UTHEALTH HOME ABOUT SBMI A-Z WEBMAIL INSIDE THE UNIVERSITY |
|
Fusion Protein:HSP90AB1-PGD |
Fusion Protein Summary |
Fusion gene summary |
Fusion partner gene information | Fusion gene name: HSP90AB1-PGD | FusionPDB ID: 37807 | FusionGDB2.0 ID: 37807 | Hgene | Tgene | Gene symbol | HSP90AB1 | PGD | Gene ID | 3326 | 26227 |
Gene name | heat shock protein 90 alpha family class B member 1 | phosphoglycerate dehydrogenase | |
Synonyms | D6S182|HSP84|HSP90B|HSPC2|HSPCB | 3-PGDH|3PGDH|HEL-S-113|NLS|NLS1|PDG|PGAD|PGD|PGDH|PHGDHD|SERA | |
Cytomap | 6p21.1 | 1p12 | |
Type of gene | protein-coding | protein-coding | |
Description | heat shock protein HSP 90-betaHSP90-betaheat shock 84 kDaheat shock 90kD protein 1, betaheat shock protein 90 kDaheat shock protein 90kDa alpha (cytosolic), class B member 1heat shock protein 90kDa alpha family class B member 1 | D-3-phosphoglycerate dehydrogenase2-oxoglutarate reductase3-phosphoglycerate dehydrogenaseepididymis secretory protein Li 113malate dehydrogenase | |
Modification date | 20200327 | 20200320 | |
UniProtAcc | P08238 | . | |
Ensembl transtripts involved in fusion gene | ENST ids | ENST00000353801, ENST00000371554, ENST00000371646, | ENST00000498356, ENST00000270776, ENST00000538557, ENST00000541529, |
Fusion gene scores for assessment (based on all fusion genes of FusionGDB 2.0) | * DoF score | 20 X 20 X 7=2800 | 9 X 7 X 8=504 |
# samples | 22 | 10 | |
** MAII score | log2(22/2800*10)=-3.66985139830767 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | log2(10/504*10)=-2.33342373372519 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | |
Context (manual curation of fusion genes in FusionPDB) | PubMed: HSP90AB1 [Title/Abstract] AND PGD [Title/Abstract] AND fusion [Title/Abstract] | ||
Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0) | HSP90AB1(44218135)-PGD(10471475), # samples:1 | ||
Anticipated loss of major functional domain due to fusion event. | HSP90AB1-PGD 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. HSP90AB1-PGD 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. HSP90AB1-PGD 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. HSP90AB1-PGD 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 | HSP90AB1 | GO:0007004 | telomere maintenance via telomerase | 10197982 |
Hgene | HSP90AB1 | GO:0030511 | positive regulation of transforming growth factor beta receptor signaling pathway | 24613385 |
Hgene | HSP90AB1 | GO:0031396 | regulation of protein ubiquitination | 16809764 |
Hgene | HSP90AB1 | GO:0032435 | negative regulation of proteasomal ubiquitin-dependent protein catabolic process | 24613385 |
Hgene | HSP90AB1 | GO:0032516 | positive regulation of phosphoprotein phosphatase activity | 26593036 |
Hgene | HSP90AB1 | GO:0051131 | chaperone-mediated protein complex assembly | 10811660 |
Hgene | HSP90AB1 | GO:0051973 | positive regulation of telomerase activity | 10197982 |
Hgene | HSP90AB1 | GO:1901389 | negative regulation of transforming growth factor beta activation | 20599762 |
Hgene | HSP90AB1 | GO:1905323 | telomerase holoenzyme complex assembly | 10197982 |
Hgene | HSP90AB1 | GO:2000010 | positive regulation of protein localization to cell surface | 23431407 |
Fusion gene breakpoints across HSP90AB1 (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 PGD (3'-gene) * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Top |
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 | STAD | TCGA-D7-5577-01A | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + |
Top |
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) |
ENST00000353801 | HSP90AB1 | chr6 | 44218135 | + | ENST00000541529 | PGD | chr1 | 10471475 | + | 1943 | 971 | 122 | 1903 | 593 |
ENST00000353801 | HSP90AB1 | chr6 | 44218135 | + | ENST00000270776 | PGD | chr1 | 10471475 | + | 2299 | 971 | 122 | 1903 | 593 |
ENST00000353801 | HSP90AB1 | chr6 | 44218135 | + | ENST00000538557 | PGD | chr1 | 10471475 | + | 2206 | 971 | 122 | 1903 | 593 |
ENST00000371646 | HSP90AB1 | chr6 | 44218135 | + | ENST00000541529 | PGD | chr1 | 10471475 | + | 1930 | 958 | 73 | 1890 | 605 |
ENST00000371646 | HSP90AB1 | chr6 | 44218135 | + | ENST00000270776 | PGD | chr1 | 10471475 | + | 2286 | 958 | 73 | 1890 | 605 |
ENST00000371646 | HSP90AB1 | chr6 | 44218135 | + | ENST00000538557 | PGD | chr1 | 10471475 | + | 2193 | 958 | 73 | 1890 | 605 |
ENST00000371554 | HSP90AB1 | chr6 | 44218135 | + | ENST00000541529 | PGD | chr1 | 10471475 | + | 2035 | 1063 | 214 | 1995 | 593 |
ENST00000371554 | HSP90AB1 | chr6 | 44218135 | + | ENST00000270776 | PGD | chr1 | 10471475 | + | 2391 | 1063 | 214 | 1995 | 593 |
ENST00000371554 | HSP90AB1 | chr6 | 44218135 | + | ENST00000538557 | PGD | chr1 | 10471475 | + | 2298 | 1063 | 214 | 1995 | 593 |
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 |
ENST00000353801 | ENST00000541529 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.002644081 | 0.99735594 |
ENST00000353801 | ENST00000270776 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.00212151 | 0.99787855 |
ENST00000353801 | ENST00000538557 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.002220675 | 0.9977793 |
ENST00000371646 | ENST00000541529 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.002754729 | 0.9972453 |
ENST00000371646 | ENST00000270776 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.002159331 | 0.99784064 |
ENST00000371646 | ENST00000538557 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.002246479 | 0.99775356 |
ENST00000371554 | ENST00000541529 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.001701868 | 0.9982981 |
ENST00000371554 | ENST00000270776 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.001517301 | 0.99848276 |
ENST00000371554 | ENST00000538557 | HSP90AB1 | chr6 | 44218135 | + | PGD | chr1 | 10471475 | + | 0.001510984 | 0.998489 |
Top |
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 >37807_37807_1_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000353801_PGD_chr1_10471475_ENST00000270776_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_2_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000353801_PGD_chr1_10471475_ENST00000538557_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_3_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000353801_PGD_chr1_10471475_ENST00000541529_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_4_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371554_PGD_chr1_10471475_ENST00000270776_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_5_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371554_PGD_chr1_10471475_ENST00000538557_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_6_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371554_PGD_chr1_10471475_ENST00000541529_length(amino acids)=593AA_BP=283 MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTG IGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYK SLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHL LPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFM LLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFY -------------------------------------------------------------- >37807_37807_7_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371646_PGD_chr1_10471475_ENST00000270776_length(amino acids)=605AA_BP=295 MLTITYNPFLFKMPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPN PQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVR ADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPD DITQEEYGEFYKSLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITAN ILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALY ASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGI -------------------------------------------------------------- >37807_37807_8_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371646_PGD_chr1_10471475_ENST00000538557_length(amino acids)=605AA_BP=295 MLTITYNPFLFKMPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPN PQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVR ADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPD DITQEEYGEFYKSLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITAN ILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALY ASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGI -------------------------------------------------------------- >37807_37807_9_HSP90AB1-PGD_HSP90AB1_chr6_44218135_ENST00000371646_PGD_chr1_10471475_ENST00000541529_length(amino acids)=605AA_BP=295 MLTITYNPFLFKMPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPN PQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVR ADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPD DITQEEYGEFYKSLTNDWEDHLAVKVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITAN ILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALY ASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGI -------------------------------------------------------------- |
Top |
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/chr6:44218135/chr1:10471475) - 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 |
HSP90AB1 | . |
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}. | 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 |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 478_481 | 173.0 | 484.0 | Nucleotide binding | NADP%3B shared with dimeric partner | |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 187_188 | 173.0 | 484.0 | Region | Substrate binding |
- 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 | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 720_724 | 0 | 725.0 | Motif | Note=TPR repeat-binding |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 720_724 | 0 | 725.0 | Motif | Note=TPR repeat-binding |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 720_724 | 0 | 725.0 | Motif | Note=TPR repeat-binding |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 10_15 | 173.0 | 484.0 | Nucleotide binding | NADP | |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 33_35 | 173.0 | 484.0 | Nucleotide binding | NADP | |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 75_77 | 173.0 | 484.0 | Nucleotide binding | NADP | |
Tgene | PGD | chr6:44218135 | chr1:10471475 | ENST00000270776 | 5 | 13 | 129_131 | 173.0 | 484.0 | Region | Substrate binding |
Top |
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 |
HSP90AB1 | |
PGD |
- 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 | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 215_552 | 0 | 725.0 | AHSA1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 215_552 | 0 | 725.0 | AHSA1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 215_552 | 0 | 725.0 | AHSA1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 2_214 | 0 | 725.0 | BIRC2 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 2_214 | 0 | 725.0 | BIRC2 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 2_214 | 0 | 725.0 | BIRC2 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 620_723 | 0 | 725.0 | NR1D1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 620_723 | 0 | 725.0 | NR1D1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 620_723 | 0 | 725.0 | NR1D1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 264_608 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 9_231 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 264_608 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 9_231 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 264_608 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 9_231 | 0 | 725.0 | NR3C1 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000353801 | + | 1 | 12 | 2_527 | 0 | 725.0 | TP53 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371554 | + | 1 | 12 | 2_527 | 0 | 725.0 | TP53 |
Hgene | HSP90AB1 | chr6:44218135 | chr1:10471475 | ENST00000371646 | + | 1 | 12 | 2_527 | 0 | 725.0 | TP53 |
Top |
Related Drugs to HSP90AB1-PGD |
Drugs used for this fusion-positive patient. (Manual curation of PubMed, 04-30-2022 + MyCancerGenome) |
Hgene | Tgene | Drug | Source | PMID |
Top |
Related Diseases to HSP90AB1-PGD |
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 |