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Fusion Protein:PPP1R15A-HSPA1A |
Fusion Protein Summary |
 Fusion gene summary |
| Fusion partner gene information | Fusion gene name: PPP1R15A-HSPA1A | FusionPDB ID: 67834 | FusionGDB2.0 ID: 67834 | Hgene | Tgene | Gene symbol | PPP1R15A | HSPA1A | Gene ID | 23645 | 3303 |
| Gene name | protein phosphatase 1 regulatory subunit 15A | heat shock protein family A (Hsp70) member 1A | |
| Synonyms | GADD34 | HEL-S-103|HSP70-1|HSP70-1A|HSP70-2|HSP70.1|HSP70.2|HSP70I|HSP72|HSPA1 | |
| Cytomap | 19q13.33 | 6p21.33 | |
| Type of gene | protein-coding | protein-coding | |
| Description | protein phosphatase 1 regulatory subunit 15Agrowth arrest and DNA damage-inducible protein GADD34growth arrest and DNA-damage-inducible 34myeloid differentiation primary response protein MyD116 homologprotein phosphatase 1, regulatory (inhibitor) subu | heat shock 70 kDa protein 1AHSP70-1/HSP70-2HSP70.1/HSP70.2Heat shock 70 kDa protein 1BHeat shock 70 kDa protein 2dnaK-type molecular chaperone HSP70-1epididymis secretory protein Li 103epididymis secretory sperm binding proteinheat shock 70 kDa pr | |
| Modification date | 20200313 | 20200327 | |
| UniProtAcc | . | P0DMV8 | |
| Ensembl transtripts involved in fusion gene | ENST ids | ENST00000200453, | ENST00000383389, ENST00000400040, ENST00000422919, ENST00000430065, ENST00000433487, ENST00000441618, ENST00000449876, ENST00000452298, ENST00000375651, ENST00000458062, ENST00000608703, |
| Fusion gene scores for assessment (based on all fusion genes of FusionGDB 2.0) | * DoF score | 5 X 6 X 2=60 | 6 X 15 X 4=360 |
| # samples | 6 | 11 | |
| ** MAII score | log2(6/60*10)=0 | log2(11/360*10)=-1.71049338280502 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | |
| Context (manual curation of fusion genes in FusionPDB) | PubMed: PPP1R15A [Title/Abstract] AND HSPA1A [Title/Abstract] AND fusion [Title/Abstract] | ||
| Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0) | PPP1R15A(49379000)-HSPA1A(31785406), # samples:3 | ||
| Anticipated loss of major functional domain due to fusion event. | PPP1R15A-HSPA1A 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. PPP1R15A-HSPA1A 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 |
| Hgene | PPP1R15A | GO:0032515 | negative regulation of phosphoprotein phosphatase activity | 11564868 |
| Hgene | PPP1R15A | GO:0032516 | positive regulation of phosphoprotein phosphatase activity | 11564868 |
| Hgene | PPP1R15A | GO:0034976 | response to endoplasmic reticulum stress | 12556489 |
| Hgene | PPP1R15A | GO:0035308 | negative regulation of protein dephosphorylation | 11564868 |
| Hgene | PPP1R15A | GO:0036496 | regulation of translational initiation by eIF2 alpha dephosphorylation | 12556489 |
| Hgene | PPP1R15A | GO:1902310 | positive regulation of peptidyl-serine dephosphorylation | 11564868|12556489|21518769 |
| Hgene | PPP1R15A | GO:1903917 | positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation | 21518769 |
| Tgene | HSPA1A | GO:0006402 | mRNA catabolic process | 10205060 |
| Tgene | HSPA1A | GO:0006986 | response to unfolded protein | 10859165 |
| Tgene | HSPA1A | GO:0031396 | regulation of protein ubiquitination | 16809764 |
| Tgene | HSPA1A | GO:0031397 | negative regulation of protein ubiquitination | 12150907 |
| Tgene | HSPA1A | GO:0032436 | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | 24613385 |
| Tgene | HSPA1A | GO:0033120 | positive regulation of RNA splicing | 20625543 |
| Tgene | HSPA1A | GO:0034605 | cellular response to heat | 24061851 |
| Tgene | HSPA1A | GO:0042026 | protein refolding | 15603737|21231916 |
| Tgene | HSPA1A | GO:0046034 | ATP metabolic process | 23921388 |
| Tgene | HSPA1A | GO:0050821 | protein stabilization | 21909508 |
| Tgene | HSPA1A | GO:0051131 | chaperone-mediated protein complex assembly | 10811660 |
| Tgene | HSPA1A | GO:0090084 | negative regulation of inclusion body assembly | 15603737|21231916 |
| Tgene | HSPA1A | GO:0097201 | negative regulation of transcription from RNA polymerase II promoter in response to stress | 9499401 |
| Tgene | HSPA1A | GO:1901029 | negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway | 20625543 |
| Tgene | HSPA1A | GO:1902236 | negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway | 12150907|20625543 |
| Tgene | HSPA1A | GO:1902380 | positive regulation of endoribonuclease activity | 20625543 |
| Fusion gene breakpoints across PPP1R15A (5'-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 breakpoints across HSPA1A (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 |
| ChiTaRS5.0 | N/A | AV701720 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + |
| ChiTaRS5.0 | N/A | AV702122 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + |
| ChiTaRS5.0 | N/A | AV705476 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + |
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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) |
| ENST00000200453 | PPP1R15A | chr19 | 49379000 | + | ENST00000375651 | HSPA1A | chr6 | 31785406 | + | 2559 | 2248 | 206 | 1948 | 580 |
| ENST00000200453 | PPP1R15A | chr19 | 49379000 | + | ENST00000458062 | HSPA1A | chr6 | 31785406 | + | 2301 | 2248 | 206 | 1948 | 580 |
| ENST00000200453 | PPP1R15A | chr19 | 49379000 | + | ENST00000608703 | HSPA1A | chr6 | 31785406 | + | 2565 | 2248 | 206 | 1948 | 580 |
| 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 |
| ENST00000200453 | ENST00000375651 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + | 0.004901171 | 0.99509877 |
| ENST00000200453 | ENST00000458062 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + | 0.00702226 | 0.9929777 |
| ENST00000200453 | ENST00000608703 | PPP1R15A | chr19 | 49379000 | + | HSPA1A | chr6 | 31785406 | + | 0.004810992 | 0.99518895 |
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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 >67834_67834_1_PPP1R15A-HSPA1A_PPP1R15A_chr19_49379000_ENST00000200453_HSPA1A_chr6_31785406_ENST00000375651_length(amino acids)=580AA_BP= MADRTGAPAPGVTRSSQPPRHMAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLA IPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPG EEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVS PRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFL KAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFL KAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPP -------------------------------------------------------------- >67834_67834_2_PPP1R15A-HSPA1A_PPP1R15A_chr19_49379000_ENST00000200453_HSPA1A_chr6_31785406_ENST00000458062_length(amino acids)=580AA_BP= MADRTGAPAPGVTRSSQPPRHMAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLA IPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPG EEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVS PRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFL KAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFL KAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPP -------------------------------------------------------------- >67834_67834_3_PPP1R15A-HSPA1A_PPP1R15A_chr19_49379000_ENST00000200453_HSPA1A_chr6_31785406_ENST00000608703_length(amino acids)=580AA_BP= MADRTGAPAPGVTRSSQPPRHMAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLA IPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPG EEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVS PRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFL KAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFL KAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPP -------------------------------------------------------------- |
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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/chr19:49379000/chr6:31785406) - 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. |
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| Main function of each fusion partner protein. (from UniProt) |
| Hgene | Tgene |
| . | HSPA1A |
| 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. | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558). {ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:27708256, ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:9499401, ECO:0000303|PubMed:24012426, ECO:0000303|PubMed:26865365}.; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. {ECO:0000269|PubMed:16537599}. |
| 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 |
| - 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 | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 112_115 | 0 | 675.0 | Compositional bias | Note=Poly-Asp |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 160_503 | 0 | 675.0 | Compositional bias | Note=Glu-rich |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 518_521 | 0 | 675.0 | Compositional bias | Note=Poly-Pro |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 661_666 | 0 | 675.0 | Compositional bias | Note=Poly-Ala |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 22_39 | 0 | 675.0 | Intramembrane | Helical |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 1_60 | 0 | 675.0 | Region | Note=Required for localization in the endoplasmic reticulum |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 337_369 | 0 | 675.0 | Repeat | Note=1 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 384_417 | 0 | 675.0 | Repeat | Note=2 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 427_460 | 0 | 675.0 | Repeat | Note=3 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 477_510 | 0 | 675.0 | Repeat | Note=4 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 1_21 | 0 | 675.0 | Topological domain | Cytoplasmic |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 40_674 | 0 | 675.0 | Topological domain | Cytoplasmic |
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Fusion Protein Structures |
| PDB and CIF files of the predicted fusion proteins * Here we show the 3D structure of the fusion proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| Fusion protein PDB link (fusion AA seq ID in FusionPDB) | Hgene | Hchr | Hbp | Hstrand | Tgene | Tchr | Tbp | Tstrand | AA seq | Len(AA seq) |
| PDB file >>>1237_PPP1R15A_49379000_HSPA1A_31785406_1237_PPP1R15A_49379000_HSPA1A_31785406_ranked_0.pdb | PPP1R15A | 49379000 | 49379000 | ENST00000608703 | HSPA1A | chr6 | 31785406 | + | MADRTGAPAPGVTRSSQPPRHMAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLA IPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPG EEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVS PRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFL KAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFL KAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPP | 580 |
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pLDDT score distribution |
| pLDDT score distribution of the predicted wild-type structures of two partner proteins from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
PPP1R15A_pLDDT.png  |
HSPA1A_pLDDT.png  |
| pLDDT score distribution of the predicted fusion protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
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Ramachandran Plot of Fusion Protein Structure |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this fusion protein peptide. |
| Fusion AA seq ID in FusionPDB and their Ramachandran plots |
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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 |
| Protein-protein interactors based on sequence similarity (STRING) |
| Gene | STRING network |
| PPP1R15A | |
| HSPA1A |
| - 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 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 483_555 | 0 | 675.0 | KMT2A/MLL1 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 337_510 | 0 | 675.0 | SMAD7 |
| Hgene | PPP1R15A | chr19:49379000 | chr6:31785406 | ENST00000200453 | + | 1 | 3 | 536_583 | 0 | 675.0 | SMARCB1 |
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Related Drugs to PPP1R15A-HSPA1A |
| 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 PPP1R15A-HSPA1A |
| 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 |
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