PRPF8 Data Analysis

HGNC Gene Name
pre-mRNA processing factor 8
HGNC Gene Symbol
PRPF8
Identifiers
hgnc:17340 NCBIGene:10594 uniprot:Q6P2Q9
Orthologs
mgi:2179381 rgd:1305467
INDRA Statements
deubiquitinations all statements
Pathway Commons
Search for PRPF8
Number of Papers
139 retrieved on 2022-05-22

DepMap Analysis

The Dependency Map (DepMap) is a genome-wide pooled CRISPR-Cas9 knockout proliferation screen conducted in more than 700 cancer cell lines spanning many different tumor lineages. Each cell line in the DepMap contains a unique barcode, and each gene knockout is assigned a “dependency score” on a per cell-line basis which quantifies the rate of CRISPR-Cas9 guide drop. It has been found that proteins with similar DepMap scores across cell lines, a phenomenon known as co-dependent genes, have closely related biological functions. This can include activity in the same or parallel pathways or membership in the same protein complex or the same pathway.

We identified the strongest seven co-dependent genes (“Symbol”) for DUBs and ran GO enrichment analysis. We used Biogrid, IntAct, and Pathway Commons PPIDs, and the NURSA protein-protein interaction databases (PPIDs) to determine whether co-dependent genes interact with one another. The “Evidence” column contains the PPIDs in which the interaction appears as well as whether there is support for the association by an INDRA statement. As another approach to identify potential interactors, we looked at proteomics data from the Broad Institute's Cancer Cell Line Encyclopedia (CCLE) for proteins whose expression across ~375 cell lines strongly correlated with the abundance of each DUB; it has previously been observed that proteins in the same complex are frequently significantly co-expressed. The correlations and associated p-values in the CCLE proteomics dataset are provided. And, we determined whether co-dependent genes yield similar transcriptomic signatures in the Broad Institute's Connectivity Map (CMap). A CMap score greater than 90 is considered significantly similar.

DepMap Correlations

Symbol Name DepMap Correlation Evidence CCLE Correlation CCLE Z-score CCLE p-value (adj) CCLE Significant CMAP Score CMAP Type
HNRNPK heterogeneous nuclear ribonucleoprotein K 0.472 INDRA (2) Reactome (4) -0.45 -2.57 8.90e-09
RAN RAN, member RAS oncogene family 0.47 Reactome (1) -0.31 -1.80 1.03e-08
PSMD7 proteasome 26S subunit, non-ATPase 7 0.44 Reactome (1) 0.04 0.11 6.18e-01
SNRNP200 small nuclear ribonucleoprotein U5 subunit 200 0.42 BioGRID IntAct INDRA (13) Reactome (5) 0.93 5.06 4.62e-166
SF3A1 splicing factor 3a subunit 1 0.418 BioGRID INDRA (1) Reactome (4) -0.06 -0.42 3.58e-01
PHF5A PHD finger protein 5A 0.41 Reactome (4) -0.34 -1.94 4.13e-10
SNRPB small nuclear ribonucleoprotein polypeptides B and B1 0.409 BioGRID INDRA (1) Reactome (5) -0.05 -0.34 5.13e-01

Dependency GO Term Enrichment

Gene set enrichment analysis was done on the genes correlated with PRPF8using the terms from Gene Ontology and gene sets derived from the Gene Ontology Annotations database via MSigDB.

Using the biological processes and other Gene Ontology terms from well characterized DUBs as a positive control, several gene set enrichment analyses were considered. Threshold-less methods like GSEA had relatively poor results. Over-representation analysis with a threshold of of the top 7 highest absolute value Dependency Map correlations yielded the best results and is reported below.

GO Identifier GO Name GO Type p-value p-value (adj.) q-value
GO:0005681 spliceosomal complex Cellular Component 1.42e-09 3.71e-07 1.84e-07
GO:0071013 catalytic step 2 spliceosome Cellular Component 1.43e-08 3.73e-06 9.24e-07
GO:0120114 Sm-like protein family complex Cellular Component 3.97e-08 1.04e-05 1.61e-06
GO:0005686 U2 snRNP Cellular Component 6.20e-08 1.62e-05 1.61e-06
GO:0000375 RNA splicing, via transesterification reactions Biological Process 6.21e-08 1.62e-05 1.61e-06
GO:0008380 RNA splicing Biological Process 1.75e-07 4.55e-05 3.77e-06
GO:0071011 precatalytic spliceosome Cellular Component 4.05e-07 1.06e-04 7.48e-06
GO:0005684 U2-type spliceosomal complex Cellular Component 2.79e-06 7.28e-04 4.51e-05
GO:0071010 prespliceosome Cellular Component 1.40e-05 3.65e-03 1.81e-04
GO:0022613 ribonucleoprotein complex biogenesis Biological Process 1.40e-05 3.65e-03 1.81e-04
GO:0005682 U5 snRNP Cellular Component 2.69e-05 7.01e-03 3.16e-04
GO:0005689 U12-type spliceosomal complex Cellular Component 4.08e-05 1.06e-02 4.40e-04
GO:0097526 spliceosomal tri-snRNP complex Cellular Component 1.05e-04 2.73e-02 1.04e-03
GO:0071826 ribonucleoprotein complex subunit organization Biological Process 1.15e-04 2.99e-02 1.06e-03

Transcriptomics

The following table shows the significantly differentially expressed genes after knocking out PRPF8 using CRISPR-Cas9.

Knockout Differential Expression

Symbol Name log2-fold-change p-value p-value (adj.)
HMGB2 high mobility group box 2 7.40e-01 2.26e-14 6.37e-11
ANKRD1 ankyrin repeat domain 1 6.05e-01 9.95e-14 1.40e-10
C4BPB complement component 4 binding protein beta 1.03e+00 1.06e-11 9.98e-09
MT-ND2 mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 2 4.02e-01 3.65e-10 2.57e-07
HMGB3 high mobility group box 3 4.71e-01 1.52e-08 8.59e-06
PDRG1 p53 and DNA damage regulated 1 7.56e-01 6.25e-08 2.93e-05
SAT1 spermidine/spermine N1-acetyltransferase 1 5.66e-01 8.44e-08 3.40e-05
G0S2 G0/G1 switch 2 -4.83e-01 2.10e-07 7.41e-05
MT-ATP8 mitochondrially encoded ATP synthase membrane subunit 8 6.96e-01 3.60e-07 1.13e-04
MRPS16 mitochondrial ribosomal protein S16 -5.26e-01 1.95e-06 5.49e-04
SRP9 signal recognition particle 9 -4.61e-01 2.85e-06 7.30e-04
SART3 spliceosome associated factor 3, U4/U6 recycling protein 7.08e-01 7.35e-06 1.72e-03
EIF4A2 eukaryotic translation initiation factor 4A2 4.92e-01 1.11e-05 2.08e-03
RND3 Rho family GTPase 3 6.65e-01 1.07e-05 2.08e-03
SLC25A5 solute carrier family 25 member 5 -2.99e-01 1.10e-05 2.08e-03
PSMB4 proteasome 20S subunit beta 4 -4.28e-01 1.73e-05 3.04e-03
UQCC2 ubiquinol-cytochrome c reductase complex assembly factor 2 -4.03e-01 1.94e-05 3.21e-03
UQCRH ubiquinol-cytochrome c reductase hinge protein 3.22e-01 2.09e-05 3.26e-03
FDPS farnesyl diphosphate synthase -4.42e-01 2.31e-05 3.27e-03
WDR83OS WD repeat domain 83 opposite strand 2.93e-01 2.32e-05 3.27e-03
EIF3K eukaryotic translation initiation factor 3 subunit K -4.23e-01 3.86e-05 5.11e-03
MT-ND1 mitochondrially encoded NADH:ubiquinone oxidoreductase core subunit 1 2.56e-01 3.99e-05 5.11e-03
ARF1 ADP ribosylation factor 1 4.08e-01 4.50e-05 5.28e-03
RBM39 RNA binding motif protein 39 3.77e-01 4.32e-05 5.28e-03
C4orf3 chromosome 4 open reading frame 3 3.42e-01 4.90e-05 5.52e-03
JMJD1C jumonji domain containing 1C 6.13e-01 5.74e-05 6.22e-03
FADS1 fatty acid desaturase 1 -5.68e-01 6.01e-05 6.27e-03
MTCO1P12 MT-CO1 pseudogene 12 3.37e-01 6.65e-05 6.69e-03
VPS29 VPS29 retromer complex component -3.76e-01 8.36e-05 8.12e-03
AKR1B1 aldo-keto reductase family 1 member B 3.44e-01 1.21e-04 1.12e-02
ARL6IP4 ADP ribosylation factor like GTPase 6 interacting protein 4 -6.08e-01 1.24e-04 1.12e-02
BDNF brain derived neurotrophic factor 6.24e-01 1.57e-04 1.34e-02
DDX55 DEAD-box helicase 55 5.58e-01 1.56e-04 1.34e-02
SF3B1 splicing factor 3b subunit 1 4.63e-01 2.06e-04 1.70e-02
CBX5 chromobox 5 4.94e-01 2.12e-04 1.71e-02
TM4SF1 transmembrane 4 L six family member 1 3.54e-01 2.19e-04 1.72e-02
CKS2 CDC28 protein kinase regulatory subunit 2 3.60e-01 2.70e-04 2.05e-02
UQCRC1 ubiquinol-cytochrome c reductase core protein 1 -3.82e-01 2.81e-04 2.08e-02
EIF3B eukaryotic translation initiation factor 3 subunit B -6.68e-01 3.18e-04 2.30e-02
VDAC2 voltage dependent anion channel 2 3.30e-01 3.26e-04 2.30e-02
ANXA3 annexin A3 -4.55e-01 3.43e-04 2.30e-02
LPXN leupaxin -5.43e-01 3.40e-04 2.30e-02
SLC3A2 solute carrier family 3 member 2 5.47e-01 3.65e-04 2.39e-02
RRM2 ribonucleotide reductase regulatory subunit M2 -5.45e-01 3.83e-04 2.40e-02
VIM vimentin -3.48e-01 3.84e-04 2.40e-02
MT-CO1 mitochondrially encoded cytochrome c oxidase I 3.56e-01 4.13e-04 2.49e-02
RNASEH2A ribonuclease H2 subunit A -3.78e-01 4.16e-04 2.49e-02
PIGN phosphatidylinositol glycan anchor biosynthesis class N 5.48e-01 5.24e-04 3.07e-02
MRPL24 mitochondrial ribosomal protein L24 -3.90e-01 5.58e-04 3.12e-02
PRPF8 pre-mRNA processing factor 8 -6.57e-01 5.47e-04 3.12e-02
SRGN serglycin 4.40e-01 5.65e-04 3.12e-02
DNAJA1 DnaJ heat shock protein family (Hsp40) member A1 2.62e-01 6.16e-04 3.19e-02
KRT19 keratin 19 -3.19e-01 6.25e-04 3.19e-02
MTCH2 mitochondrial carrier 2 -3.32e-01 6.34e-04 3.19e-02
POLR1C RNA polymerase I and III subunit C 4.43e-01 6.18e-04 3.19e-02
SRSF6 serine and arginine rich splicing factor 6 -4.29e-01 6.11e-04 3.19e-02
CLPP caseinolytic mitochondrial matrix peptidase proteolytic subunit -5.77e-01 6.86e-04 3.28e-02
SEC22B SEC22 homolog B, vesicle trafficking protein -4.74e-01 6.83e-04 3.28e-02
SYF2 SYF2 pre-mRNA splicing factor 4.03e-01 6.70e-04 3.28e-02
RBBP8 RB binding protein 8, endonuclease -6.72e-01 7.22e-04 3.39e-02
TMOD3 tropomodulin 3 5.35e-01 7.58e-04 3.50e-02
PSMB5 proteasome 20S subunit beta 5 2.83e-01 7.74e-04 3.52e-02
EXOSC7 exosome component 7 4.22e-01 7.91e-04 3.54e-02
EIF4E2 eukaryotic translation initiation factor 4E family member 2 4.56e-01 8.65e-04 3.67e-02
RBM8A RNA binding motif protein 8A 2.51e-01 8.39e-04 3.67e-02
RPL6 ribosomal protein L6 6.04e-01 8.72e-04 3.67e-02
TUBG1 tubulin gamma 1 -3.70e-01 8.73e-04 3.67e-02
AK2 adenylate kinase 2 3.10e-01 9.03e-04 3.68e-02
RPS25 ribosomal protein S25 2.35e-01 9.01e-04 3.68e-02
MTCO3P12 MT-CO3 pseudogene 12 3.11e-01 9.24e-04 3.72e-02
H6PD hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase -6.16e-01 9.67e-04 3.73e-02
PTRH2 peptidyl-tRNA hydrolase 2 3.82e-01 9.61e-04 3.73e-02
YTHDC1 YTH domain containing 1 4.75e-01 9.41e-04 3.73e-02
CBWD1 COBW domain containing 1 4.46e-01 9.93e-04 3.77e-02
DDX39A DExD-box helicase 39A -4.38e-01 1.00e-03 3.77e-02
CBWD5 COBW domain containing 5 3.98e-01 1.04e-03 3.81e-02
PHLDA1 pleckstrin homology like domain family A member 1 -3.54e-01 1.03e-03 3.81e-02
MYL12B myosin light chain 12B 2.22e-01 1.08e-03 3.89e-02
TP53 tumor protein p53 3.94e-01 1.10e-03 3.93e-02
MRPL37 mitochondrial ribosomal protein L37 -5.91e-01 1.14e-03 4.00e-02
ANKRD11 ankyrin repeat domain 11 3.42e-01 1.16e-03 4.05e-02
ZFX zinc finger protein X-linked 5.14e-01 1.18e-03 4.06e-02
CEBPZ CCAAT enhancer binding protein zeta 4.86e-01 1.24e-03 4.19e-02
ITGA3 integrin subunit alpha 3 -5.60e-01 1.28e-03 4.28e-02
RSRC2 arginine and serine rich coiled-coil 2 3.68e-01 1.29e-03 4.28e-02
SLU7 SLU7 homolog, splicing factor 5.34e-01 1.31e-03 4.30e-02
CAV1 caveolin 1 3.22e-01 1.38e-03 4.41e-02
TSG101 tumor susceptibility 101 -6.41e-01 1.37e-03 4.41e-02
MTND1P23 MT-ND1 pseudogene 23 2.55e-01 1.43e-03 4.42e-02
SDC1 syndecan 1 -5.31e-01 1.43e-03 4.42e-02
SEC61G SEC61 translocon subunit gamma 2.42e-01 1.44e-03 4.42e-02
SNRPD1 small nuclear ribonucleoprotein D1 polypeptide 2.04e-01 1.41e-03 4.42e-02
PRPS2 phosphoribosyl pyrophosphate synthetase 2 -5.65e-01 1.48e-03 4.47e-02
DMAC2L distal membrane arm assembly component 2 like -6.54e-01 1.50e-03 4.50e-02
C15orf48 chromosome 15 open reading frame 48 -4.92e-01 1.54e-03 4.53e-02
MCM7 minichromosome maintenance complex component 7 -5.23e-01 1.54e-03 4.53e-02
LSM3 LSM3 homolog, U6 small nuclear RNA and mRNA degradation associated 2.50e-01 1.56e-03 4.54e-02
AK4 adenylate kinase 4 4.61e-01 1.65e-03 4.66e-02
DDX1 DEAD-box helicase 1 -4.15e-01 1.70e-03 4.66e-02
PIH1D1 PIH1 domain containing 1 -4.60e-01 1.69e-03 4.66e-02
RFXANK regulatory factor X associated ankyrin containing protein -6.05e-01 1.64e-03 4.66e-02
SARNP SAP domain containing ribonucleoprotein 3.66e-01 1.66e-03 4.66e-02
SERPINE1 serpin family E member 1 -4.36e-01 1.70e-03 4.66e-02
UBXN4 UBX domain protein 4 -4.27e-01 1.80e-03 4.88e-02
PWP1 PWP1 homolog, endonuclein -3.97e-01 1.82e-03 4.89e-02
COIL coilin 4.82e-01 1.86e-03 4.94e-02

Gene Set Enrichment Analysis

There were too few differentially expressed genes to run a meaningful GSEA.

Literature Mining

INDRA was used to automatically assemble known mechanisms related to PRPF8 from literature and knowledge bases. The first section shows only DUB activity and the second shows all other results.

Deubiquitinase Activity

Other Statements

psp cbn pc bel_lc signor biogrid lincs_drug tas hprd trrust ctd vhn pe drugbank omnipath conib crog dgi | rlimsp isi tees geneways eidos trips medscan sparser reach
PRPF8 affects SNRNP200
| 3 3
PRPF8 inhibits SNRNP200.
| 3 1
| 3 1

sparser
Given the mechanistic analogy between histone mRNA processing and splicing, we thus envisage that SLBP ubiquitylation may suppress hPrp43 helicase activity in histone mRNA processing similar to Prp8 u[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]

sparser
In humans, phosphorylation of Prp6 that occurs after the tri-snRNP being integrated into the B-complex may release the inhibition of Brr2 by Prp8 and is important for spliceosomal B-complex activation [ xref , xref ].

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The RNase H domain of 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 XREF_BIBR - XREF_BIBR.

sparser
A model was proposed in which inhibition of Brr2 by the ubiquitinated Prp8 leads to spliceosome assembly and stabilization of the triple snRNP (U4/U6–U5).
| PMC
PRPF8 activates SNRNP200.
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Although it has been demonstrated that the PRPF8 RNase H domain inhibits SNRNP200 activity and GTP bound EFTUD2 and that the C-terminus of PRPF8 induces the activation of SNRNP200 XREF_BIBR - XREF_BIBR, the detailed molecular mechanisms of the activation of SNRNP200 remains to be determined.

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The RNase H domain of 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 XREF_BIBR - XREF_BIBR.
| 4
| 4

eidos
Functionally , the loss of Prp8 may specifically inhibit cell viability and metastasis and activated EMT and PI3K / Akt in HCC cells .

eidos
Upregulation of Prp8 promoted cell viability and migration in a human hepatic astrocyte line .

eidos
The upregulation of Prp8 promoted cell viability , metastasis and the activity of the PI3K / Akt pathway in hepatic astrocytes cells and HCC cells .

eidos
Upregulation of Prp8 promoted cell viability and migration in HCC cells .
17alpha-ethynylestradiol increases the amount of PRPF8.
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17alpha-ethynylestradiol increases the amount of PRPF8. 3 / 3
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ctd
No evidence text available

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No evidence text available

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No evidence text available
17alpha-ethynylestradiol decreases the amount of PRPF8.
1 |
17alpha-ethynylestradiol decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
PRPF8 affects PLIN2
| 3
PRPF8 activates PLIN2. 3 / 3
| 3

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PRPF8 C-terminal mutations cause an early onset and severe form of adRP, and structural analysis of this region shows that it inserts into the RNA binding tunnel of the SNRNP200 helicase.

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Nine mutations, six of which are novel, in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31, causing adRP have been identified in the Spanish population.

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Relevant to both these interpretations is the observation that adRP linked to chromosome 17p is caused by mutations in PRPC8 (McKie et al., 2001), the human ortholog of yeast splicing factor Prp8p (Br[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]

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We show that PRPF8 lesions lead to neomorphic spliceosomal activity and increased cellular proliferation resulting in a distinct phenotype of aggressive myeloid malignancies with increased RS.

eidos
( C ) The expression location of Prp8 was explored via immunofluorescence ( D ) CCK8 assay revealed that loss of Prp8 reduced cell proliferation .

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Unlike SF3B1, XREF_BIBR, XREF_BIBR PRPF8 knockdown leads to increased cellular proliferation and increased clonogenicity.
PRPF8 affects ISPH
| 3
PRPF8 inhibits ISPH.
| 2
PRPF8 inhibits ISPH. 2 / 2
| 2

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Depletion of PRPF8 and treatment with a small molecule spliceosome inhibitor (PlaB) disrupts HDR, SSA, and end resection.

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Using two independent siRNAs targeting PRPF8 (siPRPF8-2, siPRPF8-4), as well as a previously described siRNA targeting XAB2 (siXAB2-4), we found that PRPF8 and XAB2 depletion cause a significantly greater decrease in the frequency of HDR and SSA, compared to EJ.
PRPF8 activates ISPH.
| 1
PRPF8 activates ISPH. 1 / 1
| 1

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We also found that transient expression of a myc tagged siRNA resistant PRPF8 rescued the HDR and SSA defects caused by siPRPF8-2 treatment.
| 1 1
| 1 1

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Furthermore, PRPF8, AKAP9, UVRAG, HDAC10 and NFE2L1 are known to mediate the immune response.

eidos
Furthermore , PRPF8 , AKAP9 , UVRAG , HDAC10 and NFE2L1 are known to mediate the immune response .
PRPF8 affects cell death
| 2
| 2

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Knockdown of SF3B1, PRPF8, UBL5 and USP39 increased cell death in all cSCC cell lines.

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Knockdown of c-MYC attenuated cell death caused by depletion of PRPF8 or SF3B1 in SCCRDEBMet cells and depletion of PRPF8 in SCCRDEB4 cells.

eidos
Functionally , the loss of Prp8 may specifically inhibit cell viability and metastasis and activated EMT and PI3K / Akt in HCC cells .

eidos
The upregulation of Prp8 promoted cell viability , metastasis and the activity of the PI3K / Akt pathway in hepatic astrocytes cells and HCC cells .
PRPF8 affects Bloc1s3
| 2
PRPF8 activates Bloc1s3. 2 / 2
| 2

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For example, a previous study suggested that mutations in PRPF8 may cause RP by disrupting the nuclear association of Brr2p with the U5 snRNP and, consequently, the assembly of the triple snRNP.

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Herein, we sought to correlate the retinal cell-type-specific disease phenotype with the splicing profile shown by a patient with autosomal recessive RP, caused by a mutation in pre-mRNA splicing factor 8 (PRPF8).
| 2

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Interestingly, in contrast to its stimulation of Brr2 helicase activity, the wild-type Prp8 fragment actually inhibited the RNA-dependent ATPase activity of Brr2.

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WT Brr2 also demonstrates RNA stimulated ATPase activity which is inhibited by Prp8-CTR ( xref ).
2 |

ctd
No evidence text available

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No evidence text available
Vinclozolin affects PRPF8
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Vinclozolin increases the amount of PRPF8.
1 |
Vinclozolin increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
Vinclozolin decreases the amount of PRPF8.
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Vinclozolin decreases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
Permethrin affects PRPF8
2 |
Permethrin increases the amount of PRPF8.
1 |
Permethrin increases the amount of PRPF8. 1 / 1
1 |

ctd
No evidence text available
Permethrin decreases the amount of PRPF8.
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Permethrin decreases the amount of PRPF8. 1 / 1
1 |

ctd
No evidence text available
PRPF8 affects RO60
| 2
PRPF8 inhibits RO60.
| 1
PRPF8 inhibits RO60. 1 / 1
| 1

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Using two independent siRNAs targeting PRPF8 (siPRPF8-2, siPRPF8-4), as well as a previously described siRNA targeting XAB2 (siXAB2-4), we found that PRPF8 and XAB2 depletion cause a significantly greater decrease in the frequency of HDR and SSA, compared to EJ.
PRPF8 activates RO60.
| 1
PRPF8 activates RO60. 1 / 1
| 1

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We also found that transient expression of a myc tagged siRNA resistant PRPF8 rescued the HDR and SSA defects caused by siPRPF8-2 treatment.
1 |
Valproic acid decreases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
Tungsten affects PRPF8
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Tungsten decreases the amount of PRPF8. 1 / 1
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No evidence text available
Trimellitic anhydride increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
1 |
Trichostatin A decreases the amount of PRPF8. 1 / 1
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No evidence text available
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Thapsigargin increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
1 |
Selenium atom increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
Resveratrol affects PRPF8
1 |
Resveratrol decreases the amount of PRPF8. 1 / 1
1 |

ctd
No evidence text available
1 |
Phenobarbital increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
1 |
Nickel dichloride increases the amount of PRPF8. 1 / 1
1 |

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No evidence text available
Miconazole affects PRPF8
1 |
Miconazole increases the amount of PRPF8. 1 / 1
1 |

ctd
No evidence text available
1 |
Methapyrilene decreases the amount of PRPF8. 1 / 1
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No evidence text available
Indometacin affects PRPF8
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Indometacin decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
1 |
Hsa-miR-93-5p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-93-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-92a-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-615-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-532-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
Hsa-miR-484 affects PRPF8
1 |
Hsa-miR-484 decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-409-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-381-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-361-5p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-324-5p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-296-3p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-27b-3p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-25-3p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-218-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-196a-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
1 |
Hsa-miR-193b-3p decreases the amount of PRPF8. 1 / 1
1 |

biopax:mirtarbase
No evidence text available
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Hsa-miR-186-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-17-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
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Hsa-miR-16-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-140-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-10b-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-10a-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-106a-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-let-7e-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-let-7c-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-let-7b-5p decreases the amount of PRPF8. 1 / 1
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biopax:mirtarbase
No evidence text available
Hexabromocyclododecane increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Glyphosate affects PRPF8
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Glyphosate decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Gentamycin affects PRPF8
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Gentamycin increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Genistein affects PRPF8
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Genistein decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
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Fumonisin B1 decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
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Fluoranthene decreases the amount of PRPF8. 1 / 1
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ctd
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Disodium selenite increases the amount of PRPF8. 1 / 1
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ctd
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Dicrotophos affects PRPF8
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Dicrotophos increases the amount of PRPF8. 1 / 1
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ctd
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Diarsenic trioxide increases the amount of PRPF8. 1 / 1
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ctd
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Dexamethasone decreases the amount of PRPF8. 1 / 1
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ctd
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Crocidolite asbestos increases the amount of PRPF8. 1 / 1
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ctd
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Copper(II) chloride decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Cisplatin affects PRPF8
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Cisplatin decreases the amount of PRPF8. 1 / 1
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ctd
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Cadmium dichloride increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Bisphenol F affects PRPF8
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Bisphenol F decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Bisphenol A affects PRPF8
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Bisphenol A increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
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Benzo[a]pyrene increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Benzene affects PRPF8
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Benzene increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
Ametryn affects PRPF8
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Ametryn decreases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
All-trans-retinoic acid increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
SNRNP200 affects PRPF8
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SNRNP200 deubiquitinates PRPF8. 1 / 1
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Following de-ubiquitination of Prp8, Brr2 is free to promote unwinding of U4/U6, resulting in activation of the spliceosome [48].
| PMC

reach
For localization studies of PRPF8 and XAB2, cells were treated with 10 Gy of IR, but allowed to recover for 30 min, and were treated with pre-extraction buffer (20 mM HEPES, 50 mM NaCl, 1 mM EDTA, 3 mM MgCl2, 300 mM sucrose, 0.25% Triton-X 100) just prior to fixation.
RRM1 affects PRPF8
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RRM1 activates PRPF8. 1 / 1
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PRPF8, SNRNP200, GTPBP4, SMCHD1, DHX15, PRPF6, A8KAP3, DHX9 and EPRS were significantly reduced by RRM1 or ZnF1 deletion with no trend of> 2-fold for any other deletion mutant (Supplemental Table S4).
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PRPF8 bound to 3D inhibits mRNA processing. 1 / 1
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In the case of picornaviruses, it has been shown recently that the viral polymerase 3D binds to PRPF8, a core components of U5, and blocks mRNA maturation, with the consequent accumulation of the lariat intermediate [XREF_BIBR].

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The recent discovery of a small molecule inhibitor of the Prp8 intein that selectively inhibits splicing without targeting proteases and inhibits the growth of intein-containing C. gattii and C. neoformans is a particularly exciting breakthrough that suggests intein inhibitors may have therapeutic benefits (Li et al., 2021).

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Depletion of p53 binding protein 1 (53BP1) suppressed the HR defect induced by both BRCA1 loss and PRPF8 knockdown, suggesting that PRPF8 functions during HR at least in part via facilitating BRCA1 function.
| PMC

eidos
Prp8 activates EMT in HCC .

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However, this is not a general case because the Y2334N and F2314L mutations in PRPF8 do not block snRNP biogenesis while affecting splicing, similar to two RP mutations in the SNRNP200 gene.
PRPF8 affects cas9
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PRPF8 activates cas9. 1 / 1
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Fibroblasts from a patient with splicing factor retinitis pigmentosa caused by a missense mutation in the PRPF8 splicing factor were used to produce three diseased and three CRISPR and Cas9 corrected induced pluripotent stem cell (iPSC) clones.
PRPF8 affects TP53
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PRPF8 inhibits TP53. 1 / 1
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Mechanistically, loss of function mutations in zebrafishPRPF8 have been shown to result in missplicing of TP53, 36 while PRPF8 knockdown in mammalian cells led to increased compensatory transcriptional activity of TP53, 39 suggesting another possibility of synergetic interaction between PRPF8 defects and TP53.
PRPF8 affects RPS3
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Mutated PRPF8 inhibits RPS3. 1 / 1
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These RPE abnormalities are more severe in the homozygous Prpf3-T494M and Prpf8-H2309P mice, suggesting that RP18 and RP13 are caused by the gain-of-function or dominant negative effect of Prpf3 and Prpf8 mutations.
| PMC
PRPF8 affects RPL6B
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Mutated PRPF8 inhibits RPL6B. 1 / 1
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These RPE abnormalities are more severe in the homozygous Prpf3-T494M and Prpf8-H2309P mice, suggesting that RP18 and RP13 are caused by the gain-of-function or dominant negative effect of Prpf3 and Prpf8 mutations.
| PMC
PRPF8 affects RPE
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PRPF8 activates RPE. 1 / 1
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Graziotto et al. and Farkas et al. demonstrated that PRPF3, PRPF8 and PRPF31 mutations could cause dysfunction of RPE XREF_BIBR XREF_BIBR.
PRPF8 affects RHO
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PRPF8 activates RHO. 1 / 1
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It can be speculated that there is a convergent pathogenic mechanism caused by RHO haploinsufficiency, with a lack of rhodopsin due to an untranslated mutated protein and an insufficient RHO splicing rate caused by a mutation in PRPF8.
PRPF8 affects PRPF31
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PRPF8 activates PRPF31. 1 / 1
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Mutations of the splicing factor genes PRPF31, PRPF8, and HPRP3 cause RP11, 13, and 18, respectively (Baehr and Chen, 2001; Chakarova et al., 2002).
PRPF8 affects PRPF3
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PRPF8 activates PRPF3. 1 / 1
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The recent identification of mutations in human splicing factors, PRPF31 and PRPC8, led us to screen HPRP3 as a candidate in three chromosome 1q linked families.
PRPF8 affects MT-ATP6
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PRPF8 activates MT-ATP6. 1 / 1
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eidos
Interestingly , while Snu114p / EFTUD2 interacts with both Brr2p / SNRNP200 and Prp8p / PRPF8 , EFTUD2 is associated with a craniofacial phenotype while SNRNP200 and PRPF8 both cause RP ( Figure 1 ) .
PRPF8 affects MCL1
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PRPF8 increases the amount of MCL1. 1 / 1
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Mcl1 protein expression was reduced by knockdown of UBL5, SART1 or PRPF8 in Mcl1 dependent cells (in contrast to PSMD14 knockdown that led to Mcl1 accumulation, XREF_FIG).
PRPF8 affects IVNS1ABP
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PTBP1, NHP2L1, SNRP70, SF3B1, SF3A1, CLK1, UAP56, p14, and PRPF8 are necessary to splice NS1 and NEP and M1/M2 pre-mRNAs.
PRPF8 affects Histone_H4
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In cells where HiNF-P and p220(NPAT) do not activate the H4 gene promoter, HiNF-P instead represses transcription.
PRPF8 affects EFTUD2
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PRPF8 activates EFTUD2. 1 / 1
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Depletion of U5 proteins and PRPF8 RP mutation both increase the association of PRPF8 and EFTUD2 with R2TP.
PRPF8 affects DUX4
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PRPF8 inhibits DUX4. 1 / 1
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eidos
We therefore experimentally tested whether PRPF8 inhibition induced DUX4 expression .
PRPF8 affects DDR1
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PRPF8 activates DDR1. 1 / 1
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PTBP1, NHP2L1, SNRP70, SF3B1, SF3A1, CLK1, UAP56, p14, and PRPF8 are necessary to splice NS1 and NEP and M1/M2 pre-mRNAs.
PRPF31 affects PRPF8
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PRPF31 activates PRPF8. 1 / 1
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Ubiquitination of Prp31 increases its affinity for Prp8 and this PTM is reversed by USP15.
| PMC
PITX2 affects PRPF8
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PITX2 decreases the amount of PRPF8. 1 / 1
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biopax:msigdb
No evidence text available
PBRM1 affects PRPF8
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Modified PBRM1 increases the amount of PRPF8. 1 / 1
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Among the different viral proteins, expression of either the viral NS1 or PB1 gene could upregulate the PRPF8 expression.
N-methyl-4-phenylpyridinium increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
MLN7243 affects PRPF8
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MLN7243 desumoylates PRPF8. 1 / 1
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ctd
No evidence text available
IVNS1ABP affects PRPF8
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Modified IVNS1ABP increases the amount of PRPF8. 1 / 1
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Among the different viral proteins, expression of either the viral NS1 or PB1 gene could upregulate the PRPF8 expression.
HSP90 affects PRPF8
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HSP90 increases the amount of PRPF8. 1 / 1
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First, inhibiting HSP90 leads to decreased levels of PRPF8 and SNRNP200.
GDF15 affects PRPF8
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GDF15 inhibits PRPF8. 1 / 1
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We also found that PlaB treatment caused a disruption of PRPF8 and XAB2 localization in interchromatin granules.
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Dietary Fats increases the amount of PRPF8. 1 / 1
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ctd
No evidence text available
CZF1 affects PRPF8
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CZF1 activates PRPF8. 1 / 1
| 1

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PRPF8, SNRNP200, GTPBP4, SMCHD1, DHX15, PRPF6, A8KAP3, DHX9 and EPRS were significantly reduced by RRM1 or ZnF1 deletion with no trend of> 2-fold for any other deletion mutant (Supplemental Table S4).
Bloc1s3 affects PRPF8
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Bloc1s3 activates PRPF8. 1 / 1
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This brings the known RP causing mutations in PRPF8 to nineteen.
ACPs affects PRPF8
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ACPs activates PRPF8. 1 / 1
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DNA amplifications of ACPs 5, 7, and 9 produced PRPF8, while amplification of ACP 8 yielded RPLP1.
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ctd
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ctd
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ctd
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ctd
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ctd
No evidence text available