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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:MAP3K13_ATR

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: MAP3K13_ATR
KinaseFusionDB ID: KFG3355
FusionGDB2.0 ID: KFG3355
HgeneTgene
Gene symbol

MAP3K13

ATR

Gene ID

9175

390502

Gene namemitogen-activated protein kinase kinase kinase 13
SynonymsLZK|MEKK13|MLK
Cytomap

3q27.2

Type of geneprotein-coding
Descriptionmitogen-activated protein kinase kinase kinase 13leucine zipper-bearing kinasemixed lineage kinase
Modification date20240305
UniProtAcc

O43283

Q9H6X2

Ensembl transtripts involved in fusion geneENST idsENST00000446828, ENST00000424227, 
ENST00000443863, ENST00000535426, 
ENST00000265026, ENST00000448876, 
ENST00000454237, ENST00000438798, 
ENST00000350721, ENST00000383101, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: MAP3K13 [Title/Abstract] AND ATR [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgeneMAP3K13

GO:0006468

protein phosphorylation

9353328|11726277

HgeneMAP3K13

GO:0007254

JNK cascade

9353328|11726277

HgeneMAP3K13

GO:0046777

protein autophosphorylation

9353328

HgeneMAP3K13

GO:0051092

positive regulation of NF-kappaB transcription factor activity

12492477

HgeneMAP3K13

GO:0051403

stress-activated MAPK cascade

11726277


check buttonKinase Fusion gene breakpoints across MAP3K13 (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 ATR (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
CCLELN-319MAP3K13chr3

185003431

ATRchr3

142172075



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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)
ENST00000446828ENST00000350721MAP3K13chr3185003431ATRchr3142172075674105

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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

>ENST00000446828_ENST00000350721_MAP3K13_chr3_185003431_ATR_chr3_142172075_length(amino acids)=105
MYCGIQILALWESVLKTFLHDPLVEWSKPVKGHSKAPLNETGEVVNEKAKTHVLDIEQRLQGVIKTRNRVTGLPLSIEGHVHYLIQEATD

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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/chr3:/chr3:)
- 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
MAP3K13

O43283

ATR

Q9H6X2

FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B. {ECO:0000269|PubMed:11726277, ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:9353328}.FUNCTION: Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells. {ECO:0000269|PubMed:15777794, ECO:0000269|PubMed:16762926}.; FUNCTION: (Microbial infection) Acts as a receptor for protective antigen (PA) of B.anthracis. {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:16762926, ECO:0000269|PubMed:20585457}.

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
TgeneMAP3K13185003431ATR142172075ENST0000044682843462612_264424872581DomainNote=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535
TgeneMAP3K13185003431ATR142172075ENST0000044682844472612_264425512645DomainNote=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535


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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 >>>296_MAP3K13_ATRENST00000446828ENST00000350721MAP3K13chr3185003431ATRchr3142172075
MYCGIQILALWESVLKTFLHDPLVEWSKPVKGHSKAPLNETGEVVNEKAKTHVLDIEQRLQGVIKTRNRVTGLPLSIEGHVHYLIQEATD
105
3D view using mol* of 296_MAP3K13_ATR
PDB file >>>TKFP_516_MAP3K13_ATRENST00000446828ENST00000350721MAP3K13chr3185003431ATRchr3142172075
MYCGIQILALWESVLKTFLHDPLVEWSKPVKGHSKAPLNETGEVVNEKAKTHVLDIEQRLQGVIKTRNRVTGLPLSIEGHVHYLIQEATD
105_MAP3K13_ATR


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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.

check button Comparison of the Secondary Structures of Fusion Protein Isoforms

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

MAP3K13_ATR 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.


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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

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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.


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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
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

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Kinase-Substrate Information of MAP3K13_ATR


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
ATRQ13535humanPARP1P09874S179FRPEYsAsQLkGFsLzf-PARP
ATRQ13535humanRBBP8Q99708T859WEVGFPStQTCMERGSAE2
ATRQ13535humanATRIPQ8WXE1S68EELDTLAsQALsQCP
ATRQ13535humanMCCP23508S120LRsELsQsQHEVNED
ATRQ13535humanTP53BP1Q12888T302PEPEVLstQEDLFDQ
ATRQ13535humanSIRT7Q9NRC8S134TLLQkGRsVsAADLSSIR2
ATRQ13535humanSIRT7Q9NRC8S136LQkGRsVsAADLSEASIR2
ATRQ13535humanUIMC1Q96RL1S205sGsWDQSsQPVFENV
ATRQ13535humanCUX1P39880S1357ADtEEPKsQGEAERE
ATRQ13535humanE2F1Q01094S31ALRLLDSsQIVIISA
ATRQ13535humanTP53P04637S37NVLsPLPsQAMDDLMTAD2
ATRQ13535humanMDM2Q00987S407SSSIIyssQEDVKEF
ATRQ13535humanXPAP23025S196RSLEVWGsQEALEEA
ATRQ13535humanSP1P08047S101DLTATQLsQGANGWQ
ATRQ13535humanBRCA1P38398S1280QVILAkAsQEHHLsE
ATRQ13535humanGINS2Q9Y248S182QPLEstQsQDF____
ATRQ13535humanMCPH1Q8NEM0S322QKQAAGMsQETFEEkMicrocephalin
ATRQ13535humanCHEK1O14757S317ENVkYsssQPEPRTG
ATRQ13535humanDBF4Q9UBU7S502FSTDNSGsQPKQKsD
ATRQ13535humanFARSAQ9Y285S301QRVkRtHsQGGyGsQtRNA-synt_2d
ATRQ13535humanFANCD2Q9BXW9S717KDGGPVTsQESGQkLFancD2
ATRQ13535humanNPM1P06748S125AVEEDAEsEDEEEED
ATRQ13535humanFANCD2Q9BXW9T691yGLEEYDtQDGIAINFancD2
ATRQ13535humanCDKN2AP42771S7_MEPAAGssMEPSAD
ATRQ13535humanCDKN2AP42771S152IDAAEGPsDIPD___
ATRQ13535humanSMC1AQ14683S957IsQEEGssQGEDsVsSMC_N
ATRQ13535humanSUGP2Q8IX01T7_MAARRItQEtFDAV
ATRQ13535humanBRCA1P38398S1524LQNRNYPsQEELIKV
ATRQ13535humanBLMP54132T99NAPAGQEtQRGGSkSBLM_N
ATRQ13535humanFANCD2Q9BXW9T596RsEsPsLtQERANLSFancD2
ATRQ13535humanRPA2P15927S72RIGNVEIsQVTIVGI
ATRQ13535humanDCLRE1CQ96SD1S645NLSTNADsQsssDFE
ATRQ13535humanCREB1P16220S107sVDsVtDsQKRREILpKID
ATRQ13535humanIRS1P35568S270EFRPRsKsQSssNCs
ATRQ13535humanFANCAO15360S1449AAPDADLsQEPHLF_
ATRQ13535humanKMT2AQ03164S516VHPPLPIsQsPENES
ATRQ13535humanAKAP12Q02952S732TDGILAGsQEHDPGQ
ATRQ13535humanRPA2P15927S174MVLSkANsQPSAGRARPA_C
ATRQ13535humanHUWE1Q7Z6Z7S2391DEAPsNLsQAstLQA
ATRQ13535humanCNOT2Q9NZN8S101PQLNRsLsQGtQLPs
ATRQ13535humanBRCA1P38398S1423AVLEQHGsQPSNSYP
ATRQ13535humanSMC1AQ14683S966GEDsVsGsQRIssIySMC_N
ATRQ13535humanPELP1Q8IZL8S1033LAPEALPsQGEVERE
ATRQ13535humanRAD17O75943S646ETWSLPLsQNSASEL
ATRQ13535humanCHEK1O14757S345LVQGIsFsQPtCPDH
ATRQ13535humanMDC1Q14676S513PGIHLERsQAsTtVD
ATRQ13535humanSARS1P49591S241MQEVAQLsQFDEELy
ATRQ13535humanAPBB1O00213S228DSSWATLsQGSPSYG
ATRQ13535humanBRCA1P38398S1143PMGSSHAsQVCSETP
ATRQ13535humanSMARCC2Q8TAQ2S969PPALPPGsQPIPPTG
ATRQ13535humanTP53BP1Q12888S176GFGVLELsQsQDVEE
ATRQ13535humanCCAR2Q8N163T454AAEAAPPtQEAQGETDBC1
ATRQ13535humanTP53BP1Q12888S166GAEDTASsQLGFGVL
ATRQ13535humanMCM3P25205S535ATDDPNFsQEDQQDT
ATRQ13535humanNBNO60934S343TtPGPsLsQGVsVDE
ATRQ13535humanPRKDCP78527T2609LtPMFVEtQAsQGtLDNAPKcs_CC5
ATRQ13535humanZDHHC13Q8IUH4S8MEGPGLGsQCRNHSH
ATRQ13535humanSARS1P49591S101ALANLkVsQIKKVRLSeryl_tRNA_N
ATRQ13535humanCEP164Q9UPV0S186LGELMLPsQGLKTSA
ATRQ13535humanCDKN2AP42771S140AAGGTrGsNHARIDAAnk_2
ATRQ13535humanCHEK1O14757S296GFskHIQsNLDFsPV
ATRQ13535humanFANCIQ9NVI1S565CsQSLSVsQVHVDVHFANCI_HD2
ATRQ13535humanDCLRE1CQ96SD1S516SSTVAGGsQsPKLFS
ATRQ13535humanCHTF18Q8WVB6S74PAAsVGssQGGARKR
ATRQ13535humanSRPK1Q96SB4S408QNGDSSTsQETDSCT
ATRQ13535humanBRCA1P38398S1457SEKAVLTsQKsSEYP
ATRQ13535humanXPAP23025S173VKkNPHHsQWGDMKLXPA_C
ATRQ13535humanKIFC1Q9BW19S26RPLIkAPsQLPLsGs
ATRQ13535humanXRCC2O43543S247FFSkQDDsQsSNQFSRad51
ATRQ13535humanTP53BP1Q12888S452PGSLPIPsQPQFSHD
ATRQ13535humanPRKDCP78527T2647QQHDFtLtQTADGRsDNAPKcs_CC5
ATRQ13535humanMCCP23508S118SELRsELsQsQHEVN
ATRQ13535humanPRKDCP78527S2612MFVEtQAsQGtLQtRDNAPKcs_CC5
ATRQ13535humanCDKN2AP42771S8MEPAAGssMEPSADW
ATRQ13535humanFANCMQ8IYD8S1045LSHSAVNsQQNLELN
ATRQ13535humanDCKP27707S74EFEELtMsQkNGGNVdNK
ATRQ13535humanRPA2P15927S33GFGsPAPsQAEkkSR
ATRQ13535humanDBF4Q9UBU7T449DDIRQNFtQLPLHkN
ATRQ13535humanSMARCAL1Q9NZC9S652RLkSDVLsQLPAkQRSNF2-rel_dom
ATRQ13535humanKAT2BQ92831S264YWHLEAPsQRRLRsPPCAF_N
ATRQ13535humanBLMP54132T122PKEVVCTtQNtPtVkBLM_N
ATRQ13535humanRASSF1Q9NS23-2S131EWETPDLsQAEIEQK
ATRQ13535humanTUT1Q9H6E5S750HEAAQEWsQGEAGKG
ATRQ13535humanATMQ13315S1981sLAFEEGsQSTtIss
ATRQ13535humanUSP28Q96RU2S714ESSTNSSsQDYSTsQ
ATRQ13535humanFANCD2Q9BXW9T608NLSDEQCtQVTSLLQFancD2
ATRQ13535humanCHEK2O96017T68SsLEtVstQELYsIP
ATRQ13535humanSRPK1Q96SB4T326ENPPNKMtQEKLEEs
ATRQ13535humanATRQ13535T1989LCFPENEtPPEGkNMFAT
ATRQ13535humanFANCIQ9NVI1S559SLSSsQCsQSLSVsQFANCI_HD2
ATRQ13535humanRPA2P15927T21yGGAGGYtQsPGGFG
ATRQ13535humanTP53BP1Q12888S831EPVEQdssQPsLPLV
ATRQ13535humanRAD17O75943S656SASELPAsQPQPFSA
ATRQ13535humanWRNQ14191S1141PEKAYSSsQPVISAQ
ATRQ13535humanMCM2P49736S108DVEELtAsQREAAERMCM2_N
ATRQ13535humanDAXXQ9UER7S424EGPsGMAsQGCPsAS
ATRQ13535humanRPA2P15927S52HIVPCTIsQLLSATL
ATRQ13535humanPOLHQ9Y253S601EMDLAHNsQSMHASS
ATRQ13535humanDBF4Q9UBU7S539GLItINSsQEHLTVQ
ATRQ13535humanNBNO60934S615VPEssKIsQENEIGK
ATRQ13535humanTP53P04637S15PsVEPPLsQEtFsDLP53_TAD
ATRQ13535humanSUN2Q9UH99S12SQRLtRysQGDDDGs
ATRQ13535humanZSCAN5AQ9BUG6T422DVCQKQFtQKSYLKCzf-met
ATRQ13535humanPHF14O94880S294tNDsLtLsQsKsNED
ATRQ13535humanATRIPQ8WXE1S72TLAsQALsQCPAAAR
ATRQ13535humanCCDC82Q8N4S0S154DDQEKHLsQEDNDLNDUF4196
ATRQ13535humanTP53BP1Q12888S178GVLELsQsQDVEENT
ATRQ13535humanSIAH1Q8IUQ4S19GtSkCPPsQRVPALT
ATRQ13535humanEWSR1Q01844T79QPPTGYTtPTAPQAY
ATRQ13535humanBORAQ6PGQ7T501QMDsGYNtQNCGSNI
ATRQ13535humanGPS1Q13098S474ksPPREGsQGELtPA
ATRQ13535humanXRCC3O43542S225PFRCEFDsQASAPRARad51
ATRQ13535humanFANCIQ9NVI1S556VLGSLSSsQCsQSLSFANCI_HD2
ATRQ13535humanUSP28Q96RU2S67DERVkEPsQDtVATE
ATRQ13535humanVCPP55072S784NQGGAGPsQGsGGGt
ATRQ13535humanWDHD1O75717T826kAAELTAtQVEEEEE
ATRQ13535humanMARCKSL1P49006S71AIEPAPPsQGAEAKGMARCKS
MAP3K13O43283humanTRIM25Q14258S12CPLAEELsCSICLEP


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
ATRIDDescription0.00e+00
ATRGO:0006302double-strand break repair3.91e-26
ATRGO:0000077DNA damage checkpoint signaling4.49e-24
ATRGO:0000075cell cycle checkpoint signaling9.73e-24
ATRGO:0031570DNA integrity checkpoint signaling9.73e-24
ATRGO:0010948negative regulation of cell cycle process2.66e-23
ATRGO:0042770signal transduction in response to DNA damage1.74e-22
ATRGO:1901987regulation of cell cycle phase transition2.47e-22
ATRGO:0045786negative regulation of cell cycle2.70e-22
ATRGO:1901988negative regulation of cell cycle phase transition4.49e-22
ATRGO:0006260DNA replication1.06e-17
ATRGO:0044773mitotic DNA damage checkpoint signaling2.82e-17
ATRGO:0010212response to ionizing radiation2.98e-17
ATRGO:0007093mitotic cell cycle checkpoint signaling4.41e-17
ATRGO:0044774mitotic DNA integrity checkpoint signaling4.47e-17
ATRGO:0009314response to radiation1.07e-16
ATRGO:0000724double-strand break repair via homologous recombination1.09e-15
ATRGO:0000725recombinational repair1.48e-15
ATRGO:0006310DNA recombination6.39e-15
ATRGO:0006261DNA-templated DNA replication7.94e-15
ATRGO:0045930negative regulation of mitotic cell cycle2.29e-13
ATRGO:0010332response to gamma radiation5.65e-13
ATRGO:0071478cellular response to radiation1.09e-12
ATRGO:0044772mitotic cell cycle phase transition1.85e-12
ATRGO:1901991negative regulation of mitotic cell cycle phase transition2.95e-12
ATRGO:0036297interstrand cross-link repair2.95e-12
ATRGO:1901990regulation of mitotic cell cycle phase transition2.96e-12
ATRGO:0090399replicative senescence1.58e-11
ATRGO:0031297replication fork processing1.92e-11
ATRGO:0045005DNA-templated DNA replication maintenance of fidelity6.70e-11
ATRGO:0006282regulation of DNA repair1.79e-10
ATRGO:0071214cellular response to abiotic stimulus2.24e-10
ATRGO:0104004cellular response to environmental stimulus2.24e-10
ATRGO:0071479cellular response to ionizing radiation4.83e-10
ATRGO:0044839cell cycle G2/M phase transition1.49e-09
ATRGO:0000723telomere maintenance1.56e-09
ATRGO:1902749regulation of cell cycle G2/M phase transition1.71e-09
ATRGO:0044818mitotic G2/M transition checkpoint1.71e-09
ATRGO:0032200telomere organization1.01e-08
ATRGO:0010972negative regulation of G2/M transition of mitotic cell cycle1.14e-08
ATRGO:1902750negative regulation of cell cycle G2/M phase transition1.60e-08
ATRGO:0097193intrinsic apoptotic signaling pathway1.81e-08
ATRGO:0009411response to UV2.15e-08
ATRGO:0071480cellular response to gamma radiation3.90e-08
ATRGO:0032508DNA duplex unwinding3.90e-08
ATRGO:0044843cell cycle G1/S phase transition4.47e-08
ATRGO:0031571mitotic G1 DNA damage checkpoint signaling5.72e-08
ATRGO:0044819mitotic G1/S transition checkpoint signaling5.72e-08
ATRGO:0006275regulation of DNA replication6.10e-08
ATRGO:0032392DNA geometric change6.34e-08

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Related Drugs to MAP3K13_ATR


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 MAP3K13-ATR 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 MAP3K13_ATR


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