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Fusion gene ID: 16836 |
FusionGeneSummary for HSP90AA1_RNF31 |
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Fusion gene information | Fusion gene name: HSP90AA1_RNF31 | Fusion gene ID: 16836 | Hgene | Tgene | Gene symbol | HSP90AA1 | RNF31 | Gene ID | 3320 | 55072 |
Gene name | heat shock protein 90 alpha family class A member 1 | ring finger protein 31 | |
Synonyms | EL52|HEL-S-65p|HSP86|HSP89A|HSP90A|HSP90N|HSPC1|HSPCA|HSPCAL1|HSPCAL4|HSPN|Hsp103|Hsp89|Hsp90|LAP-2|LAP2 | HOIP|Paul|ZIBRA | |
Cytomap | 14q32.31 | 14q12 | |
Type of gene | protein-coding | protein-coding | |
Description | heat shock protein HSP 90-alphaHSP 86LPS-associated protein 2epididymis luminal secretory protein 52epididymis secretory sperm binding protein Li 65pheat shock 86 kDaheat shock 90kD protein 1, alphaheat shock 90kD protein 1, alpha-like 4heat shock | E3 ubiquitin-protein ligase RNF31HOIL-1-interacting proteinRING-type E3 ubiquitin transferase RNF31zinc in-between-RING-finger ubiquitin-associated domain protein | |
Modification date | 20180527 | 20180527 | |
UniProtAcc | P07900 | Q96EP0 | |
Ensembl transtripts involved in fusion gene | ENST00000216281, ENST00000334701, ENST00000441629, ENST00000558600, | ENST00000557878, ENST00000559275, ENST00000324103, ENST00000382687, | |
Fusion gene scores | * DoF score | 15 X 16 X 3=720 | 5 X 5 X 4=100 |
# samples | 17 | 6 | |
** MAII score | log2(17/720*10)=-2.08246216019197 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | log2(6/100*10)=-0.736965594166206 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0 | |
Context | PubMed: HSP90AA1 [Title/Abstract] AND RNF31 [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) |
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Partner | Gene | GO ID | GO term | PubMed ID |
Hgene | HSP90AA1 | GO:0001934 | positive regulation of protein phosphorylation | 19363271 |
Hgene | HSP90AA1 | GO:0007004 | telomere maintenance via telomerase | 10197982 |
Hgene | HSP90AA1 | GO:0031396 | regulation of protein ubiquitination | 16809764 |
Hgene | HSP90AA1 | GO:0032273 | positive regulation of protein polymerization | 19363271 |
Hgene | HSP90AA1 | GO:0045040 | protein import into mitochondrial outer membrane | 15644312 |
Hgene | HSP90AA1 | GO:0051131 | chaperone-mediated protein complex assembly | 15644312 |
Hgene | HSP90AA1 | GO:0051973 | positive regulation of telomerase activity | 10197982 |
Hgene | HSP90AA1 | GO:1902949 | positive regulation of tau-protein kinase activity | 19363271 |
Hgene | HSP90AA1 | GO:1905323 | telomerase holoenzyme complex assembly | 10197982 |
Tgene | RNF31 | GO:0000209 | protein polyubiquitination | 12629548|17006537 |
Tgene | RNF31 | GO:0043123 | positive regulation of I-kappaB kinase/NF-kappaB signaling | 19136968|21455173 |
Tgene | RNF31 | GO:0050852 | T cell receptor signaling pathway | 20005846 |
Tgene | RNF31 | GO:0051092 | positive regulation of NF-kappaB transcription factor activity | 19136968 |
Tgene | RNF31 | GO:0097039 | protein linear polyubiquitination | 21455173|21455180|21455181|23453807 |
![]() (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 | BU675940 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
* LD: Li Ding group's fusion gene list RV: Roel Verhaak group's fusion gene list ChiTaRs fusion database |
![]() * 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-intron | ENST00000216281 | ENST00000557878 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000216281 | ENST00000559275 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000216281 | ENST00000324103 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000216281 | ENST00000382687 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000334701 | ENST00000557878 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000334701 | ENST00000559275 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000334701 | ENST00000324103 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000334701 | ENST00000382687 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000441629 | ENST00000557878 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000441629 | ENST00000559275 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000441629 | ENST00000324103 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000441629 | ENST00000382687 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000558600 | ENST00000557878 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000558600 | ENST00000559275 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000558600 | ENST00000324103 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
intron-intron | ENST00000558600 | ENST00000382687 | HSP90AA1 | chr14 | 102551263 | + | RNF31 | chr14 | 24635672 | + |
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FusionProtFeatures for HSP90AA1_RNF31 |
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Hgene | Tgene |
HSP90AA1 | RNF31 |
Molecular chaperone that promotes the maturation,structural maintenance and proper regulation of specific targetproteins involved for instance in cell cycle control and signaltransduction. Undergoes a functional cycle that is linked to itsATPase activity which is essential for its chaperone activity.This cycle probably induces conformational changes in the clientproteins, thereby causing their activation. Interacts dynamicallywith various co-chaperones that modulate its substraterecognition, ATPase cycle and chaperone function (PubMed:11274138,PubMed:15577939, PubMed:15937123, PubMed:27353360,PubMed:29127155). Engages with a range of client protein classesvia its interaction with various co-chaperone proteins orcomplexes, that act as adapters, simultaneously able to interactwith the specific client and the central chaperone itself(PubMed:29127155). Recruitment of ATP and co-chaperone followed byclient protein forms a functional chaperone. After the completionof the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformationand finally, ADP is released from HSP90 which acquires an openconformation for the next cycle (PubMed:27295069,PubMed:26991466). Apart from its chaperone activity, it also playsa role in the regulation of the transcription machinery. HSP90 andits co-chaperones modulate transcription at least at threedifferent levels (PubMed:25973397). In the first place, they alterthe steady-state levels of certain transcription factors inresponse to various physiological cues(PubMed:25973397). Second,they modulate the activity of certain epigenetic modifiers, suchas histone deacetylases or DNA methyl transferases, and therebyrespond to the change in the environment (PubMed:25973397). Third,they participate in the eviction of histones from the promoterregion of certain genes and thereby turn on gene expression(PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) andmediates LPS-induced inflammatory response, including TNFsecretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).{ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205,ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123,ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:27353360,ECO:0000269|PubMed:29127155, ECO:0000303|PubMed:25973397,ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}. | E3 ubiquitin-protein ligase component of the LUBACcomplex which conjugates linear ('Met-1'-linked) polyubiquitinchains to substrates and plays a key role in NF-kappa-B activationand regulation of inflammation (PubMed:17006537, PubMed:19136968,PubMed:20005846, PubMed:21455173, PubMed:21455180,PubMed:21455181, PubMed:22863777). LUBAC conjugates linearpolyubiquitin to IKBKG and RIPK1 and is involved in activation ofthe canonical NF-kappa-B and the JNK signaling pathways(PubMed:17006537, PubMed:19136968, PubMed:20005846,PubMed:21455173, PubMed:21455180, PubMed:21455181,PubMed:22863777). Linear ubiquitination mediated by the LUBACcomplex interferes with TNF-induced cell death and therebyprevents inflammation (PubMed:21455173). LUBAC is proposed to berecruited to the TNF-R1 signaling complex (TNF-RSC) followingpolyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 andto conjugate linear polyubiquitin to IKBKG and possibly othercomponents contributing to the stability of the complex(PubMed:20005846). Together with otulin, the LUBAC complexregulates the canonical Wnt signaling during angiogenesis. Bindspolyubiquitin of different linkage types (PubMed:23708998).{ECO:0000269|PubMed:17006537, ECO:0000269|PubMed:19136968,ECO:0000269|PubMed:20005846, ECO:0000269|PubMed:21455173,ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181,ECO:0000269|PubMed:22863777, ECO:0000269|PubMed:23708998}. |
![]() * 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 HSP90AA1_RNF31 |
![]() (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 HSP90AA1_RNF31 |
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Hgene | Hgene's interactors | Tgene | Tgene's interactors |
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Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Still interaction with |
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Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Interaction lost with |
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Partner | Gene | Hbp | Tbp | ENST | Strand | BPexon | TotalExon | Protein feature loci | *BPloci | TotalLen | Interaction lost with |
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RelatedDrugs for HSP90AA1_RNF31 |
![]() (DrugBank Version 5.1.0 2018-04-02) |
Partner | Gene | UniProtAcc | DrugBank ID | Drug name | Drug activity | Drug type | Drug status |
Hgene | HSP90AA1 | P07900 | DB00615 | Rifabutin | Heat shock protein HSP 90-alpha | small molecule | approved|investigational |
Hgene | HSP90AA1 | P07900 | DB00716 | Nedocromil | Heat shock protein HSP 90-alpha | small molecule | approved|investigational |
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RelatedDiseases for HSP90AA1_RNF31 |
![]() (DisGeNet 4.0) |
Partner | Gene | Disease ID | Disease name | # pubmeds | Source |
Hgene | HSP90AA1 | C0009178 | Cocaine withdrawal | 1 | PSYGENET |
Hgene | HSP90AA1 | C0011616 | Contact Dermatitis | 1 | CTD_human |
Hgene | HSP90AA1 | C0019693 | HIV Infections | 1 | CTD_human |
Hgene | HSP90AA1 | C0027627 | Neoplasm Metastasis | 1 | CTD_human |
Hgene | HSP90AA1 | C0041696 | Unipolar Depression | 1 | PSYGENET |
Hgene | HSP90AA1 | C0206180 | Ki-1+ Anaplastic Large Cell Lymphoma | 1 | CTD_human |
Hgene | HSP90AA1 | C0525045 | Mood Disorders | 1 | PSYGENET |
Hgene | HSP90AA1 | C1269683 | Major Depressive Disorder | 1 | PSYGENET |
Hgene | HSP90AA1 | C1458155 | Mammary Neoplasms | 1 | CTD_human |