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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:AMBP_RPS6KB1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: AMBP_RPS6KB1
KinaseFusionDB ID: KFG342
FusionGDB2.0 ID: KFG342
HgeneTgene
Gene symbol

AMBP

RPS6KB1

Gene ID

259

6198

Gene namealpha-1-microglobulin/bikunin precursorribosomal protein S6 kinase B1
SynonymsA1M|EDC1|HCP|HI30|IATIL|ITI|ITIL|ITILC|UTIPS6K|S6K|S6K-beta-1|S6K1|STK14A|p70 S6KA|p70(S6K)-alpha|p70-S6K|p70-alpha
Cytomap

9q32

17q23.1

Type of geneprotein-codingprotein-coding
Descriptionprotein AMBPbikunincomplex-forming glycoprotein heterogeneous in chargegrowth-inhibiting protein 19inter-alpha-trypsin inhibitor light chainprotein HCtrypstatinuristatinuronic-acid-rich proteinribosomal protein S6 kinase beta-1ribosomal protein S6 kinase Iribosomal protein S6 kinase, 70kDa, polypeptide 1serine/threonine kinase 14 alphaserine/threonine-protein kinase 14A
Modification date2024033020240411
UniProtAcc

P02760

P23443

Ensembl transtripts involved in fusion geneENST idsENST00000265132, ENST00000225577, 
ENST00000393021, ENST00000406116, 
ENST00000443572, ENST00000587061, 
Context (manual curation of fusion genes in KinaseFusionDB)

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

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)AMBP(116822407)-RPS6KB1(57978987), # samples:1
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
TgeneRPS6KB1

GO:0031667

response to nutrient levels

29750193

TgeneRPS6KB1

GO:0031670

cellular response to nutrient

22017876

TgeneRPS6KB1

GO:0031929

TOR signaling

12150926

TgeneRPS6KB1

GO:0045948

positive regulation of translational initiation

1922062

TgeneRPS6KB1

GO:0071363

cellular response to growth factor stimulus

17936702

TgeneRPS6KB1

GO:1904263

positive regulation of TORC1 signaling

22017876


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

check buttonKinase Fusion gene breakpoints across RPS6KB1 (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.


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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
ChiTaRS5.0AV698075AMBPchr9

116822407

RPS6KB1chr17

57978987



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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)

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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

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/:116822407/:57978987)
- 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
AMBP

P02760

RPS6KB1

P23443

FUNCTION: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32823731, PubMed:32092412). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:23642167, PubMed:22096585). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:21356557, ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:23157686, ECO:0000269|PubMed:23642167, ECO:0000269|PubMed:25698971, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:32823731}.; FUNCTION: [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion (PubMed:25301953, PubMed:20463016). Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:16873769, PubMed:10480954, PubMed:15917224). As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (PubMed:7676539). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:10480954, ECO:0000269|PubMed:15917224, ECO:0000269|PubMed:16873769, ECO:0000269|PubMed:20463016, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:7676539}.; FUNCTION: [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}.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}.

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).
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote


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


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Kinase-Substrate Information of AMBP_RPS6KB1


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 AMBP_RPS6KB1


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 AMBP-RPS6KB1 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 AMBP_RPS6KB1


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