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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:CAMK2D_CAMK2A

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: CAMK2D_CAMK2A
KinaseFusionDB ID: KFG872
FusionGDB2.0 ID: KFG872
HgeneTgene
Gene symbol

CAMK2D

CAMK2A

Gene ID

817

815

Gene namecalcium/calmodulin dependent protein kinase II deltacalcium/calmodulin dependent protein kinase II alpha
SynonymsCAMKDCAMKA|CaMKIINalpha|CaMKIIalpha|MRD53|MRT63
Cytomap

4q26

5q32

Type of geneprotein-codingprotein-coding
Descriptioncalcium/calmodulin-dependent protein kinase type II subunit deltaCaM kinase II delta subunitCaM-kinase II delta chainCaMK-II delta subunitcalcium/calmodulin-dependent protein kinase (CaM kinase) II deltacalcium/calmodulin-dependent protein kinase typcalcium/calmodulin-dependent protein kinase type II subunit alphaCaM kinase II alpha subunitCaM-kinase II alpha chainCaMK-II alpha subunitcaM kinase II subunit alphacaMK-II subunit alphacalcium/calmodulin-dependent protein kinase (CaM kinase) II alp
Modification date2024040720240407
UniProtAcc

Q13557

Q9UQM7

Ensembl transtripts involved in fusion geneENST idsENST00000296402, ENST00000342666, 
ENST00000379773, ENST00000394522, 
ENST00000394524, ENST00000394526, 
ENST00000418639, ENST00000429180, 
ENST00000454265, ENST00000508738, 
ENST00000514328, ENST00000515496, 
ENST00000505990, ENST00000509907, 
ENST00000511664, 		ENST00000351010, 
ENST00000398376, ENST00000348628, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: CAMK2D [Title/Abstract] AND CAMK2A [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)CAMK2D(114469812)-CAMK2A(149636208), # 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
HgeneCAMK2D

GO:0003254

regulation of membrane depolarization

22514276

HgeneCAMK2D

GO:0006468

protein phosphorylation

17179159|23283722

HgeneCAMK2D

GO:0018105

peptidyl-serine phosphorylation

22514276|23283722

HgeneCAMK2D

GO:0018107

peptidyl-threonine phosphorylation

22514276|23283722

HgeneCAMK2D

GO:0046777

protein autophosphorylation

22514276

HgeneCAMK2D

GO:1901897

regulation of relaxation of cardiac muscle

23283722

HgeneCAMK2D

GO:1902306

negative regulation of sodium ion transmembrane transport

22514276

HgeneCAMK2D

GO:2000650

negative regulation of sodium ion transmembrane transporter activity

22514276

TgeneCAMK2A

GO:0006468

protein phosphorylation

17052756

TgeneCAMK2A

GO:0035458

cellular response to interferon-beta

35568036

TgeneCAMK2A

GO:0038166

angiotensin-activated signaling pathway

20584908

TgeneCAMK2A

GO:0046427

positive regulation of receptor signaling pathway via JAK-STAT

11972023|35568036

TgeneCAMK2A

GO:0071346

cellular response to type II interferon

11972023


check buttonKinase Fusion gene breakpoints across CAMK2D (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 CAMK2A (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
ChimerDB42397NCAMK2Dchr4

114469812

CAMK2Achr5

149636208



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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/chr4:114469812/chr5:149636208)
- 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
CAMK2D

Q13557

CAMK2A

Q9UQM7

FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program (PubMed:17179159). Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis (PubMed:16690701). May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q6PHZ2, ECO:0000269|PubMed:16690701, ECO:0000269|PubMed:17179159}.FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (PubMed:14722083). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (By similarity). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (PubMed:11972023). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (PubMed:35568036). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (By similarity). {ECO:0000250|UniProtKB:P11275, ECO:0000250|UniProtKB:P11798, ECO:0000269|PubMed:11972023, ECO:0000269|PubMed:23805378, ECO:0000269|PubMed:28130356, ECO:0000269|PubMed:29100089}.

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 CAMK2D_CAMK2A


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
CAMK2AQ9UQM7humanAKAP5P24588S92LVtRRKRsESsKQQKWSK
CAMK2AQ9UQM7humanSCN5AQ14524T455LTIRGVDtVsRssLE
CAMK2AQ9UQM7humanHRH1P35367T142YLKYRtKtRASATIL7tm_1
CAMK2AQ9UQM7humanSCN5AQ14524S484KRRKRMssGtEECGE
CAMK2AQ9UQM7humanCREB3L3Q68CJ9S395ADTTREEsPGSPGAD
CAMK2AQ9UQM7humanETS2P15036S310LDVQRVPsFEsFEDDEts1_N_flank
CAMK2AQ9UQM7humanITPKAP23677T311EHAQRAVtKPRYMQWIPK
CAMK2AQ9UQM7humanSCN5AQ14524S457IRGVDtVsRssLEMs
CAMK2AQ9UQM7humanNCOR2Q9Y618S2426AsGDRPPsVSSVHsE
CAMK2AQ9UQM7humanKCNJ11Q14654T180QAHRRAEtLIFSKHA
CAMK2AQ9UQM7humanNOX5Q96PH1-4S498RSVtMRKsQRSsKGSFAD_binding_8
CAMK2AQ9UQM7humanSCN8AQ9UQD0T642RSVKRNstVDCNGVVNa_trans_cytopl
CAMK2AQ9UQM7humanITGB1P05556T788PIyksAVttVVNPkyIntegrin_b_cyt
CAMK2AQ9UQM7humanTHP07101-4S35AIMVRGQsPRFIGRRTOH_N
CAMK2AQ9UQM7humanSCN5AQ14524S12LLPRGTssFRRFtRE
CAMK2AQ9UQM7humanETS2P15036S313QRVPsFEsFEDDCsQEts1_N_flank
CAMK2AQ9UQM7humanSCN5AQ14524S61PQLDLQAsKKLPDLY
CAMK2AQ9UQM7humanTCAPO15273S157GALRRsLsRSMsQEATelethonin
CAMK2AQ9UQM7humanSLNO00631T5___MGINtRELFLNFSarcolipin
CAMK2AQ9UQM7humanCAMK2AQ9UQM7T286sCMHRQEtVDCLKKF
CAMK2AQ9UQM7humanSCN5AQ14524S464sRssLEMsPLAPVNs
CAMK2AQ9UQM7humanCHATP28329-3T456VDNIRSAtPEALAFVCarn_acyltransf
CAMK2AQ9UQM7humanCAMK2AQ9UQM7T305kLkGAILttMLAtRN
CAMK2AQ9UQM7humanETS1P14921S285QRVPsyDsFDsEDyPEts1_N_flank
CAMK2AQ9UQM7humanSCN5AQ14524S571PWPLRRtsAQGQPsPNa_trans_cytopl
CAMK2AQ9UQM7humanSPRP35270S213QQLARETsVDPDMRKadh_short
CAMK2AQ9UQM7humanSCN8AQ9UQD0S541NRIGRKFsIMNQsLL
CAMK2AQ9UQM7humanCREB3L3Q68CJ9S360FAPVRVFsRTLHNDA
CAMK2AQ9UQM7humanSLC1A3P43003T26QQGVRKRtLLAKkkV
CAMK2AQ9UQM7humanPTTG1O95997S31LkLGsGPsIkALDGRSecurin
CAMK2AQ9UQM7humanSMAD2Q15796S260TLsPVNHsLDLQPVT
CAMK2AQ9UQM7humanTHP07101-4S19KGFRRAVsELDAKQATOH_N
CAMK2AQ9UQM7humanCDKN1BP46527S10NVRVSNGsPsLErMD
CAMK2AQ9UQM7humanSRFP11831S103RGLKRsLsEMEIGMV
CAMK2AQ9UQM7humanCYLDQ9NQC7S362FyTLNGSsVDSQPQsCYLD_phos_site
CAMK2AQ9UQM7humanAKAP5P24588T87AsLKRLVtRRKRsESWSK
CAMK2AQ9UQM7humanRYR2Q92736S2814IsQTSQVsVDAAHGY
CAMK2AQ9UQM7humanSCN5AQ14524S528KPRssrGsIFtFRRRNa_trans_cytopl
CAMK2AQ9UQM7humanHDAC5Q9UQL6S498RPLSRtQsSPLPQsP
CAMK2AQ9UQM7humanVIMP08670S83GVRLLQDsVdFsLAdFilament_head
CAMK2AQ9UQM7humanITGB1BP1O14713T38GGLsRsstVAsLDTDICAP-1_inte_bdg
CAMK2AQ9UQM7humanSCN5AQ14524S497GEDRLPKsDsEDGPR
CAMK2AQ9UQM7humanNOX5Q96PH1-4S475WTNRLYEsFKASDPLFAD_binding_8
CAMK2AQ9UQM7humanSLC6A4P31645S13LNSQKQLsACEDGED
CAMK2AQ9UQM7humanTHP07101S71RFIGRRQsLIEDARKTOH_N
CAMK2AQ9UQM7humanSMAD2Q15796S110SFSEQTRsLDGRLQVMH1
CAMK2AQ9UQM7humanNR1I2O75469T290LCQLRFNtVFNAETGHormone_recep
CAMK2AQ9UQM7humanFLNAP21333S2523VTGPRLVsNHsLHET
CAMK2AQ9UQM7humanBECN1Q14457S96MstEsANsFTLIGEA
CAMK2AQ9UQM7humanPPP1R14AQ96A00S130GLRQPsPsHDGsLsPPP1_inhibitor
CAMK2AQ9UQM7humanKCNQ2O43526-4S438QTVRRsPsADQSLEDKCNQ_channel
CAMK2AQ9UQM7humanETS1P14921S282NsLQRVPsyDsFDsEEts1_N_flank
CAMK2AQ9UQM7humanSCN5AQ14524S1925QRsLKHAsFLFRQQA
CAMK2AQ9UQM7humanSCN5AQ14524S510PRAMNHLsLTrGLsRNa_trans_cytopl
CAMK2AQ9UQM7humanGFPT1Q06210S261CNLsRVDsttCLFPV
CAMK2AQ9UQM7humanSCN5AQ14524S11FLLPRGTssFRRFtR
CAMK2AQ9UQM7humanSCN5AQ14524S577tsAQGQPsPGTSAPGNa_trans_cytopl
CAMK2AQ9UQM7humanCTNNB1P35222S552QDtQRRtsMGGtQQQ
CAMK2AQ9UQM7humanDLGAP1O14490-2S44CRRMRSGsYIKAMGD
CAMK2AQ9UQM7humanCREB3L3Q68CJ9T429TLVLRNAtEGLGQVA
CAMK2AQ9UQM7humanSCN5AQ14524S1934LFRQQAGsGLsEEDA
CAMK2AQ9UQM7humanSCN5AQ14524S539FRRRDLGsEADFADDNa_trans_cytopl
CAMK2AQ9UQM7humanITGB1P05556T789IyksAVttVVNPkyEIntegrin_b_cyt
CAMK2AQ9UQM7humanALOX5P09917S272CsLERQLsLEQEVQQLipoxygenase
CAMK2AQ9UQM7humanSCN5AQ14524S516LsLTrGLsRTsMKPRNa_trans_cytopl
CAMK2AQ9UQM7humanID1P41134S36GEVVRCLsEQSVAIS
CAMK2AQ9UQM7humanSCN5AQ14524S460VDtVsRssLEMsPLA
CAMK2AQ9UQM7humanHRH1P35367S398WKRLRsHsRQyVSGL7tm_1
CAMK2AQ9UQM7humanETS1P14921S257DsFEsIEsyDsCDRLEts1_N_flank
CAMK2AQ9UQM7humanCLCN3P51790S109ERHRRINsKKKESAW
CAMK2AQ9UQM7humanCTNNB1P35222T332VNIMRTytyEkLLWT
CAMK2AQ9UQM7humanSCN8AQ9UQD0S561PFLSRHNsKSSIFSFNa_trans_cytopl
CAMK2AQ9UQM7humanIL6STP40189S782QVFSRsEsTQPLLDS
CAMK2AQ9UQM7humanHSF1Q00613S230PkYSRQFsLEHVHGS
CAMK2AQ9UQM7humanHDAC5Q9UQL6S259FPLRkTAsEPNLKVR
CAMK2AQ9UQM7humanCAMK2AQ9UQM7-2T286SCMHRQEtVDCLKKF
CAMK2AQ9UQM7humanSMAD2Q15796S240SDQQLNQsMDTGsPA
CAMK2AQ9UQM7humanSCN8AQ9UQD0S641RRSVKRNstVDCNGVNa_trans_cytopl
CAMK2AQ9UQM7humanSCN5AQ14524S483sKRRKRMssGtEECG
CAMK2AQ9UQM7humanKCND1Q9NSA2S555TASVSRGsMQELDML
CAMK2AQ9UQM7humanFBXO43Q4G163T234FSQQKTStIDDSKDD
CAMK2AQ9UQM7humanCAMK2AQ9UQM7T306LkGAILttMLAtRNF
CAMK2AQ9UQM7humanRRADP55042S273AGTRRREsLGKKAKR
CAMK2AQ9UQM7humanTHP07101-4S44RFIGRRQsLIEDARKTOH_N
CAMK2AQ9UQM7humanRCHY1Q96PM5T154ICLEDIHtsRVVAHVzf-RING_2
CAMK2AQ9UQM7humanSTMN1P16949S16kELEKrAsGQAFELIStathmin
CAMK2AQ9UQM7humanPTTG1O95997S89KQKQPsFsAKKMTEKSecurin
CAMK2AQ9UQM7humanSCN5AQ14524T17TssFRRFtREsLAAI
CAMK2AQ9UQM7humanTHP07101S19KGFRRAVsELDAKQATOH_N
CAMK2AQ9UQM7humanSCN5AQ14524S1920RRHLLQRsLKHAsFL
CAMK2AQ9UQM7humanSCN5AQ14524S1885KFMAANPsKISYEPI
CAMK2AQ9UQM7humanGRIN2AQ12879S1459RVYKKMPsIESDV__NMDAR2_C
CAMK2AQ9UQM7humanCYLDQ9NQC7S418TTENRFHsLPFsLtKCYLD_phos_site
CAMK2AQ9UQM7humanNCOR2Q9Y618S2453VWEDRPssAGstPFP
CAMK2AQ9UQM7humanOPRM1P35372S268LKsVRMLsGsKEKDR7tm_1
CAMK2AQ9UQM7humanNOX5Q96PH1-4S659ANKEKKDsITGLQTRNAD_binding_6
CAMK2AQ9UQM7humanKIF3AQ9Y496S687KTGRRKRsAkPEtVI
CAMK2AQ9UQM7humanSCN5AQ14524S667QRALsAVsVLtsALENa_trans_cytopl
CAMK2AQ9UQM7humanDAGLAQ9Y4D2S782APLATMEsLSDTESL
CAMK2AQ9UQM7humanSCN5AQ14524S20FRRFtREsLAAIEKR
CAMK2AQ9UQM7humanCARD11Q9BXL7S116KEPTRRFstIVVEEG
CAMK2AQ9UQM7humanSCN5AQ14524S1937QQAGsGLsEEDAPER
CAMK2AQ9UQM7humanSLC1A3P43003T37KkkVQNItkEDVKSY
CAMK2AQ9UQM7humanPLCB3Q01970S537PSLEPQKsLGDEGLN
CAMK2AQ9UQM7humanPPP2R2BQ00005-2S22PNTILsssCHTEADI
CAMK2AQ9UQM7humanRCHY1Q96PM5S155CLEDIHtsRVVAHVLzf-RING_2
CAMK2AQ9UQM7humanSCN5AQ14524S1865TKRVLGEsGEMDALK
CAMK2AQ9UQM7humanSCN5AQ14524S2007DLADFPPsPDRDRES
CAMK2AQ9UQM7humanCYLDQ9NQC7S772LFKkIFPsLELNITDUCH
CAMK2AQ9UQM7humanCD44P16070S706LNGEAsksQEMVHLV
CAMK2AQ9UQM7humanNOX5Q96PH1-4S502MRKsQRSsKGSEILLFAD_binding_8
CAMK2AQ9UQM7humanESPL1Q14674S1501TDNWRKMsFEILRGs
CAMK2AQ9UQM7humanCACNA1HO95180S1198tPLRRAEsLDPRPLR
CAMK2AQ9UQM7humanTHP07101-3S40RFIGRRQsLIEDARKTOH_N
CAMK2AQ9UQM7humanDLG4P78352S73ITLERGNsGLGFsIAPDZ
CAMK2AQ9UQM7humanSCN5AQ14524S1503NAMKKLGsKKPQKPI
CAMK2AQ9UQM7humanBECN1Q14457S93ARMMstEsANsFTLI
CAMK2AQ9UQM7humanSCN5AQ14524S471sPLAPVNsHERRsKR
CAMK2AQ9UQM7humanPTTG1O95997T66AtRkALGtVNRATEKSecurin
CAMK2AQ9UQM7humanHRH1P35367S396FTWKRLRsHsRQyVS7tm_1
CAMK2AQ9UQM7humanETS2P15036S246FPkSRLSsVsVTYCSEts1_N_flank
CAMK2AQ9UQM7humanBECN1Q14457S90IPPARMMstEsANsF
CAMK2AQ9UQM7humanSCN5AQ14524S1998RGSDYSHsEDLADFP
CAMK2AQ9UQM7humanSCN5AQ14524S1003AAQGQLPsCIATPYSNa_trans_assoc
CAMK2AQ9UQM7humanCTNNB1P35222T472ICALRHLtsRHQEAEArm
CAMK2AQ9UQM7humanGRIN2BQ13224S1303NKLRRQHsyDtFVDLNMDAR2_C
CAMK2AQ9UQM7humanGRIA1P42261S567FSPYEWHsEEFEEGRLig_chan
CAMK2AQ9UQM7humanGLO1Q04760T107ELTHNWGtEDDETQSGlyoxalase
CAMK2AQ9UQM7humanRYR2Q92736S2808YNRTRRIsQTSQVsV
CAMK2AQ9UQM7humanSNCAP37840S129NEAyEMPsEEGyQDySynuclein
CAMK2AQ9UQM7humanMAPTP10636-8S262NVKskIGstENLkHQTubulin-binding
CAMK2AQ9UQM7humanMAPTP10636-8S416sNVsstGsIDMVDsP
CAMK2AQ9UQM7humanHRH1P35367T140LRYLKYRtKtRASAT7tm_1
CAMK2AQ9UQM7humanTHP07101-3S19KGFRRAVsELDAKQATOH_N
CAMK2AQ9UQM7humanDAGLAQ9Y4D2S808RSIRGsPsLHAVLER
CAMK2AQ9UQM7humanSPTBN4Q9H254S2254RRPERQEsVDQSEEA
CAMK2AQ9UQM7humanPPP2R2BQ00005-2S20RPPNTILsssCHTEA
CAMK2AQ9UQM7humanNOX5Q96PH1-4T494KRLsRSVtMRKsQRSFAD_binding_8
CAMK2AQ9UQM7humanSCN5AQ14524T570VPWPLRRtsAQGQPsNa_trans_cytopl
CAMK2AQ9UQM7humanKCNJ11Q14654T224MQVVRKTtSPEGEVVIRK_C
CAMK2AQ9UQM7humanSCN5AQ14524S664GARQRALsAVsVLtsNa_trans_cytopl
CAMK2AQ9UQM7humanSCN5AQ14524S42GSTTLQEsREGLPEE
CAMK2AQ9UQM7humanSCN5AQ14524S499DRLPKsDsEDGPRAM
CAMK2AQ9UQM7humanPTTG1O95997S87PLKQKQPsFsAKKMTSecurin
CAMK2AQ9UQM7humanPLNP26678T17SAIRRAstIEMPQQAPhospholamban
CAMK2AQ9UQM7humanTCAPO15273S161RsLsRSMsQEAQRG_Telethonin
CAMK2AQ9UQM7humanPPP2R2BQ00005-2S21PPNTILsssCHTEAD
CAMK2AQ9UQM7humanETS1P14921S251GkLGGQDsFEsIEsyEts1_N_flank
CAMK2DQ13557humanHDAC4P56524S210YGKTQHSsLDQSsPP
CAMK2DQ13557humanSCN5AQ14524T594LHGkKNStVDCNGVVNa_trans_cytopl
CAMK2DQ13557humanKCNQ1P51787T482sMPHFMRtNsFAEDL
CAMK2DQ13557humanKCNJ11Q14654T224MQVVRKTtSPEGEVVIRK_C
CAMK2DQ13557humanANKRD28O15084S1011TNTskTVsFEALPIM
CAMK2DQ13557humanRNF8O76064S157LRTKRkFsLDELAGP
CAMK2DQ13557humanTTNQ8WZ42T11922EVEVPTVtKRERKIP
CAMK2DQ13557humanCACNB2Q08289-2T499RGLSRQEtFDSETQE
CAMK2DQ13557humanKCNQ1P51787S484PHFMRtNsFAEDLDLKCNQ_channel
CAMK2DQ13557humanCEACAM1P13688-8S459LHFGKtGsSGPLQ__
CAMK2DQ13557humanTTNQ8WZ42S12022RRKLRPGsGGEKPPD
CAMK2DQ13557humanSCN5AQ14524S516LsLTrGLsRTsMKPRNa_trans_cytopl
CAMK2DQ13557humanTTNQ8WZ42T11932ERKIPEPtKVPEIKP
CAMK2DQ13557humanTTNQ8WZ42T11969PPVEPEPtPIAAPVT
CAMK2DQ13557humanCAMK2DQ13557T287sMMHRQEtVDCLKKF
CAMK2DQ13557humanOCLNQ16625S471LDDyREEsEEyMAAAOccludin_ELL
CAMK2DQ13557humanCAMK2BQ13554T287sMMHRQEtVECLKKF
CAMK2DQ13557humanCEACAM1P13688-8T457CFLHFGKtGsSGPLQ
CAMK2DQ13557humanTTNQ8WZ42S11878KEEVVLKsVLRKRPE
CAMK2DQ13557-8humanTPD52P55327S176kNsPtFksFEEkVENTPD52


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
CAMK2AIDDescription0.00e+00
CAMK2AGO:0006816calcium ion transport3.58e-08
CAMK2AGO:0034765regulation of monoatomic ion transmembrane transport3.58e-08
CAMK2AGO:0050804modulation of chemical synaptic transmission5.08e-08
CAMK2AGO:0099177regulation of trans-synaptic signaling5.08e-08
CAMK2AGO:0097553calcium ion transmembrane import into cytosol5.08e-08
CAMK2AGO:0048167regulation of synaptic plasticity6.48e-08
CAMK2AGO:0070588calcium ion transmembrane transport6.48e-08
CAMK2AGO:0042391regulation of membrane potential7.35e-08
CAMK2AGO:0009410response to xenobiotic stimulus6.47e-07
CAMK2AGO:0010038response to metal ion7.60e-07
CAMK2AGO:1902074response to salt8.59e-07
CAMK2AGO:0071248cellular response to metal ion5.61e-06
CAMK2AGO:0007611learning or memory6.01e-06
CAMK2AGO:0071241cellular response to inorganic substance1.54e-05
CAMK2AGO:0010959regulation of metal ion transport1.70e-05
CAMK2AGO:1904062regulation of monoatomic cation transmembrane transport1.70e-05
CAMK2AGO:0032355response to estradiol1.70e-05
CAMK2AGO:0050890cognition1.70e-05
CAMK2AGO:0007613memory2.81e-05
CAMK2AGO:1902075cellular response to salt5.00e-05
CAMK2AGO:0043279response to alkaloid9.45e-05
CAMK2AGO:0048168regulation of neuronal synaptic plasticity1.57e-04
CAMK2AGO:0060047heart contraction1.96e-04
CAMK2AGO:0050806positive regulation of synaptic transmission2.32e-04
CAMK2AGO:0003015heart process2.58e-04
CAMK2AGO:1903522regulation of blood circulation2.71e-04
CAMK2AGO:0003012muscle system process2.87e-04
CAMK2AGO:0050808synapse organization4.97e-04
CAMK2AGO:0006836neurotransmitter transport6.01e-04
CAMK2AGO:0008016regulation of heart contraction6.01e-04
CAMK2AGO:0019722calcium-mediated signaling6.01e-04
CAMK2AGO:0071312cellular response to alkaloid6.01e-04
CAMK2AGO:0001666response to hypoxia6.01e-04
CAMK2AGO:0098739import across plasma membrane6.01e-04
CAMK2AGO:0043270positive regulation of monoatomic ion transport6.21e-04
CAMK2AGO:0051090regulation of DNA-binding transcription factor activity6.90e-04
CAMK2AGO:0035865cellular response to potassium ion7.21e-04
CAMK2AGO:0001508action potential7.21e-04
CAMK2AGO:0036293response to decreased oxygen levels7.79e-04
CAMK2AGO:0007612learning7.99e-04
CAMK2AGO:0042136neurotransmitter biosynthetic process8.41e-04
CAMK2AGO:0030902hindbrain development9.86e-04
CAMK2AGO:0001504neurotransmitter uptake9.96e-04
CAMK2AGO:0022898regulation of transmembrane transporter activity1.01e-03
CAMK2AGO:0006813potassium ion transport1.04e-03
CAMK2AGO:0050769positive regulation of neurogenesis1.05e-03
CAMK2AGO:0061337cardiac conduction1.10e-03
CAMK2AGO:0048738cardiac muscle tissue development1.10e-03
CAMK2AGO:0090257regulation of muscle system process1.10e-03

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Related Drugs to CAMK2D_CAMK2A


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 CAMK2D-CAMK2A 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 CAMK2D_CAMK2A


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