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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:USP7_PRKCB

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: USP7_PRKCB
KinaseFusionDB ID: KFG7039
FusionGDB2.0 ID: KFG7039
HgeneTgene
Gene symbol

USP7

PRKCB

Gene ID

7874

5579

Gene nameubiquitin specific peptidase 7protein kinase C beta
SynonymsC16DELp13.2|DEL16P13.2|HAFOUS|HAUSP|TEF1PKC-beta|PKCB|PKCI(2)|PKCbeta|PRKCB1|PRKCB2
Cytomap

16p13.2

16p12.2-p12.1

Type of geneprotein-codingprotein-coding
Descriptionubiquitin carboxyl-terminal hydrolase 7Chromosome 16p13.2 deletion syndromeHerpes virus-associated ubiquitin-specific proteasedeubiquitinating enzyme 7ubiquitin specific peptidase 7 (herpes virus-associated)ubiquitin specific protease 7 (herpes virusprotein kinase C beta typePKC-Bprotein kinase C, beta 1 polypeptide
Modification date2024041120240407
UniProtAcc

Q93009

P05771

Ensembl transtripts involved in fusion geneENST idsENST00000344836, ENST00000381886, 
ENST00000535863, ENST00000566224, 
ENST00000482000, ENST00000498058, 
ENST00000303531, ENST00000321728, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: USP7 [Title/Abstract] AND PRKCB [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)USP7(9057063)-PRKCB(24043456), # samples:1
USP7(9057064)-PRKCB(24043457), # 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
HgeneUSP7

GO:0006307

DNA alkylation repair

25944111

HgeneUSP7

GO:0016579

protein deubiquitination

16964248|21258371|21745816|25172512

HgeneUSP7

GO:0031647

regulation of protein stability

27123980

HgeneUSP7

GO:0032088

negative regulation of NF-kappaB transcription factor activity

11279055

HgeneUSP7

GO:0035520

monoubiquitinated protein deubiquitination

26280536

HgeneUSP7

GO:0042752

regulation of circadian rhythm

27123980

HgeneUSP7

GO:0045721

negative regulation of gluconeogenesis

28655758

HgeneUSP7

GO:0050821

protein stabilization

21258371|25172512|35216969

HgeneUSP7

GO:0051090

regulation of DNA-binding transcription factor activity

16964248

HgeneUSP7

GO:0075342

symbiont-mediated disruption of host cell PML body

20719947

HgeneUSP7

GO:1904262

negative regulation of TORC1 signaling

35216969

TgenePRKCB

GO:0010827

regulation of glucose transmembrane transport

25982116

TgenePRKCB

GO:0043687

post-translational protein modification

20228790


check buttonKinase Fusion gene breakpoints across USP7 (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 PRKCB (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-A6-3807-01AUSP7chr16

9057064

PRKCBchr16

24043457

ChimerDB4TCGA-A6-3807USP7chr16

9057063

PRKCBchr16

24043456



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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)
ENST00000344836ENST00000321728USP7chr169057063PRKCBchr16240434562504551
ENST00000344836ENST00000321728USP7chr169057064PRKCBchr16240434572504551

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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

>ENST00000344836_ENST00000321728_USP7_chr16_9057063_PRKCB_chr16_24043456_length(amino acids)=551
MLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQ
KTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVE
KRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVA
ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF

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>ENST00000344836_ENST00000321728_USP7_chr16_9057064_PRKCB_chr16_24043457_length(amino acids)=551
MLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQ
KTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVE
KRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVA
ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF

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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/chr16:9057063/chr16:24043456)
- 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
USP7

Q93009

PRKCB

P05771

FUNCTION: Hydrolase that deubiquitinates target proteins such as FOXO4, DEPTOR, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:25865756, PubMed:26678539, PubMed:28655758, PubMed:35216969). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis (PubMed:11923872, PubMed:26786098). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML (PubMed:18716620). Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539). Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6 (PubMed:22466611, PubMed:22466612). Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1 (PubMed:21745816, PubMed:22411829). Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains (PubMed:22689415). Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins (PubMed:27123980). Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells (PubMed:21258371). Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed:26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed:26365382). Mediates the deubiquitination of phosphorylated DEPTOR, promoting its stability and leading to decreased mTORC1 signaling (PubMed:35216969). {ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:20153724, ECO:0000269|PubMed:20601937, ECO:0000269|PubMed:21258371, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22689415, ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:25283148, ECO:0000269|PubMed:25865756, ECO:0000269|PubMed:25944111, ECO:0000269|PubMed:26365382, ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:26786098, ECO:0000269|PubMed:27123980, ECO:0000269|PubMed:28655758, ECO:0000269|PubMed:35216969}.; FUNCTION: (Microbial infection) Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. {ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:18590780}.; FUNCTION: (Microbial infection) Upon infection with Epstein-Barr virus, the interaction with viral EBNA1 increases the association of USP7 with PML proteins, which is required for the polyubiquitylation and degradation of PML. {ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:24216761}.FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). {ECO:0000250|UniProtKB:P68404, ECO:0000269|PubMed:11598012, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25313067, ECO:0000269|PubMed:25982116}.

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
TgeneUSP79057063PRKCB24043456ENST0000034483602601_671058DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057063PRKCB24043456ENST00000344836217601_67196672DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057063PRKCB24043456ENST00000344836217601_67196674DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057064PRKCB24043457ENST0000034483602601_671058DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057064PRKCB24043457ENST00000344836217601_67196672DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057064PRKCB24043457ENST00000344836217601_67196674DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneUSP79057063PRKCB24043456ENST0000034483602158_275058DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057063PRKCB24043456ENST00000344836217158_27596672DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057063PRKCB24043456ENST00000344836217158_27596674DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057064PRKCB24043457ENST0000034483602158_275058DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057064PRKCB24043457ENST00000344836217158_27596672DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057064PRKCB24043457ENST00000344836217158_27596674DomainNote=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041
TgeneUSP79057063PRKCB24043456ENST0000034483602342_600058DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneUSP79057063PRKCB24043456ENST00000344836217342_60096672DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneUSP79057063PRKCB24043456ENST00000344836217342_60096674DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneUSP79057064PRKCB24043457ENST0000034483602342_600058DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneUSP79057064PRKCB24043457ENST00000344836217342_60096672DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneUSP79057064PRKCB24043457ENST00000344836217342_60096674DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159


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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 >>>546_USP7_PRKCBENST00000344836ENST00000321728USP7chr169057064PRKCBchr1624043457
MLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQ
KTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVE
KRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVA
ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF
551
3D view using mol* of 546_USP7_PRKCB
PDB file >>>TKFP_935_USP7_PRKCBENST00000344836ENST00000321728USP7chr169057063PRKCBchr1624043456
MLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQ
KTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVE
KRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVA
ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF
551_USP7_PRKCB
PDB file >>>TKFP_936_USP7_PRKCBENST00000344836ENST00000321728USP7chr169057064PRKCBchr1624043457
MLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQ
KTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVE
KRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVA
ICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF
551_USP7_PRKCB


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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

USP7_PRKCB does not have any known PDB structures.

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pLDDT score distribution

all_data/KinaseFusionDB_T_Results/KinaseFusionDB_T_ViolinPlots/546_USP7_PRKCB.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.
546_USP7_PRKCB.png
all structure sitemap plddt3 546_USP7_PRKCB.png
546_USP7_PRKCB.png
all structure sitemap plddt4 546_USP7_PRKCB.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.

546_USP7_PRKCB_ramachandran.png
all structure USP7-PRKCB

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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 USP7-PRKCB

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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
546_USP7_PRKCB-DOCK_HTVS_1-001Baricitinib-6.85982-6.85982-41.7277
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-6.414569999999999-6.59687-50.5344
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-6.414569999999999-6.59687-50.5344
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-6.41317-6.59687-50.5344
546_USP7_PRKCB-DOCK_HTVS_1-001Lapatinib-6.2001800000000005-6.2889800000000005-58.3708
546_USP7_PRKCB-DOCK_HTVS_1-001Binimetinib-6.15665-6.16535-53.1595
546_USP7_PRKCB-DOCK_HTVS_1-001Binimetinib-6.15665-6.16535-53.1595
546_USP7_PRKCB-DOCK_HTVS_1-001Selumetinib-6.10584-6.11454-55.4153
546_USP7_PRKCB-DOCK_HTVS_1-001Selumetinib-6.10584-6.11454-55.4153
546_USP7_PRKCB-DOCK_HTVS_1-001Neratinib-5.939-6.1249-56.6159
546_USP7_PRKCB-DOCK_HTVS_1-001Cabozantinib-5.914969999999999-5.959969999999999-47.3991
546_USP7_PRKCB-DOCK_HTVS_1-001Cabozantinib-5.914969999999999-5.959969999999999-47.3991
546_USP7_PRKCB-DOCK_HTVS_1-001Larotrectinib-5.89876-5.89876-44.8851
546_USP7_PRKCB-DOCK_HTVS_1-001Osimertinib-5.75093-5.75863-54.1605
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-5.7121699999999995-5.89447-52.1349
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-5.7121699999999995-5.89447-52.1349
546_USP7_PRKCB-DOCK_HTVS_1-001Afatinib-5.71077-5.89447-52.1349
546_USP7_PRKCB-DOCK_HTVS_1-001Pralsetinib-5.69971-5.7912099999999995-59.2513
546_USP7_PRKCB-DOCK_HTVS_1-001Tucatinib-5.6771199999999995-6.05232-49.0189
546_USP7_PRKCB-DOCK_HTVS_1-001Tucatinib-5.6771199999999995-6.05232-49.0189

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Kinase-Substrate Information of USP7_PRKCB


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
PRKCBP05771-2humanMAPTP10636-8S352DFKDrVQskIGsLDNTubulin-binding
PRKCBP05771-2humanITGB2P05107S745FEkEKLksQWNNDNPIntegrin_b_cyt
PRKCBP05771-2humanTRPV1Q8NER1T705WKLQRAItILDTEKS
PRKCBP05771-2humanDAB2P98082S24QAAPKAPsKKEKKKG
PRKCBP05771-2humanPRKCBP05771-2S660QsEFEGFsFVNsEFLPkinase_C
PRKCBP05771-2humanMAPTP10636-8S258PDLkNVKskIGstENTubulin-binding
PRKCBP05771-2humanPPARAQ07869S230VKARVILsGKASNNP
PRKCBP05771-2humanATF2P15336S121LAtPIIRsKIEEPSV
PRKCBP05771-2humanKIR3DL1P43629S415QRKITRPsQRPKtPP
PRKCBP05771-2humanEIF6P56537S235QPstIAtsMRDsLID
PRKCBP05771-2humanPTPN11Q06124S591GLMQQQksFR_____
PRKCBP05771-2humanGSK3BP49841S9SGRPRttsFAEsCkP
PRKCBP05771-2humanMYH9P35579S1916AMNREVssLkNkLRrMyosin_tail_1
PRKCBP05771-2humanRPS6KB2Q9UBS0S473PPSGTKKsKRGRGRP
PRKCBP05771-2humanITGB2P05107T758NPLFksAtttVMNPkIntegrin_b_cyt
PRKCBP05771-2humanTRPV6Q9H1D0S184LARRAsVsARAtGTAAnk_2
PRKCBP05771-2humanC5AR1P21730S334sVVREsKsFTRsTVD
PRKCBP05771-2humanNCF1P14598S320QRsRKRLsQDAYRRNNECFESHC
PRKCBP05771-2humanMFN1Q8IWA4S284QNRIFFVsAkEVLsA
PRKCBP05771-2humanEIF3AQ14152S1364RAEKDREsLRRtKNE
PRKCBP05771-2humanLMNB1P20700S405VtVsRAsssRsVRtt
PRKCBP05771-2humanSYT6Q5T7P8T418RLKKKKttIKKNTLNC2
PRKCBP05771-2humanMCUQ8NE86S92VISVRLPsRRERCQF
PRKCBP05771-2humanEIF4G1Q04637-8S1093FAPGGRLsWGKGSSG
PRKCBP05771-2humanMFN1Q8IWA4S290VsAkEVLsARKQKAQ
PRKCBP05771-2humanPTPN11Q06124S576CAEMREDsARVyENV
PRKCBP05771-2humanNCF1P14598S315AHsIHQRsRKRLsQDNECFESHC
PRKCBP05771-2humanTRPV6Q9H1D0T728MPSVSRstSRssANW
PRKCBP05771-2humanRAB11AP62491S177TEIYRIVsQkQMSDR
PRKCBP05771-2humanPPARAQ07869S179RFGRMPRsEKAKLkA
PRKCBP05771-2humanNCF1P14598S328QDAYRRNsVRFLQQRNECFESHC
PRKCBP05771-2humanMAPTP10636-8S324kVTskCGsLGNIHHkTubulin-binding
PRKCBP05771-2humanTP73O15350S388VPQPLVDsYRQQQQL
PRKCBP05771-2humanCHATP28329-3S476HKAAVPAsEKLLLLKCarn_acyltransf
PRKCBP05771-2humanLMNB1P20700S395LkLsPsPssRVtVsR
PRKCBP05771-2humanCHATP28329-3S346LLKHVTQssRKLIRACarn_acyltransf
PRKCBP05771-2humanCHATP28329-3S440VPTYESAsIRRFQEGCarn_acyltransf
PRKCBP05771-2humanFUSP35637S257GrGGMGGsDrGGFNk
PRKCBP05771-2humanSYT6Q5T7P8T417RRLKKKKttIKKNTLC2
PRKCBP05771-2humanCHATP28329-3S347LKHVTQssRKLIRADCarn_acyltransf
PRKCBP05771-2humanCHATP28329-3T255TVLVKDStNRDSLDMCarn_acyltransf
PRKCBP05771-2humanNCF1P14598S370PAVPPRPsADLILNRp47_phox_C
PRKCBP05771-2humanNCF1P14598S303RGAPPRRssIRNAHsNECFESHC
PRKCBP05771-2humanGHRLQ9UBU3S41RVQQRKEsKKPPAKLMotilin_ghrelin
PRKCBP05771-2humanMAPTP10636-8S293NVQskCGsKDNIkHVTubulin-binding
PRKCBP05771-2humanKCNE1P15382S102VQARVLEsYRSCYVVISK_Channel
PRKCBP05771-2humanNCF1P14598S359EERQtQRsKPQPAVPp47_phox_C
PRKCBP05771-2humanNCF1P14598S304GAPPRRssIRNAHsINECFESHC
PRKCBP05771-2humanMFN1Q8IWA4S86AFFGRTSsGKSSVINDynamin_N
PRKCBP05771-2humanGSK3AP49840S21sGrARtssFAEPGGG
PRKCBP05771-2humanNCF1P14598S379DLILNRCsEstKRKLp47_phox_C
PRKCBP05771-2humanSYT6Q5T7P8T283DRKCKLQtRVHRKTLC2
PRKCBP05771humanANXA1P04083S28yVQtVksskGGPGsA
PRKCBP05771humanMAPTP10636-8S352DFKDrVQskIGsLDNTubulin-binding
PRKCBP05771humanITGB2P05107S745FEkEKLksQWNNDNPIntegrin_b_cyt
PRKCBP05771humanPRKCBP05771-2S660QsEFEGFsFVNsEFLPkinase_C
PRKCBP05771humanPTPN11Q06124S591GLMQQQksFR_____
PRKCBP05771humanMYH9P35579S1916AMNREVssLkNkLRrMyosin_tail_1
PRKCBP05771humanANXA2P07355S26tPPsAyGsVkAytNF
PRKCBP05771humanLIN28BQ6ZN17S243EQSKkGPsVQKRKKT
PRKCBP05771humanORAI1Q96D31S27GGSTTsGsRRsRRRs
PRKCBP05771humanKCNC4Q03721S9ISSVCVssYRGRKsGPotassium_chann
PRKCBP05771humanITGB2P05107T758NPLFksAtttVMNPkIntegrin_b_cyt
PRKCBP05771humanPIK3CGP48736S582LWHFRYEsLKHPKAYPI3Ka
PRKCBP05771humanAKT1P31749S473RPHFPQFsysAsGtAPkinase_C
PRKCBP05771humanNCF1P14598S320QRsRKRLsQDAYRRNNECFESHC
PRKCBP05771humanIBTKQ9P2D0S1200ASSLHsVsSksFRDF
PRKCBP05771humanEPHA2P29317S892ADFDPRVsIRLPsts
PRKCBP05771humanKCNC4Q03721S21KsGNKPPsKTCLKEEPotassium_chann
PRKCBP05771humanPRKAA1Q13131S496AtPQRsGsVsNyRSCAdenylateSensor
PRKCBP05771humanPTPN11Q06124S576CAEMREDsARVyENV
PRKCBP05771humanNOX5Q96PH1-4T494KRLsRSVtMRKsQRSFAD_binding_8
PRKCBP05771humanEPB41P11171-4S312QAQTRQAsALIDRPAFA
PRKCBP05771humanSTMN1P16949S25QAFELILsPrskEsVStathmin
PRKCBP05771humanTYRP14679S527DYHsLYQsHL_____
PRKCBP05771humanMAPTP10636-8S324kVTskCGsLGNIHHkTubulin-binding
PRKCBP05771humanMARCKSP29966S163KRFsFkKsFkLsGFsMARCKS
PRKCBP05771humanCHATP28329-3S440VPTYESAsIRRFQEGCarn_acyltransf
PRKCBP05771humanSTMN1P16949S38sVPEFPLsPPkKkDLStathmin
PRKCBP05771humanMSX2P35548T135HMsPTTCtLRKHKtN
PRKCBP05771humanCHATP28329-3S347LKHVTQssRKLIRADCarn_acyltransf
PRKCBP05771humanCHATP28329-3T255TVLVKDStNRDSLDMCarn_acyltransf
PRKCBP05771humanTYRP14679S523MEKEDYHsLYQsHL_
PRKCBP05771humanMAPTP10636-8S293NVQskCGsKDNIkHVTubulin-binding
PRKCBP05771humanNCF1P14598S304GAPPRRssIRNAHsINECFESHC
PRKCBP05771humanSHC1P29353T206VPGAkGAtRRRKPCsPID
PRKCBP05771humanGSK3AP49840S21sGrARtssFAEPGGG
PRKCBP05771humanIBTKQ9P2D0S1203LHsVsSksFRDFLLE
PRKCBP05771humanTRPM8Q7Z2W7S1040CKEKNMEssVCCFKN
PRKCBP05771humanMARCKSP29966S159kkKKKRFsFkKsFkLMARCKS
PRKCBP05771humanNOX5Q96PH1-4S498RSVtMRKsQRSsKGSFAD_binding_8
PRKCBP05771humanGRNP28799S81IFTVSGTsSCCPFPEGranulin
PRKCBP05771humanSHC1P29353S213tRRRKPCsRPLSSILPID
PRKCBP05771humanMAPTP10636-8S258PDLkNVKskIGstENTubulin-binding
PRKCBP05771humanKCNC4Q03721S8MISSVCVssYRGRKsPotassium_chann
PRKCBP05771humanATF2P15336S121LAtPIIRsKIEEPSV
PRKCBP05771humanGSK3BP49841S9SGRPRttsFAEsCkP
PRKCBP05771humanOCLNQ16625S490RLKQVkGsADYKSKKOccludin_ELL
PRKCBP05771humanRPS6KB2Q9UBS0S473PPSGTKKsKRGRGRP
PRKCBP05771humanORAI1Q96D31S30TTsGsRRsRRRsGDG
PRKCBP05771humanMSX2P35548T141CtLRKHKtNRKPRTP
PRKCBP05771humanCFLARO15519-2S193LQAAIQKsLKDPSNN
PRKCBP05771humanC5AR1P21730S334sVVREsKsFTRsTVD
PRKCBP05771humanKCNC4Q03721S15ssYRGRKsGNKPPsKPotassium_chann
PRKCBP05771humanCLDN1O95832T191CSCPRkTtsYPtPRP
PRKCBP05771humanKLHL3Q9UH77S433PMNTRRSsVGVGVVEKelch_1
PRKCBP05771humanIRS1P35568S323MVGGKPGsFRVRAss
PRKCBP05771humanSHC1P29353S139EEWTRHGsFVNkPtR
PRKCBP05771humanNCF1P14598S315AHsIHQRsRKRLsQDNECFESHC
PRKCBP05771humanCFLARO15519S193LQAAIQksLkDPSNN
PRKCBP05771humanTRPM8Q7Z2W7S1041KEKNMEssVCCFKNE
PRKCBP05771humanNCF1P14598S328QDAYRRNsVRFLQQRNECFESHC
PRKCBP05771humanCHATP28329-3S476HKAAVPAsEKLLLLKCarn_acyltransf
PRKCBP05771humanCHATP28329-3S346LLKHVTQssRKLIRACarn_acyltransf
PRKCBP05771humanILF3Q12906S647rGrGRGGsIRGRGRG
PRKCBP05771humanH3C1P68431T6__ArtkQtArkstGGHistone
PRKCBP05771humanFCER1GP30273S69DGVytGLstRNQEtyITAM
PRKCBP05771humanIRS1P35568S441SPCDFRSsFRsVtPD
PRKCBP05771humanACSL4O60488T328LAHVLELtAEISCFTAMP-binding
PRKCBP05771humanAKT1P31749T308kDGAtMKtFCGtPEyPkinase


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
PRKCBIDDescription0.00e+00
PRKCBGO:0043434response to peptide hormone6.72e-08
PRKCBGO:1903829positive regulation of protein localization1.29e-07
PRKCBGO:0032868response to insulin3.59e-07
PRKCBGO:0008286insulin receptor signaling pathway2.13e-06
PRKCBGO:0097284hepatocyte apoptotic process2.13e-06
PRKCBGO:0032869cellular response to insulin stimulus4.55e-06
PRKCBGO:0046879hormone secretion8.73e-06
PRKCBGO:0071375cellular response to peptide hormone stimulus8.73e-06
PRKCBGO:0009914hormone transport1.02e-05
PRKCBGO:0002790peptide secretion1.27e-05
PRKCBGO:0046883regulation of hormone secretion1.37e-05
PRKCBGO:0015833peptide transport1.81e-05
PRKCBGO:0010827regulation of glucose transmembrane transport2.50e-05
PRKCBGO:0030073insulin secretion2.60e-05
PRKCBGO:1901653cellular response to peptide2.70e-05
PRKCBGO:0023061signal release2.82e-05
PRKCBGO:1903532positive regulation of secretion by cell2.82e-05
PRKCBGO:0043467regulation of generation of precursor metabolites and energy2.82e-05
PRKCBGO:0046887positive regulation of hormone secretion2.95e-05
PRKCBGO:0045834positive regulation of lipid metabolic process3.39e-05
PRKCBGO:1903828negative regulation of protein localization3.49e-05
PRKCBGO:0051222positive regulation of protein transport3.89e-05
PRKCBGO:0051047positive regulation of secretion3.90e-05
PRKCBGO:0001774microglial cell activation3.90e-05
PRKCBGO:0042060wound healing4.85e-05
PRKCBGO:0002269leukocyte activation involved in inflammatory response4.85e-05
PRKCBGO:1904951positive regulation of establishment of protein localization4.85e-05
PRKCBGO:0002274myeloid leukocyte activation5.41e-05
PRKCBGO:0030072peptide hormone secretion5.41e-05
PRKCBGO:0050796regulation of insulin secretion5.43e-05
PRKCBGO:0032386regulation of intracellular transport5.72e-05
PRKCBGO:0006816calcium ion transport6.04e-05
PRKCBGO:0061900glial cell activation6.04e-05
PRKCBGO:0019216regulation of lipid metabolic process6.04e-05
PRKCBGO:0006887exocytosis6.94e-05
PRKCBGO:0035265organ growth7.07e-05
PRKCBGO:0046324regulation of glucose import7.07e-05
PRKCBGO:0042886amide transport7.20e-05
PRKCBGO:0050994regulation of lipid catabolic process7.28e-05
PRKCBGO:0051098regulation of binding7.36e-05
PRKCBGO:1904659glucose transmembrane transport8.83e-05
PRKCBGO:0006109regulation of carbohydrate metabolic process9.31e-05
PRKCBGO:0008645hexose transmembrane transport9.76e-05
PRKCBGO:0015749monosaccharide transmembrane transport1.10e-04
PRKCBGO:0090276regulation of peptide hormone secretion1.11e-04
PRKCBGO:0046626regulation of insulin receptor signaling pathway1.15e-04
PRKCBGO:0002791regulation of peptide secretion1.17e-04
PRKCBGO:0005979regulation of glycogen biosynthetic process1.17e-04
PRKCBGO:0010962regulation of glucan biosynthetic process1.17e-04

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Related Drugs to USP7_PRKCB


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 USP7-PRKCB 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 USP7_PRKCB


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