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Fusion gene ID: 36034 |
FusionGeneSummary for SRPK1_SRPK1 |
 Fusion gene summary |
| Fusion gene information | Fusion gene name: SRPK1_SRPK1 | Fusion gene ID: 36034 | Hgene | Tgene | Gene symbol | SRPK1 | SRPK1 | Gene ID | 6732 | 6732 |
| Gene name | SRSF protein kinase 1 | SRSF protein kinase 1 | |
| Synonyms | SFRSK1 | SFRSK1 | |
| Cytomap | 6p21.31 | 6p21.31 | |
| Type of gene | protein-coding | protein-coding | |
| Description | SRSF protein kinase 1SFRS protein kinase 1SR-protein-specific kinase 1serine/arginine-rich splicing factor kinase 1serine/threonine-protein kinase SRPK1 | SRSF protein kinase 1SFRS protein kinase 1SR-protein-specific kinase 1serine/arginine-rich splicing factor kinase 1serine/threonine-protein kinase SRPK1 | |
| Modification date | 20180523 | 20180523 | |
| UniProtAcc | Q96SB4 | Q96SB4 | |
| Ensembl transtripts involved in fusion gene | ENST00000373825, ENST00000423325, ENST00000373822, ENST00000373821, | ENST00000373825, ENST00000423325, ENST00000373822, ENST00000373821, | |
| Fusion gene scores | * DoF score | 13 X 7 X 11=1001 | 2 X 2 X 2=8 |
| # samples | 13 | 2 | |
| ** MAII score | log2(13/1001*10)=-2.94485844580754 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | log2(2/8*10)=1.32192809488736 | |
| Context | PubMed: SRPK1 [Title/Abstract] AND SRPK1 [Title/Abstract] AND fusion [Title/Abstract] | ||
| Functional or gene categories assigned by FusionGDB annotation | |||
| * 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 |
| Hgene | SRPK1 | GO:0006468 | protein phosphorylation | 9237760|11509566 |
| Hgene | SRPK1 | GO:0007059 | chromosome segregation | 15034300 |
| Hgene | SRPK1 | GO:0035556 | intracellular signal transduction | 11509566 |
| Hgene | SRPK1 | GO:0045070 | positive regulation of viral genome replication | 20498328 |
| Hgene | SRPK1 | GO:0045071 | negative regulation of viral genome replication | 12417631 |
| Hgene | SRPK1 | GO:0050684 | regulation of mRNA processing | 8208298 |
| Tgene | SRPK1 | GO:0006468 | protein phosphorylation | 9237760|11509566 |
| Tgene | SRPK1 | GO:0007059 | chromosome segregation | 15034300 |
| Tgene | SRPK1 | GO:0035556 | intracellular signal transduction | 11509566 |
| Tgene | SRPK1 | GO:0045070 | positive regulation of viral genome replication | 20498328 |
| Tgene | SRPK1 | GO:0045071 | negative regulation of viral genome replication | 12417631 |
| Tgene | SRPK1 | GO:0050684 | regulation of mRNA processing | 8208298 |
| Fusion gene information from three resources (ChiTars (NAR, 2018), tumorfusions (NAR, 2018), Gao et al. (Cell, 2018)) * 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. |
| Data type | Source | Cancer type | Sample | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand |
| ChiTaRS3.1 | AL117648 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| * LD: Li Ding group's fusion gene list RV: Roel Verhaak group's fusion gene list ChiTaRs fusion database |
| Open reading frame (ORF) analsis of fusion genes based on Ensembl gene isoform structure. * Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser. |
| ORF | Henst | Tenst | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand |
| intron-3UTR | ENST00000373825 | ENST00000373825 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373825 | ENST00000423325 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373825 | ENST00000373822 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-intron | ENST00000373825 | ENST00000373821 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000423325 | ENST00000373825 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000423325 | ENST00000423325 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000423325 | ENST00000373822 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-intron | ENST00000423325 | ENST00000373821 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373822 | ENST00000373825 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373822 | ENST00000423325 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373822 | ENST00000373822 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-intron | ENST00000373822 | ENST00000373821 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373821 | ENST00000373825 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373821 | ENST00000423325 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-3UTR | ENST00000373821 | ENST00000373822 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
| intron-intron | ENST00000373821 | ENST00000373821 | SRPK1 | chr6 | 35801792 | + | SRPK1 | chr6 | 35801777 | - |
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FusionProtFeatures for SRPK1_SRPK1 |
| Main function of each fusion partner protein. (from UniProt) |
| Hgene | Tgene |
| SRPK1 | SRPK1 |
| Serine/arginine-rich protein-specific kinase whichspecifically phosphorylates its substrates at serine residueslocated in regions rich in arginine/serine dipeptides, known as RSdomains and is involved in the phosphorylation of SR splicingfactors and the regulation of splicing. Plays a central role inthe regulatory network for splicing, controlling the intranucleardistribution of splicing factors in interphase cells and thereorganization of nuclear speckles during mitosis. Can influenceadditional steps of mRNA maturation, as well as other cellularactivities, such as chromatin reorganization in somatic and spermcells and cell cycle progression. Isoform 2 phosphorylates SFRS2,ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using adirectional (C-terminal to N-terminal) and a dual-track mechanismincorporating both processive phosphorylation (in which the kinasestays attached to the substrate after each round ofphosphorylation) and distributive phosphorylation steps (in whichthe kinase and substrate dissociate after each phosphorylationevent). The RS domain of SRSF1 binds first to a docking groove inthe large lobe of the kinase domain of SRPK1. This induces certainstructural changes in SRPK1 and/or RRM2 domain of SRSF1, allowingRRM2 to bind the kinase and initiate phosphorylation. The cyclescontinue for several phosphorylation steps in a processive manner(steps 1-8) until the last few phosphorylation steps(approximately steps 9-12). During that time, a mechanical stressinduces the unfolding of the beta-4 motif in RRM2, which thendocks at the docking groove of SRPK1. This also signals RRM2 tobegin to dissociate, which facilitates SRSF1 dissociation afterphosphorylation is completed. Isoform 2 can mediate hepatitis Bvirus (HBV) core protein phosphorylation. It plays a negative rolein the regulation of HBV replication through a mechanism notinvolving the phosphorylation of the core protein but by reducingthe packaging efficiency of the pregenomic RNA (pgRNA) withoutaffecting the formation of the viral core particles. Isoform 1 andisoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio ofisoform 1/isoform 2 plays a decisive role in determining cell fatein K-562 leukaemic cell line: isoform 2 favors proliferation whereas isoform 1 favors differentiation. {ECO:0000269|PubMed:10049757,ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566,ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757,ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776,ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240,ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134,ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675,ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298,ECO:0000269|PubMed:9237760}. | Serine/arginine-rich protein-specific kinase whichspecifically phosphorylates its substrates at serine residueslocated in regions rich in arginine/serine dipeptides, known as RSdomains and is involved in the phosphorylation of SR splicingfactors and the regulation of splicing. Plays a central role inthe regulatory network for splicing, controlling the intranucleardistribution of splicing factors in interphase cells and thereorganization of nuclear speckles during mitosis. Can influenceadditional steps of mRNA maturation, as well as other cellularactivities, such as chromatin reorganization in somatic and spermcells and cell cycle progression. Isoform 2 phosphorylates SFRS2,ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using adirectional (C-terminal to N-terminal) and a dual-track mechanismincorporating both processive phosphorylation (in which the kinasestays attached to the substrate after each round ofphosphorylation) and distributive phosphorylation steps (in whichthe kinase and substrate dissociate after each phosphorylationevent). The RS domain of SRSF1 binds first to a docking groove inthe large lobe of the kinase domain of SRPK1. This induces certainstructural changes in SRPK1 and/or RRM2 domain of SRSF1, allowingRRM2 to bind the kinase and initiate phosphorylation. The cyclescontinue for several phosphorylation steps in a processive manner(steps 1-8) until the last few phosphorylation steps(approximately steps 9-12). During that time, a mechanical stressinduces the unfolding of the beta-4 motif in RRM2, which thendocks at the docking groove of SRPK1. This also signals RRM2 tobegin to dissociate, which facilitates SRSF1 dissociation afterphosphorylation is completed. Isoform 2 can mediate hepatitis Bvirus (HBV) core protein phosphorylation. It plays a negative rolein the regulation of HBV replication through a mechanism notinvolving the phosphorylation of the core protein but by reducingthe packaging efficiency of the pregenomic RNA (pgRNA) withoutaffecting the formation of the viral core particles. Isoform 1 andisoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio ofisoform 1/isoform 2 plays a decisive role in determining cell fatein K-562 leukaemic cell line: isoform 2 favors proliferation whereas isoform 1 favors differentiation. {ECO:0000269|PubMed:10049757,ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566,ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757,ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776,ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240,ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134,ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675,ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298,ECO:0000269|PubMed:9237760}. |
| 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. |
| - In-frame and 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 |
| - In-frame and 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 |
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FusionGeneSequence for SRPK1_SRPK1 |
| For in-frame fusion transcripts, we provide the fusion transcript sequences and fusion amino acid sequences. (nt: nucleotides, aa: amino acids) |
| * Fusion amino acid sequences. |
| * Fusion transcript sequences (only coding sequence (CDS) region). |
| * Fusion transcript sequences (Full-length transcript). |
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FusionGenePPI for SRPK1_SRPK1 |
| 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 (BIOGRID-3.4.160) |
| Hgene | Hgene's interactors | Tgene | Tgene's interactors |
| - Retained PPIs in in-frame fusion. |
| Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Still interaction with |
| - Lost PPIs in in-frame fusion. |
| Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Interaction lost with |
| - Retained PPIs, but lost function due to frame-shift fusion. |
| Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Interaction lost with |
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RelatedDrugs for SRPK1_SRPK1 |
| Drugs targeting genes involved in this fusion gene. (DrugBank Version 5.1.0 2018-04-02) |
| Partner | Gene | UniProtAcc | DrugBank ID | Drug name | Drug activity | Drug type | Drug status |
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RelatedDiseases for SRPK1_SRPK1 |
| Diseases associated with fusion partners. (DisGeNet 4.0) |
| Partner | Gene | Disease ID | Disease name | # pubmeds | Source |
Copyright 2018-Present -The University of Texas Health Science Center at Houston (UTHealth)
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