Publication for HNRNPL and U2AF2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	HNRNPL	heterogeneous nuclear ribonucleoprotein L	3191			[link]
hsa	U2AF2	U2 small nuclear RNA auxiliary factor 2	11338

Pubmed ID	Priority	Text
28934469	0.98	U2AF65, hnRNP A1, hnRNP L or U1-70K, followed by Western blotting with antibodies to hnRNP L, PSF, Sam68 or hnRNP C1.
	0.98	hnRNP L and U2AF65 interacted with each other.
	0.98	hnRNP L interacted with U2AF65 (Figure 8).
	0.97	hnRNP L, hnRNP A1 and U2AF65 of on proteins pulled down by the shorter biotinylated ssDNA oligos.
	0.97	hnRNP L and U2AF65 distinct (Figure 3E).
	0.97	hnRNP L, hnRNP A1, PSF and PTB could interfere negatively with the recognition of SA5639 by interacting or interfering with U2AF65/35.
	0.97	hnRNP L binds well to U2AF65 (Figure 8C), thereby connecting the splicing regulatory protein hnRNP L to the splicing factor U2AF65.
	0.97	hnRNP L and U2AF65 could be either caused by hnRNP L dephosphorylation, or increased Sam68 ubiquitination, or both.
	0.97	hnRNP L, hnRNP A1, hnRNP C1, Sam68 and U2AF65 are associated with each other in C33A2 cells.
	0.97	hnRNP L is phosphorylated by different kinases, the effects of hnRNP L phosphorylation appears to converge on U2AF65.
	0.96	hnRNP L, hnRNP A1 and U2AF65 of on proteins pulled down by the shorter biotinylated ssDNA oligos.
	0.96	hnRNP L and/or U2AF65.
	0.96	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).
	0.96	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.
	0.95	hnRNP L, hnRNP A1, U2AF65 and U2AF35, such as SRSF1, PSF, hnRNP A2B1, Sam68, Tra2b, hnRNP LL and hnRNP C1 (Figure 4B).
	0.95	hnRNP L and hnRNP A1 to specific sites upstream of, or at SA3358, and that this resulted in increased binding of positive splicing factor U2AF65 to SA3358.
	0.95	U2AF65 binds efficiently upstream of SA3358, as expected, whereas binding of hnRNP L was undetectable (Figure 3).
	0.94	hnRNP L with oligos downstream of SA3358 were either unaffected by Akt inhibitor GDC0068, or increased, but that did not substantially affect binding of U2AF65 (Figure 6B and C).
	0.91	U2AF65 and U2AF35 are pulled-down together, supporting the idea that they form a splicing-active complex at SA3358, in the absence of 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.
	0.88	U2AF65/35 at the efficiently used 3'-splice sites SA3358 in the E4 exon, U2AF65/35 at the suppressed 3'-splice site SA5639 was pulled down with the same oligos as hnRNP L and hnRNP A1 (Figure 4B and C), and additional splicing inhibitory factors such as PTB and PSF (Figure 4B).
	0.77	hnRNP L and U2AF65 has been suggested to account for the inhibitory effect of hnRNP L on splicing.
	0.74	hnRNP L and hnRNP A1 and increased pull down of U2AF65 with extracts from Akt kinase inhibitor treated cells
26260686	0.98	U2AF65, hnRNP L and PTB mostly assemble at 3' splice sites.
	0.98	U2AF65 and (e) hnRNP L show the distributions of the entire population of fragments (blue), fragments of group A (orange) and group B (green).
	0.97	U2AF65 (ref.), hnRNP L and PTB.
	0.97	hnRNP L, U2AF65 and PTB, which are known to bind to T-rich motifs (Fig. 5c-f).
	0.55	hnRNP L, (d) U2AF65, (e) PTB Heidelberg lab, (f) PTB Ule lab and (g) a HITS-CLIP library of PTB.
24121633	0.98	hnRNP L-PTB interaction prevents association of U2AF65 (65) to PPT and U1 snRNP (U1) to the 5' splice site.
	0.97	hnRNP L, allowing association of U2AF65 and U1 snRNP to the upstream PPT and downstream 5' splice site, respectively; this, in turn, leads to the exon P3A definition that favors formation of the exon P3A-included species of mRNA (Fig. 6b).
	0.97	hnRNP L facilitates binding of PTB to the upstream PPT that suppresses subsequent association of U2AF65 and U1 snRNP in the exon-defined E complex.
	0.96	hnRNP L with PTB inhibits association of U2AF65 and U1 snRNP with the upstream and downstream of P3A, respectively, which causes a defect in exon P3A definition.
27565572	0.96	U2AF2, SF3A2, RBM8A, RBM4, PRPF4B, NOVA1, KHSRP, HNRPU, HNRPL, HNRPH1, HNRPC, and HNRPA1.
	0.61	U2AF2, SF3A2, RBM8A, RBM4, PRPF4B, NOVA1, KHSRP, HNRPU, HNRPL, HNRPH1, HNRPC, and HNRPA1) were individually knocked-down in different cell lines to assess their implication in splicing of 96 differents transcripts.
30216987	0.96	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).
24069033	0.94	hnRNP L reduces its interaction with the U2AF65 subunit of the U2 auxiliary factor.
22264826	0.92	hnRNP L (Figure 3B), as well as U1-70K and U2AF65, which are a component of the U1 snRNP and an auxiliary factor for U2 snRNP, respectively (Figures 3C and 3D).
27825848	0.91	U2AF65 and hnRNP L has been predicted to cooperatively regulate titin splicing with RBM20.
29304022	0.61	U2AF65, heterogeneous nuclear ribonucleoprotein L (hnRNP L)) enhances repression activity of RBM20, which indicates the repression occurs in a dose dependent manner.
23307558	0.55	U2AF65 and hnRNP L. Results using LV showed that during development, the ratio between the latter three splicing factors remained essentially constant, but the ratio of Rbm20 to these splicing factors increased with development.