Publication for PRPF8 and SNRNP200

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	PRPF8	pre-mRNA processing factor 8	10594			[link]
hsa	SNRNP200	small nuclear ribonucleoprotein U5 subunit 200	23020

Pubmed ID	Priority	Text
28515276	0.98	PRPF8, EFTUD2, and SNRNP200 in association with the HSP90/R2TP complex, its ZNHIT2 cofactor, and additional proteins.
	0.98	SNRNP200 unwinds the U4/U6 duplex to activate the spliceosome, whereas EFTUD2, along with PRPF8, controls SNRNP200 activity.
	0.97	PRPF8 also holds two other U5-specific proteins that perform essential functions during splicing: the helicase SNRNP200 (Brr2 in yeast) and the GTPase EFTUD2 (Snu114 in yeast).
	0.97	PRPF8, EFTUD2, and SNRNP200 in splicing, the biogenesis of these proteins is still uncharacterized in mammals.
	0.97	PRPF8, and SNRNP200.
	0.97	SNRNP200-GFP was not recruited on p54-ZNHIT2 P-bodies, whereas EFTUD2 and PRPF8 were (Fig. S3 E).
	0.97	PRPF8, SNRNP200, and SNRNP40), and proteins found in U5 assembly intermediates (AAR2, RUVBL1/2, ZNHIT2, and Chaperonin).
	0.97	PRPF8 and SNRNP200 are potential client proteins of HSP90.
	0.97	PRPF8 maturation and impair its interaction with SNRNP200 and U5 snRNA (Fig. 3).
	0.97	PRPF8, EFTUD2, and SNRNP200 but only small amounts of Sm proteins or other U5-specific proteins (Fig. 4 C).
	0.95	PRPF8 do not block snRNP biogenesis while affecting splicing, similar to two RP mutations in the SNRNP200 gene.
	0.94	PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central module of the spliceosome.
	0.94	PRPF8, EFTUD2, and SNRNP200 were clients of HSP90, we inhibited its activity using geldanamycin (GA).
	0.93	PRPF8 and SNRNP200, but not of EFTUD2 (Fig. 8 A).
	0.71	PRPF8-LAP with its partners EFTUD2 and SNRNP200, and conversely, GFP-EFTUD2 strongly bound PRPF8 and SNRNP200.
	0.64	PRPF8-WT-LAP was properly incorporated into U5 and tri-snRNPs, as documented by the coprecipitation of U5-specific proteins (SNRNP200, EFTUD2, and PRPF6) and of the U4/U6-specific factor PRPF31.
25450007	0.98	SNRNP200 is regulated by both PRPF8 and EFTUD2.
	0.97	PRPF8 (PRP8), SNRNP200 (Brr2), and EFTUD2 (Snu114) form a stable protein complex and are constitutive components of the U5 snRNP.
	0.97	SNRNP200 or GFP-PRPF8, and after 24 h, cells were lysed and immunoprecipitated with anti-Flag antibody.
	0.97	PRPF8 RNase H domain inhibits SNRNP200 activity and GTP-bound EFTUD2 and that the C-terminus of PRPF8 induces the activation of SNRNP200, the detailed molecular mechanisms of the activation of SNRNP200 remains to be determined.
	0.96	PRPF8 inhibits loading of SNRNP200 to U4 snRNA, and a C-terminal part of PRPF8 modulates the SNRNP200 activity for the unwinding of U4/U6 snRNA duplex.
	0.95	PRPF8, SNRNP200, and EFTUD2.
	0.94	PRPF8, SNRNP200, and EFTUD2 were identified with relatively high scores (Table S1).
	0.74	PRPF8/EFTUD2/SNRNP200 complex, our proteomics analysis as well as previous analyses found that SNW1 was in complex with another splicing subcomplex, PRP19 complex.
30315277	0.98	Brr2 and Prp8 in the pre-B-to-B transition.
	0.98	Brr2 also contacts the Linker and the RNaseH-like domains of Prp8.
	0.97	Prp8, which stably associates with Brr2, is similarly translocated.
	0.96	Brr2 is connected to the core of the tri-snRNP through three patches of direct interactions: between its NC and the Jab1 domain of Prp8, between its NC and the convex side of three tetratricopeptide repeats (TPR) of Prp6 (residues 272-373), and between its PWI domain and Sad1 (Fig. 3a; Supplementary information, Fig. S9a).
	0.64	Prp8, Brr2 directly contacts the WD40 domain of Smu1 (Fig. 1a, right panel).
30975767	0.98	Prp8 Jab1 domain and Brr2 C-terminal helicase cassette.
	0.97	Brr2 N-terminal helicase cassette is supported by Prp6 bound to the RNaseH and RT domains of Prp8, and Snu13, whereas the Brr2 C-terminal helicase cassette is packed against its PWI domain, which in turn contacts Sad1 bound to Snu114 and the Prp8 RT domain.
	0.95	Prp8 Endonuclease and RNaseH domains, U4/U6 stem III and the quasi-pseudoknot thereby solidifying the organization of the U4 region prior to Brr2 relocation.
	0.86	Brr2 is tightly bound to the Prp8 Jab domain which interacts with the Reverse Transcriptase (RT) and Linker domains of Prp8.
20572804	0.98	Prp8 that weaken the interaction with Brr2 and Snu114 have been linked to retinitis pigmentosa.
	0.90	Brr2 and is controlled by Snu114 and Prp8.
23727230	0.98	Prp8 cause the degenerative eye disease retinitis pigmentosa, are found at or near the interface with Brr2, clarifying its molecular pathology.
	0.94	Brr2, Prp8, and Snu114 can be isolated from human U5 snRNP, and these three proteins interact functionally and genetically.
20519033	0.98	PRPC8 (human homolog of yeast pre-mRNA splicing factor C8), PRP31 (human homolog of yeast pre-mRNA splicing factor 31), HPRP3 (human homolog of yeast pre-mRNA splicing factor 3), PAP-1 (PIM-1 kinase), TOPORS (topoisomerase-I-binding arginine/serine-rich protein) and SNRNP200 (small nuclear ribonucleoprotein, 200 kDa) are associated with adRP, although the mechanisms behind the process remain unclear.
28768202	0.98	Prp8, snRNP200, Prp3, Prp4, and NHP2L1 (Table S2).
21080498	0.97	Prp8 are associated with a wide range of spliceosomal defects including alterations in the ability of spliceosomes to reject suboptimal splice sites and suppression of defects caused by mutations in other spliceosomal components, for example mutations in Prp28, Brr2, U4 and U6 snRNAs.
	0.97	Prp8-mediated regulation of the function of Brr2.
	0.96	Prp8/P220K, Brr2/200K, Snu114/116K, Prp6/102K, Prp28/100K, 40K, 15K and 52K in addition to the set of the seven common Sm proteins.
	0.96	Prp8, Brr2, Snu114, Prp6, Prp3 and Prp31 within the tri-snRNP.
	0.95	Prp8 which fall in this domain result in the hereditary blindness Retinitis Pigmentosa, and these mutations, once introduced into Prp8, result in weakening of the interaction of Prp8 with Brr2 and Snu114.
	0.94	Prp8 and Brr2, and thus may have additional roles in spliceosomal function.
	0.92	Prp8 interacts with several spliceosomal proteins including Snu114 and Brr2.
	0.88	Prp8, Prp28 and Brr2.
	0.80	Brr2, at least in vitro, is modulated by Snu114 and the C-terminal domain of Prp8, which also improves the binding of Brr2 to one of its targets, the U4/U6 basepaired complex.
28076437	0.97	PRPF8, RHO, RP1, SNRNP200, and TOPORS-associated adRP by the identification of 17 novel mutations.
	0.97	SNRNP200, PRPF8, PRPF31
	0.97	PRPF8, SNRNP200, and TOPORS genes, thereby expanding their molecular spectrum.
	0.96	BRR2 interacts extensively with the U5-specific protein PRPF8.
	0.94	PRPF8, RHO, RP1, SNRNP200, and TOPORS.
	0.90	SNRNP200, PRPF8, and PRPF31), one frameshift mutation in PRPH2, and one frameshift mutation in TOPORS.
	0.73	PRPF8, PRPF31 and SNRNP200) is high (altogether 19.8%).
24968230	0.97	Prp8/220K, Brr2/200K, Snu114/116K, Prp6/102K, Prp28/100K, Lin1/52K, SNRNP40/40K, and Dib1/15K.
	0.97	Prp8 also interacts with several spliceosomal proteins, including the RNA helicase Brr2, the GTPase Snu114, and Prp6 of the U5 snRNP.
	0.97	Prp8 provides a large platform for the RNA helicase Brr2, the GTPase Snu114, and Prp6 to form U5 snRNP complexes.
	0.93	Prp8, Brr2, Snu114, Prp6, and SNRNP40.
	0.90	Prp8, Brr2, Snu114, Prp6, and SNRNP40.
	0.83	Prp8 and could be pulled down with other components of U5 snRNPs, including Brr2, Snu114, Prp6, and SNRNP40, by Co-IP and WB analysis.
27302685	0.97	Prpf8, Prpf31, and SNRNP200/Brr2) and splicing factors (RP9 and DHX38).
	0.96	Prpf8 domain, which regulates SNRNP200 function, suggests that malfunction or ill-timing of SNRNP200 has a deleterious effect on splicing resulting in cell death.
	0.94	SNRNP200 unwinds U4/U6 snRNAs during spliceosome activation and the helicase activity is regulated by the C-terminus of Prpf8 and GTPase activity of EFTUD2 proteins.
	0.91	Prpf8-SNRNP200 interaction has a negative effect on helicase stimulation.
	0.91	SNRNP200 is a large nuclear protein of 200 kDa, which interacts extensively with U5-specific proteins EFTUD2 (hSnu114) and Prpf8.
28408981	0.97	Brr2 sitting on Prp8 (PDB ID 3jcr).
	0.97	Brr2 sits on the Jab1 domain of Prp8, but its orientation and contacts change during activation of the particle.
	0.97	Prp8's Jab1 domain has a C-terminal disordered tail that sneaks into the RNA tunnel of Brr2 to compete with U4 .
	0.93	Prp8 is entwined with other proteins and the snRNAs in this complex, even as it binds Brr2.
29144457	0.97	PRP8 and BRR2 (Extended Data Fig. 8G), consistent with previous studies suggesting it nominally serves as a spliceosome component.
	0.97	BRR2, or its partner PRP8, significantly reduced ASCC3 foci formation upon MMS damage (Extended Data Fig. 10F-G and Fig. 4F).
	0.96	BRR2, PRP8, and TFII-I had 2-3 fold higher total peptide numbers from cells exposed to MMS, suggesting an increased association with the ASCC complex in response to alkylation-induced damage.
	0.93	BRR2 and PRP8 upon alkylation damage (Fig. 1D-E).
26392272	0.97	BRR2 and EFTUD2, which interact directly with PRPF8 to form the U5 snRNP, most strongly phenocopy PRPF8 deficiency (Fig. 5b; Additional file 5b, c).
	0.96	BRR2 and EFTUD2, which interact directly with PRPF8 to form the U5 snRNP complex, phenocopy PRPF8 most strongly. Indeed, spliceosome activation and disassembly are regulated by both EFTUD2 and BRR2.
	0.96	PRPF8 and BRR2 are found in autosomal dominant retinitis pigmentosa.
28549094	0.97	PRPF8, RP1, TOPORS, and SNRNP200.
	0.95	PRPF8, RP1, TOPORS, and SNRNP200.
19098916	0.97	Prp8 contacts a region of the second helicase motif, specifically amino acids 1301 to 1816 in human Brr2 (ref.), in which case the stimulatory effect on unwinding is likely to be via an allosteric mechanism.
23354046	0.97	Prp8 forms a salt-stable complex with the EF2-like GTPase Snu114 and the DExD/H-box family helicase Brr2.
27627834	0.97	Prp8p-Aar2p interaction is disrupted upon Aar2p phosphorylation which represents the molecular switch between Aar2p and Brr2p binding to Prp8p.
32098976	0.97	SNRNP200 (E), MAK (F,I), PRPF8 (G), BBS1 (H), and SPATA7 (K).
19525970	0.96	hBrr2 and hPrp8 as well as hSnu114 have also been observed previously using yeast two-hybrid analyses.
	0.95	Prp8-CTR has a much higher binding affinity with a U2/U6 mimic than other RNAs, consistent with the possibility that Prp8 may also help Brr2 confer specificity toward U2/U6 to facilitate Brr2's role in U2/U6 unwinding.
17576664	0.96	p220 is human U5-220 (splicing factor Prp8 in yeast), p200 is human U5-200 (DEXH box RNA helicase, Brr2 in yeast), p116 is human U5-116 (a putative GTPase homologous to the ribosomal elongation factor EF-2, Snu114 in yeast).
25263594	0.96	PRPF8 and SNRNP200.
28379520	0.96	Brr2, an RNA helicase required for spliceosome activation, the GTPase Snu114, and the catalytic core scaffold protein Prp8, were identified as likely SUMO substrates.
28510639	0.96	PRPF8, RP2, SNRNP200, TRPM1
31126147	0.96	BRR2, together with PRPF31, PRPF3, PRPF6 and PRPF8, belongs to the group of splicing factors that are part of the U4/U6-U5 tri-snRNP complex and which, when mutated, cause adRP.
24959063	0.95	PRPF8, 1-4% for PRPF3, 1.6% for SNRNP200, and to be rare for PAP-1 and PRPF6, globally accounting for more than 12% of all adRP cases.
	0.69	PRPF8 (RP13; ID: 10594, OMIM 607300), PRPF31 (RP11; ID: 26121, OMIM 606419), PRPF3 (RP18; ID: 9129, OMIM 607301), PAP-1 (RP9; ID: 6100, OMIM 607331), SNRNP200 (RP33; ID: 23020, OMIM 601664), and PRPF6 (ID: 24148, OMIM 613979).
28045043	0.95	SNRNP200 (7) and PRPF8 (2), which code for core spliceosomal proteins, although a splice site mutation in RHO was also detected (2/29).
	0.74	SNRNP200 and PRPF8) but also due to splice-site mutations in RHO.
24940031	0.95	PRPF8, PRPF31, RP9, SNRNP200, PRPF6, and PRPF4.
24319334	0.93	Prp8 and that disease-associated mutations in Prp8 weaken binding to hBrr2.
27391102	0.93	SNRNP200 due to mutations in the C-terminus of PRPF8 has been hypothesized to be associated with PRPF8-linked RP.
31671093	0.93	PRPF8, PRPF31 and SNRNP200 (also called BRR2), that cause the autosomal dominant eye disease retinitis pigmentosa (adRP).
26118977	0.92	PRPF8, PRPF31 and SNRNP200 cause isolated retinitis pigmentosa (RP).
27058959	0.92	Brr2 by Prp8 and is important for spliceosomal B-complex activation.
25304133	0.89	PRPF8, PRPF31, and SNRNP200, are essential components of the U4/U6-U5 tri-snRNP complex of the spliceo-some involved in mRNA splicing.
28372848	0.86	Prp8-Brr2 and the U1 snRNP.
29995849	0.86	BRR2 helicase is held near SNU114 by the SAD1 protein and PRP28 is bound to the PRP8 N-terminal domain (PRP8N).
25383878	0.84	PRPF8, PRPF31 and SNRNP200, cause retinitis pigmentosa (RP), a disease characterized by progressive photoreceptor degeneration.
31216022	0.83	SNRNP200, EFTUD2, SNW1, PRPF8, PLRG1 and AQR also caused a reduction at POLR2A RNA and protein levels, but depletion of Prp19 or CDC5L showed no apparent effect on POLR2A protein expression (Figure 5C-F).
31570875	0.83	PRPF8, a protein that is essential for later stages of spliceosomal assembly, a role it plays together with EFTUD2 and BRR2 as part of U5 snRNP.
30967900	0.74	PRPF8, and SNRNP200, all of which are also genetic causes of RP.
28561026	0.63	PRPF8 and SNRNP200) and the TSC1-TSC2 complex (TSC1, TSC2 and TBC1D7).