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:PAK1_PAK2

Kinase Fusion Protein Summary

check button Kinase Fusion gene summary
Kinase Fusion partner gene informationKinase Fusion gene name: PAK1_PAK2
KinaseFusionDB ID: KFG4422
FusionGDB2.0 ID: KFG4422
HgeneTgene
Gene symbol

PAK1

PAK2

Gene ID

5585

5586

Gene nameprotein kinase N1protein kinase N2
SynonymsDBK|PAK-1|PAK1|PKN|PKN-ALPHA|PRK1|PRKCL1PAK2|PRK2|PRKCL2|PRO2042|Pak-2|STK7
Cytomap

19p13.12

1p22.2

Type of geneprotein-codingprotein-coding
Descriptionserine/threonine-protein kinase N1protease-activated kinase 1protein kinase C-like 1protein kinase C-like PKNprotein kinase C-related kinase 1protein kinase PKN-alphaserine-threonine kinase Nserine/threonine protein kinase Nserine/threonine-protein kinase N2PKN gammacardiolipin-activated protein kinase Pak2protein kinase C-like 2protein-kinase C-related kinase 2
Modification date2024030520240323
UniProtAcc

Q16512

Q13177

Ensembl transtripts involved in fusion geneENST idsENST00000356341, ENST00000530617, 
ENST00000278568, ENST00000528203, 
ENST00000525542, 
ENST00000327134, 
Context (manual curation of fusion genes in KinaseFusionDB)

PubMed: PAK1 [Title/Abstract] AND PAK2 [Title/Abstract] AND fusion [Title/Abstract]

Most frequent breakpoint (based on all fusion genes of FusionGDB 2.0)
check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
HgenePAK1

GO:0006357

regulation of transcription by RNA polymerase II

12514133

HgenePAK1

GO:0006468

protein phosphorylation

17332740

HgenePAK1

GO:0043687

post-translational protein modification

18066052

TgenePAK2

GO:0006468

protein phosphorylation

17332740

TgenePAK2

GO:0010631

epithelial cell migration

21754995


check buttonKinase Fusion gene breakpoints across PAK1 (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 PAK2 (3'-gene)
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.


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
CCLEMDA-MB-134-VIPAK1chr11

77047130

PAK2chr3

196547409



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)
ENST00000530617ENST00000327134PAK1chr1177047130PAK2chr31965474096221485

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

>ENST00000530617_ENST00000327134_PAK1_chr11_77047130_PAK2_chr3_196547409_length(amino acids)=485
MLLVVTMSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHT
IHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVS
EDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVG
DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD
VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPK

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

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/chr11:/chr3:)
- 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
PAK1

Q16512

PAK2

Q13177

FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. {ECO:0000269|PubMed:11104762, ECO:0000269|PubMed:12514133, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:24248594, ECO:0000269|PubMed:8557118, ECO:0000269|PubMed:8621664, ECO:0000269|PubMed:9175763}.FUNCTION: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:7744004, PubMed:19273597, PubMed:19923322, PubMed:9171063, PubMed:12853446, PubMed:16617111, PubMed:33693784). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:9171063, PubMed:12853446, PubMed:16617111). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964). {ECO:0000269|PubMed:12853446, ECO:0000269|PubMed:15234964, ECO:0000269|PubMed:16617111, ECO:0000269|PubMed:19273597, ECO:0000269|PubMed:19923322, ECO:0000269|PubMed:21177766, ECO:0000269|PubMed:21317288, ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:21724829, ECO:0000269|PubMed:27889207, ECO:0000269|PubMed:33693784, ECO:0000269|PubMed:7744004, ECO:0000269|PubMed:9171063}.

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).
471471
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote
HgenePAK177047130PAK2196547409ENST00000530617131575_881546DomainNote=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057
HgenePAK177047130PAK2196547409ENST00000530617131675_881554DomainNote=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057


check button - Retained domain in the 3'-partner of fusion protein (protein functional feature from UniProt).
PartnerHgeneeneHbpTgeneeneTbpENSTBPexonTotalExonProtein feature lociBPlociTotalLenFeatureNote
TgenePAK177047130PAK2196547409ENST0000053061701574_870525DomainNote=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057
TgenePAK177047130PAK2196547409ENST00000530617015249_4990525DomainNote=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 >>>189_PAK1_PAK2ENST00000530617ENST00000327134PAK1chr1177047130PAK2chr3196547409
MLLVVTMSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHT
IHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVS
EDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVG
DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD
VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPK
485
3D view using mol* of 189_PAK1_PAK2
PDB file >>>HKFP_275_PAK1_PAK2ENST00000530617ENST00000327134PAK1chr1177047130PAK2chr3196547409
MLLVVTMSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHT
IHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVS
EDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVG
DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD
VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPK
485_PAK1_PAK2
PDB file >>>359_PAK1_PAK2ENST00000530617ENST00000327134PAK1chr1177047130PAK2chr3196547409
MLLVVTMSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHT
IHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVS
EDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVG
DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD
VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPK
485
3D view using mol* of 359_PAK1_PAK2
PDB file >>>TKFP_614_PAK1_PAK2ENST00000530617ENST00000327134PAK1chr1177047130PAK2chr3196547409
MLLVVTMSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHT
IHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVS
EDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVG
DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTD
VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPK
485_PAK1_PAK2


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

check button Abstract of the Multiple Sequence Alignment of the Longest Fusion Protein Sequence and Known Sequence from PDB Search Using Fusion Gene Names
check button Multiple Sequence Alignment of the Longest Fusion Protein Sequence and Known Sequence from PDB Search Using Fusion Gene Names

check button Superimpose the 3D Structures Between the Longest Fusion Protein and the Longest Known PDB
3D view using mol* of viewer/superimpose_pdbs/PAK1_PAK2_4EQC_superimposed.pdb.html
3D view using mol* of viewer/superimpose_pdbs/PAK1_PAK2_5IME_superimposed.pdb.html


Top

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.
189_PAK1_PAK2.png
all structure sitemap plddt 189_PAK1_PAK2.png
189_PAK1_PAK2.png
all structure sitemap plddt2 189_PAK1_PAK2.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

check button Binding site residues of the found PDBs.
PDB accessionAA sequenceResidue position
4EQCASP1
4EQCPRO2
4EQCPHE3
4EQCTHR4
4EQCSER249
4EQCASP250
4EQCGLU251
4EQCGLU252
4EQCILE253
4EQCLEU254
4EQCGLU255
4EQCLYS256
4EQCLEU257
4EQCARG258
4EQCSER259
4EQCILE260
4EQCVAL261
4EQCSER262
4EQCVAL263
4EQCGLY264
4EQCASP265
4EQCPRO266
4EQCLYS267
4EQCLYS268
4EQCLYS269
4EQCTYR270
4EQCTHR271
4EQCARG272
4EQCPHE273
4EQCGLU274
4EQCLYS275
4EQCILE276
4EQCGLY277
4EQCGLN278
4EQCGLY279
4EQCALA280
4EQCSER281
4EQCGLY282
4EQCTHR283
4EQCVAL284
4EQCTYR285
4EQCTHR286
4EQCALA287
4EQCMET288
4EQCASP289
4EQCVAL290
4EQCALA291
4EQCTHR292
4EQCGLY293
4EQCGLN294
4EQCGLU295
4EQCVAL296
4EQCALA297
4EQCILE298
4EQCARG299
4EQCGLN300
4EQCMET301
4EQCASN302
4EQCLEU303
4EQCGLN304
4EQCGLN305
4EQCGLN306
4EQCPRO307
4EQCLYS308
4EQCLYS309
4EQCGLU310
4EQCLEU311
4EQCILE312
4EQCILE313
4EQCASN314
4EQCGLU315
4EQCILE316
4EQCLEU317
4EQCVAL318
4EQCMET319
4EQCARG320
4EQCGLU321
4EQCASN322
4EQCLYS323
4EQCASN324
4EQCPRO325
4EQCASN326
4EQCILE327
4EQCVAL328
4EQCASN329
4EQCTYR330
4EQCLEU331
4EQCASP332
4EQCSER333
4EQCTYR334
4EQCLEU335
4EQCVAL336
4EQCGLY337
4EQCASP338
4EQCGLU339
4EQCLEU340
4EQCTRP341
4EQCVAL342
4EQCVAL343
4EQCMET344
4EQCGLU345
4EQCTYR346
4EQCLEU347
4EQCALA348
4EQCGLY349
4EQCGLY350
4EQCSER351
4EQCLEU352
4EQCTHR353
4EQCASP354
4EQCVAL355
4EQCVAL356
4EQCTHR357
4EQCGLU358
4EQCTHR359
4EQCCYS360
4EQCMET361
4EQCASP362
4EQCGLU363
4EQCGLY364
4EQCGLN365
4EQCILE366
4EQCALA367
4EQCALA368
4EQCVAL369
4EQCCYS370
4EQCARG371
4EQCGLU372
4EQCCYS373
4EQCLEU374
4EQCGLN375
4EQCALA376
4EQCLEU377
4EQCGLU378
4EQCPHE379
4EQCLEU380
4EQCHIS381
4EQCSER382
4EQCASN383
4EQCGLN384
4EQCVAL385
4EQCILE386
4EQCHIS387
4EQCARG388
4EQCASP389
4EQCILE390
4EQCLYS391
4EQCSER392
4EQCASP393
4EQCASN394
4EQCILE395
4EQCLEU396
4EQCLEU397
4EQCGLY398
4EQCMET399
4EQCASP400
4EQCGLY401
4EQCSER402
4EQCVAL403
4EQCLYS404
4EQCLEU405
4EQCTHR406
4EQCASP407
4EQCPHE408
4EQCGLY409
4EQCPHE410
4EQCCYS411
4EQCALA412
4EQCGLN413
4EQCILE414
4EQCTHR415
4EQCPRO416
4EQCGLU417
4EQCGLN418
4EQCSER419
4EQCLYS420
4EQCARG421
4EQCSER422
4EQCMET424
4EQCVAL425
4EQCGLY426
4EQCTHR427
4EQCPRO428
4EQCTYR429
4EQCTRP430
4EQCMET431
4EQCALA432
4EQCPRO433
4EQCGLU434
4EQCVAL435
4EQCVAL436
4EQCTHR437
4EQCARG438
4EQCLYS439
4EQCALA440
4EQCTYR441
4EQCGLY442
4EQCPRO443
4EQCLYS444
4EQCVAL445
4EQCASP446
4EQCILE447
4EQCTRP448
4EQCSER449
4EQCLEU450
4EQCGLY451
4EQCILE452
4EQCMET453
4EQCALA454
4EQCILE455
4EQCGLU456
4EQCMET457
4EQCILE458
4EQCGLU459
4EQCGLY460
4EQCGLU461
4EQCPRO462
4EQCPRO463
4EQCTYR464
4EQCLEU465
4EQCASN466
4EQCGLU467
4EQCASN468
4EQCPRO469
4EQCLEU470
4EQCARG471
4EQCALA472
4EQCLEU473
4EQCTYR474
4EQCLEU475
4EQCILE476
4EQCALA477
4EQCTHR478
4EQCASN479
4EQCGLY480
4EQCTHR481
4EQCPRO482
4EQCGLU483
4EQCLEU484
4EQCGLN485
4EQCASN486
4EQCPRO487
4EQCGLU488
4EQCLYS489
4EQCLEU490
4EQCSER491
4EQCALA492
4EQCILE493
4EQCPHE494
4EQCARG495
4EQCASP496
4EQCPHE497
4EQCLEU498
4EQCASN499
4EQCARG500
4EQCCYS501
4EQCLEU502
4EQCGLU503
4EQCMET504
4EQCASP505
4EQCVAL506
4EQCGLU507
4EQCLYS508
4EQCARG509
4EQCGLY510
4EQCSER511
4EQCALA512
4EQCLYS513
4EQCGLU514
4EQCLEU515
4EQCLEU516
4EQCGLN517
4EQCHIS518
4EQCGLN519
4EQCPHE520
4EQCLEU521
4EQCLYS522
4EQCILE523
4EQCALA524
4EQCLYS525
4EQCPRO526
4EQCLEU527
4EQCSER528
4EQCSER529
4EQCLEU530
4EQCTHR531
4EQCPRO532
4EQCLEU533
4EQCILE534
4EQCALA535
4EQCALA536
4EQCALA537
4EQCLYS538
4EQCGLU539
4EQCALA540
4EQCTHR541
5IMEGLU251
5IMEGLU252
5IMEILE253
5IMELEU254
5IMEGLU255
5IMELYS256
5IMELEU257
5IMEARG258
5IMESER259
5IMEILE260
5IMEVAL261
5IMESER262
5IMEVAL263
5IMEGLY264
5IMEASP265
5IMEPRO266
5IMELYS267
5IMELYS275
5IMEILE276
5IMEGLY277
5IMEGLN278
5IMEGLY279
5IMEALA280
5IMESER281
5IMEGLY282
5IMETHR283
5IMEVAL284
5IMETYR285
5IMETHR286
5IMEALA287
5IMEMET288
5IMEASP289
5IMEGLN294
5IMEGLU295
5IMEVAL296
5IMEALA297
5IMEILE298
5IMELYS299
5IMEGLN300
5IMEMET301
5IMEASN302
5IMELEU303
5IMELYS309
5IMEGLU310
5IMELEU311
5IMEILE312
5IMEILE313
5IMEASN314
5IMEGLU315
5IMEILE316
5IMELEU317
5IMEVAL318
5IMEMET319
5IMEARG320
5IMEGLU321
5IMEASN322
5IMELYS323
5IMEASN324
5IMEPRO325
5IMEASN326
5IMEILE327
5IMEVAL328
5IMEASN329
5IMETYR330
5IMELEU331
5IMEASP332
5IMESER333
5IMETYR334
5IMELEU335
5IMEVAL336
5IMEGLY337
5IMEASP338
5IMEGLU339
5IMELEU340
5IMETRP341
5IMEVAL342
5IMEVAL343
5IMEMET344
5IMEGLU345
5IMETYR346
5IMELEU347
5IMEALA348
5IMEGLY349
5IMEGLY350
5IMESER351
5IMELEU352
5IMETHR353
5IMEASP354
5IMEVAL355
5IMEVAL356
5IMETHR357
5IMEGLU358
5IMETHR359
5IMECYS360
5IMEMET361
5IMEASP362
5IMEGLU363
5IMEGLY364
5IMEGLN365
5IMEILE366
5IMEALA367
5IMEALA368
5IMEVAL369
5IMECYS370
5IMEARG371
5IMEGLU372
5IMECYS373
5IMELEU374
5IMEGLN375
5IMEALA376
5IMELEU377
5IMEGLU378
5IMEPHE379
5IMELEU380
5IMEHIS381
5IMESER382
5IMEASN383
5IMEGLN384
5IMEVAL385
5IMEILE386
5IMEHIS387
5IMEARG388
5IMEASN389
5IMEILE390
5IMELYS391
5IMESER392
5IMEASP393
5IMEASN394
5IMEILE395
5IMELEU396
5IMELEU397
5IMEGLY398
5IMEMET399
5IMEASP400
5IMEGLY401
5IMESER402
5IMEVAL403
5IMELYS404
5IMELEU405
5IMETHR406
5IMEASP407
5IMEPHE408
5IMEGLY409
5IMEPHE410
5IMECYS411
5IMEALA412
5IMEGLN413
5IMEILE414
5IMETHR415
5IMEPRO416
5IMEGLU417
5IMEGLN418
5IMESER419
5IMELYS420
5IMEARG421
5IMESER422
5IMEGLU423
5IMEMET424
5IMEVAL425
5IMEGLY426
5IMETHR427
5IMEPRO428
5IMETYR429
5IMETRP430
5IMEMET431
5IMEALA432
5IMEPRO433
5IMEGLU434
5IMEVAL435
5IMEVAL436
5IMETHR437
5IMEARG438
5IMELYS439
5IMEALA440
5IMETYR441
5IMEGLY442
5IMEPRO443
5IMELYS444
5IMEVAL445
5IMEASP446
5IMEILE447
5IMETRP448
5IMESER449
5IMELEU450
5IMEGLY451
5IMEILE452
5IMEMET453
5IMEALA454
5IMEILE455
5IMEGLU456
5IMEMET457
5IMEILE458
5IMEGLU459
5IMEGLY460
5IMEGLU461
5IMEPRO462
5IMEPRO463
5IMETYR464
5IMELEU465
5IMEASN466
5IMEGLU467
5IMEASN468
5IMEPRO469
5IMELEU470
5IMEARG471
5IMEALA472
5IMELEU473
5IMETYR474
5IMELEU475
5IMEILE476
5IMEALA477
5IMETHR478
5IMEASN479
5IMEGLY480
5IMETHR481
5IMEPRO482
5IMEGLU483
5IMELEU484
5IMEGLN485
5IMEASN486
5IMEPRO487
5IMEGLU488
5IMELYS489
5IMELEU490
5IMESER491
5IMEALA492
5IMEILE493
5IMEPHE494
5IMEARG495
5IMEASP496
5IMEPHE497
5IMELEU498
5IMEASN499
5IMEARG500
5IMECYS501
5IMELEU502
5IMEGLU503
5IMEMET504
5IMEASP505
5IMEVAL506
5IMEGLU507
5IMELYS508
5IMEARG509
5IMEGLY510
5IMESER511
5IMEALA512
5IMELYS513
5IMEGLU514
5IMELEU515
5IMELEU516
5IMEGLN517
5IMEHIS518
5IMEGLN519
5IMEPHE520
5IMELEU521
5IMELYS522
5IMEILE523
5IMEALA524
5IMELYS525
5IMEPRO526
5IMELEU527
5IMESER528
5IMESER529
5IMELEU530
5IMETHR531
5IMEPRO532
5IMELEU533
5IMEILE534
5IMEALA535
5IMEALA536
5IMEALA537
5IMELYS538
5IMEGLU539
5IMEALA540
5IMETHR541
5IMELYS542
5IMEASN543
5IMEASN544
5IMEHIS545
5IMEGLY546
5IMEASP250
5IMEGLU251
5IMEGLU252
5IMEILE253
5IMELEU254
5IMEGLU255
5IMELYS256
5IMELEU257
5IMEARG258
5IMESER259
5IMEILE260
5IMEVAL261
5IMESER262
5IMEVAL263
5IMEGLY264
5IMEASP265
5IMEPRO266
5IMELYS267
5IMELYS268
5IMELYS269
5IMETYR270
5IMETHR271
5IMEARG272
5IMEPHE273
5IMEGLU274
5IMELYS275
5IMEILE276
5IMEGLY277
5IMEGLN278
5IMEGLY279
5IMEALA280
5IMESER281
5IMEGLY282
5IMETHR283
5IMEVAL284
5IMETYR285
5IMETHR286
5IMEALA287
5IMEMET288
5IMEASP289
5IMEVAL290
5IMEALA291
5IMETHR292
5IMEGLY293
5IMEGLN294
5IMEGLU295
5IMEVAL296
5IMEALA297
5IMEILE298
5IMELYS299
5IMEGLN300
5IMEMET301
5IMEASN302
5IMEPRO307
5IMELYS308
5IMELYS309
5IMEGLU310
5IMELEU311
5IMEILE312
5IMEILE313
5IMEASN314
5IMEGLU315
5IMEILE316
5IMELEU317
5IMEVAL318
5IMEMET319
5IMEARG320
5IMEGLU321
5IMEASN322
5IMELYS323
5IMEASN324
5IMEPRO325
5IMEASN326
5IMEILE327
5IMEVAL328
5IMEASN329
5IMETYR330
5IMELEU331
5IMEASP332
5IMESER333
5IMETYR334
5IMELEU335
5IMEVAL336
5IMEGLY337
5IMEASP338
5IMEGLU339
5IMELEU340
5IMETRP341
5IMEVAL342
5IMEVAL343
5IMEMET344
5IMEGLU345
5IMETYR346
5IMELEU347
5IMEALA348
5IMEGLY349
5IMEGLY350
5IMESER351
5IMELEU352
5IMETHR353
5IMEASP354
5IMEVAL355
5IMEVAL356
5IMETHR357
5IMEGLU358
5IMETHR359
5IMECYS360
5IMEMET361
5IMEASP362
5IMEGLU363
5IMEGLY364
5IMEGLN365
5IMEILE366
5IMEALA367
5IMEALA368
5IMEVAL369
5IMECYS370
5IMEARG371
5IMEGLU372
5IMECYS373
5IMELEU374
5IMEGLN375
5IMEALA376
5IMELEU377
5IMEGLU378
5IMEPHE379
5IMELEU380
5IMEHIS381
5IMESER382
5IMEASN383
5IMEGLN384
5IMEVAL385
5IMEILE386
5IMEHIS387
5IMEARG388
5IMEASN389
5IMEILE390
5IMELYS391
5IMESER392
5IMEASP393
5IMEASN394
5IMEILE395
5IMELEU396
5IMELEU397
5IMEGLY398
5IMEMET399
5IMEASP400
5IMEGLY401
5IMESER402
5IMEVAL403
5IMELYS404
5IMELEU405
5IMETHR406
5IMEASP407
5IMEPHE408
5IMEGLU417
5IMEGLN418
5IMESER419
5IMELYS420
5IMEARG421
5IMESER422
5IMEGLU423
5IMEMET424
5IMEVAL425
5IMEGLY426
5IMETHR427
5IMEPRO428
5IMETYR429
5IMETRP430
5IMEMET431
5IMEALA432
5IMEPRO433
5IMEGLU434
5IMEVAL435
5IMEVAL436
5IMETHR437
5IMEARG438
5IMELYS439
5IMEALA440
5IMETYR441
5IMEGLY442
5IMEPRO443
5IMELYS444
5IMEVAL445
5IMEASP446
5IMEILE447
5IMETRP448
5IMESER449
5IMELEU450
5IMEGLY451
5IMEILE452
5IMEMET453
5IMEALA454
5IMEILE455
5IMEGLU456
5IMEMET457
5IMEILE458
5IMEGLU459
5IMEGLY460
5IMEGLU461
5IMEPRO462
5IMEPRO463
5IMETYR464
5IMELEU465
5IMEASN466
5IMEGLU467
5IMEASN468
5IMEPRO469
5IMELEU470
5IMEARG471
5IMEALA472
5IMELEU473
5IMETYR474
5IMELEU475
5IMEILE476
5IMEALA477
5IMETHR478
5IMEASN479
5IMEGLY480
5IMETHR481
5IMEPRO482
5IMEGLU483
5IMELEU484
5IMEGLN485
5IMEASN486
5IMEPRO487
5IMEGLU488
5IMELYS489
5IMELEU490
5IMESER491
5IMEALA492
5IMEILE493
5IMEPHE494
5IMEARG495
5IMEASP496
5IMEPHE497
5IMELEU498
5IMEASN499
5IMEARG500
5IMECYS501
5IMELEU502
5IMEGLU503
5IMEMET504
5IMEASP505
5IMEVAL506
5IMEGLU507
5IMELYS508
5IMEARG509
5IMEGLY510
5IMESER511
5IMEALA512
5IMELYS513
5IMEGLU514
5IMELEU515
5IMELEU516
5IMEGLN517
5IMEHIS518
5IMEGLN519
5IMEPHE520
5IMELEU521
5IMELYS522
5IMEILE523
5IMEALA524
5IMELYS525
5IMEPRO526
5IMELEU527
5IMESER528
5IMESER529
5IMELEU530
5IMETHR531
5IMEPRO532
5IMELEU533
5IMEILE534
5IMEALA535
5IMEALA536
5IMEALA537
5IMELYS538
5IMEGLU539
5IMEALA540
5IMETHR541


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.

189_PAK1_PAK2_ramachandran.png
all structure PAK1-PAK2

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
all structure PAK1-PAK2
3'-kinase fusion protein case

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
189_PAK1_PAK2-DOCK_HTVS_1-001Pralsetinib-8.47723-8.56873-43.7312
189_PAK1_PAK2-DOCK_HTVS_1-001Acalabrutinib-7.51242-7.52652-38.8977
189_PAK1_PAK2-DOCK_HTVS_1-001Acalabrutinib-7.51242-7.52652-38.8977
189_PAK1_PAK2-DOCK_HTVS_1-001Midostaurin-7.3859699999999995-7.3859699999999995-43.0655
189_PAK1_PAK2-DOCK_HTVS_1-001Neratinib-6.982480000000001-7.16838-60.2967
189_PAK1_PAK2-DOCK_HTVS_1-001Neratinib-6.94039-7.1226899999999995-59.2826
189_PAK1_PAK2-DOCK_HTVS_1-001Neratinib-6.94039-7.1226899999999995-59.2826
189_PAK1_PAK2-DOCK_HTVS_1-001Midostaurin-6.901860000000001-6.901860000000001-39.0018
189_PAK1_PAK2-DOCK_HTVS_1-001Larotrectinib-6.82308-6.82308-33.4717
189_PAK1_PAK2-DOCK_HTVS_1-001Lapatinib-6.742999999999999-6.8318-57.4458
189_PAK1_PAK2-DOCK_HTVS_1-001Lapatinib-6.71192-6.80072-57.7045
189_PAK1_PAK2-DOCK_HTVS_1-001Larotrectinib-6.6882399999999995-6.6882399999999995-37.8026
189_PAK1_PAK2-DOCK_HTVS_1-001Encorafenib-6.600060000000001-6.9885600000000005-46.4323
189_PAK1_PAK2-DOCK_HTVS_1-001Lenvatinib-6.506530000000001-6.506530000000001-41.4377
189_PAK1_PAK2-DOCK_HTVS_1-001Zanubrutinib-6.505719999999999-6.505719999999999-46.6558
189_PAK1_PAK2-DOCK_HTVS_1-001Midostaurin-6.42277-6.42277-30.2677
189_PAK1_PAK2-DOCK_HTVS_1-001Binimetinib-6.3872-6.3959-48.0055
189_PAK1_PAK2-DOCK_HTVS_1-001Binimetinib-6.3872-6.3959-48.0055
189_PAK1_PAK2-DOCK_HTVS_1-001Selpercatinib-6.37918-6.409680000000001-41.7146
189_PAK1_PAK2-DOCK_HTVS_1-001Belumosudil-6.34066-6.34836-45.8752

Top

Kinase-Substrate Information of PAK1_PAK2


check button Phosphorylation target of the kinase
(phosphosite, 03-17-2024)
KinaseKinase UniProt AccKinase speciesSubstrateSubstrate UniProt AccSubstrate phosphorylated residuesSubstrate phosphorylated sites (+/-7AA)Domain
PAK1Q13153humanFXR1P51114S420sERkDELsDWsLAGEFXMRP1_C_core
PAK1Q13153humanARPC1BO15143T21HAWNkDRtQIAICPN
PAK1Q13153humanGNAZP19086S16EKEAARRsRRIDRHLG-alpha
PAK1Q13153humanARHGEF2Q92974S886PVDPRRRsLPAGDAL
PAK1Q13153humanMAP3K1Q13233S67RQLRKVRsVELDQLP
PAK1Q13153humanTBCBQ99426S128VRsFLKRsKLGRyNE
PAK1Q13153humanCRKP46108S41VFLVRDsstsPGDyVSH2
PAK1Q13153humanCTNNB1P35222S675QDykKRLsVELtsSL
PAK1Q13153humanGDI2P50395T248LSAIyGGtYMLNkPIGDI
PAK1Q13153humanMICAL1Q8TDZ2S817sPERQRLssLNLtPD
PAK1Q13153humanPXNP49023S258tQQQtRIsAssAtRE
PAK1Q13153humanGDI2P50395S382PIEQkFVsIsDLLVPGDI
PAK1Q13153humanTBCBQ99426S65GVDDKFYskLDQEDAUbiquitin_2
PAK1Q13153humanPXNP49023-2S272ELDELMAsLSDFKFM
PAK1Q13153humanPLK1P53350S49EVLVDPRsRRRYVRG
PAK1Q13153humanH3C1P68431S10tkQtArkstGGkAPrHistone
PAK1Q13153humanPAK1Q13153S204tKsVyTRsVIEPLPV
PAK1Q13153humanSNAI1O95863S246QACARTFsRMsLLHK
PAK1Q13153humanFLNAP21333S2292FEDRkDGsCGVAYVVFilamin
PAK1Q13153humanARHGDIAP52565S174kGMLARGsYsIkSRFRho_GDI
PAK1Q13153humanPCBP1Q15365T60NCPERIItLTGPTNAKH_1
PAK1Q13153humanCTTNQ14247S405KtQtPPVsPAPQPtE
PAK1Q13153humanDYNLL1P63167S88VAILLFKsG______Dynein_light
PAK1Q13153humanARL4AP40617S143QDLRNSLsLSEIEKLArf
PAK1Q13153humanNLRP3Q96P20S198GKTKTCEsPVSPIKMFISNA
PAK1Q13153humanARL4DP49703S144QDQPGALsAAEVEkRArf
PAK1Q13153humanSPENQ96T58T3568EGVARRMtVETDYCLSPOC
PAK1Q13153humanARHGEF2Q92974-2S885PVDPRRRsLPAGDAL
PAK1Q13153humanAURKAO14965S342QETYKRIsRVEFTFPPkinase
PAK1Q13153humanSTMN1P16949S38sVPEFPLsPPkKkDLStathmin
PAK1Q13153humanGIT1Q9Y2X7S700PALEPVRsSLRLLNAGIT1_C
PAK1Q13153humanPCBP1Q15365T127IKEIREStGAQVQVAKH_1
PAK1Q13153humanNF2P35240S518DTDMKRLsMEIEKEKERM_C
PAK1Q13153humanPA2G4Q9UQ80T261QyGLkMktSRAFFsEPeptidase_M24
PAK1Q13153humanRUNX3Q13761T209ERLRMRVtPstPsPr
PAK1Q13153humanARHGDIAP52565S101LEsFKkQsFVLkEGVRho_GDI
PAK1Q13153humanSTMN1P16949S16kELEKrAsGQAFELIStathmin
PAK1Q13153humanMAP2K1Q02750S298RtPGRPLssyGMDSRPkinase
PAK1Q13153humanBADQ92934S99PFrGrsRsAPPNLWABcl-2_BAD
PAK1Q13153humanKIF2CQ99661S111kEsLRsRstRMstVS
PAK1Q13153humanAURKAO14965T288APSsRRttLCGtLDyPkinase
PAK1Q13153humanPGM1P36871T467SANDKVYtVEkADNF
PAK1Q13153humanPAK1Q13153S199PRPEHtKsVyTRsVI
PAK1Q13153humanRAF1P04049S339PRGQRDssyyWEIEA
PAK1Q13153humanILKQ13418S246CPRLRIFsHPNVLPVPK_Tyr_Ser-Thr
PAK1Q13153humanBADQ92934S75EIRsRHssyPAGtEDBcl-2_BAD
PAK1Q13153humanKIF2CQ99661S192VNsVRRKsCLVkEVE
PAK1Q13153humanPGAM1P18669S23WNLENrFsGWyDADLHis_Phos_1
PAK1Q13153humanARHGDIAP52565S176MLARGsYsIkSRFTDRho_GDI
PAK1Q13153humanELF3P78545S207GTGASRSsHSSDsGG
PAK1Q13153humanMORC2Q9Y6X9S739AtPsRKRsVAVsDEE
PAK1Q13153humanCTTNQ14247S113skLskHCsQVDsVrGHS1_rep
PAK1Q13153humanNLRP3Q96P20T659KIEINLStRMDHMVS
PAK1Q13153humanBADQ92934S118GRELRRMsDEFVDsFBcl-2_BAD
PAK1Q13153humanGIT1Q9Y2X7S508RRDRQAFsMyEPGsA
PAK1Q13153humanITGB3BPQ13352S28SkITRKKsVITysPTCENP-R
PAK1Q13153humanBADQ92934S74VEIRsRHssyPAGtEBcl-2_BAD
PAK1Q13153humanNLRP3Q96P20S163ARLGEsVsLNKRYTRFISNA
PAK1Q13153humanMYL9P24844S20KRPQRAtsNVFAMFD
PAK1Q13153humanFLNAP21333S2152tRRRRAPsVANVGsHFilamin
PAK1Q13153humanSNAI2O43623S251KNCsKTFsRMsLLHKzf-C2H2
PAK1Q13153humanFLNAP21333S2370AIDAkVHsPsGALEEFilamin
PAK1Q13153humanBRAFP15056S446KtLGRRDssDDWEIP
PAK1Q13153humanPGAM1P18669S118QVkIWRRsyDVPPPPHis_Phos_1
PAK1Q13153humanCTNNB1P35222S552QDtQRRtsMGGtQQQ
PAK1Q13153humanSPENQ96T58S3486QPAPKQDssPHLTSQ
PAK1Q13153humanCTTNQ14247S418tEErLPssPVyEDAA
PAK1Q13153humanLIMK1P53667T508PDRKKRYtVVGNPYWPK_Tyr_Ser-Thr
PAK1Q13153humanPAK1Q13153S144sNsQKyMsFtDksAE
PAK1Q13153humanRAF1P04049S338RPRGQRDssyyWEIE
PAK1Q13153humanPREX2Q70Z35S1107DTISNRDsYSDCNSN
PAK1Q13153humanILKQ13418T173DTFWkGttRTRPRNG
PAK1Q13153humanCTBP1Q13363S158REGTRVQsVEQIREV2-Hacid_dh_C; 2-Hacid_dh
PAK1Q13153humanPAK1Q13153T423PEQSkRstMVGtPYWPkinase
PAK1Q13153humanMICAL1Q8TDZ2S960ELALRRQssSPEQQKbMERB_dom
PAK1Q13153humanHACE1Q8IYU2S385LMKNKRDsTEITsIL
PAK1Q13153humanESR1P03372S305IkRSkkNsLALSLtA
PAK1Q13153humanMYLKQ15746S1772SGLsGRKsstGsPts
PAK1Q13153humanBADQ92934S134KGLPRPKsAGtAtQMBcl-2_BAD
PAK1Q13153humanVIMP08670S56srsLyAssPGGVyAtFilament_head
PAK1Q13153humanATG5Q9H1Y0T101SALPWNItVHFKSFPAPG5
PAK2Q13177humanMYCP01106S388RRNELkRsFFALRDQHLH
PAK2Q13177humanARHGAP15Q53QZ3S292kVCERENsTVPWFVk
PAK2Q13177humanH4C1P62805S47RGGVKrIsGLIyEEtCENP-T_C
PAK2Q13177humanJUNP05412T2______MtAKMETtF
PAK2Q13177humanCALD1Q05682S744GLKVGVSsRINEWLTCaldesmon
PAK2Q13177humanJUNP05412T286RLEEKVKtLKAQNSEbZIP_1
PAK2Q13177humanMYCP01106T373EENVkRRtHNVLERQHLH
PAK2Q13177humanMICAL1Q8TDZ2S817sPERQRLssLNLtPD
PAK2Q13177humanSORT1Q99523S793RFLVHRYsVLQQHAE
PAK2Q13177humanCASP7P55210S239WRsPGRGsWFVQALCPeptidase_C14
PAK2Q13177humanABL1P00519S619PtPPKRsssFREMDG
PAK2Q13177humanPAK2Q13177S192PRPDHTksIytRsVI
PAK2Q13177humanPAK2Q13177S141tVkQKyLsFtPPEkd
PAK2Q13177humanSMAD2Q15796S467sVRCssMs_______
PAK2Q13177humanNF2P35240S518DTDMKRLsMEIEKEKERM_C
PAK2Q13177humanSMAD2Q15796S417RMCTIRMsFVkGWGAMH2
PAK2Q13177humanEIF4G1Q04637S895RDIARRRsLGNIkFIMIF4G
PAK2Q13177humanARHGAP15Q53QZ3S4____MQKsTNsDTSV
PAK2Q13177humanARHGAP15Q53QZ3S43DRLsQsksMILTDVG
PAK2Q13177humanPAK2Q13177T402PEQSkRstMVGtPYWPkinase
PAK2Q13177humanJUNP05412T8MtAKMETtFYDDALNJun
PAK2Q13177humanSMAD2Q15796S465sPsVRCssMs_____
PAK2Q13177humanMYCP01106T415VVILKkAtAYILsVQHLH
PAK2Q13177humanPXNP49023S272ELDELMAsLsDFkIQ
PAK2Q13177humanCASP7P55210S30DAKPDRssFVPsLFs
PAK2Q13177humanCALD1Q05682S714EGVRNIksMWEkGNVCaldesmon
PAK2Q13177humanARHGAP15Q53QZ3S41HHDRLsQsksMILTD
PAK2Q13177humanMAPK6Q16659S189ySHKGHLsEGLVTkWPkinase
PAK2Q13177humanPXNP49023S274DELMAsLsDFkIQGL
PAK2Q13177humanPAK2Q13177S197TksIytRsVIDPVPA
PAK2Q13177humanCASP7P55210T173FRGDRCktLLEkPKLPeptidase_C14
PAK2Q13177humanCTNNB1P35222S552QDtQRRtsMGGtQQQ
PAK2Q13177humanSMAD2Q15796S464GsPsVRCssMs____
PAK2Q13177humanJUNP05412T89QSSNGHItTtPtPtQJun
PAK2Q13177humanPREX2Q70Z35S1107DTISNRDsYSDCNSN
PAK2Q13177humanRAF1P04049S338RPRGQRDssyyWEIE
PAK2Q13177humanMICAL1Q8TDZ2S960ELALRRQssSPEQQKbMERB_dom
PAK2Q13177humanHACE1Q8IYU2S385LMKNKRDsTEITsIL
PAK2Q13177humanSLC25A5P05141T107LGGVDkRtQFWLyFA
PAK2Q13177humanJUNP05412T93GHItTtPtPtQFLCPJun
PAK2Q13177humanABL1P00519S618APtPPKRsssFREMD


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
PAK1IDDescription0.00e+00
PAK1GO:0051017actin filament bundle assembly7.15e-06
PAK1GO:0061572actin filament bundle organization7.15e-06
PAK1GO:0032233positive regulation of actin filament bundle assembly7.15e-06
PAK1GO:0032231regulation of actin filament bundle assembly7.15e-06
PAK1GO:1902905positive regulation of supramolecular fiber organization8.29e-06
PAK1GO:0051495positive regulation of cytoskeleton organization9.71e-06
PAK1GO:0007015actin filament organization9.71e-06
PAK1GO:1902903regulation of supramolecular fiber organization1.82e-05
PAK1GO:0051492regulation of stress fiber assembly4.26e-05
PAK1GO:0051496positive regulation of stress fiber assembly4.66e-05
PAK1GO:0032956regulation of actin cytoskeleton organization4.66e-05
PAK1GO:0110020regulation of actomyosin structure organization6.18e-05
PAK1GO:0030038contractile actin filament bundle assembly6.98e-05
PAK1GO:0043149stress fiber assembly6.98e-05
PAK1GO:0007264small GTPase mediated signal transduction7.90e-05
PAK1GO:0110053regulation of actin filament organization7.90e-05
PAK1GO:0032970regulation of actin filament-based process8.07e-05
PAK1GO:0031032actomyosin structure organization1.50e-04
PAK1GO:0010720positive regulation of cell development2.67e-04
PAK1GO:0007265Ras protein signal transduction3.33e-04
PAK1GO:0031589cell-substrate adhesion4.35e-04
PAK1GO:1900026positive regulation of substrate adhesion-dependent cell spreading4.38e-04
PAK1GO:0022411cellular component disassembly5.51e-04
PAK1GO:1903034regulation of response to wounding5.70e-04
PAK1GO:0034446substrate adhesion-dependent cell spreading5.74e-04
PAK1GO:0048538thymus development6.92e-04
PAK1GO:0046578regulation of Ras protein signal transduction6.98e-04
PAK1GO:0071470cellular response to osmotic stress8.16e-04
PAK1GO:0051056regulation of small GTPase mediated signal transduction9.24e-04
PAK1GO:1900024regulation of substrate adhesion-dependent cell spreading1.44e-03
PAK1GO:0048732gland development1.44e-03
PAK1GO:0031109microtubule polymerization or depolymerization1.86e-03
PAK1GO:0007266Rho protein signal transduction2.00e-03
PAK1GO:0061311cell surface receptor signaling pathway involved in heart development2.67e-03
PAK1GO:2001234negative regulation of apoptotic signaling pathway2.67e-03
PAK1GO:0044342type B pancreatic cell proliferation3.17e-03
PAK1GO:0032886regulation of microtubule-based process3.47e-03
PAK1GO:0006970response to osmotic stress3.47e-03
PAK1GO:0039694viral RNA genome replication3.47e-03
PAK1GO:0048679regulation of axon regeneration3.47e-03
PAK1GO:0070507regulation of microtubule cytoskeleton organization3.47e-03
PAK1GO:0035023regulation of Rho protein signal transduction3.47e-03
PAK1GO:0030878thyroid gland development3.60e-03
PAK1GO:0050767regulation of neurogenesis3.60e-03
PAK1GO:0061351neural precursor cell proliferation3.66e-03
PAK1GO:0070570regulation of neuron projection regeneration3.72e-03
PAK1GO:2001233regulation of apoptotic signaling pathway3.83e-03
PAK1GO:0031110regulation of microtubule polymerization or depolymerization5.14e-03
PAK1GO:0042060wound healing5.36e-03

Top

Related Drugs to PAK1_PAK2


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 PAK1-PAK2 and kinase inhibitors the PubMed Abstract (04-01-2024)

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

Top

Related Diseases to PAK1_PAK2


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