UTHEALTH HOME    ABOUT SBMI    A-Z    WEBMAIL    INSIDE THE UNIVERSITY
FusionGDB Logo

Home

Download

Statistics

Examples

Help

Contact

Terms of Use
Center for Computational Systems Medicine
leaf

Kinase Fusion Gene Summary

leaf

Kinase Fusion Gene Sample Information

leaf

Kinase Fusion ORF Analysis

leaf

Kinase Fusion Amino Acid Sequences

leaf

Multiple Sequence Alignment of All Fusion Protein Isoforms

leaf

Kinase Fusion Protein Functional Features

leaf

Kinase Fusion Protein Structures

leaf

Comparison of Fusion Protein Isoforms

leaf

Comparison of Fusion Protein Sequences/Structures with Known Sequences/Structures from PDB

leaf

pLDDT Scores and Difference Analysis of pLDDT Scores Between the Active Sites (Best) and Non-Active Sites.

leaf

Ramachandran Plot of Kinase Fusion Protein Structure

leaf

Potential Active Site Information

leaf

Virtual Screening Results

leaf

Kinase-Substrate Information

leaf

Related Drugs with This Kinase Fusion Protein

leaf

Related Disease with This Kinase Fusion Protein

leaf

Clinical Trials of the Found Drugs/Small Molecules

Kinase Fusion Gene:ANP32B_PRKG1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: ANP32B_PRKG1
KinaseFusionDB ID: KFG370
FusionGDB2.0 ID: KFG370
HgeneTgene
Gene symbol

ANP32B

PRKG1

Gene ID

10541

5592

Gene nameacidic nuclear phosphoprotein 32 family member Bprotein kinase cGMP-dependent 1
SynonymsAPRIL|PHAPI2|SSP29AAT8|PKG|PKG1|PRKG1B|PRKGR1B|cGK|cGK 1|cGK1|cGKI|cGKI-BETA|cGKI-alpha
Cytomap

9q22.33

10q11.23-q21.1

Type of geneprotein-codingprotein-coding
Descriptionacidic leucine-rich nuclear phosphoprotein 32 family member Bacidic (leucine-rich) nuclear phosphoprotein 32 family, member Bacidic protein rich in leucinesputative HLA-DR-associated protein I-2silver-stainable protein SSP29cGMP-dependent protein kinase 1protein kinase, cGMP-dependent, regulatory, type I, betaprotein kinase, cGMP-dependent, type I
Modification date2024031020240411
UniProtAcc

Q92688

Q13976

Ensembl transtripts involved in fusion geneENST idsENST00000339399, ENST00000473205, 
ENST00000373975, ENST00000373980, 
ENST00000373985, ENST00000401604, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: ANP32B [Title/Abstract] AND PRKG1 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)ANP32B(100745891)-PRKG1(53814244), # 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
HgeneANP32B

GO:0006334

nucleosome assembly

20538007

HgeneANP32B

GO:0045596

negative regulation of cell differentiation

22705300

TgenePRKG1

GO:0006468

protein phosphorylation

15905169

TgenePRKG1

GO:1904706

negative regulation of vascular associated smooth muscle cell proliferation

25447536

TgenePRKG1

GO:1904753

negative regulation of vascular associated smooth muscle cell migration

25447536


check buttonKinase Fusion gene breakpoints across ANP32B (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 PRKG1 (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
all structure


Top

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-13-0720-01AANP32Bchr9

100745891

PRKG1chr10

53814244



Top

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)
ENST00000339399ENST00000401604ANP32Bchr9100745891PRKG1chr10538142443162501

Top

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

>ENST00000339399_ENST00000401604_ANP32B_chr9_100745891_PRKG1_chr10_53814244_length(amino acids)=501
MPARRPPPRTAPPASAASKPFRRPSLRKPGRLSPLRPRRGKLSLKRGEEGNMDMKRRIHLELRNRTPAATHYENGEYIIRQGARGDTFFI
ISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAA
FFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEA
CLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEII
LNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFE

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

Multiple Sequence Alignment of All Fusion Protein Isoforms



Top

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/chr9:100745891/chr10:53814244)
- 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
ANP32B

Q92688

PRKG1

Q13976

FUNCTION: Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription (PubMed:20015864, PubMed:18039846). Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis (PubMed:20015864). Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes (PubMed:20538007, PubMed:18039846). Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1 (PubMed:17178712). Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity). {ECO:0000250|UniProtKB:Q9EST5, ECO:0000269|PubMed:17178712, ECO:0000269|PubMed:18039846, ECO:0000269|PubMed:20015864, ECO:0000269|PubMed:20538007}.; FUNCTION: (Microbial infection) Plays an essential role in influenza A and B viral genome replication (PubMed:33045004, PubMed:31217244). Also plays a role in foamy virus mRNA export from the nucleus to the cytoplasm (PubMed:21159877). {ECO:0000269|PubMed:21159877, ECO:0000269|PubMed:31217244, ECO:0000269|PubMed:33045004}.FUNCTION: Serine/threonine protein kinase that acts as a key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates IRAG1 and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle. {ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11162591, ECO:0000269|PubMed:11723116, ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:14608379, ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:16990611, ECO:0000269|PubMed:8182057}.

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
TgeneANP32B100745891PRKG153814244ENST00000339399418620_671239672DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneANP32B100745891PRKG153814244ENST00000339399418620_671254687DomainNote=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618
TgeneANP32B100745891PRKG153814244ENST00000339399418360_619239672DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneANP32B100745891PRKG153814244ENST00000339399418360_619254687DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159


Top

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 >>>25_ANP32B_PRKG1ENST00000339399ENST00000401604ANP32Bchr9100745891PRKG1chr1053814244
MPARRPPPRTAPPASAASKPFRRPSLRKPGRLSPLRPRRGKLSLKRGEEGNMDMKRRIHLELRNRTPAATHYENGEYIIRQGARGDTFFI
ISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAA
FFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEA
CLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEII
LNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFE
501
3D view using mol* of 25_ANP32B_PRKG1
PDB file >>>TKFP_40_ANP32B_PRKG1ENST00000339399ENST00000401604ANP32Bchr9100745891PRKG1chr1053814244
MPARRPPPRTAPPASAASKPFRRPSLRKPGRLSPLRPRRGKLSLKRGEEGNMDMKRRIHLELRNRTPAATHYENGEYIIRQGARGDTFFI
ISKGTVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAA
FFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEA
CLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEII
LNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFE
501_ANP32B_PRKG1


Top

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

Top

Comparison of Fusion Protein Sequences/Structures with Known Sequences/Structures from PDB

ANP32B_PRKG1 does not have any known PDB structures.

Top

pLDDT score distribution

all_data/KinaseFusionDB_T_Results/KinaseFusionDB_T_ViolinPlots/25_ANP32B_PRKG1.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.
25_ANP32B_PRKG1.png
all structure sitemap plddt3 25_ANP32B_PRKG1.png
25_ANP32B_PRKG1.png
all structure sitemap plddt4 25_ANP32B_PRKG1.png


Top

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

Top

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.

25_ANP32B_PRKG1_ramachandran.png
all structure ANP32B-PRKG1

Top

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 ANP32B-PRKG1

Top

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
25_ANP32B_PRKG1-DOCK_HTVS_1-001Sunitinib-7.29282-7.29702-43.6323
25_ANP32B_PRKG1-DOCK_HTVS_1-001Abrocitinib-6.33824-6.34934-37.5673
25_ANP32B_PRKG1-DOCK_HTVS_1-001Abrocitinib-6.33824-6.34934-37.5673
25_ANP32B_PRKG1-DOCK_HTVS_1-001Crizotinib-6.3275-6.8234-46.2289
25_ANP32B_PRKG1-DOCK_HTVS_1-001Crizotinib-6.3275-6.8234-46.2289
25_ANP32B_PRKG1-DOCK_HTVS_1-001Netarsudil-6.0894-6.1005-7.830369999999999
25_ANP32B_PRKG1-DOCK_HTVS_1-001Netarsudil-6.0894-6.1005-7.830369999999999
25_ANP32B_PRKG1-DOCK_HTVS_1-001Netarsudil-5.86908-5.88018-50.6219
25_ANP32B_PRKG1-DOCK_HTVS_1-001Netarsudil-5.86908-5.88018-50.6219
25_ANP32B_PRKG1-DOCK_HTVS_1-001Sunitinib-5.827459999999999-5.83166-41.928999999999995
25_ANP32B_PRKG1-DOCK_HTVS_1-001Asciminib-5.76805-6.13115-25.0666
25_ANP32B_PRKG1-DOCK_HTVS_1-001Afatinib-5.6507-5.832999999999999-40.7201
25_ANP32B_PRKG1-DOCK_HTVS_1-001Afatinib-5.6507-5.832999999999999-40.7201
25_ANP32B_PRKG1-DOCK_HTVS_1-001Afatinib-5.6493-5.832999999999999-40.7201
25_ANP32B_PRKG1-DOCK_HTVS_1-001Crizotinib-5.55661-5.89281-46.2839
25_ANP32B_PRKG1-DOCK_HTVS_1-001Crizotinib-5.55661-5.89281-46.2839
25_ANP32B_PRKG1-DOCK_HTVS_1-001Tofacitinib-5.4407-5.4522-17.2654
25_ANP32B_PRKG1-DOCK_HTVS_1-001Tofacitinib-5.4407-5.4522-17.2654
25_ANP32B_PRKG1-DOCK_HTVS_1-001Upadacitinib-5.3943-5.3953-28.074
25_ANP32B_PRKG1-DOCK_HTVS_1-001Crizotinib-5.32501-5.66121-23.5325

Top

Kinase-Substrate Information of ANP32B_PRKG1


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
PRKG1Q13976-2humanHSPB1P04792T143RCFtRkytLPPGVDPHSP20
PRKG1Q13976-2humanHSPB1P04792S15FsLLrGPsWDPFrDW
PRKG1Q13976-2humanPRKG1Q13976-2S65TQQAQKQsASTLQGE
PRKG1Q13976-2humanHSPB1P04792S82RALsRQLssGVsEIr
PRKG1Q13976-2humanHSPB1P04792S78PAysRALsRQLssGV
PRKG1Q13976-2humanPRKG1Q13976-2S81RtKRQAIsAEPTAFD
PRKG1Q13976-2humanPAK1Q13153S21APPMRNtsTMIGAGs
PRKG1Q13976-2humanLASP1Q14847S146MEPERRDsQDGssyR
PRKG1Q13976humanGATA4P43694S262IkPQRRLsAsRRVGL
PRKG1Q13976humanPRKAR1AP10644S101RRRRGAIsAEVYTEE
PRKG1Q13976humanSRFP11831T159DNkLRRYtTFsKRkTSRF-TF
PRKG1Q13976humanVASPP50552T278LARRRKAtQVGEktP
PRKG1Q13976humanTBXA2RP21731-2T332TRPRRsLtLWPSLEY
PRKG1Q13976humanCBSP35520S227LDQYRNAsNPLAHYDPALP
PRKG1Q13976humanTRPC6Q9Y210T70RLAHRRQtVLREKGR
PRKG1Q13976humanHRH1P35367S398WKRLRsHsRQyVSGL7tm_1
PRKG1Q13976humanRGS18Q9NS28S216PTNLRRRsRsFTCNE
PRKG1Q13976humanTBXA2RP21731-2S330LSTRPRRsLtLWPSL
PRKG1Q13976humanENSAO43768S109DLPQRkssLVtskLAEndosulfine
PRKG1Q13976humanFHOD1Q9Y613S1131AARERKRsRGNRKsL
PRKG1Q13976humanGTF2IP78347S784GVPFRRPstFGIPRLGTF2I
PRKG1Q13976humanORAI1Q96D31S34sRRsRRRsGDGEPPG
PRKG1Q13976humanPPP1R14AQ96A00T38QkRHARVtVkYDRREPP1_inhibitor
PRKG1Q13976humanTRPC3Q13507-3T11SPSLRRMtVMREKGR
PRKG1Q13976humanRAP1GAP2Q684P5S7_MFGRKRsVsFGGFG
PRKG1Q13976humanSTMN1P16949S63AAEERRksHEAEVLkStathmin
PRKG1Q13976humanRGS2P41220S46kDWKTRLsYFLQNSS
PRKG1Q13976humanTTNQ8WZ42S4099sEQPGLFsEWLRNIE
PRKG1Q13976humanTBXA2RP21731S331sTRPRsLsLQPQLtQ
PRKG1Q13976humanPRKG1Q13976S65TtRAQGIsAEPQTYR
PRKG1Q13976humanGTF2IP78347S412GIPFRRPstYGIPRLGTF2I
PRKG1Q13976humanRGS2P41220S64kPKTGKKsKQQAFIk
PRKG1Q13976humanTRPC1P48995S206SAKNKKDsLRHSRFRTRP_2
PRKG1Q13976humanCCDC80Q76M96S434PQTTRRPsKATSLES
PRKG1Q13976humanHRH1P35367S396FTWKRLRsHsRQyVS7tm_1
PRKG1Q13976humanARPP19P56211S104DLPQRkPsLVAskLAEndosulfine
PRKG1Q13976humanCCDC80Q76M96S409VITARRPsVsENLYP
PRKG1Q13976humanPDE5AO76074S102GTPTRKIsAsEFDRP
PRKG1Q13976humanVASPP50552S239GAKLRKVsKQEEASG
PRKG1Q13976humanRAP1BP61224S179PGkARKKsscQLL__
PRKG1Q13976humanRHOAP61586S188ARRGKKKsGCLVL__
PRKG1Q13976humanLASP1Q14847S146MEPERRDsQDGssyR
PRKG1Q13976humanTRPC6Q9Y210S322KNDYKKLsMQCKDFV
PRKG1Q13976humanTTNQ8WZ42S4185IQQGAKtsLQEEMDs
PRKG1Q13976humanLIPEQ05469S853IAEPMRRsVsEAALA
PRKG1Q13976humanTSC2P49815S1364IPIERVVssEGGRPs
PRKG1Q13976humanTRPC1P48995T347SGYRRKPtCKKIMTV
PRKG1Q13976humanGTF2IP78347-2S743GVPFRRPstFGIPRLGTF2I
PRKG1Q13976humanSLC6A4P31645T276SIWKGVKtsGKVVWVSNF
PRKG1Q13976humanTTNQ8WZ42S4092ALQAAVAsEQPGLFs
PRKG1Q13976humanTRPC3Q13507S336KNDYRKLsMQCKDFV
PRKG1Q13976humanPTSQ03393S19AQVSRRIsFSASHRLPTPS
PRKG1Q13976humanCBSP35520S525YHSTGKSsQRQMVFG
PRKG1Q13976humanARHGEF6Q15052S684GSSTRkDsIPQVLLP
PRKG1Q13976humanTTNQ8WZ42S4010VRIEEGKsLRFPLAL
PRKG1Q13976humanVASPP50552S157EHIERRVsNAGGPPA
PRKG1Q13976humanTTNQ8WZ42S11878KEEVVLKsVLRKRPE
PRKG1Q13976humanGTF2IP78347-2S371GIPFRRPsTYGIPRLGTF2I


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
PRKG1IDDescription0.00e+00
PRKG1GO:0035296regulation of tube diameter3.05e-06
PRKG1GO:0097746blood vessel diameter maintenance3.05e-06
PRKG1GO:0035150regulation of tube size3.05e-06
PRKG1GO:0090257regulation of muscle system process3.50e-06
PRKG1GO:0006937regulation of muscle contraction4.78e-06
PRKG1GO:0003300cardiac muscle hypertrophy4.78e-06
PRKG1GO:0014897striated muscle hypertrophy4.83e-06
PRKG1GO:0014896muscle hypertrophy4.83e-06
PRKG1GO:0003012muscle system process9.44e-06
PRKG1GO:0031032actomyosin structure organization9.44e-06
PRKG1GO:0006940regulation of smooth muscle contraction9.44e-06
PRKG1GO:0006936muscle contraction1.76e-05
PRKG1GO:0007584response to nutrient3.10e-05
PRKG1GO:1903522regulation of blood circulation3.10e-05
PRKG1GO:0003018vascular process in circulatory system3.68e-05
PRKG1GO:0055013cardiac muscle cell development3.68e-05
PRKG1GO:0055006cardiac cell development4.85e-05
PRKG1GO:0042060wound healing4.85e-05
PRKG1GO:0055001muscle cell development8.42e-05
PRKG1GO:0006939smooth muscle contraction8.72e-05
PRKG1GO:0045933positive regulation of muscle contraction8.72e-05
PRKG1GO:0030038contractile actin filament bundle assembly8.72e-05
PRKG1GO:0043149stress fiber assembly8.72e-05
PRKG1GO:0055007cardiac muscle cell differentiation1.98e-04
PRKG1GO:0045936negative regulation of phosphate metabolic process2.10e-04
PRKG1GO:0010563negative regulation of phosphorus metabolic process2.10e-04
PRKG1GO:0048738cardiac muscle tissue development2.33e-04
PRKG1GO:0014706striated muscle tissue development3.29e-04
PRKG1GO:0045932negative regulation of muscle contraction4.28e-04
PRKG1GO:0051017actin filament bundle assembly4.33e-04
PRKG1GO:0060537muscle tissue development4.35e-04
PRKG1GO:0035051cardiocyte differentiation4.44e-04
PRKG1GO:0061572actin filament bundle organization4.44e-04
PRKG1GO:0042310vasoconstriction5.71e-04
PRKG1GO:0035265organ growth5.71e-04
PRKG1GO:0051146striated muscle cell differentiation5.71e-04
PRKG1GO:0007015actin filament organization5.71e-04
PRKG1GO:0055017cardiac muscle tissue growth6.71e-04
PRKG1GO:0003298physiological muscle hypertrophy6.71e-04
PRKG1GO:0003301physiological cardiac muscle hypertrophy6.71e-04
PRKG1GO:0045987positive regulation of smooth muscle contraction6.71e-04
PRKG1GO:0061049cell growth involved in cardiac muscle cell development6.71e-04
PRKG1GO:0031667response to nutrient levels7.29e-04
PRKG1GO:0051492regulation of stress fiber assembly7.29e-04
PRKG1GO:0045907positive regulation of vasoconstriction7.60e-04
PRKG1GO:0060562epithelial tube morphogenesis7.60e-04
PRKG1GO:0060419heart growth7.72e-04
PRKG1GO:0090075relaxation of muscle8.61e-04
PRKG1GO:0110020regulation of actomyosin structure organization1.01e-03

Top

Related Drugs to ANP32B_PRKG1


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 ANP32B-PRKG1 and kinase inhibitors the PubMed Abstract (04-01-2024)

Fusion gene - drug pair 1Fusion gene - drug pair 2PMIDPublication dateDOIStudy title

Top

Related Diseases to ANP32B_PRKG1


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


Top

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