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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:LMNA_RAF1

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: LMNA_RAF1
KinaseFusionDB ID: KFG3176
FusionGDB2.0 ID: KFG3176
HgeneTgene
Gene symbol

LMNA

RAF1

Gene ID

4000

6037

Gene namelamin A/C
SynonymsCDCD1|CDDC|CMD1A|CMT2B1|EMD2|FPL|FPLD|FPLD2|HGPS|IDC|LDP1|LFP|LGMD1B|LMN1|LMNC|LMNL1|MADA|PRO1
Cytomap

1q22

Type of geneprotein-coding
Descriptionlamin70 kDa laminepididymis secretory sperm binding proteinlamin A/C-like 1lamin Cmandibuloacral dysplasia type Aprelamin-A/Cprogerinrenal carcinoma antigen NY-REN-32
Modification date20240411
UniProtAcc

P02545

P04049

Ensembl transtripts involved in fusion geneENST idsENST00000496738, ENST00000361308, 
ENST00000368297, ENST00000368301, 
ENST00000392353, ENST00000368299, 
ENST00000368300, ENST00000448611, 
ENST00000473598, ENST00000347559, 
ENST00000251849, ENST00000442415, 
ENST00000534997, ENST00000542177, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: LMNA [Title/Abstract] AND RAF1 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)LMNA(156107534)-RAF1(12641914), # samples:2
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgeneLMNA

GO:0006998

nuclear envelope organization

2188730|24741066|37788673|37832547

HgeneLMNA

GO:0090398

cellular senescence

20458013

HgeneLMNA

GO:1990683

DNA double-strand break attachment to nuclear envelope

31548606


check buttonKinase Fusion gene breakpoints across LMNA (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 RAF1 (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-EB-A5SF-01ALMNAchr1

156107534

RAF1chr3

12641914



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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)
ENST00000368300ENST00000251849LMNAchr1156107534RAF1chr3126419143936979

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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

>ENST00000368300_ENST00000251849_LMNA_chr1_156107534_RAF1_chr3_12641914_length(amino acids)=979
MPGASREPAGRRTPTPSSLCPSTRAPRPFRDPCPAGSAANLPAMETPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYID
RVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDL
EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLV
EIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKE
AKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSS
QTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTI
WAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHDAIRSHSESASPSALSSSPNN
LSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQA
FRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG
LTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPD

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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/chr1:156107534/chr3:12641914)
- 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
LMNA

P02545

RAF1

P04049

FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:23666920, PubMed:18611980). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:31548606}.; FUNCTION: Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence. {ECO:0000269|PubMed:20458013}.FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation. {ECO:0000269|PubMed:11427728, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:15618521, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:16924233, ECO:0000269|PubMed:9360956}.

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
TgeneLMNA156107534RAF112641914ENST00000368300617349_609278649DomainNote=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159
TgeneLMNA156107534RAF112641914ENST00000368300718349_609298669DomainNote=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 >>>284_LMNA_RAF1ENST00000368300ENST00000251849LMNAchr1156107534RAF1chr312641914
MPGASREPAGRRTPTPSSLCPSTRAPRPFRDPCPAGSAANLPAMETPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYID
RVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDL
EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLV
EIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKE
AKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSS
QTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTI
WAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHDAIRSHSESASPSALSSSPNN
LSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQA
FRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG
LTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPD
979
3D view using mol* of 284_LMNA_RAF1
PDB file >>>TKFP_498_LMNA_RAF1ENST00000368300ENST00000251849LMNAchr1156107534RAF1chr312641914
MPGASREPAGRRTPTPSSLCPSTRAPRPFRDPCPAGSAANLPAMETPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYID
RVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDL
EALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLV
EIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKE
AKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSS
QTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTI
WAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHDAIRSHSESASPSALSSSPNN
LSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQA
FRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG
LTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPD
979_LMNA_RAF1


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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

LMNA_RAF1 does not have any known PDB structures.

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pLDDT score distribution

check button pLDDT score distribution of the predicted fusion protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
* The blue color at the bottom marks the best active site residues.


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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.

284_LMNA_RAF1_ramachandran.png
all structure LMNA-RAF1

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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

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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

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Kinase-Substrate Information of LMNA_RAF1


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
RAF1P04049humanRAF1P04049S621PKINRsAsEPsLHRA
RAF1P04049humanKLF10Q13118T93TIPAFCLtPPYsPSD
RAF1P04049humanBADQ92934S75EIRsRHssyPAGtEDBcl-2_BAD
RAF1P04049humanBADQ92934S118GRELRRMsDEFVDsFBcl-2_BAD
RAF1P04049humanMAP2K1Q02750S222LIDsMANsFVGtRSYPkinase
RAF1P04049humanRAF1P04049S359StRIGsGsFGtVYkGPK_Tyr_Ser-Thr
RAF1P04049humanEEF1A2Q05639S21GHVDSGkstttGHLIGTP_EFTU
RAF1P04049humanMAP2K1Q02750S218VsGQLIDsMANsFVGPkinase
RAF1P04049humanRAF1P04049S259sQRQRststPNVHMV
RAF1P04049humanMYCP01106T23MPLNVsFtNRNyDLDMyc_N
RAF1P04049humanRAF1P04049S338RPRGQRDssyyWEIE
RAF1P04049humanBADQ92934S99PFrGrsRsAPPNLWABcl-2_BAD
RAF1P04049humanPPP1R12AO14974T696ARQsRRstQGVtLtD


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
RAF1IDDescription0.00e+00
RAF1GO:0044342type B pancreatic cell proliferation4.58e-05
RAF1GO:0035019somatic stem cell population maintenance3.64e-04
RAF1GO:0051347positive regulation of transferase activity1.14e-03
RAF1GO:0035270endocrine system development1.22e-03
RAF1GO:0050673epithelial cell proliferation1.22e-03
RAF1GO:0043281regulation of cysteine-type endopeptidase activity involved in apoptotic process1.62e-03
RAF1GO:0019827stem cell population maintenance1.83e-03
RAF1GO:0098727maintenance of cell number1.83e-03
RAF1GO:2000116regulation of cysteine-type endopeptidase activity1.84e-03
RAF1GO:0030878thyroid gland development2.45e-03
RAF1GO:0052548regulation of endopeptidase activity4.55e-03
RAF1GO:0048538thymus development4.55e-03
RAF1GO:0052547regulation of peptidase activity4.55e-03
RAF1GO:0048009insulin-like growth factor receptor signaling pathway4.55e-03
RAF1GO:0060324face development4.55e-03
RAF1GO:1902105regulation of leukocyte differentiation4.55e-03
RAF1GO:0033674positive regulation of kinase activity4.95e-03
RAF1GO:0035773insulin secretion involved in cellular response to glucose stimulus5.56e-03
RAF1GO:2001244positive regulation of intrinsic apoptotic signaling pathway5.56e-03
RAF1GO:2001233regulation of apoptotic signaling pathway6.87e-03
RAF1GO:1903706regulation of hemopoiesis7.50e-03
RAF1GO:0010720positive regulation of cell development8.29e-03
RAF1GO:0008625extrinsic apoptotic signaling pathway via death domain receptors8.29e-03
RAF1GO:0048534hematopoietic or lymphoid organ development1.03e-02
RAF1GO:0043280positive regulation of cysteine-type endopeptidase activity involved in apoptotic process1.27e-02
RAF1GO:0002761regulation of myeloid leukocyte differentiation1.52e-02
RAF1GO:2001056positive regulation of cysteine-type endopeptidase activity1.58e-02
RAF1GO:0071333cellular response to glucose stimulus1.68e-02
RAF1GO:0071331cellular response to hexose stimulus1.68e-02
RAF1GO:0071326cellular response to monosaccharide stimulus1.68e-02
RAF1GO:2001235positive regulation of apoptotic signaling pathway1.73e-02
RAF1GO:0071456cellular response to hypoxia1.73e-02
RAF1GO:0071322cellular response to carbohydrate stimulus1.77e-02
RAF1GO:0010950positive regulation of endopeptidase activity1.78e-02
RAF1GO:0001678intracellular glucose homeostasis1.78e-02
RAF1GO:0036294cellular response to decreased oxygen levels1.78e-02
RAF1GO:0010952positive regulation of peptidase activity2.00e-02
RAF1GO:0071453cellular response to oxygen levels2.03e-02
RAF1GO:1902107positive regulation of leukocyte differentiation2.10e-02
RAF1GO:1903708positive regulation of hemopoiesis2.10e-02
RAF1GO:0032872regulation of stress-activated MAPK cascade2.10e-02
RAF1GO:0070302regulation of stress-activated protein kinase signaling cascade2.10e-02
RAF1GO:2001242regulation of intrinsic apoptotic signaling pathway2.10e-02
RAF1GO:0071466cellular response to xenobiotic stimulus2.10e-02
RAF1GO:0009749response to glucose2.10e-02
RAF1GO:0009746response to hexose2.10e-02
RAF1GO:0002520immune system development2.10e-02
RAF1GO:0030073insulin secretion2.10e-02
RAF1GO:0034284response to monosaccharide2.20e-02

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Related Drugs to LMNA_RAF1


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 LMNA-RAF1 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 LMNA_RAF1


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
TgeneRAF1C0028326Noonan Syndrome10CLINGEN;CTD_human;GENOMICS_ENGLAND;ORPHANET
TgeneRAF1C0175704LEOPARD Syndrome7CLINGEN;CTD_human;GENOMICS_ENGLAND
TgeneRAF1C1969057Noonan Syndrome 54CTD_human;GENOMICS_ENGLAND;UNIPROT
TgeneRAF1C1969056LEOPARD SYNDROME 23CTD_human;GENOMICS_ENGLAND;UNIPROT
TgeneRAF1C0007194Hypertrophic Cardiomyopathy2CTD_human
TgeneRAF1C0041409Turner Syndrome, Male2CTD_human
TgeneRAF1C1519086Pilomyxoid astrocytoma2ORPHANET
TgeneRAF1C1527404Female Pseudo-Turner Syndrome2CTD_human
TgeneRAF1C4551472Hypertrophic obstructive cardiomyopathy2CTD_human
TgeneRAF1C4551602Noonan Syndrome 12CTD_human


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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