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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:PRKDC_CEP290

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: PRKDC_CEP290
KinaseFusionDB ID: KFG5024
FusionGDB2.0 ID: KFG5024
HgeneTgene
Gene symbol

PRKDC

CEP290

Gene ID

5591

80184

Gene nameprotein kinase, DNA-activated, catalytic subunitcentrosomal protein 290
SynonymsDNA-PKC|DNA-PKcs|DNAPK|DNAPKc|DNPK1|HYRC|HYRC1|IMD26|XRCC7|p3503H11Ag|BBS14|CT87|JBTS5|LCA10|MKS4|NPHP6|POC3|SLSN6|rd16
Cytomap

8q11.21

12q21.32

Type of geneprotein-codingprotein-coding
DescriptionDNA-dependent protein kinase catalytic subunitDNA-PK catalytic subunithyper-radiosensitivity of murine scid mutation, complementing 1p460protein kinase, DNA-activated, catalytic polypeptidecentrosomal protein of 290 kDaBardet-Biedl syndrome 14 proteinCTCL tumor antigen se2-2Meckel syndrome, type 4POC3 centriolar protein homologcancer/testis antigen 87centrosomal protein 290kDamonoclonal antibody 3H11 antigennephrocytsin-6prostate c
Modification date2024041120240403
UniProtAcc

P78527

O15078

Ensembl transtripts involved in fusion geneENST idsENST00000314191, ENST00000338368, 
ENST00000523565, 		ENST00000309041, 
ENST00000397838, ENST00000547691, 
ENST00000552810, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: PRKDC [Title/Abstract] AND CEP290 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)PRKDC(48744375)-CEP290(88533341), # samples:3
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgenePRKDC

GO:0000460

maturation of 5.8S rRNA

32103174

HgenePRKDC

GO:0002218

activation of innate immune response

28712728

HgenePRKDC

GO:0006468

protein phosphorylation

26237645

HgenePRKDC

GO:0006974

DNA damage response

26237645|29478807|35460603

HgenePRKDC

GO:0018105

peptidyl-serine phosphorylation

15194694

HgenePRKDC

GO:0018105

peptidyl-serine phosphorylation

19303849|32103174

HgenePRKDC

GO:0018107

peptidyl-threonine phosphorylation

32103174

HgenePRKDC

GO:0034462

small-subunit processome assembly

32103174

HgenePRKDC

GO:0160049

negative regulation of cGAS/STING signaling pathway

33273464

HgenePRKDC

GO:2001034

positive regulation of double-strand break repair via nonhomologous end joining

26237645

TgeneCEP290

GO:0045893

positive regulation of DNA-templated transcription

16682973

TgeneCEP290

GO:0060271

cilium assembly

26386044


check buttonKinase Fusion gene breakpoints across PRKDC (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 CEP290 (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
ChimerDB4TCGA-AN-A0FD-01APRKDCchr8

48744375

CEP290chr12

88533341



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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/:48744375/:88533341)
- 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
PRKDC

P78527

CEP290

O15078

FUNCTION: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination (PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234, PubMed:34352203). Must be bound to DNA to express its catalytic properties (PubMed:11955432). Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) (PubMed:11955432). Recruited by XRCC5 and XRCC6 to DNA ends and is required to (1) protect and align broken ends of DNA, thereby preventing their degradation, (2) and sequester the DSB for repair by NHEJ (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805, PubMed:33854234). Act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion (By similarity). Also involved in modulation of transcription (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome (PubMed:32103174). Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome (PubMed:32103174). Recognizes the substrate consensus sequence [ST]-Q (PubMed:15574326, PubMed:11955432, PubMed:12649176, PubMed:14734805). Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism (PubMed:14627815, PubMed:16046194). Phosphorylates ASF1A, DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2 (PubMed:2507541, PubMed:2247066, PubMed:1597196, PubMed:8407951, PubMed:8464713, PubMed:9362500, PubMed:9139719, PubMed:10026262, PubMed:10467406, PubMed:12509254, PubMed:11889123, PubMed:14612514, PubMed:14599745, PubMed:15177042, PubMed:18644470, PubMed:26666690, PubMed:30247612, PubMed:14704337, PubMed:16397295, PubMed:26237645, PubMed:28712728, PubMed:29478807). Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA (PubMed:9679063). Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D (PubMed:9363941). Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation (PubMed:33273464). Also regulates the cGAS-STING pathway by mediating phosphorylation of PARP1 (PubMed:35460603). {ECO:0000250|UniProtKB:P97313, ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:10467406, ECO:0000269|PubMed:11889123, ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:12509254, ECO:0000269|PubMed:12649176, ECO:0000269|PubMed:14599745, ECO:0000269|PubMed:14612514, ECO:0000269|PubMed:14627815, ECO:0000269|PubMed:14704337, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:15177042, ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:16046194, ECO:0000269|PubMed:16397295, ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:2247066, ECO:0000269|PubMed:2507541, ECO:0000269|PubMed:26237645, ECO:0000269|PubMed:26666690, ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:30247612, ECO:0000269|PubMed:32103174, ECO:0000269|PubMed:33273464, ECO:0000269|PubMed:33854234, ECO:0000269|PubMed:34352203, ECO:0000269|PubMed:35460603, ECO:0000269|PubMed:8407951, ECO:0000269|PubMed:8464713, ECO:0000269|PubMed:9139719, ECO:0000269|PubMed:9362500, ECO:0000269|PubMed:9363941, ECO:0000269|PubMed:9679063}.FUNCTION: Involved in early and late steps in cilia formation. Its association with CCP110 is required for inhibition of primary cilia formation by CCP110 (PubMed:18694559). May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1 (PubMed:24421332). Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes (By similarity). Required for efficient recruitment of RAB8A to primary cilium (PubMed:17705300). In the ciliary transition zone is part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2, BBS5 and BBS8/TTC8 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating IQCB1/NPHP5 (PubMed:25552655). Activates ATF4-mediated transcription (PubMed:16682973). {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:18694559, ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:25552655}.

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 PRKDC_CEP290


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
PRKDCP78527humanPOU2F1P14859S92sQPsQQPsVQAAIPQ
PRKDCP78527humanFUSP35637T19QSYGAYPtQPGQGYs
PRKDCP78527humanDCLRE1CQ96SD1S503NDEITDEsLENFPSS
PRKDCP78527humanMCCP23508S120LRsELsQsQHEVNED
PRKDCP78527humanPOU5F1Q01860S93PQGGLEtsQPEGEAG
PRKDCP78527humanIRF3Q14653T135GGGSTSDtQEDILDE
PRKDCP78527humanPOU2F1P14859T226LQAQNLLtQLPQQsQ
PRKDCP78527humanXRCC4Q13426S327sLEtLRNssPEDLFDXRCC4
PRKDCP78527humanWRNQ14191S319SNNLNLLsFEDSTTG
PRKDCP78527humanXRCC4Q13426S304ENsRPDSsLPETSKKXRCC4
PRKDCP78527humanTP53P04637S37NVLsPLPsQAMDDLMTAD2
PRKDCP78527humanPOLLQ9UGP5T204EASDGEEtQVSAADL
PRKDCP78527humanXPAP23025S196RSLEVWGsQEALEEA
PRKDCP78527humanFUSP35637S42QQSYSGYsQSTDTSG
PRKDCP78527humanPOU2F1P14859S78QSKSNEEsGDsQQPs
PRKDCP78527humanIGFBP3P17936S183KKGHAKDsQRYKVDy
PRKDCP78527humanWRNQ14191S440DTsYVIEsDEDLEME
PRKDCP78527humanHSP90AA1P07900T7_MPEEtQtQDQPMEE
PRKDCP78527humanXRCC5P13010S580GAHFsVSsLAEGsVT
PRKDCP78527humanH2AXP16104T136PsGGkkAtQAsQEy_
PRKDCP78527humanPOU2F1P14859T100VQAAIPQtQLMLAGG
PRKDCP78527humanHNRNPUQ00839S59AMEPGNGsLDLGGDs
PRKDCP78527humanRPA2P15927S29QsPGGFGsPAPsQAE
PRKDCP78527humanTP53P04637S9EEPQsDPsVEPPLsQP53_TAD
PRKDCP78527humanFHP07954T236IkIGRTHtQDAVPLTLyase_1
PRKDCP78527humanPNKPQ96T60S114EEtRtPEsQPDtPPG
PRKDCP78527humanPOU2F1P14859T162ASAATPMtQIPLsQP
PRKDCP78527humanTP53P04637S46AMDDLMLsPDDIEQWTAD2
PRKDCP78527humanHOXA11P31270T119ANVYHHPtPAVSSNFDUF3528
PRKDCP78527humanSRFP11831S446STMQVSHsQVQEPGG
PRKDCP78527humanTP53P04637T18EPPLsQEtFsDLWkLP53_TAD
PRKDCP78527humanAKT1P31749S473RPHFPQFsysAsGtAPkinase_C
PRKDCP78527humanXRCC6P12956S6__MsGWEsyykTEGD
PRKDCP78527humanSOX2P48431S251VksEAsssPPVVtSS
PRKDCP78527humanFUSP35637S131QPQSGSYsQQPSYGG
PRKDCP78527humanMAPKAP1Q9BPZ7S186VYLPLHssQDRLLPMCRIM
PRKDCP78527humanFUSP35637S30QGYsQQSsQPYGQQS
PRKDCP78527humanDCLRE1CQ96SD1S553QGsQGWDsQSDTVLL
PRKDCP78527humanGOLPH3Q9H4A6T148KEtQPPEtVQNWIELGPP34
PRKDCP78527humanWRNQ14191S467DTsYVIEsDEDLEME
PRKDCP78527humanFUSP35637T68sQNTGYGtQSTPQGY
PRKDCP78527humanNHEJ1Q9H9Q4S55QVDTSVVsQRAKELNXLF
PRKDCP78527humanPOU2F1P14859S167PMtQIPLsQPIQIAQ
PRKDCP78527humanSRFP11831S435LTVLNAFsQAPSTMQ
PRKDCP78527humanDCLRE1CQ96SD1S645NLSTNADsQsssDFE
PRKDCP78527humanRPA2P15927S4____MWNsGFEsyGs
PRKDCP78527humanEGR1P18146S301AFATQSGsQDLKALN
PRKDCP78527humanIKBKGQ9Y6K9S43PAMLHLPsEQGAPEt
PRKDCP78527humanPOU2F1P14859S85sGDsQQPsQPsQQPs
PRKDCP78527humanNABP2Q9BQ15S134NDSNPSAsQPTTGPS
PRKDCP78527humanHNRNPUQ00839-2S59AMEPGNGsLDLGGDS
PRKDCP78527humanLIG4P49917T650HLkAPNLtNVNKISN
PRKDCP78527humanVIMP08670S459GQVINEtsQHHDDLE
PRKDCP78527humanPRKDCP78527T3950GHAFGSAtQFLPVPEPI3_PI4_kinase
PRKDCP78527humanMAPKAP1Q9BPZ7S367DGVFEEDsQIDIATV
PRKDCP78527humanXRCC5P13010S577EQGGAHFsVSsLAEG
PRKDCP78527humanPOU2F1P14859S81SNEEsGDsQQPsQPs
PRKDCP78527humanXRCC1P18887S371FANtPKysQVLGLGGBRCT
PRKDCP78527humanPELP1Q8IZL8S1033LAPEALPsQGEVERE
PRKDCP78527humanVIMP08670S430LREtNLDsLPLVDtH
PRKDCP78527humanPOU2F1P14859S232LtQLPQQsQANLLQS
PRKDCP78527humanFUSP35637T11NDYtQQAtQSYGAYP
PRKDCP78527humanXRCC4Q13426S320HISAENMsLEtLRNsXRCC4
PRKDCP78527humanRAG2P55895S365EQTTFTNsQTSTEDPRAG2
PRKDCP78527humanXRCC6P12956S51AsKAMFEsQsEDELTKu_N
PRKDCP78527humanXRCC5P13010T715KDkPsGDtAAVFEEG
PRKDCP78527humanPDX1P52945T11EEQYYAAtQLYKDPC
PRKDCP78527humanPRKDCP78527T2638VAGQIRAtQQQHDFtDNAPKcs_CC5
PRKDCP78527humanTOP1P11387S10GDHLHNDsQIEADFR
PRKDCP78527humanPRKDCP78527T2609LtPMFVEtQAsQGtLDNAPKcs_CC5
PRKDCP78527humanPOU2F1P14859S147HsAsQQHsAAGATIS
PRKDCP78527humanFUSP35637S54TSGYGQSsYSSYGQs
PRKDCP78527humanXRCC6P12956S27QEENLEAsGDykYsG
PRKDCP78527humanMAPKAP1Q9BPZ7S343DLDSTLEsQSAWEFC
PRKDCP78527humanPNKPQ96T60S126PPGtPLVsQDEKRDA
PRKDCP78527humanFUSP35637S142SYGGQQQsYGQQQSY
PRKDCP78527humanDCLRE1CQ96SD1S516SSTVAGGsQsPKLFS
PRKDCP78527humanNHEJ1Q9H9Q4T266QLVssAPtLsAPEKE
PRKDCP78527humanH1-2P16403T146KkAAGGAtPkKSAKK
PRKDCP78527humanPPARGC1AQ9UBK2S636SRRPRyDsYEEYQHE
PRKDCP78527humanCDKN1BP46527S140PkTDPSDsQTGLAEQ
PRKDCP78527humanXPAP23025S173VKkNPHHsQWGDMKLXPA_C
PRKDCP78527humanPOU5F1Q01860S111EsNsDGAsPEPCtVt
PRKDCP78527humanNFKB1P19838S20QMFHLDPsLTHTIFN
PRKDCP78527humanPRKDCP78527T2647QQHDFtLtQTADGRsDNAPKcs_CC5
PRKDCP78527humanDCLRE1CQ96SD1S548THITEQGsQGWDsQS
PRKDCP78527humanMCCP23508S118SELRsELsQsQHEVN
PRKDCP78527humanPRKDCP78527S2612MFVEtQAsQGtLQtRDNAPKcs_CC5
PRKDCP78527humanYBX1P67809T89EDVFVHQtAIkkNNPCSD
PRKDCP78527humanPOLR2AP24928S1616TPQSPSysPtsPsYSRNA_pol_Rpb1_R
PRKDCP78527humanMED1Q15648T1457HsKsPAytPQNLDsE
PRKDCP78527humanRPA2P15927S8MWNsGFEsyGsssyG
PRKDCP78527humanASF1AQ9Y294S192GWSTSENsLNVMLES
PRKDCP78527humanHSP90AA1P07900T5___MPEEtQtQDQPM
PRKDCP78527humanFUSP35637S84STGGYGSsQSsQSSY
PRKDCP78527humanAIREO43918T68ALLSWLLtQDSTAILHSR
PRKDCP78527humanHOXA11P31270S98RDCLQAPsAAGVPGDDUF3528
PRKDCP78527humanRPA2P15927S33GFGsPAPsQAEkkSR
PRKDCP78527humanTP53P04637S20PLsQEtFsDLWkLLPP53_TAD
PRKDCP78527humanFUSP35637S117SGsYGSSsQSSSYGQ
PRKDCP78527humanAIREO43918S156RGTASPGsQLKAKPP
PRKDCP78527humanPRKAG1P54619T284LKCYLHEtLETIINRCBS
PRKDCP78527humanRPA2P15927S23GAGGYtQsPGGFGsP
PRKDCP78527humanNHEJ1Q9H9Q4S263QPEQLVssAPtLsAP
PRKDCP78527humanFUSP35637S61sYSSYGQsQNTGYGt
PRKDCP78527humanFUSP35637S26tQPGQGYsQQSsQPY
PRKDCP78527humanGOLPH3Q9H4A6T143ALkHVKEtQPPEtVQGPP34
PRKDCP78527humanDCLRE1CQ96SD1S538HISsQNSsQSTHITE
PRKDCP78527humanXRCC4Q13426S260KDDsIIssLDVtDIAXRCC4
PRKDCP78527humanPOU2F1P14859S141AAAVQQHsAsQQHsA
PRKDCP78527humanXRCC4Q13426S328LEtLRNssPEDLFDEXRCC4
PRKDCP78527humanPRKDCP78527S3205tPLPEDNsMNVDQDGFAT
PRKDCP78527humanPOLR2AP24928S1621SysPtsPsYSPTSPSRNA_pol_Rpb1_R
PRKDCP78527humanTRIM28Q13263S824LPGAGLssQELsGGP
PRKDCP78527humanCHEK2O96017T68SsLEtVstQELYsIP
PRKDCP78527humanXRCC6P12956S33AsGDykYsGRDsLIF
PRKDCP78527humanCASP2P42575S139LSCDYDLsLPFPVCE
PRKDCP78527humanRPA2P15927T21yGGAGGYtQsPGGFG
PRKDCP78527humanH2AXP16104S139GkkAtQAsQEy____
PRKDCP78527humanTGM2P21980T162ERQEyVLtQQGFIYQ
PRKDCP78527humanPRKAG1P54619S192KPEFMSKsLEELQIGCBS
PRKDCP78527humanFUSP35637S87GYGSsQSsQSSYGQQ
PRKDCP78527humanNHEJ1Q9H9Q4S251AsLQGIDsQCVNQPE
PRKDCP78527humanCHEK2O96017T387LMRtLCGtPtyLAPEPkinase
PRKDCP78527humanPOU2F1P14859S88sQQPsQPsQQPsVQA
PRKDCP78527humanTP53P04637S15PsVEPPLsQEtFsDLP53_TAD
PRKDCP78527humanNHEJ1Q9H9Q4S245PHTSNSAsLQGIDsQ
PRKDCP78527humanPOU2F1P14859S143AVQQHsAsQQHsAAG
PRKDCP78527humanTDP1Q9NUW8S81PKRQKsGsQEDLGWC
PRKDCP78527humanUSF1P22415S262RQSNHRLsEELQGLD
PRKDCP78527humanPARP1P09874T594RSWGRVGtVIGSNkLWGR
PRKDCP78527humanNHEJ1Q9H9Q4T223DLYMAVTtQEVQVGQ
PRKDCP78527humanPRKDCP78527S2056VQsYsYSsQDPRPATDNAPKcs_CC3
PRKDCP78527humanNHEJ1Q9H9Q4S132LASPSLVsQHLIRPLXLF
PRKDCP78527humanVCPP55072S784NQGGAGPsQGsGGGt
PRKDCP78527humanDCLRE1CQ96SD1S534GESTHISsQNSsQST
PRKDCP78527humanPNPT1Q8TCS8S776IVMGEPIsQSSSNsQ
PRKDCP78527humanVIMP08670S56srsLyAssPGGVyAtFilament_head
PRKDCP78527humanCHEK2O96017T383GEtsLMRtLCGtPtyPkinase
PRKDCP78527humanAKT1P31749T308kDGAtMKtFCGtPEyPkinase
PRKDCP78527humanFUSP35637T7_MASNDYtQQAtQSY
PRKDCP78527humanFUSP35637S112APSSTSGsYGSSsQS


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
PRKDCIDDescription0.00e+00
PRKDCGO:0006302double-strand break repair1.34e-18
PRKDCGO:0010212response to ionizing radiation3.95e-15
PRKDCGO:0006310DNA recombination7.61e-14
PRKDCGO:0009314response to radiation1.28e-13
PRKDCGO:0010332response to gamma radiation1.34e-13
PRKDCGO:0006303double-strand break repair via nonhomologous end joining1.52e-12
PRKDCGO:0000723telomere maintenance1.03e-11
PRKDCGO:0032200telomere organization7.93e-11
PRKDCGO:0071480cellular response to gamma radiation3.10e-10
PRKDCGO:0051054positive regulation of DNA metabolic process8.10e-10
PRKDCGO:0006266DNA ligation8.67e-10
PRKDCGO:0033151V(D)J recombination1.23e-09
PRKDCGO:0071479cellular response to ionizing radiation5.50e-09
PRKDCGO:0006284base-excision repair8.28e-09
PRKDCGO:0000725recombinational repair1.89e-08
PRKDCGO:0071478cellular response to radiation1.98e-08
PRKDCGO:0031571mitotic G1 DNA damage checkpoint signaling2.83e-08
PRKDCGO:0044819mitotic G1/S transition checkpoint signaling2.83e-08
PRKDCGO:0071214cellular response to abiotic stimulus2.83e-08
PRKDCGO:0104004cellular response to environmental stimulus2.83e-08
PRKDCGO:0002520immune system development3.82e-08
PRKDCGO:0002200somatic diversification of immune receptors3.36e-07
PRKDCGO:0071897DNA biosynthetic process5.73e-07
PRKDCGO:2000628regulation of miRNA metabolic process6.14e-07
PRKDCGO:1902807negative regulation of cell cycle G1/S phase transition1.19e-06
PRKDCGO:0010165response to X-ray1.91e-06
PRKDCGO:0010586miRNA metabolic process2.21e-06
PRKDCGO:0000012single strand break repair2.73e-06
PRKDCGO:2000630positive regulation of miRNA metabolic process2.75e-06
PRKDCGO:0090398cellular senescence2.75e-06
PRKDCGO:0000724double-strand break repair via homologous recombination3.55e-06
PRKDCGO:0048732gland development4.67e-06
PRKDCGO:0060218hematopoietic stem cell differentiation4.67e-06
PRKDCGO:0002562somatic diversification of immune receptors via germline recombination within a single locus4.67e-06
PRKDCGO:0016444somatic cell DNA recombination4.67e-06
PRKDCGO:0000077DNA damage checkpoint signaling5.86e-06
PRKDCGO:0000075cell cycle checkpoint signaling6.09e-06
PRKDCGO:0045739positive regulation of DNA repair6.89e-06
PRKDCGO:1901988negative regulation of cell cycle phase transition7.29e-06
PRKDCGO:0006260DNA replication7.33e-06
PRKDCGO:0031570DNA integrity checkpoint signaling8.27e-06
PRKDCGO:1903131mononuclear cell differentiation8.45e-06
PRKDCGO:0044773mitotic DNA damage checkpoint signaling8.95e-06
PRKDCGO:1902806regulation of cell cycle G1/S phase transition9.77e-06
PRKDCGO:0006289nucleotide-excision repair9.77e-06
PRKDCGO:0006977DNA damage respons2.22e-07
PRKDCGO:2000134negative regulation of G1/S transition of mitotic cell cycle9.77e-06
PRKDCGO:0007093mitotic cell cycle checkpoint signaling9.77e-06
PRKDCGO:0033077T cell differentiation in thymus1.00e-05

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Related Drugs to PRKDC_CEP290


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 PRKDC-CEP290 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 PRKDC_CEP290


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