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Fusion gene ID: 16126 |
FusionGeneSummary for HEXA_HSPA8 |
Fusion gene summary |
Fusion gene information | Fusion gene name: HEXA_HSPA8 | Fusion gene ID: 16126 | Hgene | Tgene | Gene symbol | HEXA | HSPA8 | Gene ID | 3073 | 3312 |
Gene name | hexosaminidase subunit alpha | heat shock protein family A (Hsp70) member 8 | |
Synonyms | TSD | HEL-33|HEL-S-72p|HSC54|HSC70|HSC71|HSP71|HSP73|HSPA10|LAP-1|LAP1|NIP71 | |
Cytomap | 15q23 | 11q24.1 | |
Type of gene | protein-coding | protein-coding | |
Description | beta-hexosaminidase subunit alphaN-acetyl-beta-glucosaminidase subunit alphabeta-N-acetylhexosaminidase subunit alphahexosaminidase A (alpha polypeptide)hexosaminidase subunit A | heat shock cognate 71 kDa proteinLPS-associated protein 1N-myristoyltransferase inhibitor protein 71constitutive heat shock protein 70epididymis luminal protein 33epididymis secretory sperm binding protein Li 72pheat shock 70kDa protein 8heat shock | |
Modification date | 20180519 | 20180527 | |
UniProtAcc | P06865 | P11142 | |
Ensembl transtripts involved in fusion gene | ENST00000268097, ENST00000566304, ENST00000457859, ENST00000567159, ENST00000429918, ENST00000567213, | ENST00000532636, ENST00000533540, ENST00000453788, ENST00000534624, ENST00000227378, ENST00000534319, ENST00000526110, ENST00000526862, | |
Fusion gene scores | * DoF score | 5 X 5 X 3=75 | 13 X 14 X 4=728 |
# samples | 6 | 16 | |
** MAII score | log2(6/75*10)=-0.321928094887362 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | log2(16/728*10)=-2.18586654531133 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | |
Context | PubMed: HEXA [Title/Abstract] AND HSPA8 [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 | HEXA | GO:0006024 | glycosaminoglycan biosynthetic process | 25645918 |
Tgene | HSPA8 | GO:0042026 | protein refolding | 21231916|25719862 |
Tgene | HSPA8 | GO:0045892 | negative regulation of transcription, DNA-templated | 10722728 |
Tgene | HSPA8 | GO:0046034 | ATP metabolic process | 23921388 |
Tgene | HSPA8 | GO:1902904 | negative regulation of supramolecular fiber organization | 23921388 |
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 | BQ324959 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
* 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-3CDS | ENST00000268097 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000268097 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000268097 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000566304 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000566304 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000566304 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000457859 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000457859 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000457859 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000567159 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000567159 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567159 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000429918 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000429918 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000429918 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000567213 | ENST00000532636 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-3CDS | ENST00000567213 | ENST00000533540 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000453788 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000534624 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000227378 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000534319 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000526110 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
intron-intron | ENST00000567213 | ENST00000526862 | HEXA | chr15 | 72638935 | + | HSPA8 | chr11 | 122929161 | - |
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FusionProtFeatures for HEXA_HSPA8 |
Main function of each fusion partner protein. (from UniProt) |
Hgene | Tgene |
HEXA | HSPA8 |
Responsible for the degradation of GM2 gangliosides, anda variety of other molecules containing terminal N-acetylhexosamines, in the brain and other tissues. The form B is activeagainst certain oligosaccharides. The form S has no measurableactivity. | Molecular chaperone implicated in a wide variety ofcellular processes, including protection of the proteome fromstress, folding and transport of newly synthesized polypeptides,activation of proteolysis of misfolded proteins and the formationand dissociation of protein complexes. Plays a pivotal role in theprotein quality control system, ensuring the correct folding ofproteins, the re-folding of misfolded proteins and controlling thetargeting of proteins for subsequent degradation (PubMed:21150129,PubMed:21148293, PubMed:24732912, PubMed:27916661,PubMed:23018488). This is achieved through cycles of ATP binding,ATP hydrolysis and ADP release, mediated by co-chaperones(PubMed:21150129, PubMed:21148293, PubMed:24732912,PubMed:27916661, PubMed:23018488). The co-chaperones have beenshown to not only regulate different steps of the ATPase cycle ofHSP70, but they also have an individual specificity such that oneco-chaperone may promote folding of a substrate while another maypromote degradation (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinityof HSP70 for polypeptides is regulated by its nucleotide boundstate. In the ATP-bound form, it has a low affinity for substrateproteins. However, upon hydrolysis of the ATP to ADP, it undergoesa conformational change that increases its affinity for substrateproteins. HSP70 goes through repeated cycles of ATP hydrolysis andnucleotide exchange, which permits cycles of substrate binding andrelease. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis byHSP70), 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 TPRdomain chaperones such as HOPX and STUB1 (PubMed:24318877,PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as arepressor of transcriptional activation. Inhibits thetranscriptional coactivator activity of CITED1 on Smad-mediatedtranscription. Component of the PRP19-CDC5L complex that forms anintegral part of the spliceosome and is required for activatingpre-mRNA splicing. May have a scaffolding role in the spliceosomeassembly as it contacts all other components of the core complex.Binds bacterial lipopolysaccharide (LPS) and mediates LPS-inducedinflammatory response, including TNF secretion by monocytes(PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway inconjunction with J domain-containing co-chaperones and the E3ligase STUB1 (PubMed:23990462). {ECO:0000269|PubMed:10722728,ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:21148293,ECO:0000269|PubMed:21150129, ECO:0000269|PubMed:23018488,ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24318877,ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27474739,ECO:0000269|PubMed:27916661, ECO:0000303|PubMed:24121476,ECO:0000303|PubMed:26865365}. |
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 HEXA_HSPA8 |
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 HEXA_HSPA8 |
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 HEXA_HSPA8 |
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 |
Tgene | HSPA8 | P11142 | DB01254 | Dasatinib | Heat shock cognate 71 kDa protein | small molecule | approved|investigational |
Tgene | HSPA8 | P11142 | DB11638 | Artenimol | Heat shock cognate 71 kDa protein | small molecule | approved|investigational |
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RelatedDiseases for HEXA_HSPA8 |
Diseases associated with fusion partners. (DisGeNet 4.0) |
Partner | Gene | Disease ID | Disease name | # pubmeds | Source |
Hgene | HEXA | C0039373 | Tay-Sachs Disease | 22 | CTD_human;UNIPROT |
Hgene | HEXA | C3714756 | Intellectual Disability | 1 | CTD_human |
Tgene | HSPA8 | C0001418 | Adenocarcinoma | 1 | CTD_human |
Tgene | HSPA8 | C0007137 | Squamous cell carcinoma | 1 | CTD_human |
Tgene | HSPA8 | C0026640 | Mouth Neoplasms | 1 | CTD_human |
Tgene | HSPA8 | C0035126 | Reperfusion Injury | 1 | CTD_human |
Tgene | HSPA8 | C0038356 | Stomach Neoplasms | 1 | CTD_human |
Tgene | HSPA8 | C0948089 | Acute Coronary Syndrome | 1 | CTD_human |
Tgene | HSPA8 | C1846707 | SPINOCEREBELLAR ATAXIA 17 | 1 | CTD_human |