	0.97	hnRNPA1 (upper panel) or hnRNPL (lower panel) antibodies.
	0.96	hnRNPA1 or anti-hnRNPL antibodies.
	0.96	hnRNPA1 and hnRNPL at the end point of EGF-treatment was the same in the two cell lines.
	0.95	hnRNPA1 or hnRNPL.
	0.94	hnRNPA1 and hnRNPL (Fig 6B).
	0.65	hnRNPA1 or hnRNPL (Left panel).
	0.58	hnRNPA1 and hnRNPL were analyzed by qPCR in control and 2h EGF-treated cells.
24650050	0.97	hnRNP L, hnRNP A1, and hnRNP M) are implicated in many AS events in human and several other eukaryotes and play a role in regulating splicing events by inhibiting the use of splice-sites from the spliceosome.
	0.97	hnRNP L and hnRNP A1 to direct exon-skipping by the spliceosome whereas hnRNP M leads to exon-inclusion, in the production of the L-isoform (Figure 1A).
	0.97	hnRNP L) and DeltaA1 (hnRNP A1) (Figure 5A).
	0.95	hnRNP L and hnRNP A1 interact specifically with exon 7 to control splice-site recognition in the formation of CEACAM1-S mRNA.
	0.92	hnRNP L, hnRNP M, hnRNP A1 and IRF-1, we tested for the ability to pull-down CEACAM1 transcripts that included or lacked exon 7 (Figure 6).
	0.80	hnRNP A1 and hnRNP L coordinate spliceosome functioning to generate the CEACAM1-S isoform, WT ISRE coupled-exon 7 DeltaLDeltaA1 double mutants revert double positive GFP/mCherry cells towards WT levels (7.0% compared to 8.9%).
23646903	0.97	hnRNP L and hnRNP LL bind to a similar region of CD45 exon 4; (ii) hnRNP L and hnRNP LL are not functionally redundant on this exon; and (iii) repression of exon 4 by hnRNP L does not involve mere steric hindrance, rather hnRNP L recruits hnRNP A1 to induce an extended interaction between the exon and the spliceosomal U1 snRNP (small nuclear ribonucleoprotein) component to inhibit proper spliceosome assembly (; see below).
	0.97	hnRNP L represses CD45 exon 4 by recruiting hnRNP A1 to the 3'-end of the exon and inducing extended base-pair interactions between the U1 snRNA and the exon.
	0.97	hnRNP L (or hnRNP LL) the A1 and A1 + U1 mutations reduce exon skipping as hnRNP A1 can bind weakly to its cognate site without the assistance of hnRNP L (; Figure 6b, MS2).
	0.96	hnRNP L and hnRNP LL function by an overlapping mechanism that involves recruitment of hnRNP A1 and the U1 snRNA to the exon (see below for further discussion).
	0.93	hnRNP L-mediated exon repression in which hnRNP L (dark grey oval) bound upstream in exon recruits hnRNP A1 (white circle) to a UAGUG element at the 3'-end of the exon.
19912651	0.97	hnRNP A1, hnRNP A2/B1, hnRNP G and hnRNP L as its four major nuclear interacting protein partners in LNCaP cells.
	0.96	hnRNP A1, A2/B1 and G), we identified hnRNP L as a novel Sam68-interacting protein partner.
	0.84	hnRNP A1), ROA2_HUMAN (C: hnRNP A2/B1), HNRPG_HUMAN (D: hnRNP G), and HNRPL_HUMAN (E: hnRNP L).
28600288	0.97	hnRNP A1 synergizes with hnRNP L to block splicing of exons 4, 5, and 6 in CD45.
	0.93	hnRNP L and hnRNP A1 were both phosphorylated by Akt during low dose stimulation (Fig. 3A, 3B), suggesting that their activity could be important for Treg differentiation.
31010097	0.97	hnRNPA1, hnRNPA2B1, hnRNPK, hnRNPL and hnRNPU and TNPO1 (positive control) mRNA normalized to B2M determined in HeLa cells stably transduced with control miR, anti-miR-128 or miR-128 are shown as mean +- SD (n = 3 technical replicates, * p < 0.05, ** p < 0.01, *** p < 0.001).
	0.96	hnRNPA1, hnRNPA2B1, hnRNPK, hnRNPL and hnRNPU) as potential miR-128 targets and ORF1p interaction partners, see Figure 1A, shown in grey.
23520512	0.97	hnRNPA1, and hnRNPL (compare lanes 1 and 2).
24452469	0.97	hnRNP L and hnRNP A1 induce extended contacts between U1 snRNA at the 5'ss and neighbouring exonic sequences that, in turn, inhibit stable association of U6 snRNA and subsequent spliceosomal catalysis.
25599992	0.97	hnRNP-L, PSF, hnRNPA1, hnRNPA2B1, hnRNPC and MRG15 (Patton et al,; Hahm et al,; Luco et al,; King et al,), although we did identify the helicase DDX3X (King et al,).
26641092	0.97	hnRNPL, hnRNPLL, hnRNPA1 and SFPQ that cooperate in aligning intron/exon junctions or regulate the recruitment of the spliceosome.
28934469	0.96	hnRNP L and hnRNP A1 (Figure 4B and C), and additional splicing inhibitory factors such as PTB and PSF (Figure 4B).
	0.95	hnRNP A1, hnRNP L or U1-70K, followed by Western blotting with antibodies to hnRNP L, PSF, Sam68 or hnRNP C1.
	0.95	hnRNP L was also found in these complexes with hnRNP A1 and A2B1.
	0.94	hnRNP L, while hnRNP A1 did not interact with these oligos at all, as expected (Supplementary Figure S2D).
	0.92	hnRNP L, hnRNP A1 and U2AF65 of on proteins pulled down by the shorter biotinylated ssDNA oligos.
	0.92	hnRNP L and hnRNP A1 to sequences upstream of SD3632 and immediately at SD880, and that this resulted in increased binding of U1snRNP to at least SD880.
	0.92	hnRNP L in C33A2 cells transfect with scrambled siRNA or siRNA to hnRNP L. (C) RT-PCR of HPV16 L1/L1i mRNAs, GAPDH mRNAs (upper panel) and HPV16 L2 mRNAs (lower panel) in C33A2 cells transfect with scrambled siRNAs or siRNAs to hnRNP L. (D) RT-qPCR of HPV16 L1 or E4 mRNAs in C33A2 cells transfect with scrambled siRNAs or siRNAs to hnRNP L. (E) sLuc activity in the cell culture medium of C33A2 cells at different time points after mock transfection or transfection with scrambled siRNA or siRNA to hnRNP A1+A2 or hnRNP L. (F) Western blot of hnRNP L, hnRNP A1, hnRNP A2 or actin in C33A2 cells transfected with scrambled siRNA (scr) or siRNAs to hnRNP L or hnRNP A1 + hnRNP A2.
	0.86	hnRNP L, hnRNP A1, PSF and PTB could interfere negatively with the recognition of SA5639 by interacting or interfering with U2AF65/35.
	0.83	hnRNP A1, hnRNP L and U2AF65 distinct (Figure 3E).
	0.80	hnRNP A1 and hnRNP L have been shown to repress exon 4 on the CD45 mRNAs, by suppressing a 5'-splice site.
	0.75	hnRNP L, hnRNP A1 and U2AF65.
	0.75	hnRNP L are interacting with each other in C33A2 cells, and that binding of hnRNP L to hnRNP C is reduced in the presence of Akt inhibitor, while interactions between hnRNP L and a number of other RNA binding proteins such as hnRNP A1 and U2AF65 is unaffected (Figure 8C).
	0.65	hnRNP L and/or hnRNP A1 were either competing with splicing factor U2A65 for its binding sites upstream of SA5639, or binding to the U2AF65 protein to inhibit its function.
	0.60	hnRNP L, hnRNP A1, hnRNP C1, Sam68 and U2AF65 are associated with each other in C33A2 cells.
	0.60	hnRNP L. In contrast, oligos located upstream of SA5639, some of which covered the polypyrimidine tract, pulled down U2AF65/U2AF35 together with hnRNP L and hnRNP A1.
	0.59	hnRNP L and Sam68 decreased over time in Akt kinase inhibitor treated cells (Supplementary Figure S7A), and was specific for hnRNP L since Sam68 did not interact with hnRNP A1 (Figure 8B).
21569507	0.96	HNRNPA1: heterogeneous nuclear ribonucleoprotein A1; HNRNPA2B1: heterogeneous nuclear ribonucleoprotein A2/B1; HNRNPL: heterogeneous nuclear ribonucleoprotein L; HSPD1: heat shock 60-kDa protein 1; KHSRP: KH-type splicing regulatory protein (far upstream element-binding protein 2); LMNA: lamin A/C; PCBP2: poly(rC)-binding protein 2; PRDX2: peroxiredoxin 2; RB1: retinoblastoma-associated protein; RBBP4: retinoblastoma-binding protein 4; SOD2: superoxide dismutase 2, mitochondrial; SSc: systemic sclerosis; STMN1: stathmin 1; TGFB1: transforming growth factor beta1; TPI1: triosephosphate isomerase 1; VIM: vimentin.
23765697	0.96	hnRNP L represses exon 4 inclusion by binding to an ESS element in this exon and subsequent recruitment of hnRNPA1.
24121633	0.96	hnRNP L binds to hnRNP A1 in an RNA-dependent manner and binding of both molecules to CD45 exon 4 causes skipping of exon 4.
25354590	0.96	hnRNP L stabilizes the binding of hnRNP A1 in exon 4, in which binding of hnRNP A1 and the subsequent splicing suppression is dependent on hnRNP L. The authors demonstrate that hnRNP L interacts with hnRNP A1, which is lost by RNase.
29684050	0.96	hnRNPL, hnRNPH, hnRNPE2 and hnRNPA1.
30939845	0.96	heterogeneous nuclear ribonucleoprotein L. HNRNPA1: heterogeneous nuclear ribonucleoprotein A1.
26979993	0.95	hnRNP-L, hnRNP-A1, Matrin-3 or RBM14 antibody, while IgG pull-down was used for IP control.
	0.94	hnRNP-A1, followed by hnRNP-A3 and hnRNP-L, with low, non-significant co-localization observed with hnRNP-A2/B1 (Fig. 5).
20126623	0.95	HNRNPL and HNRNPA1 like, chromosome 19 and 2, respectively (Table 3)].
22132154	0.92	hnRNP L and hnRNP A1/A2.
29693319	0.91	HNRNPL, SRSF2, PTBP1, HNRNPE2, and HNRNPA1 have been all implicated in the regulation of CD45 splicing.
20639884	0.89	hnRNP A1 in the biogenesis of let-7a we performed in vitro processing assays using control, hnRNP A1-depleted or hnRNP L-depleted HeLa cell extracts (see Supplementary Fig. 5b for levels of hnRNP A1 depletion).
25112293	0.78	hnRNP A1 and EWS) in response to osmotic stress or DNA damage, enhanced RNA-binding activity of an RBP (for example, SAM68) upon activation of the mitogen-activated protein kinase (MAPK) pathway or in response to depolarization, conversion from an activator to a repressor in response to heat shock, release from inhibitory protein complexes (for example, PTB-associated splicing factor (PSF) and hnRNP L) and/ or transcriptional induction of a cofactor during T cell signalling.
	0.57	hnRNP L and hnRNP A1 (REF.).
18995836	0.78	hnRNP A1, band 2 corresponds to hnRNP L, and band 4 corresponds to hnRNP I (PTB).
25056543	0.67	hnRNPA1 antibody (upper panel) and hnRNPL (lower panel).
29458410	0.57	HNRNPL, HNRNPD/AUF1, HuR, HNRNPA1, LIN28, NONO, and HNRNPC (Fig. 3a).
	0.52	HNRNPA1 (heterogeneous nuclear ribonucleoprotein A1), HNRNPC, HNRNPL, HuR (human antigen R), and protein LIN28A (lin-28 homolog A) were predicted to bind ebv-sisRNA-1 and/or ebv-sisRNA-2; FUS (fused in sarcoma) was predicted to associate with ebv-sisRNA-2.