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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:CHD1_MTOR

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: CHD1_MTOR
KinaseFusionDB ID: KFG1259
FusionGDB2.0 ID: KFG1259
HgeneTgene
Gene symbol

CHD1

MTOR

Gene ID

1105

2475

Gene namechromodomain helicase DNA binding protein 1mechanistic target of rapamycin kinase
SynonymsCHD-1|PILBOSFRAP|FRAP1|FRAP2|RAFT1|RAPT1|SKS
Cytomap

5q15-q21.1

1p36.22

Type of geneprotein-codingprotein-coding
Descriptionchromodomain-helicase-DNA-binding protein 1ATP-dependent helicase CHD1serine/threonine-protein kinase mTORFK506 binding protein 12-rapamycin associated protein 2FK506-binding protein 12-rapamycin complex-associated protein 1FKBP-rapamycin associated proteinFKBP12-rapamycin complex-associated protein 1mammalian target o
Modification date2024041120240411
UniProtAcc

Q86WJ1

P42345

Ensembl transtripts involved in fusion geneENST idsENST00000284049, ENST00000511067, 
ENST00000376838, ENST00000495435, 
ENST00000361445, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: CHD1 [Title/Abstract] AND MTOR [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)CHD1(98199112)-MTOR(11273623), # samples:4
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
TgeneMTOR

GO:0001558

regulation of cell growth

18762023

TgeneMTOR

GO:0006468

protein phosphorylation

15467718

TgeneMTOR

GO:0006468

protein phosphorylation

18925875

TgeneMTOR

GO:0007040

lysosome organization

22692423

TgeneMTOR

GO:0009267

cellular response to starvation

22343943|22576015|22692423|28223137

TgeneMTOR

GO:0010507

negative regulation of autophagy

22576015|30704899|32561715

TgeneMTOR

GO:0016242

negative regulation of macroautophagy

25327288

TgeneMTOR

GO:0016310

phosphorylation

25327288

TgeneMTOR

GO:0016310

phosphorylation

11853878

TgeneMTOR

GO:0018105

peptidyl-serine phosphorylation

22343943|22576015|22692423

TgeneMTOR

GO:0031648

protein destabilization

36608670

TgeneMTOR

GO:0031667

response to nutrient levels

29750193

TgeneMTOR

GO:0031669

cellular response to nutrient levels

29750193|32561715

TgeneMTOR

GO:0031670

cellular response to nutrient

22017875|22017876|22017877

TgeneMTOR

GO:0032869

cellular response to insulin stimulus

18372248

TgeneMTOR

GO:0034198

cellular response to amino acid starvation

22343943|22424946|22576015|22692423

TgeneMTOR

GO:0038202

TORC1 signaling

12087098|17517883|18372248|22017875|22017876|22017877|24403073|24448649|28223137|29236692|29750193|31112131|32612235|36608670

TgeneMTOR

GO:0043200

response to amino acid

18497260

TgeneMTOR

GO:0045727

positive regulation of translation

18762023

TgeneMTOR

GO:0045948

positive regulation of translational initiation

22578813|29750193

TgeneMTOR

GO:0046777

protein autophosphorylation

15467718

TgeneMTOR

GO:0051647

nucleus localization

22343943|22576015|22692423

TgeneMTOR

GO:0071230

cellular response to amino acid stimulus

22424946

TgeneMTOR

GO:0071233

cellular response to L-leucine

22424946

TgeneMTOR

GO:1900181

negative regulation of protein localization to nucleus

22692423|24448649|32612235|35662396

TgeneMTOR

GO:1905672

negative regulation of lysosome organization

24448649|32612235

TgeneMTOR

GO:1990253

cellular response to leucine starvation

22424946

TgeneMTOR

GO:2000785

regulation of autophagosome assembly

23524951


check buttonKinase Fusion gene breakpoints across CHD1 (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 MTOR (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-AB-2939-03ACHD1chr5

98199112

MTORchr1

11273623

ChimerDB4TCGA-AB-2939_61FFWAAXX_7CHD1chr5

98204199

MTORchr1

11273623

ChimerDB4TCGA-AB-2939CHD1chr5

98199111

MTORchr1

11273623



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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)
ENST00000284049ENST00000361445CHD1chr598204199MTORchr11127362398812926

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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

>ENST00000284049_ENST00000361445_CHD1_chr5_98204199_MTOR_chr1_11273623_length(amino acids)=2926
MNGHSDEESVRNSSGESSQSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSESGSQSESESDTSRENKVQAKPPKVDGAEFWKSS
PSILAVQRSAILKKQQQQQQQQQHQASSNSGSEEDSSSSEDSDDSSSEVKRKKHKDEDWQMSGSGSPSQSGSDSESEEEREKSSCDETES
DYEPKNKVKSRKPQNRSKSKNGKKILGQKKRQIDSSEEDDDEEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEEEE
FETIERFMDCRIGRKGATGATTTIYAVEADGDPNAGFEKNKEPGEIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETK
RWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALISKKFQACIDEYFSRNQSKTTP
FKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS
TLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWTHHQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTL
IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSA
LQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIF
SQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHR
IGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEM
DIDEILKRAETHENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEDQRRRLEEEERQKELEEIYMLPRMRNCAKQI
SFNGSEGRRSRSRRYSGSDSDSISEGKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGE
LVHNGCIKALKDSSSGTERTGGRLGKVKGPTFRISGVQVNAKLVISHEEELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSN
LLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKKEALSGAGSSKRRKARAKKNKAMKSIKVKEE
IKSDSSPLPSEKSDEDDDKLSESKSDGRERSKKSSVSDAPVHITASGEPVPISEESEELDQKTFSIEFWVMNTSIQSTIILLIEQIVVAL
GGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYAS
RIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGD
ALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQ
QDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKL
QQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMA
RMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVI
QYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVH
PQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHD
RSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDL
SKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTD
IGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEP
LHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGT
YDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTN
SGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRS
LAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDS
VMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINR

--------------------------------------------------------------

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/chr5:98199112/chr1:11273623)
- 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
CHD1

Q86WJ1

MTOR

P42345

FUNCTION: ATP-dependent chromatin remodeler that mediates chromatin-remodeling following DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:33357431, PubMed:34486521, PubMed:34874266, PubMed:34210977). Recruited to DNA damage sites through interaction with poly-ADP-ribose: specifically recognizes and binds histones that are poly-ADP-ribosylated on serine residues in response to DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34874266, PubMed:34486521). Poly-ADP-ribose-binding activates the ATP-dependent chromatin remodeler activity, thereby regulating chromatin during DNA repair (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34874266, PubMed:34486521). Catalyzes nucleosome sliding away from DNA breaks in an ATP-dependent manner (PubMed:19661379, PubMed:29220652, PubMed:29220653). Chromatin remodeling activity promotes PARP2 removal from chromatin (PubMed:33275888). {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:33275888, ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34210977, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}.FUNCTION: Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:31112131, PubMed:31601708, PubMed:32561715, PubMed:34519269, PubMed:29236692, PubMed:37751742). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed:15268862, PubMed:15467718, PubMed:17517883, PubMed:18925875, PubMed:18372248, PubMed:18497260, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704, PubMed:29236692, PubMed:37751742). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862, PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:31112131, PubMed:34519269, PubMed:29236692). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed:24403073, PubMed:29236692). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:12150925, PubMed:12087098, PubMed:18925875, PubMed:29150432, PubMed:29236692). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed:23429704, PubMed:23429703). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation (PubMed:36691768). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1 (PubMed:32561715). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed:32561715). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed:23524951, PubMed:25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:24403073). The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation (PubMed:22576015, PubMed:22343943, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670, PubMed:36697823). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed:22576015, PubMed:22343943, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670). The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization (PubMed:34289345). MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). mTORC2 plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (PubMed:15718470). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity). Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex (By similarity). {ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:17517883, ECO:0000269|PubMed:18372248, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:21659604, ECO:0000269|PubMed:22343943, ECO:0000269|PubMed:22576015, ECO:0000269|PubMed:22692423, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:23524951, ECO:0000269|PubMed:24403073, ECO:0000269|PubMed:24448649, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25799227, ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:29150432, ECO:0000269|PubMed:29236692, ECO:0000269|PubMed:30704899, ECO:0000269|PubMed:31112131, ECO:0000269|PubMed:31601708, ECO:0000269|PubMed:32561715, ECO:0000269|PubMed:32612235, ECO:0000269|PubMed:34289345, ECO:0000269|PubMed:34519269, ECO:0000269|PubMed:36608670, ECO:0000269|PubMed:36691768, ECO:0000269|PubMed:36697823, ECO:0000269|PubMed:37751742}.

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
TgeneCHD198204199MTOR11273623ENST0000028404919581382_198210392550DomainNote=FAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534
TgeneCHD198204199MTOR11273623ENST0000028404919582517_254910392550DomainNote=FATC;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00534,ECO:0000255|PROSITE-ProRule:PRU00535
TgeneCHD198204199MTOR11273623ENST0000028404919582156_246910392550DomainNote=PI3K/PI4K catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00269


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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 >>>101_CHD1_MTORENST00000284049ENST00000361445CHD1chr598204199MTORchr111273623
MNGHSDEESVRNSSGESSQSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSESGSQSESESDTSRENKVQAKPPKVDGAEFWKSS
PSILAVQRSAILKKQQQQQQQQQHQASSNSGSEEDSSSSEDSDDSSSEVKRKKHKDEDWQMSGSGSPSQSGSDSESEEEREKSSCDETES
DYEPKNKVKSRKPQNRSKSKNGKKILGQKKRQIDSSEEDDDEEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEEEE
FETIERFMDCRIGRKGATGATTTIYAVEADGDPNAGFEKNKEPGEIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETK
RWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALISKKFQACIDEYFSRNQSKTTP
FKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS
TLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWTHHQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTL
IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSA
LQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIF
SQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHR
IGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEM
DIDEILKRAETHENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEDQRRRLEEEERQKELEEIYMLPRMRNCAKQI
SFNGSEGRRSRSRRYSGSDSDSISEGKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGE
LVHNGCIKALKDSSSGTERTGGRLGKVKGPTFRISGVQVNAKLVISHEEELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSN
LLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKKEALSGAGSSKRRKARAKKNKAMKSIKVKEE
IKSDSSPLPSEKSDEDDDKLSESKSDGRERSKKSSVSDAPVHITASGEPVPISEESEELDQKTFSIEFWVMNTSIQSTIILLIEQIVVAL
GGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYAS
RIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGD
ALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQ
QDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKL
QQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMA
RMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVI
QYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVH
PQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHD
RSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDL
SKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTD
IGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEP
LHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGT
YDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTN
SGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRS
LAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDS
VMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINR
2926
3D view using mol* of 101_CHD1_MTOR
PDB file >>>TKFP_173_CHD1_MTORENST00000284049ENST00000361445CHD1chr598204199MTORchr111273623
MNGHSDEESVRNSSGESSQSDDDSGSASGSGSGSSSGSSSDGSSSQSGSSDSDSGSESGSQSESESDTSRENKVQAKPPKVDGAEFWKSS
PSILAVQRSAILKKQQQQQQQQQHQASSNSGSEEDSSSSEDSDDSSSEVKRKKHKDEDWQMSGSGSPSQSGSDSESEEEREKSSCDETES
DYEPKNKVKSRKPQNRSKSKNGKKILGQKKRQIDSSEEDDDEEDYDNDKRSSRRQATVNVSYKEDEEMKTDSDDLLEVCGEDVPQPEEEE
FETIERFMDCRIGRKGATGATTTIYAVEADGDPNAGFEKNKEPGEIQYLIKWKGWSHIHNTWETEETLKQQNVRGMKKLDNYKKKDQETK
RWLKNASPEDVEYYNCQQELTDDLHKQYQIVERIIAHSNQKSAAGYPDYYCKWQGLPYSECSWEDGALISKKFQACIDEYFSRNQSKTTP
FKDCKVLKQRPRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS
TLTSWQREIQTWASQMNAVVYLGDINSRNMIRTHEWTHHQTKRLKFNILLTTYEILLKDKAFLGGLNWAFIGVDEAHRLKNDDSLLYKTL
IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRRVKKDVEKSLPAKVEQILRMEMSA
LQKQYYKWILTRNYKALSKGSKGSTSGFLNIMMELKKCCNHCYLIKPPDNNEFYNKQEALQHLIRSSGKLILLDKLLIRLRERGNRVLIF
SQMVRMLDILAEYLKYRQFPFQRLDGSIKGELRKQALDHFNAEGSEDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQARAHR
IGQKKQVNIYRLVTKGSVEEDILERAKKKMVLDHLVIQRMDTTGKTVLHTGSAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEM
DIDEILKRAETHENEPGPLTVGDELLSQFKVANFSNMDEDDIELEPERNSKNWEEIIPEDQRRRLEEEERQKELEEIYMLPRMRNCAKQI
SFNGSEGRRSRSRRYSGSDSDSISEGKRPKKRGRPRTIPRENIKGFSDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSETDLRRLGE
LVHNGCIKALKDSSSGTERTGGRLGKVKGPTFRISGVQVNAKLVISHEEELIPLHKSIPSDPEERKQYTIPCHTKAAHFDIDWGKEDDSN
LLIGIYEYGYGSWEMIKMDPDLSLTHKILPDDPDKKPQAKQLQTRADYLIKLLSRDLAKKEALSGAGSSKRRKARAKKNKAMKSIKVKEE
IKSDSSPLPSEKSDEDDDKLSESKSDGRERSKKSSVSDAPVHITASGEPVPISEESEELDQKTFSIEFWVMNTSIQSTIILLIEQIVVAL
GGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYAS
RIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGD
ALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQ
QDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKL
QQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMA
RMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVI
QYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVH
PQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHD
RSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDL
SKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTD
IGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEP
LHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGT
YDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTN
SGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRS
LAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDS
VMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINR
2926_CHD1_MTOR


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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

CHD1_MTOR does not have any known PDB structures.

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pLDDT score distribution

all_data/KinaseFusionDB_T_Results/KinaseFusionDB_T_ViolinPlots/101_CHD1_MTOR.png
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.
101_CHD1_MTOR.png
all structure sitemap plddt3 101_CHD1_MTOR.png
101_CHD1_MTOR.png
all structure sitemap plddt4 101_CHD1_MTOR.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.

101_CHD1_MTOR_ramachandran.png
all structure CHD1-MTOR

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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
all structure CHD1-MTOR

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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
101_CHD1_MTOR-DOCK_HTVS_1-001Crizotinib-6.38428-6.88018-42.9757
101_CHD1_MTOR-DOCK_HTVS_1-001Crizotinib-6.38428-6.88018-42.9757
101_CHD1_MTOR-DOCK_HTVS_1-001Vandetanib-6.37434-6.37434-39.9729
101_CHD1_MTOR-DOCK_HTVS_1-001Vandetanib-6.3529599999999995-6.3529599999999995-36.7263
101_CHD1_MTOR-DOCK_HTVS_1-001Pralsetinib-6.19346-6.28496-42.1743
101_CHD1_MTOR-DOCK_HTVS_1-001Nilotinib-6.13823-6.277830000000001-51.2568
101_CHD1_MTOR-DOCK_HTVS_1-001Nilotinib-6.13823-6.277830000000001-51.2568
101_CHD1_MTOR-DOCK_HTVS_1-001Lapatinib-5.93938-6.02818-54.2932
101_CHD1_MTOR-DOCK_HTVS_1-001Lapatinib-5.73787-5.82667-49.4771
101_CHD1_MTOR-DOCK_HTVS_1-001Pralsetinib-5.67788-5.76938-33.5879
101_CHD1_MTOR-DOCK_HTVS_1-001Belumosudil-5.51393-5.52163-27.1343
101_CHD1_MTOR-DOCK_HTVS_1-001Pralsetinib-5.45437-5.54587-39.1125
101_CHD1_MTOR-DOCK_HTVS_1-001Zanubrutinib-5.26627-5.26627-35.7842
101_CHD1_MTOR-DOCK_HTVS_1-001Upadacitinib-5.25355-5.25455-28.1047
101_CHD1_MTOR-DOCK_HTVS_1-001Neratinib-5.2247900000000005-5.40709-43.6152
101_CHD1_MTOR-DOCK_HTVS_1-001Neratinib-5.2247900000000005-5.40709-43.6152
101_CHD1_MTOR-DOCK_HTVS_1-001Neratinib-5.22371-5.40961-42.145
101_CHD1_MTOR-DOCK_HTVS_1-001Pralsetinib-4.87351-4.9650099999999995-40.4922
101_CHD1_MTOR-DOCK_HTVS_1-001Pexidartinib-4.791919999999999-5.008719999999999-31.5873
101_CHD1_MTOR-DOCK_HTVS_1-001Pexidartinib-4.791919999999999-5.008719999999999-31.5873

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Kinase-Substrate Information of CHD1_MTOR


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
MTORP42345humanANKRD17O75179S2047VssPssPsPPAQPGG
MTORP42345humanIRS1P35568S636sGDyMPMsPKsVSAP
MTORP42345humanRRAGCQ9HB90S21GsYGAADsFPKDFGY
MTORP42345humanMKNK2Q9HBH9S74KRGRAtDsFsGRFED
MTORP42345humanULK1O75385S758PVVFtVGsPPsGStP
MTORP42345humanBRD9Q9H8M2S588DPYEFLQsPEPAAsA
MTORP42345humanWASHC2AQ641Q2S700DDVDSGGsLFGsPPT
MTORP42345humanESR1P03372S104FPPLNsVsPsPLMLLOest_recep
MTORP42345humanUVRAGQ9P2Y5S549RKItsLSssLDTsLD
MTORP42345humanTFEBP19484S122PkPPPAAsPGVRAGHMITF_TFEB_C_3_N
MTORP42345humanSRRM1Q8IYB3T574PRRRRtPtPPPRRRt
MTORP42345humanSENP3Q9H4L4S143LLYsKstsLtFHWKL
MTORP42345humanSENP3Q9H4L4T145YsKstsLtFHWKLWG
MTORP42345humanMTORP42345S2448RsRtRtDsysAGQsV
MTORP42345humanDAPP51397S51DQEWEsPsPPkPtVFDAP
MTORP42345humanSENP3Q9H4L4S25PGIPPAyssPRRERL
MTORP42345humanPKN2Q16513T958TsEAPILtPPREPRIPkinase_C
MTORP42345humanRPS6KB1P23443T412NQVFLGFtyVAPsVLPkinase_C
MTORP42345humanMCL1Q07820S64IGGSAGAsPPStLtP
MTORP42345humanAKT1P31749S473RPHFPQFsysAsGtAPkinase_C
MTORP42345humanNRBF2Q96F24S120sPLsQkYsPSTEKCLNRBF2
MTORP42345humanSRRM1Q8IYB3T572PPPRRRRtPtPPPRR
MTORP42345humanELP1O95163S1174SETSsVVsGSEMSGK
MTORP42345humanNAA10P41227S228StDVKDssEAsDSAS
MTORP42345humanTFEBP19484S211LVGVTSSsCPADLTQ
MTORP42345humanPRKNO60260S127AVILHTDsRkDsPPA
MTORP42345humanARP10275S96QQQGEDGsPQAHRRGAndrogen_recep
MTORP42345humanMTORP42345S2478tGttVPEsIHsFIGD
MTORP42345humanPASKQ96RG2T640MAGLSFGtPtLDEPW
MTORP42345humanAKT1S1Q96B36S183PTQQYAKsLPVSVPVPRAS
MTORP42345humanLARP6Q9BRS8S409GRLNCStsPEIFRKC
MTORP42345humanSRRM2Q9UQ35S1318sPEHKELsNsPLREN
MTORP42345humanUNKQ9C0B0S611GtsAsHGsLGLNGMN
MTORP42345humanUVRAGQ9P2Y5S498GFsGGIPsPDKGHRK
MTORP42345humanDNMT1P26358S714DNIPEMPsPkKMHQG
MTORP42345humanULK1O75385S638FDFPKtPssQNLLAL
MTORP42345humanMAPKAP1Q9BPZ7S260PIHKFGFsTLALVEKCRIM
MTORP42345humanUNKQ9C0B0S606ENTFLGtsAsHGsLG
MTORP42345humanHOXB13Q92826S31GRNLVAHsPLTSHPA
MTORP42345humanAKT1P31749T450tAQMItItPPDQDDsPkinase_C
MTORP42345humanRRM1P23921S631IYTRRVLsGEFQIVNRibonuc_red_lgC
MTORP42345humanGRB10Q13322S476MNILGsQsPLHPSTL
MTORP42345humanDUSP10Q9Y6W6S224SCREGKDsFKRIFsKRhodanese
MTORP42345humanWASHC2AQ641Q2S704SGGsLFGsPPTSVPP
MTORP42345humanPRKCEQ02156T710TREEPVLtLVDEAIVPkinase_C
MTORP42345humanSTK11IPQ8N1F8S404EPRTLNPsPAGWFVQ
MTORP42345humanLARP1Q6PKG0S774LPttVPEsPNyRNtR
MTORP42345humanUNKQ9C0B0S336QPSsAVssPtQPGPV
MTORP42345humanUNKQ9C0B0S608TFLGtsAsHGsLGLN
MTORP42345humanMAF1Q9H063S60PHVLEALsPPQtsGLMaf1
MTORP42345humanAMOTL2Q9Y2J4S759SsSQRAAsLDsVATS
MTORP42345humanEIF4EBP1Q13541S44tPGGtLFsttPGGtReIF_4EBP
MTORP42345humanPASKQ96RG2S953FLAsLPGstHsTAAE
MTORP42345humanUVRAGQ9P2Y5S582GHANVHPsQEQGEAL
MTORP42345humanSENP3Q9H4L4S141RMLLYsKstsLtFHW
MTORP42345humanMTORP42345T2473PAHKKtGttVPEsIH
MTORP42345humanMYCNP04198S62LLPtPPLsPsrGFAEMyc_N
MTORP42345humanRPTORQ8N122S859DtssLtQsAPAsPtN
MTORP42345humanEIF4EBP1Q13541S65FLMECrNsPVtktPPeIF_4EBP
MTORP42345humanNDRG1Q92597T346GtRsRsHtsEGtRsR
MTORP42345humanSOD1P00441T40WGsIkGLtEGLHGFHSod_Cu
MTORP42345humanPRKCBP05771T642TRQPVELtPtDKLFIPkinase_C
MTORP42345humanEEF2KO00418S72ksERysssGsPANsF
MTORP42345humanSRRM2Q9UQ35S1329LRENsFGsPLEFRNs
MTORP42345humanMTORP42345S2454DsysAGQsVEILDGV
MTORP42345humanMTORP42345S2481tVPEsIHsFIGDGLV
MTORP42345humanELLP55199S309LGDPAAssPPGERGR
MTORP42345humanEEF2KO00418S74ERysssGsPANsFHF
MTORP42345humanESR1P03372S118LHPPPQLsPFLQPHGOest_recep
MTORP42345humanDEPTORQ8TB45T295GyFsssPtLsssPPV
MTORP42345humanRPS6KB1P23443S394TRQtPVDsPDDStLSPkinase_C
MTORP42345humanPASKQ96RG2S956sLPGstHsTAAELTG
MTORP42345humanESR1P03372S106PLNsVsPsPLMLLHPOest_recep
MTORP42345humanSENP3Q9H4L4S26GIPPAyssPRRERLR
MTORP42345humanDEPTORQ8TB45S293ssGyFsssPtLsssP
MTORP42345humanSENP3Q9H4L4S139AFRMLLYsKstsLtF
MTORP42345humanHOXB13Q92826T41TSHPAAPtLMPAVNY
MTORP42345humanBAG3O95817T285GsPARsstPLHsPsP
MTORP42345humanRPRD1BQ9NQG5S166DDyPGsysPQDPsAG
MTORP42345humanSLC7A11Q9UPY5S26NVNGRLPsLGNkEPP
MTORP42345humanPASKQ96RG2T642GLSFGtPtLDEPWLG
MTORP42345humanEIF4EBP1Q13541T70rNsPVtktPPRDLPteIF_4EBP
MTORP42345humanPRKCEQ02156S729QEEFKGFsYFGEDLMPkinase_C
MTORP42345humanSRRM2Q9UQ35S1326NsPLRENsFGsPLEF
MTORP42345humanUNKQ9C0B0S255RKHKYRSsPCPNVKH
MTORP42345humanPATL1Q86TB9S179ALPRRstsPIIGsPP
MTORP42345humanRRAGCQ9HB90T394kALTHNGtPRNAI__
MTORP42345humanGRB10Q13322S428stPVRsVsENsLVAMBPS
MTORP42345humanUVRAGQ9P2Y5S571KGEDLVGsLNGGHAN
MTORP42345humanSGK1O00141S422AEAFLGFsYAPPTDSPkinase_C
MTORP42345humanAPBA3O96018S7_MDFPtIsRsPsGPP
MTORP42345humanYAP1P46937S436INQSTLPsQQNRFPD
MTORP42345humanZNRF2Q8NHG8S145GPRLVIGsLPAHLsP
MTORP42345humanRPS6P62753S236AKRRRLssLRAstsK
MTORP42345humanRPTORQ8N122S863LtQsAPAsPtNkGVH
MTORP42345humanOXSR1O95747S339EDGGWEWsDDEFDEE
MTORP42345humanISCUQ9H1K1S14FRLRRAAsALLLRsP
MTORP42345humanPATL1Q86TB9S184stsPIIGsPPVRAVP
MTORP42345humanUVRAGQ9P2Y5S550KItsLSssLDTsLDF
MTORP42345humanBAG3O95817S289RsstPLHsPsPIRVH
MTORP42345humanDEPTORQ8TB45S286ssMssCGssGyFsss
MTORP42345humanIRS1P35568S639yMPMsPKsVSAPQQI
MTORP42345humanEIF4EBP1Q13541T37PPGDysttPGGtLFseIF_4EBP
MTORP42345humanHSF1Q00613S303RVkEEPPsPPQsPRVVert_HS_TF
MTORP42345humanRPS6KB1P23443S434sFEPKIRsPRRFIGs
MTORP42345humanMYCP01106S77LLPtPPLsPsRRsGLMyc_N
MTORP42345humanEIF4EBP1Q13541T41ysttPGGtLFsttPGeIF_4EBP
MTORP42345humanDUSP10Q9Y6W6S230DsFKRIFsKEIIVyDRhodanese
MTORP42345humanUVRAGQ9P2Y5S522QyktPPPsyNSALAQ
MTORP42345humanAKT1S1Q96B36S221DLDRIAAsMRALVLRPRAS
MTORP42345humanUVRAGQ9P2Y5S508KGHRKRAssENERLQ
MTORP42345humanUNKQ9C0B0S359DSVPVsPssPHAPDL
MTORP42345humanDEPTORQ8TB45S265stsFMsVsPsKEIKI
MTORP42345humanPIP4K2CQ8TBX8S328LVGsYGTsPEGIGGYPIP5K
MTORP42345humanAMBRA1Q9C0C7S52KRVELPDsPRSTFLL
MTORP42345humanANKRD17O75179S2045yPVssPssPsPPAQP
MTORP42345humanHSF1Q00613S326ssVDtLLsPTALIDsVert_HS_TF
MTORP42345humanUBR4Q5T4S7S2932GHPAGPGsVsSStGA
MTORP42345humanRUBCNLQ9H714S157sPGILATsPYPETDS
MTORP42345humanSCYL1Q96KG9S754sTQPRPDsWGEDNWE
MTORP42345humanRPS6KB1P23443-2T389NQVFLGFtYVAPSVLPkinase_C
MTORP42345humanEIF4EBP1Q13541T46GGtLFsttPGGtRIIeIF_4EBP
MTORP42345humanZNF768Q9H5H4S139sPGyEPRsPGyEsESRNA_pol_Rpb1_R
MTORP42345humanSENP3Q9H4L4T142MLLYsKstsLtFHWK
MTORP42345humanLARP6Q9BRS8S348DPESNPTsPMAGRRH
MTORP42345humanRPS6P62753S235IAKRRRLssLRAsts
MTORP42345humanNRBF2Q96F24S113AEDAEGQsPLsQkYsNRBF2
MTORP42345humanMAF1Q9H063S75sPsRLsksQGGEEEGMaf1
MTORP42345humanMAF1Q9H063S68PPQtsGLsPsRLsksMaf1
MTORP42345humanAPBA3O96018T5___MDFPtIsRsPsG
MTORP42345humanUVRAGQ9P2Y5S493GGADVGFsGGIPsPD
MTORP42345humanPASKQ96RG2S949RTRLFLAsLPGstHs
MTORP42345humanPIP4K2CQ8TBX8S324GPPALVGsYGTsPEGPIP5K
MTORP42345humanGRB10Q13322T155PGsPPVLtPGsLPPS
MTORP42345humanDEPTORQ8TB45S299ssPtLsssPPVLCNP
MTORP42345humanHOXB13Q92826T8MEPGNYAtLDGAKDI
MTORP42345humanMTORP42345T2474AHKKtGttVPEsIHs
MTORP42345humanWNK1Q9H4A3S2032DGsGsPHsPHQLssK
MTORP42345humanLARP1Q6PKG0S766EPStIARsLPttVPE
MTORP42345humanPRKCEQ02156T566LNGVTTTtFCGTPDyPkinase


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
MTORIDDescription0.00e+00
MTORGO:0010506regulation of autophagy2.32e-10
MTORGO:0031929TOR signaling2.02e-08
MTORGO:0031331positive regulation of cellular catabolic process8.18e-08
MTORGO:0018105peptidyl-serine phosphorylation3.10e-07
MTORGO:0018209peptidyl-serine modification4.05e-07
MTORGO:0038202TORC1 signaling8.92e-07
MTORGO:0010508positive regulation of autophagy1.02e-06
MTORGO:0045931positive regulation of mitotic cell cycle4.85e-06
MTORGO:0031667response to nutrient levels4.85e-06
MTORGO:0010507negative regulation of autophagy7.39e-06
MTORGO:1901654response to ketone1.12e-05
MTORGO:0006359regulation of transcription by RNA polymerase III1.26e-05
MTORGO:0016241regulation of macroautophagy1.72e-05
MTORGO:0062197cellular response to chemical stress2.97e-05
MTORGO:0031669cellular response to nutrient levels3.52e-05
MTORGO:0016236macroautophagy3.52e-05
MTORGO:0016239positive regulation of macroautophagy3.52e-05
MTORGO:0000082G1/S transition of mitotic cell cycle3.52e-05
MTORGO:0045787positive regulation of cell cycle3.54e-05
MTORGO:0046627negative regulation of insulin receptor signaling pathway3.85e-05
MTORGO:0006109regulation of carbohydrate metabolic process3.85e-05
MTORGO:1900077negative regulation of cellular response to insulin stimulus3.98e-05
MTORGO:0071496cellular response to external stimulus4.05e-05
MTORGO:0045945positive regulation of transcription by RNA polymerase III4.13e-05
MTORGO:0043467regulation of generation of precursor metabolites and energy5.72e-05
MTORGO:0044843cell cycle G1/S phase transition5.72e-05
MTORGO:0031668cellular response to extracellular stimulus5.78e-05
MTORGO:0032869cellular response to insulin stimulus5.78e-05
MTORGO:0031330negative regulation of cellular catabolic process6.00e-05
MTORGO:0042594response to starvation8.27e-05
MTORGO:1990928response to amino acid starvation1.01e-04
MTORGO:0036294cellular response to decreased oxygen levels1.05e-04
MTORGO:0071375cellular response to peptide hormone stimulus1.05e-04
MTORGO:0097191extrinsic apoptotic signaling pathway1.05e-04
MTORGO:1901655cellular response to ketone1.18e-04
MTORGO:0006383transcription by RNA polymerase III1.61e-04
MTORGO:0071453cellular response to oxygen levels1.79e-04
MTORGO:0062012regulation of small molecule metabolic process1.86e-04
MTORGO:0019216regulation of lipid metabolic process2.04e-04
MTORGO:0008361regulation of cell size2.62e-04
MTORGO:0046626regulation of insulin receptor signaling pathway2.62e-04
MTORGO:0032868response to insulin2.81e-04
MTORGO:1900076regulation of cellular response to insulin stimulus2.87e-04
MTORGO:0008286insulin receptor signaling pathway2.90e-04
MTORGO:0043200response to amino acid2.97e-04
MTORGO:0046777protein autophosphorylation3.48e-04
MTORGO:1901653cellular response to peptide3.49e-04
MTORGO:0010827regulation of glucose transmembrane transport4.09e-04
MTORGO:0098781ncRNA transcription4.23e-04

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Related Drugs to CHD1_MTOR


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 CHD1-MTOR 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 CHD1_MTOR


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