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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:NEK9_EPC1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: NEK9_EPC1
KinaseFusionDB ID: KFG4164
FusionGDB2.0 ID: KFG4164
HgeneTgene
Gene symbol

NEK9

EPC1

Gene ID

91754

80314

Gene nameNIMA related kinase 9enhancer of polycomb homolog 1
SynonymsAPUG|LCCS10|NC|NERCC|NERCC1Epl1
Cytomap

14q24.3

10p11.22

Type of geneprotein-codingprotein-coding
Descriptionserine/threonine-protein kinase Nek9NIMA (never in mitosis gene a)- related kinase 9nercc1 kinasenimA-related protein kinase 9enhancer of polycomb homolog 1
Modification date2024040720240305
UniProtAcc

Q8TD19

Q9H2F5

Ensembl transtripts involved in fusion geneENST idsENST00000238616, ENST00000555763, 
ENST00000480402, ENST00000263062, 
ENST00000319778, ENST00000375110, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: NEK9 [Title/Abstract] AND EPC1 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)NEK9(75562074)-EPC1(32562209), # samples:1
NEK9(75562075)-EPC1(32562209), # 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
HgeneNEK9

GO:0000278

mitotic cell cycle

12840024|19941817

HgeneNEK9

GO:0007346

regulation of mitotic cell cycle

19941817

TgeneEPC1

GO:0000122

negative regulation of transcription by RNA polymerase II

10976108

TgeneEPC1

GO:0000724

double-strand break repair via homologous recombination

27153538

TgeneEPC1

GO:0045814

negative regulation of gene expression, epigenetic

10976108

TgeneEPC1

GO:0045892

negative regulation of DNA-templated transcription

10976108

TgeneEPC1

GO:0045944

positive regulation of transcription by RNA polymerase II

10976108

TgeneEPC1

GO:1905168

positive regulation of double-strand break repair via homologous recombination

27153538


check buttonKinase Fusion gene breakpoints across NEK9 (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 EPC1 (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure


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Kinase Fusion Gene Sample Information

check buttonKinase Fusion gene information.
check button Kinase Fusion gene information from four resources (ChiTars 5.0, ChimerDB 4.0, COSMIC, and CCLE)
* All genome coordinats were lifted-over on hg19.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.
SourceSampleHgeneHchrHbpTgeneTchrTbp
ChimerDB4TCGA-BR-8364-01ANEK9chr14

75562075

EPC1chr10

32562209

ChimerDB4TCGA-BR-8364NEK9chr14

75562074

EPC1chr10

32562209



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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)
ENST00000238616ENST00000375110NEK9chr1475562074EPC1chr10325622094402976
ENST00000238616ENST00000375110NEK9chr1475562075EPC1chr10325622094402976

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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

>ENST00000238616_ENST00000375110_NEK9_chr14_75562074_EPC1_chr10_32562209_length(amino acids)=976
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSE
KERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAM
EVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAF
GSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLG
VGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQGFVSKTLDSASAQFAASALVTSEQLM
GFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVP

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>ENST00000238616_ENST00000375110_NEK9_chr14_75562075_EPC1_chr10_32562209_length(amino acids)=976
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSE
KERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAM
EVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAF
GSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLG
VGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQGFVSKTLDSASAQFAASALVTSEQLM
GFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVP

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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/chr14:75562074/chr10:32562209)
- 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
NEK9

Q8TD19

EPC1

Q9H2F5

FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817, PubMed:26522158). {ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:12101123, ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158}.FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:14966270). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR) (PubMed:27153538). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone acetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). In the NuA4 complex, EPC1 is required to recruit MBTD1 into the complex (PubMed:32209463). {ECO:0000250|UniProtKB:Q8C9X6, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:27153538, ECO:0000269|PubMed:32209463}.

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).
744744
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote
HgeneNEK975562074EPC132562209ENST00000238616182252_3081980DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
HgeneNEK975562075EPC132562209ENST00000238616182252_3081980DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159


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


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Kinase Fusion Protein Structures

check button CIF files of the predicted kinase fusion proteins
* Here we show the 3D structure of the fusion proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
Kinase Fusion protein CIF link (fusion AA seq ID in KinaseFusionDB)HenstTenstHgeneHchrHbpTgeneTchrTbpAA seqLen(AA seq)
PDB file >>>178_NEK9_EPC1ENST00000238616ENST00000375110NEK9chr1475562075EPC1chr1032562209
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSE
KERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAM
EVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAF
GSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLG
VGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQGFVSKTLDSASAQFAASALVTSEQLM
GFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVP
976
3D view using mol* of 178_NEK9_EPC1
PDB file >>>HKFP_257_NEK9_EPC1ENST00000238616ENST00000375110NEK9chr1475562074EPC1chr1032562209
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSE
KERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAM
EVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAF
GSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLG
VGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQGFVSKTLDSASAQFAASALVTSEQLM
GFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVP
976_NEK9_EPC1
PDB file >>>HKFP_258_NEK9_EPC1ENST00000238616ENST00000375110NEK9chr1475562075EPC1chr1032562209
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSE
KERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAM
EVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAF
GSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLG
VGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQGFVSKTLDSASAQFAASALVTSEQLM
GFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVP
976_NEK9_EPC1


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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

NEK9_EPC1 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.
178_NEK9_EPC1.png
all structure sitemap plddt 178_NEK9_EPC1.png
178_NEK9_EPC1.png
all structure sitemap plddt2 178_NEK9_EPC1.png


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Potential Active Site Information


check button The potential binding sites of these fusion proteins were identified using SiteMap, a module of the Schrodinger suite.
Kinase Fusion AA seq ID in KinaseFusionDBSite scoreSizeDscoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues

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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.

178_NEK9_EPC1_ramachandran.png
all structure NEK9-EPC1

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Virtual Screening Results


check button Distribution of the average docking score across all approved kinase inhibitors.
Distribution of the number of occurrence across all approved kinase inhibitors.
5'-kinase fusion protein case
all structure NEK9-EPC1
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
178_NEK9_EPC1-DOCK_HTVS_1-001Mobocertinib-6.669630000000001-6.67733-53.553999999999995
178_NEK9_EPC1-DOCK_HTVS_1-001Pazopanib-5.77864-5.78554-44.8228
178_NEK9_EPC1-DOCK_HTVS_1-001Pazopanib-5.77864-5.78554-44.8228
178_NEK9_EPC1-DOCK_HTVS_1-001Larotrectinib-5.7775-5.7775-42.2876
178_NEK9_EPC1-DOCK_HTVS_1-001Temsirolimus-5.6950400000000005-5.69644-51.786
178_NEK9_EPC1-DOCK_HTVS_1-001Netarsudil-5.54857-5.55967-28.8455
178_NEK9_EPC1-DOCK_HTVS_1-001Netarsudil-5.54857-5.55967-28.8455
178_NEK9_EPC1-DOCK_HTVS_1-001Tofacitinib-5.39049-5.4019900000000005-37.1367
178_NEK9_EPC1-DOCK_HTVS_1-001Tofacitinib-5.39049-5.4019900000000005-37.1367
178_NEK9_EPC1-DOCK_HTVS_1-001Ruxolitinib-5.3633-5.3633-37.3568
178_NEK9_EPC1-DOCK_HTVS_1-001Tucatinib-5.278519999999999-5.74132-46.7979
178_NEK9_EPC1-DOCK_HTVS_1-001Tucatinib-5.278519999999999-5.74132-46.7979
178_NEK9_EPC1-DOCK_HTVS_1-001Abrocitinib-5.25413-5.26523-42.0374
178_NEK9_EPC1-DOCK_HTVS_1-001Abrocitinib-5.25413-5.26523-42.0374
178_NEK9_EPC1-DOCK_HTVS_1-001Pexidartinib-5.24017-5.45697-42.6446
178_NEK9_EPC1-DOCK_HTVS_1-001Pexidartinib-5.24017-5.45697-42.6446
178_NEK9_EPC1-DOCK_HTVS_1-001Temsirolimus-5.23754-5.23894-51.9654
178_NEK9_EPC1-DOCK_HTVS_1-001Netarsudil-5.21864-5.2297400000000005-46.9278
178_NEK9_EPC1-DOCK_HTVS_1-001Netarsudil-5.21864-5.2297400000000005-46.9278
178_NEK9_EPC1-DOCK_HTVS_1-001Upadacitinib-5.2146-5.2156-40.8568

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Kinase-Substrate Information of NEK9_EPC1


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
NEK9Q8TD19humanNEK9Q8TD19S944GQQVGMHskGTQTAK
NEK9Q8TD19humanNEDD1Q8NHV4S377EkAGLPRsINTDtLS
NEK9Q8TD19humanMAP1LC3BQ9GZQ8T50QLPVLDktkFLVPDHATG8
NEK9Q8TD19humanNEK7Q8TDX7S195skttAAHsLVGtPyyPkinase
NEK9Q8TD19humanNEK6Q9HC98S206sEttAAHsLVGtPyyPkinase
NEK9Q8TD19humanNEK9Q8TD19T210SEYsMAEtLVGtPYYPkinase


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
NEK9IDDescription0.00e+00
NEK9GO:0051225spindle assembly3.68e-02
NEK9GO:0007051spindle organization3.68e-02
NEK9GO:0033044regulation of chromosome organization3.68e-02
NEK9GO:0018105peptidyl-serine phosphorylation3.68e-02
NEK9GO:0018209peptidyl-serine modification3.68e-02
NEK9GO:0051081nuclear membrane disassembly3.68e-02
NEK9GO:0030397membrane disassembly3.68e-02
NEK9GO:0006995cellular response to nitrogen starvation3.68e-02
NEK9GO:0043562cellular response to nitrogen levels3.68e-02
NEK9GO:0035865cellular response to potassium ion3.68e-02
NEK9GO:0140694non-membrane-bounded organelle assembly3.68e-02
NEK9GO:1904355positive regulation of telomere capping3.68e-02
NEK9GO:0035864response to potassium ion3.68e-02
NEK9GO:0007059chromosome segregation3.68e-02
NEK9GO:1900227positive regulation of NLRP3 inflammasome complex assembly3.71e-02
NEK9GO:0141087positive regulation of inflammasome-mediated signaling pathway3.71e-02
NEK9GO:0022411cellular component disassembly4.08e-02
NEK9GO:1904353regulation of telomere capping4.08e-02
NEK9GO:0032212positive regulation of telomere maintenance via telomerase4.08e-02
NEK9GO:0051973positive regulation of telomerase activity4.08e-02
NEK9GO:1900225regulation of NLRP3 inflammasome complex assembly4.08e-02
NEK9GO:0044546NLRP3 inflammasome complex assembly4.08e-02
NEK9GO:0141085regulation of inflammasome-mediated signaling pathway4.08e-02
NEK9GO:1904358positive regulation of telomere maintenance via telomere lengthening4.08e-02
NEK9GO:0000423mitophagy4.08e-02
NEK9GO:0016233telomere capping4.08e-02
NEK9GO:0140632canonical inflammasome complex assembly4.08e-02
NEK9GO:0141084inflammasome-mediated signaling pathway4.19e-02
NEK9GO:0071763nuclear membrane organization4.19e-02
NEK9GO:0007020microtubule nucleation4.19e-02
NEK9GO:0051972regulation of telomerase activity4.19e-02
NEK9GO:0032210regulation of telomere maintenance via telomerase4.48e-02
NEK9GO:0006998nuclear envelope organization4.48e-02
NEK9GO:2000772regulation of cellular senescence4.48e-02
NEK9GO:0097352autophagosome maturation4.75e-02
NEK9GO:1904356regulation of telomere maintenance via telomere lengthening4.77e-02
NEK9GO:0062208positive regulation of pattern recognition receptor signaling pathway4.87e-02
NEK9GO:0007004telomere maintenance via telomerase4.93e-02
NEK9GO:2000573positive regulation of DNA biosynthetic process4.93e-02
NEK9GO:0032206positive regulation of telomere maintenance4.93e-02
NEK9GO:0006278RNA-templated DNA biosynthetic process5.15e-02
NEK9GO:0010833telomere maintenance via telomere lengthening5.39e-02
NEK9GO:0030071regulation of mitotic metaphase/anaphase transition5.39e-02
NEK9GO:0039531regulation of viral-induced cytoplasmic pattern recognition receptor signaling pathway5.39e-02
NEK9GO:1902099regulation of metaphase/anaphase transition of cell cycle5.39e-02
NEK9GO:0007091metaphase/anaphase transition of mitotic cell cycle5.39e-02
NEK9GO:0046785microtubule polymerization5.39e-02
NEK9GO:0061912selective autophagy5.39e-02
NEK9GO:0044784metaphase/anaphase transition of cell cycle5.39e-02

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Related Drugs to NEK9_EPC1


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 NEK9-EPC1 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 NEK9_EPC1


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