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Center for Computational Systems Medicine
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Kinase Fusion Gene Summary

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Kinase Fusion Gene Sample Information

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Kinase Fusion ORF Analysis

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Kinase Fusion Amino Acid Sequences

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Multiple Sequence Alignment of All Fusion Protein Isoforms

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Kinase Fusion Protein Functional Features

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Kinase Fusion Protein Structures

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Comparison of Fusion Protein Isoforms

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Comparison of Fusion Protein Sequences/Structures with Known Sequences/Structures from PDB

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pLDDT Scores and Difference Analysis of pLDDT Scores Between the Active Sites (Best) and Non-Active Sites.

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Ramachandran Plot of Kinase Fusion Protein Structure

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Potential Active Site Information

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Virtual Screening Results

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Kinase-Substrate Information

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Related Drugs with This Kinase Fusion Protein

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Related Disease with This Kinase Fusion Protein

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Clinical Trials of the Found Drugs/Small Molecules

Kinase Fusion Gene:RPS6KB1_VMP1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: RPS6KB1_VMP1
KinaseFusionDB ID: KFG5604
FusionGDB2.0 ID: KFG5604
HgeneTgene
Gene symbol

RPS6KB1

VMP1

Gene ID

6198

81671

Gene nameribosomal protein S6 kinase B1vacuole membrane protein 1
SynonymsPS6K|S6K|S6K-beta-1|S6K1|STK14A|p70 S6KA|p70(S6K)-alpha|p70-S6K|p70-alphaEPG3|TANGO5|TMEM49
Cytomap

17q23.1

17q23.1

Type of geneprotein-codingprotein-coding
Descriptionribosomal protein S6 kinase beta-1ribosomal protein S6 kinase Iribosomal protein S6 kinase, 70kDa, polypeptide 1serine/threonine kinase 14 alphaserine/threonine-protein kinase 14Avacuole membrane protein 1ectopic P-granules autophagy protein 3 homologtransmembrane protein 49transport and golgi organization 5 homolog
Modification date2024041120240416
UniProtAcc

P23443

Q96GC9

Ensembl transtripts involved in fusion geneENST idsENST00000225577, ENST00000393021, 
ENST00000406116, ENST00000443572, 
ENST00000587061, 
ENST00000588617, 
ENST00000262291, ENST00000536180, 
ENST00000537567, ENST00000539763, 
ENST00000545362, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: RPS6KB1 [Title/Abstract] AND VMP1 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)RPS6KB1(57970686)-VMP1(57886157), # samples:14
VMP1(57915758)-RPS6KB1(57987922), # samples:4
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgeneRPS6KB1

GO:0031667

response to nutrient levels

29750193

HgeneRPS6KB1

GO:0031670

cellular response to nutrient

22017876

HgeneRPS6KB1

GO:0031929

TOR signaling

12150926

HgeneRPS6KB1

GO:0045948

positive regulation of translational initiation

1922062

HgeneRPS6KB1

GO:0071363

cellular response to growth factor stimulus

17936702

HgeneRPS6KB1

GO:1904263

positive regulation of TORC1 signaling

22017876

TgeneVMP1

GO:0000045

autophagosome assembly

28890335

TgeneVMP1

GO:0006914

autophagy

28890335

TgeneVMP1

GO:0016240

autophagosome membrane docking

28890335

TgeneVMP1

GO:0140056

organelle localization by membrane tethering

28890335

TgeneVMP1

GO:1901896

positive regulation of ATPase-coupled calcium transmembrane transporter activity

28890335

TgeneVMP1

GO:1990456

mitochondrion-endoplasmic reticulum membrane tethering

28890335


check buttonKinase Fusion gene breakpoints across RPS6KB1 (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 buttonKinase Fusion gene breakpoints across VMP1 (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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Kinase Fusion Gene Sample Information

check buttonKinase Fusion gene information.
check button Kinase Fusion gene information from four resources (ChiTars 5.0, ChimerDB 4.0, COSMIC, and CCLE)
* 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.
SourceSampleHgeneHchrHbpTgeneTchrTbp
ChimerDB4TCGA-4Z-AA7QRPS6KB1chr17

57992064

VMP1chr17

57917128

ChimerDB4TCGA-4Z-AA7QRPS6KB1chr17

57992064

VMP1chr17

57917129

ChimerDB4TCGA-86-7711-01ARPS6KB1chr17

58003943

VMP1chr17

57917129

ChimerDB4TCGA-86-7711RPS6KB1chr17

58003943

VMP1chr17

57917128

ChimerDB4TCGA-D7-6519RPS6KB1chr17

57970686

VMP1chr17

57917128

ChimerDB4TCGA-LN-A4A8RPS6KB1chr17

57992064

VMP1chr17

57808781

ChimerDB4TCGA-LN-A4A8RPS6KB1chr17

57992064

VMP1chr17

57808782

ChimerDB4TCGA-93-A4JQ-01ARPS6KB1chr17

57992063

VMP1chr17

57842331

ChimerDB4TCGA-93-A4JQ-01ARPS6KB1chr17

57992064

VMP1chr17

57842332

ChimerDB4TCGA-93-A4JQRPS6KB1chr17

57992064

VMP1chr17

57842331

ChimerDB4TCGA-D8-A27H-01ARPS6KB1chr17

57970686

VMP1chr17

57842332

ChimerDB4TCGA-D8-A27HRPS6KB1chr17

57970686

VMP1chr17

57842331

ChimerDB4TCGA-69-7978-01ARPS6KB1chr17

57970686

VMP1chr17

57814814

ChimerDB4TCGA-24-2280-01ARPS6KB1chr17

57970686

VMP1chr17

57889031

ChimerDB4TCGA-24-2280RPS6KB1chr17

57970686

VMP1chr17

57889030

ChimerDB4TCGA-49-AAQVRPS6KB1chr17

58013902

VMP1chr17

57915656

ChimerDB4TCGA-50-6592-01ARPS6KB1chr17

58007535

VMP1chr17

57915656

ChimerDB4TCGA-50-6592RPS6KB1chr17

58007535

VMP1chr17

57915655

ChimerDB4TCGA-55-A490RPS6KB1chr17

58012661

VMP1chr17

57886157

ChimerDB4TCGA-69-7978-01ARPS6KB1chr17

57992064

VMP1chr17

57886157

ChimerDB4TCGA-69-7978RPS6KB1chr17

57992064

VMP1chr17

57886156

ChimerDB4TCGA-94-8035RPS6KB1chr17

57992064

VMP1chr17

57889031

ChimerDB4TCGA-A8-A09IRPS6KB1chr17

57970686

VMP1chr17

57886156

ChimerDB4TCGA-AC-A2BK-01ARPS6KB1chr17

57987972

VMP1chr17

57886157

ChimerDB4TCGA-AC-A2BKRPS6KB1chr17

57987972

VMP1chr17

57886156

ChimerDB4TCGA-BA-6868RPS6KB1chr17

57990165

VMP1chr17

57915655

ChimerDB4TCGA-BA-6868RPS6KB1chr17

57990165

VMP1chr17

57915656

ChimerDB4TCGA-BH-A0B9RPS6KB1chr17

57992064

VMP1chr17

57915655

ChimerDB4TCGA-C5-A7X5-01ARPS6KB1chr17

58009083

VMP1chr17

57895073

ChimerDB4TCGA-DK-A2I4-01ARPS6KB1chr17

57970686

VMP1chr17

57915656

ChimerDB4TCGA-EY-A1GS-01ARPS6KB1chr17

57992064

VMP1chr17

57851115

ChimerDB4TCGA-HQ-A2OE-01ARPS6KB1chr17

57970686

VMP1chr17

57886157

ChimerDB4TCGA-JL-A3YW-01ARPS6KB1chr17

57970685

VMP1chr17

57915655

ChimerDB4TCGA-JL-A3YWRPS6KB1chr17

57970686

VMP1chr17

57915655

ChimerDB4TCGA-P3-A6T4RPS6KB1chr17

57990165

VMP1chr17

57886157

ChimerDB4TCGA-PQ-A6FI-01ARPS6KB1chr17

57992064

VMP1chr17

57915656

ChimerDB4TCGA-CR-7369RPS6KB1chr17

57971285

VMP1chr17

57915656

ChimerKB4.RPS6KB1chr17

57987922

VMP1chr17

57987922

CCLECOLO-680NRPS6KB1chr17

58018304

VMP1chr17

57889031

CCLETE-11RPS6KB1chr17

58007535

VMP1chr17

57886157

CCLETE-11RPS6KB1chr17

58009083

VMP1chr17

57886157

CCLEMCF7RPS6KB1chr17

57987972

VMP1chr17

57915656

CCLEKPL-1RPS6KB1chr17

57987972

VMP1chr17

57915656

CCLECME-1RPS6KB1chr17

57987972

VMP1chr17

57915656

CCLEC-33 ARPS6KB1chr17

57987972

VMP1chr17

57915656

CCLESNU-1105RPS6KB1chr17

58013902

VMP1chr17

57886157

CCLEVM-CUB1RPS6KB1chr17

58022879

VMP1chr17

57915656

CCLE1273/99RPS6KB1chr17

58003943

VMP1chr17

57895073

CCLETFK-1RPS6KB1chr17

58003943

VMP1chr17

57915656

CCLENCI-H2196RPS6KB1chr17

57970686

VMP1chr17

57842413

CCLENCI-H1385RPS6KB1chr17

57992064

VMP1chr17

57812699

CCLEHMC-1-8RPS6KB1chr17

58022879

VMP1chr17

57917129

CCLEU-251 MGRPS6KB1chr17

57992064

VMP1chr17

57895073

CCLECOV504RPS6KB1chr17

57992064

VMP1chr17

57895073

CCLEC-33 ARPS6KB1chr17

58011885

VMP1chr17

57886157

CCLEICC4RPS6KB1chr17

57970686

VMP1chr17

57917129



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Kinase Fusion ORF Analysis


check buttonKinase Fusion information from ORFfinder translation from full-length transcript sequence from KinaseFusionDB.
HenstTenstHgeneHchrHbpTgeneTchrTbpSeq length
(transcript)
Seq length
(amino acids)
ENST00000443572ENST00000262291RPS6KB1chr1758018304VMP1chr17578890312820527
ENST00000443572ENST00000262291RPS6KB1chr1758013902VMP1chr17578861572793518
ENST00000443572ENST00000262291RPS6KB1chr1758022879VMP1chr17579156562754505
ENST00000443572ENST00000539763RPS6KB1chr1758022879VMP1chr17579171291690463

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Kinase Fusion Amino Acid Sequences


check button For individual full-length fusion transcript sequence from KinaseFusionDB, we ran ORFfinder and chose the longest ORF among the all predicted ones.
>Henst_Tenst_Hgene_Hchr_Hbp_Tgene_Tchr_Tbp_length(fusion AA)_AAseq

>ENST00000443572_ENST00000262291_RPS6KB1_chr17_58018304_VMP1_chr17_57889031_length(amino acids)=527
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIITFSKHIVEQMVAFIGAVPG

--------------------------------------------------------------

>ENST00000443572_ENST00000262291_RPS6KB1_chr17_58013902_VMP1_chr17_57886157_length(amino acids)=518
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLDFASRAKLAV
QKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIITFSKHIVEQMVAFIGAVPGIGPSLQKPF

--------------------------------------------------------------

>ENST00000443572_ENST00000262291_RPS6KB1_chr17_58022879_VMP1_chr17_57915656_length(amino acids)=505
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSAVPGIGPSLQKPFQEYLEAQRQKLHH

--------------------------------------------------------------

>ENST00000443572_ENST00000539763_RPS6KB1_chr17_58022879_VMP1_chr17_57917129_length(amino acids)=463
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVREKTGCPGCLKSWSLSWCVTSSYLSLT

--------------------------------------------------------------

Multiple Sequence Alignment of All Fusion Protein Isoforms



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Kinase Fusion Protein Functional Features


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/chr17:57970686/chr17:57886157)
- 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 buttonMain function of each fusion partner protein. (from UniProt)
HgeneTgene
RPS6KB1

P23443

VMP1

Q96GC9

FUNCTION: Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:23429703, PubMed:28178239, PubMed:22017876). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:23429703, PubMed:28178239, PubMed:22017876). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed:16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed:16286006). The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B (PubMed:16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed:17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed:15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed:11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:19720745, PubMed:19935711, PubMed:19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed:17936702). The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function (PubMed:17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed:18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed:17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239). {ECO:0000250|UniProtKB:P67999, ECO:0000250|UniProtKB:Q8BSK8, ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:12801526, ECO:0000269|PubMed:14673156, ECO:0000269|PubMed:15071500, ECO:0000269|PubMed:15341740, ECO:0000269|PubMed:16286006, ECO:0000269|PubMed:17052453, ECO:0000269|PubMed:17053147, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:18952604, ECO:0000269|PubMed:19085255, ECO:0000269|PubMed:19720745, ECO:0000269|PubMed:19935711, ECO:0000269|PubMed:19995915, ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:28178239}.FUNCTION: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (PubMed:33929485, PubMed:33850023). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (PubMed:33929485, PubMed:33850023). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly (PubMed:28890335, PubMed:30093494, PubMed:30933966, PubMed:33929485, PubMed:33850023). Regulates ATP2A2 activity to control ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required (PubMed:31526472, PubMed:33850023). Modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). Plays an essential role in formation of cell junctions (PubMed:17724469). Upon stress such as bacterial and viral infection, promotes formation of cytoplasmic vacuoles followed by cell death (By similarity). Involved in the cytoplasmic vacuolization of acinar cells during the early stage of acute pancreatitis (By similarity). {ECO:0000250|UniProtKB:Q91ZQ0, ECO:0000269|PubMed:17724469, ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30933966, ECO:0000269|PubMed:31526472, ECO:0000269|PubMed:33850023, ECO:0000269|PubMed:33929485}.; FUNCTION: (Microbial infection) Host factor required for infection by all flaviviruses tested such as Zika virus and Yellow fever virus (PubMed:33338421). Probably required post-entry of the virus to facilitate the ER membrane remodeling necessary to form replication organelles (PubMed:33338421). {ECO:0000269|PubMed:33338421}.

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, 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

download page

* Minus value of BPloci means that the break pointn is located before the CDS.

check button - Retained domain in the 5'-partner of fusion protein (protein functional feature from UniProt).
446446373409446446
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote
HgeneRPS6KB158022879VMP157915656ENST000004435721415353_4231526DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
HgeneRPS6KB158022879VMP157917129ENST000004435721415353_4231526DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
HgeneRPS6KB158013902VMP157886157ENST00000443572121591_3521526DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
HgeneRPS6KB158018304VMP157889031ENST00000443572131591_3521526DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
HgeneRPS6KB158022879VMP157915656ENST00000443572141591_3521526DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
HgeneRPS6KB158022879VMP157917129ENST00000443572141591_3521526DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159


check button - Retained domain in the 3'-partner of fusion protein (protein functional feature from UniProt).
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote


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Kinase Fusion Protein Structures

check button CIF files of the predicted kinase 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.
Kinase Fusion protein CIF link (fusion AA seq ID in KinaseFusionDB)HenstTenstHgeneHchrHbpTgeneTchrTbpAA seqLen(AA seq)
PDB file >>>246_RPS6KB1_VMP1ENST00000443572ENST00000539763RPS6KB1chr1758022879VMP1chr1757917129
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVREKTGCPGCLKSWSLSWCVTSSYLSLT
463
3D view using mol* of 246_RPS6KB1_VMP1
PDB file >>>HKFP_358_RPS6KB1_VMP1ENST00000443572ENST00000262291RPS6KB1chr1758018304VMP1chr1757889031
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIITFSKHIVEQMVAFIGAVPG
527_RPS6KB1_VMP1
PDB file >>>HKFP_359_RPS6KB1_VMP1ENST00000443572ENST00000262291RPS6KB1chr1758013902VMP1chr1757886157
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLDFASRAKLAV
QKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIITFSKHIVEQMVAFIGAVPGIGPSLQKPF
518_RPS6KB1_VMP1
3D view using mol* of HKFP_359_RPS6KB1_VMP1
PDB file >>>HKFP_360_RPS6KB1_VMP1ENST00000443572ENST00000262291RPS6KB1chr1758022879VMP1chr1757915656
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSAVPGIGPSLQKPFQEYLEAQRQKLHH
505_RPS6KB1_VMP1
3D view using mol* of HKFP_360_RPS6KB1_VMP1
PDB file >>>HKFP_361_RPS6KB1_VMP1ENST00000443572ENST00000539763RPS6KB1chr1758022879VMP1chr1757917129
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC
FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS
MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF
TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD
SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVREKTGCPGCLKSWSLSWCVTSSYLSLT
463_RPS6KB1_VMP1
3D view using mol* of HKFP_361_RPS6KB1_VMP1


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Comparison of Fusion Protein Isoforms

check button Superimpose the 3D Structures Among All Fusion Protein Isoforms
* Download the pdb file and open it from the molstar online viewer.
3D view using mol* of viewer/superimpose_isoforms/HKFP_358_RPS6KB1_VMP1_vs_HKFP_359_RPS6KB1_VMP1_superimposed.pdb.html
3D view using mol* of viewer/superimpose_isoforms/HKFP_358_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1_superimposed.pdb.html
3D view using mol* of viewer/superimpose_isoforms/HKFP_358_RPS6KB1_VMP1_vs_HKFP_361_RPS6KB1_VMP1_superimposed.pdb.html
3D view using mol* of viewer/superimpose_isoforms/HKFP_359_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1_superimposed.pdb.html
3D view using mol* of viewer/superimpose_isoforms/HKFP_359_RPS6KB1_VMP1_vs_HKFP_361_RPS6KB1_VMP1_superimposed.pdb.html
3D view using mol* of viewer/superimpose_isoforms/HKFP_360_RPS6KB1_VMP1_vs_HKFP_361_RPS6KB1_VMP1_superimposed.pdb.html

check button Comparison of the Secondary Structures of Fusion Protein Isoforms
./secondary_str/HKFP_359_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_359_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
./secondary_str/HKFP_359_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_359_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1.png
./secondary_str/HKFP_360_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_360_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_358_RPS6KB1_VMP1.png
./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_359_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_359_RPS6KB1_VMP1.png
./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1.png
secondary structure of ./secondary_str/HKFP_361_RPS6KB1_VMP1_vs_HKFP_360_RPS6KB1_VMP1.png

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Comparison of Fusion Protein Sequences/Structures with Known Sequences/Structures from PDB

RPS6KB1_VMP1 does not have any known PDB structures.

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pLDDT score distribution

check button pLDDT score distribution of the predicted fusion protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
* The blue color at the bottom marks the best active site residues.
246_RPS6KB1_VMP1.png
all structure sitemap plddt 246_RPS6KB1_VMP1.png
246_RPS6KB1_VMP1.png
all structure sitemap plddt2 246_RPS6KB1_VMP1.png
HKFP_359_RPS6KB1_VMP1.png
all structure sitemap plddt HKFP_359_RPS6KB1_VMP1.png
HKFP_360_RPS6KB1_VMP1.png
all structure sitemap plddt HKFP_360_RPS6KB1_VMP1.png
HKFP_361_RPS6KB1_VMP1.png
all structure sitemap plddt HKFP_361_RPS6KB1_VMP1.png


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Potential Active Site Information


check button The potential binding sites of these fusion proteins were identified using SiteMap, a module of the Schrodinger suite.
Kinase Fusion AA seq ID in KinaseFusionDBSite scoreSizeDscoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
HKFP_359_RPS6KB1_VMP11.0531691.089326.8790.5240.7350.9780.890.8940.9950.779Chain A: 112,116,187,190,191,192,194,195,196,197,2
15,216,217,218,220,221,222,223,224,225,226,227,228
,229,230,231,232,233,236,237,238,240,241,244,246,2
47,248,249,251,255,319
HKFP_360_RPS6KB1_VMP11.0356551.0521509.8860.4970.7480.9540.5341.0340.5170.799Chain A: 1,2,3,91,93,94,95,96,97,98,99,100,101,102
,103,104,105,106,107,108,112,113,116,117,120,124,1
33,136,137,145,146,147,148,149,150,151,152,153,156
,159,187,190,191,192,194,195,196,197,199,202,204,2
05,212,213,214,215,216,217,218,219,220,221,222,223
,224,225,226,227,228,229,230,231,232,233,234,236,2
37,238,241,242,244,246,247,248,249,251,255,279,350
,352,353,354,356,359,360,363,368,369,370
HKFP_361_RPS6KB1_VMP11.0971101.088286.7480.50.8431.1680.7561.0990.6880.72Chain A: 102,115,116,119,194,195,196,197,216,217,2
18,219,227,228,229,230,231,232,233,236,237,238,241
,242,244,247,251,252,255

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Ramachandran Plot of Kinase Fusion Protein Structure


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this fusion protein peptide.

246_RPS6KB1_VMP1_ramachandran.png
all structure RPS6KB1-VMP1
HKFP_359_RPS6KB1_VMP1_ramachandran.png
all structure RPS6KB1-VMP1
HKFP_360_RPS6KB1_VMP1_ramachandran.png
all structure RPS6KB1-VMP1
HKFP_361_RPS6KB1_VMP1_ramachandran.png
all structure RPS6KB1-VMP1

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Virtual Screening Results


check button Distribution of the average docking score across all approved kinase inhibitors.
Distribution of the number of occurrence across all approved kinase inhibitors.
5'-kinase fusion protein case
all structure RPS6KB1-VMP1
3'-kinase fusion protein case

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check button Drug information from DrugBank of the top 20 interacting small molecules.
* The detailed information of individual kinase inhibitors are available in the download page.
Fusion gene name infoDrugDocking scoreGlide g scoreGlide energy
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Ripretinib-6.2699099999999985-6.27691-51.3774
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Ripretinib-6.2699099999999985-6.27691-51.3774
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Sunitinib-6.2695-6.2737-54.1429
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Sorafenib-6.22241-6.23451-45.5832
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Sorafenib-6.22241-6.23451-45.5832
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Asciminib-6.2155-6.6805-37.5782
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Asciminib-6.20927-6.67427-38.1841
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Abrocitinib-5.99199-6.00309-42.0783
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Abrocitinib-5.99199-6.00309-42.0783
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Baricitinib-5.9853-5.9853-43.9125
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Upadacitinib-5.96638-5.96738-43.1799
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Lenvatinib-5.83875-5.83875-44.5716
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Cabozantinib-5.77464-5.81964-49.8536
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Cabozantinib-5.77464-5.81964-49.8536
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Tivozanib-5.64131-5.64131-46.226000000000006
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Larotrectinib-5.62903-5.62903-31.1636
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Fedratinib-5.53558-5.5869800000000005-63.0163
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Fedratinib-5.53558-5.5869800000000005-63.0163
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Tofacitinib-5.4676300000000015-5.4791300000000005-31.5994
HKFP_360_RPS6KB1_VMP1_vsw_3-DOCK_HTVS_1-001Tofacitinib-5.4676300000000015-5.4791300000000005-31.5994
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Baricitinib-4.69586-4.69586-36.9878
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Ibrutinib-4.62661-4.62661-41.878
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Tucatinib-4.55999-4.93519-44.4708
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Vemurafenib-4.55195-4.99595-41.9236
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Vemurafenib-4.55195-4.99595-41.9236
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Vandetanib-4.45964-4.45964-42.2799
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Lenvatinib-4.31174-4.31174-31.5182
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Tepotinib-4.2987-4.2998-48.5758
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Ponatinib-4.2811-4.4877-44.3021
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Ponatinib-4.2811-4.4877-44.3021
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Ponatinib-4.2811-4.4877-44.3021
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Imatinib-4.1469-4.3535-43.2204
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Imatinib-4.1469-4.3535-43.2204
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Imatinib-4.1469-4.3535-43.2204
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Sorafenib-4.12129-4.13339-39.7904
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Sorafenib-4.12129-4.13339-39.7904
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Pexidartinib-3.99972-4.21652-31.6439
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Pexidartinib-3.99972-4.21652-31.6439
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Zanubrutinib-3.89963-3.89963-34.9466
HKFP_361_RPS6KB1_VMP1_vsw_4-DOCK_HTVS_1-001Fostamatinib-3.85766-3.92126-43.8182
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Imatinib-6.67938-7.434080000000001-43.4699
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Imatinib-6.67938-7.434080000000001-43.4699
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Imatinib-6.67938-7.434080000000001-43.4699
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pexidartinib-6.45726-6.674060000000001-43.951
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pexidartinib-6.45726-6.674060000000001-43.951
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Cabozantinib-6.27254-6.31754-46.7445
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Cabozantinib-6.27254-6.31754-46.7445
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pralsetinib-6.174580000000001-7.32678-35.4534
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Selpercatinib-6.1304099999999995-6.160909999999999-43.2315
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Ibrutinib-6.014530000000001-6.014530000000001-43.0274
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Neratinib-6.00401-6.18631-52.5765
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Neratinib-6.00401-6.18631-52.5765
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Sorafenib-5.93014-5.94224-46.9252
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Sorafenib-5.93014-5.94224-46.9252
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Ruxolitinib-5.92469-5.92469-32.2087
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pazopanib-5.85025-5.85715-42.1085
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pazopanib-5.85025-5.85715-42.1085
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Baricitinib-5.8394-5.8394-39.3011
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Pralsetinib-5.81118-5.90268-31.49
246_RPS6KB1_VMP1-DOCK_HTVS_1-001Osimertinib-5.7612-5.7689-37.7112

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Kinase-Substrate Information of RPS6KB1_VMP1


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
RPS6KB1P23443humanBACH2Q9BYV9S521ETRTRTssSCSsYsY
RPS6KB1P23443humanIRS1P35568S636sGDyMPMsPKsVSAP
RPS6KB1P23443humanNDRG2Q9UN36S350RsRsRtLsQssEsGt
RPS6KB1P23443humanKHSRPQ92945S395DLLQSLrsGPPGPPG
RPS6KB1P23443humanPDCD4Q53EL6S67kRRLRKNssRDsGrG
RPS6KB1P23443humanTP63Q9H3D4S560LARLGCSsCLDYFTTSAM_2
RPS6KB1P23443humanMTORP42345S2448RsRtRtDsysAGQsV
RPS6KB1P23443humanTRIB2Q92519S83FRAVHLHsGEELVCKPkinase
RPS6KB1P23443humanRPS6P62753S240RLssLRAstsKsEss
RPS6KB1P23443humanRPS6KB1P23443T412NQVFLGFtyVAPsVLPkinase_C
RPS6KB1P23443humanSMN1Q16637S49AyDkAVAsFkHALkNSMN
RPS6KB1P23443humanEEF2KO00418S366sPQVRtLsGSRPPLL
RPS6KB1P23443humanBACH2Q9BYV9S520LETRTRTssSCSsYs
RPS6KB1P23443humanMXD1Q05195S145IERIRMDsIGSTVSS
RPS6KB1P23443humanIRS1P35568S307TRRsRtEsItAtsPA
RPS6KB1P23443humanURI1O94763S372AKRKRKNstGsGHsA
RPS6KB1P23443humanMAPTP10636-8S262NVKskIGstENLkHQTubulin-binding
RPS6KB1P23443humanPDCD4Q53EL6S457RGRKRFVsEGDGGRL
RPS6KB1P23443humanIRS1P35568S527RFRKRtHsAGtsPtI
RPS6KB1P23443humanNCBP1Q09161S7_MSRRRHsDENDGGQ
RPS6KB1P23443humanIRS1P35568S270EFRPRsKsQSssNCs
RPS6KB1P23443humanH2BC3P33778S36RKRsRkEsysIyVykHistone
RPS6KB1P23443humanPIP5K1CO60331T553QPRYRRRtQssGQDG
RPS6KB1P23443humanPOLDIP3Q9BY77S385PRRVNsAsSsNPPAE
RPS6KB1P23443humanTARBP2Q15633S283ILSLRsCsLGsLGAL
RPS6KB1P23443humanMTORP42345T2446NKRsRtRtDsysAGQ
RPS6KB1P23443humanFMR1Q06787S500NSEASNAsETESDHRFXMRP1_C_core
RPS6KB1P23443humanIRS1P35568S1101GCRRRHssEtFsStP
RPS6KB1P23443humanRPS6P62753S244LRAstsKsEssQK__
RPS6KB1P23443humanGSK3BP49841S9SGRPRttsFAEsCkP
RPS6KB1P23443humanZBTB33Q86T24T606yLSDRSStIPAMkDD
RPS6KB1P23443humanNDRG2Q9UN36S332LsRsRtAsLtsAAsV
RPS6KB1P23443humanMAPTP10636-8S214GsRsRtPsLPtPPtR
RPS6KB1P23443humanDEPTORQ8TB45S287sMssCGssGyFsssP
RPS6KB1P23443humanESR1P03372S167GGRERLAsTNDkGSMOest_recep
RPS6KB1P23443humanLTC4SQ16873S36ARRAFRVsPPLtTGPMAPEG
RPS6KB1P23443humanRPS6P62753S236AKRRRLssLRAstsK
RPS6KB1P23443humanMRE11P49959T597sQrGrADtGLETSTr
RPS6KB1P23443humanCADP27708S1859PPRIhRAsDPGLPAE
RPS6KB1P23443humanNCBP1Q09161S22PHKRRKtsDANEtED
RPS6KB1P23443humanDEPTORQ8TB45S286ssMssCGssGyFsss
RPS6KB1P23443humanEGLN1Q9GZT9S125ADPAAAAsPCRAAAG
RPS6KB1P23443humanCCT2P78371S260GsRVRVDstAkVAEICpn60_TCP1
RPS6KB1P23443humanMAPTP10636-8T212tPGsRsRtPsLPtPP
RPS6KB1P23443humanPIP5K1CO60331S555RYRRRtQssGQDGRP
RPS6KB1P23443humanGLI1P08151S84LTKKRALsISPLSDA
RPS6KB1P23443humanMSH6P52701S309RMVtGNGsLKRKSSR
RPS6KB1P23443humanRICTORQ6R327T1135NRRIRtLtEPsVDFNRICTOR_phospho
RPS6KB1P23443humanSRPK2P78362S494HDRSRtVsAsstGDL
RPS6KB1P23443humanNCBP1Q09161T21QPHKRRKtsDANEtE
RPS6KB1P23443humanEIF4BP23588S422RERsRtGsEssQtGt
RPS6KB1P23443humanRPS6P62753S235IAKRRRLssLRAsts
RPS6KB1P23443humanPOLDIP3Q9BY77S383ELPRRVNsAsSsNPP
RPS6KB1P23443humanDEPTORQ8TB45S291CGssGyFsssPtLss
RPS6KB1P23443humanEPRS1P07814S999NQGGGLsssGAGEGQ
RPS6KB1P23443humanCDK1P06493S39MkkIRLEsEEEGVPsPkinase
RPS6KB1P23443-2humanGSK3BP49841S9SGRPRttsFAEsCkP
RPS6KB1P23443-2humanEPRS1P07814S999NQGGGLsssGAGEGQ


check button Biological Network Integration of This Kinase and Substrates
(GeneMANIA website)

check button Enriched GO biological processes of the phosphorylation target genes of the kinase
KinaseGOIDGO termP.adjust
RPS6KB1IDDescription0.00e+00
RPS6KB1GO:0045927positive regulation of growth4.45e-04
RPS6KB1GO:0006446regulation of translational initiation4.45e-04
RPS6KB1GO:0032868response to insulin4.45e-04
RPS6KB1GO:0032869cellular response to insulin stimulus9.65e-04
RPS6KB1GO:0043086negative regulation of catalytic activity9.65e-04
RPS6KB1GO:1900034regulation of cellular response to heat9.65e-04
RPS6KB1GO:0006413translational initiation9.65e-04
RPS6KB1GO:0051348negative regulation of transferase activity9.69e-04
RPS6KB1GO:0045936negative regulation of phosphate metabolic process1.25e-03
RPS6KB1GO:0010563negative regulation of phosphorus metabolic process1.25e-03
RPS6KB1GO:0043434response to peptide hormone2.49e-03
RPS6KB1GO:0031929TOR signaling2.49e-03
RPS6KB1GO:0018105peptidyl-serine phosphorylation2.79e-03
RPS6KB1GO:0018209peptidyl-serine modification3.19e-03
RPS6KB1GO:0071375cellular response to peptide hormone stimulus3.19e-03
RPS6KB1GO:0033673negative regulation of kinase activity3.47e-03
RPS6KB1GO:0006403RNA localization3.47e-03
RPS6KB1GO:0006913nucleocytoplasmic transport3.47e-03
RPS6KB1GO:0051169nuclear transport3.47e-03
RPS6KB1GO:0046777protein autophosphorylation3.47e-03
RPS6KB1GO:1901653cellular response to peptide6.48e-03
RPS6KB1GO:0051028mRNA transport8.35e-03
RPS6KB1GO:0033002muscle cell proliferation8.39e-03
RPS6KB1GO:0030850prostate gland development8.98e-03
RPS6KB1GO:0001558regulation of cell growth9.68e-03
RPS6KB1GO:0043467regulation of generation of precursor metabolites and energy9.68e-03
RPS6KB1GO:0045727positive regulation of translation9.68e-03
RPS6KB1GO:0060525prostate glandular acinus development9.68e-03
RPS6KB1GO:1905214regulation of RNA binding9.68e-03
RPS6KB1GO:1900180regulation of protein localization to nucleus9.68e-03
RPS6KB1GO:0031400negative regulation of protein modification process1.03e-02
RPS6KB1GO:0010921regulation of phosphatase activity1.20e-02
RPS6KB1GO:0002181cytoplasmic translation1.20e-02
RPS6KB1GO:0050657nucleic acid transport1.20e-02
RPS6KB1GO:0050658RNA transport1.20e-02
RPS6KB1GO:0031100animal organ regeneration1.20e-02
RPS6KB1GO:0048524positive regulation of viral process1.20e-02
RPS6KB1GO:0051236establishment of RNA localization1.20e-02
RPS6KB1GO:0030307positive regulation of cell growth1.23e-02
RPS6KB1GO:0034605cellular response to heat1.23e-02
RPS6KB1GO:0001655urogenital system development1.23e-02
RPS6KB1GO:0048639positive regulation of developmental growth1.23e-02
RPS6KB1GO:0051168nuclear export1.23e-02
RPS6KB1GO:0034250positive regulation of amide metabolic process1.23e-02
RPS6KB1GO:0038203TORC2 signaling1.23e-02
RPS6KB1GO:1900452regulation of long-term synaptic depression1.23e-02
RPS6KB1GO:0006406mRNA export from nucleus1.25e-02
RPS6KB1GO:0016049cell growth1.28e-02
RPS6KB1GO:0043201response to leucine1.28e-02

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Related Drugs to RPS6KB1_VMP1


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

check button Distribution of the number of studies mentioning RPS6KB1-VMP1 and kinase inhibitors the PubMed Abstract (04-01-2024)

Fusion gene - drug pair 1Fusion gene - drug pair 2PMIDPublication dateDOIStudy title

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Related Diseases to RPS6KB1_VMP1


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

check button Related diseases from the literature mentioned this fusion gene and drug.
(PubMed, 04-01-2024)
MeSH IDMeSH term

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


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Clinical Trials of the Found Drugs/Small Molecules


check button Statistics of the Clinical Trials of the Found Kinase Inibitors from clinicaltrials.gov (06-17-2024)

check button Clinical Trials from clinicaltrials.gov (06-17-2024)

Fusion GeneKinase InhibitorNCT IDStudy StatusPhasesDisease# EnrolmentDate