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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:ROCK1_CABYR

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: ROCK1_CABYR
KinaseFusionDB ID: KFG5418
FusionGDB2.0 ID: KFG5418
HgeneTgene
Gene symbol

ROCK1

CABYR

Gene ID

6093

26256

Gene nameRho associated coiled-coil containing protein kinase 1calcium binding tyrosine phosphorylation regulated
SynonymsP160ROCK|ROCK-ICABYRa|CABYRc|CABYRc/d|CABYRe|CBP86|CT88|FSP-2|FSP2
Cytomap

18q11.1

18q11.2

Type of geneprotein-codingprotein-coding
Descriptionrho-associated protein kinase 1p160 ROCK-1renal carcinoma antigen NY-REN-35calcium-binding tyrosine phosphorylation-regulated proteincalcium binding tyrosine-(Y)-phosphorylation regulated (fibrousheathin 2)calcium-binding protein 86cancer/testis antigen 88fibrousheathin IIfibrousheathin-2testis tissue sperm-binding protein
Modification date2024030520240411
UniProtAcc

Q13464

O75952

Ensembl transtripts involved in fusion geneENST idsENST00000399799, ENST00000327201, 
ENST00000399481, ENST00000399499, 
ENST00000415309, ENST00000581397, 
ENST00000399496, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: ROCK1 [Title/Abstract] AND CABYR [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)ROCK1(18690779)-CABYR(21735665), # samples:3
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgeneROCK1

GO:0006468

protein phosphorylation

23093407

HgeneROCK1

GO:0007159

leukocyte cell-cell adhesion

12082081

HgeneROCK1

GO:0018105

peptidyl-serine phosphorylation

18573880

HgeneROCK1

GO:0022614

membrane to membrane docking

12082081

HgeneROCK1

GO:0030334

regulation of cell migration

23093407

HgeneROCK1

GO:0032091

negative regulation of protein binding

18573880

HgeneROCK1

GO:0032956

regulation of actin cytoskeleton organization

25911094

HgeneROCK1

GO:0050900

leukocyte migration

12082081

HgeneROCK1

GO:0050901

leukocyte tethering or rolling

12082081

HgeneROCK1

GO:0070507

regulation of microtubule cytoskeleton organization

23093407


check buttonKinase Fusion gene breakpoints across ROCK1 (5'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

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


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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-97-7552-01AROCK1chr18

18690779

CABYRchr18

21735665

ChimerDB4TCGA-97-7552ROCK1chr18

18690778

CABYRchr18

21735664



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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)

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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

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/:18690779/:21735665)
- 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
ROCK1

Q13464

CABYR

O75952

FUNCTION: Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579, PubMed:23093407, PubMed:23355470). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity). {ECO:0000250|UniProtKB:P70335, ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}.FUNCTION: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium.

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


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Kinase-Substrate Information of ROCK1_CABYR


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
ROCK1Q13464humanNOS3P29474T495TGITRKKtFKEVANA
ROCK1Q13464humanRDXP35241T564AGRDKyKtLRQIRQGERM_C
ROCK1Q13464humanSLC9A1P19634T653LRsYNRHtLVADPyENEXCaM_BD
ROCK1Q13464humanARHGAP35Q9NRY4T1173GRFASYRtsFsVGsDRhoGAP_pG1_pG2
ROCK1Q13464humanFHOD1Q9Y613S1137RsRGNRKsLRRtLKs
ROCK1Q13464humanARHGAP24Q8N264S391RsSMNNGsPtALSGs
ROCK1Q13464humanFHOD1Q9Y613T1141NRKsLRRtLKsGLGD
ROCK1Q13464humanEZRP15311T567QGRDkyKtLRQIRQGERM_C
ROCK1Q13464humanGFAPP14136S38LGPGTRLsLARMPPPFilament_head
ROCK1Q13464humanPTENP60484S229VkIYSsNsGPtRREDPTEN_C2
ROCK1Q13464humanARHGAP35Q9NRY4S1236PKPKPRPsITKATWERhoGAP_pG1_pG2
ROCK1Q13464humanDESP17661T17RVssYRRtFGGAPGFFilament_head
ROCK1Q13464humanAQP2P41181T269PQsLPRGtkA_____
ROCK1Q13464humanFHOD1Q9Y613S1131AARERKRsRGNRKsL
ROCK1Q13464humanPRMT5O14744T80LsGRDWNtLIVGkLSPRMT5_TIM
ROCK1Q13464humanRND3P61587S11RRAsQkLsSksIMDP
ROCK1Q13464humanMYL9P24844T19KKRPQRAtsNVFAMF
ROCK1Q13464humanDESP17661S60VyQVsRtsGGAGGLGFilament_head
ROCK1Q13464humanKCNK3O14649S336IPRDLStsDTCVEQS
ROCK1Q13464humanARHGAP24Q8N264T452GLEKTQTtPNGSLQA
ROCK1Q13464humanPFN1P07737S138MAsHLRRsQy_____Profilin
ROCK1Q13464humanRND3P61587S218QRATKRIsHMPsRPE
ROCK1Q13464humanH3C1P68431S10tkQtArkstGGkAPrHistone
ROCK1Q13464humanARHGAP24Q8N264S437SGIVTNGsFSSSNAE
ROCK1Q13464humanRND3P61587S7_MKERRAsQkLsSks
ROCK1Q13464humanLIMK2P53671T505NDRKKRYtVVGNPYWPK_Tyr_Ser-Thr
ROCK1Q13464humanARHGAP35Q9NRY4S1174RFASYRtsFsVGsDDRhoGAP_pG1_pG2
ROCK1Q13464humanH3C1P68431S28ATkAArksAPATGGVHistone
ROCK1Q13464humanVIMP08670S72ssAVrLrssVPGVRLFilament_head
ROCK1Q13464humanGFAPP14136S13ItsAArrsyVSsGEMFilament_head
ROCK1Q13464humanDESP17661T76LRAsRLGttRtPssyFilament_head
ROCK1Q13464humanPTK2Q05397S732SsEGFYPsPQHMVQT
ROCK1Q13464humanPAWRQ96IZ0T163LREKRRstGVVNIPA
ROCK1Q13464humanSOX9P48436S181YQPRRRKsVKNGQAE
ROCK1Q13464humanPPP1R12AO14974T853PREKRRstGVsFWtQ
ROCK1Q13464humanPPP1R12AO14974T696ARQsRRstQGVtLtD
ROCK1Q13464humanMAPK8IP3Q9UPT6S365RLDRtGssPTQGIVN
ROCK1Q13464humanSCRIBQ14160S1508WRAARMksLEQDALR
ROCK1Q13464humanMARCKSP29966S159kkKKKRFsFkKsFkLMARCKS
ROCK1Q13464humanRND3P61587S240LRKDKAKsCTVM___
ROCK1Q13464humanTPPPO94811S107FSKIKGKsCRTITFEp25-alpha
ROCK1Q13464humanGFAPP14136T7_MERRRItsAArrsyFilament_head
ROCK1Q13464humanARHGAP35Q9NRY4S1150LERGRKVsIVsKPVLRhoGAP_pG1_pG2
ROCK1Q13464humanARHGAP24Q8N264S415HKLDVsRsPPLMVkk
ROCK1Q13464humanARHGAP19Q14CB8S422QkRARsRsFsGLIkR
ROCK1Q13464humanMYL12BO14950S20KRPQRAtsNVFAMFD
ROCK1Q13464humanDPYSL2Q16555T555DNIPRRttQRIVAPP
ROCK1Q13464humanTPPPO94811S159sGVtKAIssPtVSRLp25-alpha
ROCK1Q13464humanARHGAP35Q9NRY4T1226LRsLRRNtKKPKPKPRhoGAP_pG1_pG2
ROCK1Q13464humanADD1P35611T445QkQQREKtRWLNSGR
ROCK1Q13464humanNR3C1P04150T519SENPGNKtIVPAtLP
ROCK1Q13464humanMYL9P24844S20KRPQRAtsNVFAMFD
ROCK1Q13464humanDESP17661T77RAsRLGttRtPssyGFilament_head
ROCK1Q13464humanADD1P35611T480TKEDGHRtstsAVPN
ROCK1Q13464humanSCRIBQ14160S1378EGPPKRVsLVGADDL
ROCK1Q13464humanMSNP26038T558LGRDKyKtLRQIRQGERM_C
ROCK1Q13464humanNR3C1P04150S617WRSYRQSsANLLCFAHormone_recep
ROCK1Q13464humanPPP1R12BO60237T646ARQtRRstQGVtLtD
ROCK1Q13464humanARHGAP24Q8N264S413sVHKLDVsRsPPLMV
ROCK1Q13464humanDAPK3O43293T265KDPKRRMtIAQSLEHPkinase
ROCK1Q13464humanMYL12BO14950T19KKRPQRAtsNVFAMF
ROCK1Q13464humanARHGAP24Q8N264S402LSGsKTNsPKNsVHK
ROCK1Q13464humanDESP17661S12ysSSQRVssYRRtFGFilament_head
ROCK1Q13464humanLIMK1P53667T508PDRKKRYtVVGNPYWPK_Tyr_Ser-Thr
ROCK1Q13464humanDAPK3O43293T299PERRRLKtTRLkEyt
ROCK1Q13464humanMAPK8IP3Q9UPT6S314RAREKRDsRNMEVQV
ROCK1Q13464humanTPPPO94811S32DRAAKRLsLEsEGAG
ROCK1Q13464humanMAPK8IP3Q9UPT6S364TRLDRtGssPTQGIV
ROCK1Q13464humanPTENP60484T232YSsNsGPtRREDKFMPTEN_C2
ROCK1Q13464humanKCNK3O14649S393GLMKRRssV______
ROCK1Q13464humanPPP1R12AO14974S852RPREKRRstGVsFWt


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
ROCK1IDDescription0.00e+00
ROCK1GO:0051017actin filament bundle assembly1.38e-08
ROCK1GO:0061572actin filament bundle organization1.38e-08
ROCK1GO:0007015actin filament organization1.55e-08
ROCK1GO:1902946protein localization to early endosome2.04e-06
ROCK1GO:0008360regulation of cell shape2.21e-06
ROCK1GO:0032956regulation of actin cytoskeleton organization3.56e-05
ROCK1GO:0036010protein localization to endosome3.56e-05
ROCK1GO:0042063gliogenesis3.56e-05
ROCK1GO:0022604regulation of cell morphogenesis5.66e-05
ROCK1GO:0032535regulation of cellular component size5.66e-05
ROCK1GO:0010001glial cell differentiation5.66e-05
ROCK1GO:0032970regulation of actin filament-based process5.66e-05
ROCK1GO:1902903regulation of supramolecular fiber organization6.36e-05
ROCK1GO:0110053regulation of actin filament organization7.54e-05
ROCK1GO:0030953astral microtubule organization7.54e-05
ROCK1GO:1905668positive regulation of protein localization to endosome1.29e-04
ROCK1GO:0032231regulation of actin filament bundle assembly1.49e-04
ROCK1GO:1905666regulation of protein localization to endosome1.49e-04
ROCK1GO:0061028establishment of endothelial barrier1.75e-04
ROCK1GO:1903651positive regulation of cytoplasmic transport2.07e-04
ROCK1GO:0002064epithelial cell development2.07e-04
ROCK1GO:2000641regulation of early endosome to late endosome transport3.81e-04
ROCK1GO:0051893regulation of focal adhesion assembly3.81e-04
ROCK1GO:0090109regulation of cell-substrate junction assembly3.81e-04
ROCK1GO:0001885endothelial cell development3.90e-04
ROCK1GO:0150116regulation of cell-substrate junction organization4.78e-04
ROCK1GO:0043254regulation of protein-containing complex assembly6.69e-04
ROCK1GO:0042060wound healing6.86e-04
ROCK1GO:0048041focal adhesion assembly1.04e-03
ROCK1GO:0048708astrocyte differentiation1.10e-03
ROCK1GO:0008361regulation of cell size1.28e-03
ROCK1GO:1900027regulation of ruffle assembly1.29e-03
ROCK1GO:0051492regulation of stress fiber assembly1.30e-03
ROCK1GO:0031345negative regulation of cell projection organization1.30e-03
ROCK1GO:1903649regulation of cytoplasmic transport1.30e-03
ROCK1GO:0007044cell-substrate junction assembly1.30e-03
ROCK1GO:0120032regulation of plasma membrane bounded cell projection assembly1.59e-03
ROCK1GO:0060491regulation of cell projection assembly1.59e-03
ROCK1GO:0150115cell-substrate junction organization1.59e-03
ROCK1GO:0031032actomyosin structure organization1.64e-03
ROCK1GO:0110020regulation of actomyosin structure organization1.64e-03
ROCK1GO:0044319wound healin4.74e-05
ROCK1GO:0048709oligodendrocyte differentiation1.64e-03
ROCK1GO:0090504epiboly1.70e-03
ROCK1GO:1902115regulation of organelle assembly1.73e-03
ROCK1GO:0030038contractile actin filament bundle assembly1.73e-03
ROCK1GO:0043149stress fiber assembly1.73e-03
ROCK1GO:0007163establishment or maintenance of cell polarity2.08e-03
ROCK1GO:0045022early endosome to late endosome transport2.34e-03

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Related Drugs to ROCK1_CABYR


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 ROCK1-CABYR 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 ROCK1_CABYR


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