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Fusion Protein:SFPQ-FAM134B |
Fusion Protein Summary |
Fusion gene summary |
Fusion partner gene information | Fusion gene name: SFPQ-FAM134B | FusionPDB ID: 81132 | FusionGDB2.0 ID: 81132 | Hgene | Tgene | Gene symbol | SFPQ | FAM134B | Gene ID | 654780 | 54463 |
Gene name | splicing factor proline/glutamine-rich | reticulophagy regulator 1 | |
Synonyms | SFPQ | FAM134B|JK-1|JK1 | |
Cytomap | 16q24.1 | 5p15.1 | |
Type of gene | ncRNA | protein-coding | |
Description | - | reticulophagy regulator 1family with sequence similarity 134 member Bprotein FAM134Breticulophagy receptor 1reticulophagy receptor FAM134B | |
Modification date | 20200303 | 20200313 | |
UniProtAcc | P23246 | . | |
Ensembl transtripts involved in fusion gene | ENST ids | ENST00000357214, ENST00000468598, | ENST00000399793, ENST00000509048, ENST00000306320, |
Fusion gene scores for assessment (based on all fusion genes of FusionGDB 2.0) | * DoF score | 14 X 16 X 8=1792 | 9 X 6 X 6=324 |
# samples | 19 | 10 | |
** MAII score | log2(19/1792*10)=-3.23749931372666 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | log2(10/324*10)=-1.6959938131099 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | |
Context (manual curation of fusion genes in FusionPDB) | PubMed: SFPQ [Title/Abstract] AND FAM134B [Title/Abstract] AND fusion [Title/Abstract] | ||
Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0) | SFPQ(35654603)-FAM134B(16572211), # samples:1 | ||
Anticipated loss of major functional domain due to fusion event. | SFPQ-FAM134B seems lost the major protein functional domain in Hgene partner, which is a CGC by not retaining the major functional domain in the partially deleted in-frame ORF. SFPQ-FAM134B seems lost the major protein functional domain in Hgene partner, which is a CGC by not retaining the major functional domain in the partially deleted in-frame ORF. SFPQ-FAM134B seems lost the major protein functional domain in Hgene partner, which is a essential gene by not retaining the major functional domain in the partially deleted in-frame ORF. SFPQ-FAM134B seems lost the major protein functional domain in Hgene partner, which is a essential gene by not retaining the major functional domain in the partially deleted in-frame ORF. |
* DoF score (Degree of Frequency) = # partners X # break points X # cancer types ** MAII score (Major Active Isofusion Index) = log2(# samples/DoF score*10) |
Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
Partner | Gene | GO ID | GO term | PubMed ID |
Fusion gene breakpoints across SFPQ (5'-gene) * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Fusion gene breakpoints across FAM134B (3'-gene) * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
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Fusion Gene Sample Information |
Fusion gene information from FusionGDB2.0. |
Fusion gene information from two resources (ChiTars 5.0 and ChimerDB 4.0) * All genome coordinats were lifted-over on hg19. * Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser. |
Source | Disease | Sample | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand |
ChimerDB4 | LGG | TCGA-HT-8110 | SFPQ | chr1 | 35654603 | - | FAM134B | chr5 | 16572211 | - |
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Fusion ORF Analysis |
Fusion information from ORFfinder translation from full-length transcript sequence from FusionPDB. |
Henst | Tenst | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand | Seq length (transcript) | BP loci (transcript) | Predicted start (transcript) | Predicted stop (transcript) | Seq length (amino acids) |
ENST00000357214 | SFPQ | chr1 | 35654603 | - | ENST00000306320 | FAM134B | chr5 | 16572211 | - | 4657 | 1796 | 87 | 2969 | 960 |
DeepORF prediction of the coding potential based on the fusion transcript sequence of in-frame fusion genes. DeepORF is a coding potential classifier based on convolutional neural network by comparing the real Ribo-seq data. If the no-coding score < 0.5 and coding score > 0.5, then the in-frame fusion transcript is predicted as being likely translated. |
Henst | Tenst | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand | No-coding score | Coding score |
ENST00000357214 | ENST00000306320 | SFPQ | chr1 | 35654603 | - | FAM134B | chr5 | 16572211 | - | 0.000461548 | 0.9995384 |
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Fusion Amino Acid Sequences |
For individual full-length fusion transcript sequence from FusionPDB, we ran ORFfinder and chose the longest ORF among the all predicted ones. |
>FusionGDB ID_FusionGDB isoform ID_FGname_Hgene_Hchr_Hbp_Henst_Tgene_Tchr_Tbp_Tenst_length(fusion AA) seq_BP >81132_81132_1_SFPQ-FAM134B_SFPQ_chr1_35654603_ENST00000357214_FAM134B_chr5_16572211_ENST00000306320_length(amino acids)=960AA_BP=569 MTTDMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQ PPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPT TPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGG RSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTP MRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVI VEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLR QDLMRRQEELRRMEELHNQEMQKRKEMQLRFLALTPWRVYHLISVMILGRVIMQIIKDMVLSRTRGAQLWRSLSESWEVINSKPDERPRL SHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGI GEYINQKKRERSEADKEKSHKDDSELDFSALCPKISLTVAAKELSVSDTDVSEVSWTDNGTFNLSEGYTPQTDTSDDLDRPSEEVFSRDL SDFPSLENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGLTLPLNSDQTFHLMSNLAGDVITAAVTAAIKDQLEGVQQALS -------------------------------------------------------------- |
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Fusion Protein Functional Features |
Four levels of functional features of fusion genes Go to FGviewer search page for the most frequent breakpoint (https://ccsmweb.uth.edu/FGviewer/chr1:35654603/chr5:16572211) - FGviewer provides the online visualization of the retention search of the protein functional features across DNA, RNA, protein, and pathological levels. - How to search 1. Put your fusion gene symbol. 2. Press the tab key until there will be shown the breakpoint information filled. 4. Go down and press 'Search' tab twice. 4. Go down to have the hyperlink of the search result. 5. Click the hyperlink. 6. See the FGviewer result for your fusion gene. |
Main function of each fusion partner protein. (from UniProt) |
Hgene | Tgene |
SFPQ | . |
FUNCTION: DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA (PubMed:25765647). The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (PubMed:25765647). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (By similarity). Required for the assembly of nuclear speckles (PubMed:25765647). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). {ECO:0000250|UniProtKB:Q8VIJ6, ECO:0000269|PubMed:10847580, ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:10931916, ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:25765647, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8045264, ECO:0000269|PubMed:8449401}. | FUNCTION: Might normally function as a transcriptional repressor. EWS-fusion-proteins (EFPS) may play a role in the tumorigenic process. They may disturb gene expression by mimicking, or interfering with the normal function of CTD-POLII within the transcription initiation complex. They may also contribute to an aberrant activation of the fusion protein target genes. |
Retention analysis result of each fusion partner protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
- Retained protein feature among the 13 regional features. |
Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Protein feature | Protein feature note |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 10_15 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gly |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 10_266 | 565.6666666666666 | 708.0 | Compositional bias | Note=Gln/Glu/Pro-rich |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 184_188 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Pro |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 20_27 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gly |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 56_65 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Pro |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 67_71 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gln |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 95_98 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gln |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 99_103 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Pro |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 297_369 | 565.6666666666666 | 708.0 | Domain | RRM 1 |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 371_452 | 565.6666666666666 | 708.0 | Domain | RRM 2 |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 9_27 | 565.6666666666666 | 708.0 | Region | Note=3 X 3 AA repeats of R-G-G |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 19_21 | 565.6666666666666 | 708.0 | Repeat | Note=2 |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 25_27 | 565.6666666666666 | 708.0 | Repeat | Note=3 |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 9_11 | 565.6666666666666 | 708.0 | Repeat | Note=1 |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 84_233 | 0 | 357.0 | Region | Reticulon homology domain | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 117_118 | 106.66666666666667 | 498.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 140_208 | 106.66666666666667 | 498.0 | Topological domain | Lumenal | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 230_497 | 106.66666666666667 | 498.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 117_118 | 0 | 357.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 140_208 | 0 | 357.0 | Topological domain | Lumenal | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 1_59 | 0 | 357.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 230_497 | 0 | 357.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 81_95 | 0 | 357.0 | Topological domain | Lumenal | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 119_139 | 106.66666666666667 | 498.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 209_229 | 106.66666666666667 | 498.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 119_139 | 0 | 357.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 209_229 | 0 | 357.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 60_80 | 0 | 357.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000399793 | 0 | 7 | 96_116 | 0 | 357.0 | Transmembrane | Helical |
- Not-retained protein feature among the 13 regional features. |
Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Protein feature | Protein feature note |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 497_596 | 565.6666666666666 | 708.0 | Coiled coil | Ontology_term=ECO:0000255,ECO:0000269 |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 571_574 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Arg |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 613_616 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gly |
Hgene | SFPQ | chr1:35654603 | chr5:16572211 | ENST00000357214 | - | 6 | 10 | 635_641 | 565.6666666666666 | 708.0 | Compositional bias | Note=Poly-Gly |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 84_233 | 106.66666666666667 | 498.0 | Region | Reticulon homology domain | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 1_59 | 106.66666666666667 | 498.0 | Topological domain | Cytoplasmic | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 81_95 | 106.66666666666667 | 498.0 | Topological domain | Lumenal | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 60_80 | 106.66666666666667 | 498.0 | Transmembrane | Helical | |
Tgene | FAM134B | chr1:35654603 | chr5:16572211 | ENST00000306320 | 0 | 9 | 96_116 | 106.66666666666667 | 498.0 | Transmembrane | Helical |
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Fusion Protein-Protein Interaction |
Go to ChiPPI (Chimeric Protein-Protein interactions) to see the chimeric PPI interaction in |
Protein-protein interactors with each fusion partner protein in wild-type from validated records (BIOGRID-3.4.160) |
Gene | PPI interactors |
SFPQ | NONO, FHL2, EXOSC5, HN1, SFPQ, UBC, PTBP1, TOP1, CDC5L, ZMYM2, SP1, SP3, HDAC1, HDAC2, SIN3A, NR3C1, PITX3, NR4A2, RAC1, SRRM1, SRRM2, Rxra, Nono, Sin3a, Thra, SMARCD1, SMARCA2, AR, TOPORS, MAPK1, PRKCI, TADA2A, POT1, SMN1, SNW1, Mapk13, STAT6, HDAC5, AI837181, Mki67, EBNA-LP, PPP1CA, SNRPA, U2AF2, SREK1, RAD21, CEBPA, ELAVL1, ARRB2, SIRT7, HNRNPA1, TSG101, NR2C1, CBLL1, CDK2, COPS5, AP2M1, PARK7, PPARGC1A, U2AF1, SF3B1, EFTUD2, TCERG1, HNRNPR, HNRNPC, SNRPA1, SRSF5, HNRNPM, SRSF7, SF3B3, SRSF3, SRSF4, SNRPD2, SF3A1, DDX21, PHF5A, SART1, HTATSF1, ILF3, TOP2B, HNRNPL, SLTM, SSR4, DNAJC19, TIMM10, TPR, STAG2, SON, THRAP3, SMC3, UTP14A, SMARCA5, TXN, ZC3HAV1, VTN, APEX1, UQCRFS1P1, TOMM40, TIMM9, TIMM23B, BTK, FN1, VCAM1, RNF43, CSNK2A1, SMAD5, ITGA4, PAN2, CD81, PARK2, PRPF40A, WBP4, APBB1, GAS7, PIN1, WWOX, rev, RPA3, RPA2, RPA1, ERG, ASB3, ASB12, ASB18, STAU1, MDM2, HUWE1, FUS, MOV10, NXF1, PPARG, HIST3H3, CUL7, OBSL1, CCDC8, UBE2I, EED, ESR1, ORC6, RPS6KB2, UNK, ACAT1, CARS, COX5A, DPH5, HNRNPA2B1, HNRNPA3, HNRNPD, IMMT, KHDRBS1, LMO7, NDUFS3, NUP210, PFKM, SERBP1, DDX17, PGK1, TARS, WBP11, UQCRC2, YTHDF2, SFN, NTRK1, SCARNA22, KRAS, MUS81, AHSA1, Lin7c, Tsc1, Rpl35, Cxxc1, CRY1, MCM2, MCM5, EGFR, RC3H1, ZNF746, RBMXL1, PSPC1, DIDO1, MMADHC, PRRC2A, EWSR1, LSM14A, FAM98A, DHPS, SYNCRIP, SMARCC1, PRMT5, SMARCC2, NCOA5, PRRC2C, ALYREF, SF1, RBM27, HIP1R, CYLD, CD2BP2, TRIM25, UBE2A, BRCA1, LMNA, PAWR, CTNNB1, PCBP1, CUL4B, UBE2M, PRPF8, AAR2, PIH1D1, TNIP2, YLPM1, NKX2-1, RNF4, CHD3, CHD4, TNF, RIOK1, BPLF1, FGF11, HEXIM1, MEPCE, LARP7, RUNX1, RNF123, AGR2, RECQL4, DCPS, TNRC6A, PIK3R1, RNF144A, REST, ZFP36L2, MYC, CDK9, TP53BP1, MDC1, KIAA1429, METTL3, METTL14, PSMA3, ACTC1, RAD51D, PHB, ARMC12, CHEK2, USP14, NR2C2, ZFYVE21, XRCC6, ATXN3, VRK1, SND1, HIST1H4A, DYRK1A, MAB21L2, SCARB2, SNRNP70, Dppa3, TAF15, MATR3, GSK3B, BIRC3, WWP2, ERCC6, PPIA, PLEKHA4, PINK1, FANCD2, HCVgp1, LINC01554, MIRLET7A1, MIRLET7A2, MIRLET7A3, MIRLET7B, MIRLET7C, MIRLET7D, MIRLET7E, MIRLET7F1, MIRLET7F2, MIRLET7G, MIRLET7I, MIR98, MIR1-1, MIR1-2, MIR7-1, MIR7-2, MIR7-3, MIR9-1, MIR9-2, MIR9-3, MIR10B, MIR15A, MIR15B, MIR16-1, MIR16-2, MIR17, MIR18A, MIR18B, MIR19A, MIR19B1, MIR19B2, MIR20A, MIR20B, MIR21, MIR25, MIR29A, MIR29B1, MIR29B2, MIR29C, MIR31, MIR34A, MIR34B, MIR34C, MIR92A1, MIR92A2, MIR93, MIR106A, MIR106B, MIR107, MIR122, MIR128-1, MIR128-2, MIR138-1, MIR138-2, MIR140, MIR141, MIR143, MIR145, MIR155, MIR199A1, MIR199A2, MIR200A, MIR200B, MIR200C, MIR205, MIR206, MIR214, MIR221, MIR222, MIR363, MIR429, MIR451A, VIM, NFKB1, ZC3H18, PRKD1, MTHFS, UTP20, WDR7, SLC12A2, ATP11C, IGFBP3, PRKDC, WAPAL, MAU2, LAMTOR5, CELF1, NEK4, DUX4, DUX4L9, CIT, CHMP4B, CHMP4C, KIF14, KIF20A, KIF23, PRC1, C8orf82, HNRNPH1, INS, NDN, BIN1, DHX9, HULC, ZNF263, BRD4, NUPR1, RBM45, CIC, Apc2, TARDBP, RBM39, FBP1, LGALS9, YWHAE, IFI16, WDR76, EIF3F, NEAT1, LOC100506753, vpr, EIF5A, RPL23A, NUDT21, NUFIP2, RPS19, NDC80, PPIL4, DDX42, TSPYL5, METTL17, CPSF7, PPP1R10, SP100, FAM76B, MKRN1, KDF1, DDX58, OGT, CD274, SPOP, UFL1, DDRGK1, TP53, TRIM37, ATG10, FZR1, FMR1, FXR1, FXR2, WDR5, NAA40, BGLT3, PTP4A3, ANKRD50, TMEM14B, TRIM68, LONP1, CYCS, BTF3, SLFN11, EP300, FBXW7, CTTN, CTBP1, DMRTB1, TFIP11, EXOSC8, CEP55, KRT31, SF3B4, Ewsr1, Rbm14, Pspc1, Cpsf6, Cstf2t, CCNF, HECTD1, nsp14, PER2, PEG10, |
Protein-protein interactors based on sequence similarity (STRING) |
Gene | STRING network |
SFPQ | |
FAM134B |
- Retained interactions in fusion protein (protein functional feature from UniProt). |
Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Still interaction with |
- Lost interactions due to fusion (protein functional feature from UniProt). |
Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Interaction lost with |
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Related Drugs to SFPQ-FAM134B |
Drugs used for this fusion-positive patient. (Manual curation of PubMed, 04-30-2022 + MyCancerGenome) |
Hgene | Tgene | Drug | Source | PMID |
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Related Diseases to SFPQ-FAM134B |
Diseases that have this fusion gene. (Manual curation of PubMed, 04-30-2022 + MyCancerGenome) |
Hgene | Tgene | Disease | Source | PMID |
Diseases associated with fusion partners. (DisGeNet 4.0) |
Partner | Gene | Disease ID | Disease name | # pubmeds | Source |
Hgene | SFPQ | C4518356 | MiT family translocation renal cell carcinoma | 2 | ORPHANET |
Hgene | SFPQ | C0019693 | HIV Infections | 1 | CTD_human |
Hgene | SFPQ | C0037274 | Dermatologic disorders | 1 | CTD_human |
Hgene | SFPQ | C0274861 | Arsenic Poisoning, Inorganic | 1 | CTD_human |
Hgene | SFPQ | C0274862 | Nervous System, Organic Arsenic Poisoning | 1 | CTD_human |
Hgene | SFPQ | C0311375 | Arsenic Poisoning | 1 | CTD_human |
Hgene | SFPQ | C0751851 | Arsenic Encephalopathy | 1 | CTD_human |
Hgene | SFPQ | C0751852 | Arsenic Induced Polyneuropathy | 1 | CTD_human |
Hgene | SFPQ | C4505456 | HIV Coinfection | 1 | CTD_human |