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Center for Computational Systems Medicine
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Fusion Gene and Fusion Protein Summary

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Fusion Amino Acid Sequences (multiple BPs and multiple gene isoforms)

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Fusion Protein Breakpoint Sequences - (for the Screening of the FusionNeoAntigens)

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Potential FusionNeoAntigens in HLA I - (netMHCpan v4.1 + deepHLApan v1.1)

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Potential FusionNeoAntigens in HLA II - (netMHCIIpan v4.1)

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Fusion Breakpoint 14 AA Peptide Structure - (RoseTTAFold)

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Filtering FusionNeoAntigens Through Checking the Interaction with HLAs in 3D - (Glide)

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Vaccine Design for the FusionNeoAntigens (RNA/protein sequences)

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Potential target of CAR-T therapy development

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Information on the samples that have these potential fusion neoantigens

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Fusion Protein Targeting Drugs - (Manual Curation)

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Fusion Protein Related diseases - (Manual Curation)

Fusion Protein:HSP90B1-ACVR1B

Fusion Gene and Fusion Protein Summary

check button Fusion gene summary
Fusion partner gene informationFusion gene name: HSP90B1-ACVR1B
FusionPDB ID: 37817
FusionGDB2.0 ID: 37817
HgeneTgene
Gene symbol

HSP90B1

ACVR1B

Gene ID

7184

91

Gene nameheat shock protein 90 beta family member 1activin A receptor type 1B
SynonymsECGP|GP96|GRP94|HEL-S-125m|HEL35|TRA1ACTRIB|ACVRLK4|ALK4|SKR2
Cytomap

12q23.3

12q13.13

Type of geneprotein-codingprotein-coding
Descriptionendoplasmin94 kDa glucose-regulated proteinendothelial cell (HBMEC) glycoproteinepididymis luminal protein 35epididymis secretory sperm binding protein Li 125mheat shock protein 90 kDa beta member 1heat shock protein 90kDa beta (Grp94), member 1heaactivin receptor type-1Bactivin A receptor, type IBactivin A receptor, type II-like kinase 4activin receptor-like kinase 4serine/threonine-protein kinase receptor R2
Modification date2020032020200313
UniProtAcc

P14625

Main function of 5'-partner protein: FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000250|UniProtKB:P08113, ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:32272059}.

P36896

Main function of 5'-partner protein: FUNCTION: Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor. ACVR1B also phosphorylates TDP2. {ECO:0000269|PubMed:12364468, ECO:0000269|PubMed:12639945, ECO:0000269|PubMed:18039968, ECO:0000269|PubMed:20226172, ECO:0000269|PubMed:8196624, ECO:0000269|PubMed:9032295, ECO:0000269|PubMed:9892009}.
Ensembl transtripts involved in fusion geneENST idsENST00000299767, ENST00000563121, 
ENST00000415850, ENST00000257963, 
ENST00000426655, ENST00000541224, 
ENST00000542485, 
Fusion gene scores for assessment (based on all fusion genes of FusionGDB 2.0)* DoF score19 X 19 X 10=36106 X 5 X 6=180
# samples 256
** MAII scorelog2(25/3610*10)=-3.85199883711245
possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs).
DoF>8 and MAII<0
log2(6/180*10)=-1.58496250072116
possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs).
DoF>8 and MAII<0
Fusion gene context

PubMed: HSP90B1 [Title/Abstract] AND ACVR1B [Title/Abstract] AND fusion [Title/Abstract]

Fusion neoantigen context

PubMed: HSP90B1 [Title/Abstract] AND ACVR1B [Title/Abstract] AND neoantigen [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)HSP90B1(104337652)-ACVR1B(52380602), # samples:1
Anticipated loss of major functional domain due to fusion event.HSP90B1-ACVR1B 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.
HSP90B1-ACVR1B 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.
HSP90B1-ACVR1B seems lost the major protein functional domain in Hgene partner, which is a essential gene due to the frame-shifted ORF.
HSP90B1-ACVR1B seems lost the major protein functional domain in Hgene partner, which is a IUPHAR drug target due to the frame-shifted ORF.
HSP90B1-ACVR1B seems lost the major protein functional domain in Hgene partner, which is a tumor suppressor due to the frame-shifted ORF.
HSP90B1-ACVR1B seems lost the major protein functional domain in Tgene partner, which is a IUPHAR drug target due to the frame-shifted ORF.
HSP90B1-ACVR1B seems lost the major protein functional domain in Tgene partner, which is a kinase due to the frame-shifted ORF.
* DoF score (Degree of Frequency) = # partners X # break points X # cancer types
** MAII score (Major Active Isofusion Index) = log2(# samples/DoF score*10)

check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgeneHSP90B1

GO:0001666

response to hypoxia

15620698

HgeneHSP90B1

GO:0031247

actin rod assembly

19000834

HgeneHSP90B1

GO:0043666

regulation of phosphoprotein phosphatase activity

19000834

HgeneHSP90B1

GO:0071318

cellular response to ATP

19000834

TgeneACVR1B

GO:0000082

G1/S transition of mitotic cell cycle

11117535

TgeneACVR1B

GO:0006355

regulation of transcription, DNA-templated

8622651|12665502

TgeneACVR1B

GO:0006468

protein phosphorylation

12065756

TgeneACVR1B

GO:0007165

signal transduction

8622651|12665502

TgeneACVR1B

GO:0018107

peptidyl-threonine phosphorylation

18039968

TgeneACVR1B

GO:0030308

negative regulation of cell growth

11117535

TgeneACVR1B

GO:0032924

activin receptor signaling pathway

9892009

TgeneACVR1B

GO:0032927

positive regulation of activin receptor signaling pathway

16720724

TgeneACVR1B

GO:0045648

positive regulation of erythrocyte differentiation

9032295

TgeneACVR1B

GO:0046777

protein autophosphorylation

18039968

TgeneACVR1B

GO:1901165

positive regulation of trophoblast cell migration

21356369



check button Four levels of functional features of fusion genes
Go to FGviewer search page for the most frequent breakpoint (https://ccsmweb.uth.edu/FGviewer/chr12:104337652/chr12:52380602)
- 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.
FGviewer

check buttonRetention analysis results 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, are available here.

check buttonFusion gene breakpoints across HSP90B1 (5'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure

check buttonFusion gene breakpoints across ACVR1B (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure


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Fusion Amino Acid Sequences


check buttonFusion information from ORFfinder translation from full-length transcript sequence from FusionPDB.
HenstTenstHgeneHchrHbpHstrandTgeneTchrTbpTstrandSeq length
(transcript)
BP loci
(transcript)
Predicted start
(transcript)
Predicted stop
(transcript)
Seq length
(amino acids)
ENST00000299767HSP90B1chr12104337652+ENST00000257963ACVR1Bchr1252380602+555922091822590802
ENST00000299767HSP90B1chr12104337652+ENST00000541224ACVR1Bchr1252380602+269822091822590802
ENST00000299767HSP90B1chr12104337652+ENST00000426655ACVR1Bchr1252380602+281322091822503773
ENST00000299767HSP90B1chr12104337652+ENST00000542485ACVR1Bchr1252380602+340622091822590802

check buttonDeepORF 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.
HenstTenstHgeneHchrHbpHstrandTgeneTchrTbpTstrandNo-coding scoreCoding score
ENST00000299767ENST00000257963HSP90B1chr12104337652+ACVR1Bchr1252380602+0.0002363470.99976367
ENST00000299767ENST00000541224HSP90B1chr12104337652+ACVR1Bchr1252380602+0.0006423920.99935764
ENST00000299767ENST00000426655HSP90B1chr12104337652+ACVR1Bchr1252380602+0.0003626280.99963737
ENST00000299767ENST00000542485HSP90B1chr12104337652+ACVR1Bchr1252380602+0.0004804010.9995196

check button Predicted full-length fusion amino acid sequences. For individual full-length fusion transcript sequence from FusionPDB, we ran ORFfinder and chose the longest ORF among all the predicted ones.

Get the fusion protein sequences from here.

Fusion protein sequence information is available in the fasta format.
>FusionGDB ID_FusionGDB isoform ID_FGname_Hgene_Hchr_Hbp_Henst_Tgene_Tchr_Tbp_Tenst_length(fusion AA) seq_BP

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Fusion Protein Breakpoint Sequences for HSP90B1-ACVR1B

check button +/-13 AA sequence from the breakpoints of the fusion protein sequences.
HgeneHchrHbpTgeneTchrTbpLength(fusion protein)BP in fusion proteinPeptide
HSP90B1chr12104337652ACVR1Bchr12523806022209676AQAYQTGKDISTKYMAPEVLDETINM

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Potential FusionNeoAntigen Information of HSP90B1-ACVR1B in HLA I

check button Multiple sequence alignments of the potential FusionNeoAntigens per fusion breakpoints. If the MSA is empty, then it means that there were predicted fusion neoantigens in this fusion breakpoint, but those predicted fusion neoantigens were not across the breakpoint, which is not fusion-specific.
HSP90B1-ACVR1B_104337652_52380602.msa

check button Potential FusionNeoAntigen Information
* We used NetMHCpan v4.1 (%rank<0.5) and deepHLApan v1.1 (immunogenic score>0.5)
Fusion geneHchrHbpTgeneTchrTbpHLA IFusionNeoAntigen peptideBinding scoreImmunogenic scoreNeoantigen start (at BP 13)Neoantigen end (at BP 13)
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:01TKYMAPEVL0.99750.96271120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:24TKYMAPEVL0.99730.60761120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:06TKYMAPEVL0.99620.81491120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-A30:08STKYMAPEV0.99430.77971019
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B38:02TKYMAPEVL0.99210.98921120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:13TKYMAPEVL0.9910.97631120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B38:01TKYMAPEVL0.99080.98561120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:01TGKDISTKY0.98890.8182514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:02TGKDISTKY0.96570.8062514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B14:01TKYMAPEVL0.93390.85231120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B14:02TKYMAPEVL0.93390.85231120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:10TKYMAPEVL0.92520.65011120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:05TGKDISTKY0.7670.51514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B48:01TKYMAPEVL0.54850.77111120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:37TKYMAPEVL0.53880.67041120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:18TKYMAPEVL0.34870.81711120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:03TKYMAPEVL0.2580.84231120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:01QTGKDISTKY0.95890.7799414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:01YQTGKDISTKY10.8135314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:25YQTGKDISTKY0.99380.8088314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:02YQTGKDISTKY0.98820.8289314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:03YQTGKDISTKY0.91280.6205314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:09TKYMAPEVL0.99780.77461120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:12TKYMAPEVL0.99660.96651120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:05TKYMAPEVL0.99170.95561120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:07TGKDISTKY0.97880.6065514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C07:13TKYMAPEVL0.92390.96531120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C07:29TKYMAPEVL0.92060.97071120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C12:16TGKDISTKY0.78410.9146514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C15:04TGKDISTKY0.54940.8271514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C12:04TGKDISTKY0.25210.9817514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C12:12TGKDISTKY0.22470.8155514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C06:03TGKDISTKY0.22140.9782514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B14:03TKYMAPEVL0.220.84181120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C03:14TGKDISTKY0.18970.9168514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B48:03TKYMAPEVL0.06020.51871120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:07YQTGKDISTKY0.99990.5722314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:04YQTGKDISTKY0.99860.8616314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:21YQTGKDISTKY0.98730.7673314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:05YQTGKDISTKY0.98040.759314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:31YQTGKDISTKY0.97730.7731314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C14:02KYMAPEVL0.87350.97191220
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C14:03KYMAPEVL0.87350.97191220
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:31TKYMAPEVL0.99730.96361120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:02TKYMAPEVL0.99720.97661120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B38:05TKYMAPEVL0.99080.98561120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:27TGKDISTKY0.98970.814514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-A68:02STKYMAPEV0.98910.58351019
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:135TGKDISTKY0.9890.838514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:34TGKDISTKY0.98890.8182514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:33TGKDISTKY0.98890.8182514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:125TGKDISTKY0.98890.8182514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:50TGKDISTKY0.97610.798514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:11TGKDISTKY0.97470.7812514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:53TGKDISTKY0.97020.7844514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:08TGKDISTKY0.96880.7719514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:11TGKDISTKY0.96110.7712514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:43TGKDISTKY0.95560.7723514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:35TGKDISTKY0.95330.8061514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:12TGKDISTKY0.87560.8555514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:17TGKDISTKY0.83270.6254514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:30TGKDISTKY0.83270.6254514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:09TKYMAPEVL0.82590.84441120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C03:02TGKDISTKY0.78910.9071514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:54TGKDISTKY0.71090.7665514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C12:02TGKDISTKY0.67360.9242514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C07:22TGKDISTKY0.60570.5562514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B39:11TKYMAPEVL0.55240.83091120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C15:09TGKDISTKY0.54940.8271514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B48:02TKYMAPEVL0.46250.87891120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C12:03TGKDISTKY0.33020.943514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C16:04TGKDISTKY0.32630.9187514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:68TGKDISTKY0.31110.5092514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B18:04TGKDISTKY0.28560.7826514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C02:02TGKDISTKY0.09870.9689514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C02:10TGKDISTKY0.09870.9689514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:68TKYMAPEVL0.06060.74461120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B40:12TKYMAPEVL0.06020.51871120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:54TKYMAPEVL0.02370.88031120
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C16:01TGKDISTKY0.01780.9298514
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:12QTGKDISTKY0.96680.8259414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:50QTGKDISTKY0.95920.7711414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:125QTGKDISTKY0.95890.7799414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:34QTGKDISTKY0.95890.7799414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:33QTGKDISTKY0.95890.7799414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:135QTGKDISTKY0.95550.8301414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:35QTGKDISTKY0.93210.7398414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-A25:01QTGKDISTKY0.4240.5492414
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:34YQTGKDISTKY10.8135314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:125YQTGKDISTKY10.8135314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:135YQTGKDISTKY10.849314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:33YQTGKDISTKY10.8135314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:27YQTGKDISTKY10.8184314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:24YQTGKDISTKY0.99990.8604314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:53YQTGKDISTKY0.99990.78314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:50YQTGKDISTKY0.99990.7988314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:35YQTGKDISTKY0.99990.7851314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:54YQTGKDISTKY0.99950.7542314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:12YQTGKDISTKY0.99930.8314314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C02:02YQTGKDISTKY0.99710.9288314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-C02:10YQTGKDISTKY0.99710.9288314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:39YQTGKDISTKY0.99280.711314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B15:20YQTGKDISTKY0.98270.8227314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:28YQTGKDISTKY0.97450.8402314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B35:20YQTGKDISTKY0.97310.8523314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B18:04YQTGKDISTKY0.90840.8225314
HSP90B1-ACVR1Bchr12104337652chr12523806022209HLA-B48:02YQTGKDISTKY0.85130.8175314

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Potential FusionNeoAntigen Information of HSP90B1-ACVR1B in HLA II

check button Multiple sequence alignments of the potential FusionNeoAntigens per fusion breakpoints. If the MSA is empty, then it means that there were predicted fusion neoantigens in this fusion breakpoint, but those predicted fusion neoantigens were not across the breakpoint, which is not fusion-specific.

check button Potential FusionNeoAntigen Information
* We used NetMHCIIpan v4.1 (%rank<0.5).
Fusion geneHchrHbpTgeneTchrTbpHLA IIFusionNeoAntigen peptideNeoantigen start (at BP 13)Neoantigen end (at BP 13)

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Fusion breakpoint peptide structures of HSP90B1-ACVR1B

check button3D structures of the fusion breakpoint peptide of 14AA sequence that have potential fusion neoantigens
* The minimum length of the amino acid sequence in RoseTTAFold is 14AA. Here, we predicted the 14AA fusion protein breakpoint sequence not the fusion neoantigen peptide, which is shorter than 14 AA.
File nameBPseqHgeneTgeneHchrHbpTchrTbpAAlen
2888GKDISTKYMAPEVLHSP90B1ACVR1Bchr12104337652chr12523806022209

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Filtering FusionNeoAntigens Through Checking the Interaction with HLAs in 3D of HSP90B1-ACVR1B

check buttonVirtual screening between 25 HLAs (from PDB) and FusionNeoAntigens
* We used Glide to predict the interaction between HLAs and neoantigens.
HLA allelePDB IDFile nameBPseqDocking scoreGlide score
HLA-B14:023BVN2888GKDISTKYMAPEVL-7.9962-8.1096
HLA-B14:023BVN2888GKDISTKYMAPEVL-5.70842-6.74372
HLA-B52:013W392888GKDISTKYMAPEVL-6.83737-6.95077
HLA-B52:013W392888GKDISTKYMAPEVL-4.4836-5.5189
HLA-A11:014UQ22888GKDISTKYMAPEVL-10.0067-10.1201
HLA-A11:014UQ22888GKDISTKYMAPEVL-9.03915-10.0745
HLA-A24:025HGA2888GKDISTKYMAPEVL-6.56204-6.67544
HLA-A24:025HGA2888GKDISTKYMAPEVL-5.42271-6.45801
HLA-B44:053DX82888GKDISTKYMAPEVL-7.85648-8.89178
HLA-B44:053DX82888GKDISTKYMAPEVL-5.3978-5.5112
HLA-A02:016TDR2888GKDISTKYMAPEVL-3.37154-4.40684

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Vaccine Design for the FusionNeoAntigens of HSP90B1-ACVR1B

check button mRNA and peptide sequences of FusionNeoAntigens that have potential interaction with HLA-Is.
Fusion geneHchrHbpTchrTbpStart in +/-13AAEnd in +/-13AAFusionNeoAntigen peptide sequenceFusionNeoAntigen RNA sequence
HSP90B1-ACVR1Bchr12104337652chr12523806021019STKYMAPEVCTCTACAAAATACATGGCCCCTGAAGT
HSP90B1-ACVR1Bchr12104337652chr12523806021120TKYMAPEVLTACAAAATACATGGCCCCTGAAGTACT
HSP90B1-ACVR1Bchr12104337652chr12523806021220KYMAPEVLAAAATACATGGCCCCTGAAGTACT
HSP90B1-ACVR1Bchr12104337652chr1252380602314YQTGKDISTKYGTACCAAACGGGCAAGGACATCTCTACAAAATA
HSP90B1-ACVR1Bchr12104337652chr1252380602414QTGKDISTKYCCAAACGGGCAAGGACATCTCTACAAAATA
HSP90B1-ACVR1Bchr12104337652chr1252380602514TGKDISTKYAACGGGCAAGGACATCTCTACAAAATA

check button mRNA and peptide sequences of FusionNeoAntigens that have potential interaction with HLA-IIs.
Fusion geneHchrHbpTchrTbpStart in +/-13AAEnd in +/-13AAFusionNeoAntigen peptideFusionNEoAntigen RNA sequence

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Information of the samples that have these potential fusion neoantigens of HSP90B1-ACVR1B

check button These samples were reported as having these fusion breakpoints. For individual breakpoints, we checked the open reading frames considering multiple gene isoforms and chose the in-frame fusion genes only. Then, we made fusion protein sequences and predicted the fusion neoantigens. These fusion-positive samples may have these potential fusion neoantigens.
Cancer typeFusion geneHchrHbpHenstTchrTbpTenstSample
STADHSP90B1-ACVR1Bchr12104337652ENST00000299767chr1252380602ENST00000257963TCGA-CD-8531-01A

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Potential target of CAR-T therapy development for HSP90B1-ACVR1B

check button Predicted 3D structure. We used RoseTTAFold.

check buttonRetention 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, to provide the retention of the transmembrane domain, we only show the protein feature retention information of those transmembrane features


* Minus value of BPloci means that the break point is located before the CDS.
- In-frame and retained 'Transmembrane'.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenProtein featureProtein feature note

check button Subcellular localization prediction of the transmembrane domain retained fusion proteins
* We used DeepLoc 1.0. The order of the X-axis of the barplot is as follows: Entry_ID, Localization, Type, Nucleus, Cytoplasm, Extracellular, Mitochondrion, Cell_membrane, Endoplasmic_reticulum, Plastid, Golgi.apparatus, Lysosome.Vacuole, Peroxisome. Y-axis is the output score of DeepLoc. Clicking the image will open a new tab with a large image.
HgeneHchrHbpHenstTgeneTchrTbpTenstDeepLoc result

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Related Drugs to HSP90B1-ACVR1B

check button Drugs used for this fusion-positive patient.
(Manual curation of PubMed, 04-30-2022 + MyCancerGenome)
HgeneTgeneDrugSourcePMID

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Related Diseases to HSP90B1-ACVR1B

check button Diseases that have this fusion gene.
(Manual curation of PubMed, 04-30-2022 + MyCancerGenome)
HgeneTgeneDiseaseSourcePMID

check button Diseases associated with fusion partners.
(DisGeNet 4.0)
PartnerGeneDisease IDDisease name# pubmedsSource