Q05397B4E2N6F5H4S4J3QT16Q14291Q8IYN9Q9UD85FAK1_HUMANFocal adhesion kinase 1FADK 12.7.10.2Focal adhesion kinase-related nonkinaseFRNKProtein phosphatase 1 regulatory subunit 71PPP1R71Protein-tyrosine kinase 2p125FAKpp125FAKPTK2FAKFAK1Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoHuman T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)TISSUE SPECIFICITYExpression of an N-terminally truncated form of human focal adhesion kinase in brain.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4)TISSUE SPECIFICITYComplete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5)DNA sequence and analysis of human chromosome 8.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7)PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042CLEAVAGE OF INITIATOR METHIONINEACETYLATION AT ALA-2IDENTIFICATION BY MASS SPECTROMETRYA survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes.NUCLEOTIDE SEQUENCE [MRNA] OF 552-602TISSUE SPECIFICITYTyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates.FUNCTIONINTERACTION WITH NEDD9MUTAGENESIS OF TYR-397Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions.INTERACTION WITH TGFB1I1Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase.INTERACTION WITH TGFB1I1MUTAGENESIS OF VAL-928 AND LEU-1034Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation.FUNCTION IN PXN PHOSPHORYLATION; REGULATION OF CELL SHAPE AND MIGRATIONINTERACTION WITH EPHA2AUTOPHOSPHORYLATIONCATALYTIC ACTIVITYACTIVITY REGULATIONDEPHOSPHORYLATION BY PTPN11SUBCELLULAR LOCATIONRegulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain.FUNCTION IN CELL MIGRATION AND ACTIVATION OF BMXCATALYTIC ACTIVITYAUTOPHOSPHORYLATIONMUTAGENESIS OF TYR-397INTERACTION WITH BMXFocal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples.FUNCTION IN PHOSPHORYLATION OF SHC1AUTOPHOSPHORYLATIONINTERACTION WITH SHC1 AND SRCROLE IN DISEASERegulation of focal adhesion kinase by a novel protein inhibitor FIP200.INTERACTION WITH RB1CC1Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein.PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925INTERACTION WITH FGRFocal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway.FUNCTION IN INTEGRIN SIGNALING; REGULATION OF APOPTOSIS; REGULATION OF CELL SHAPE AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND AKT1 SIGNALING PATHWAYThe proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization.FUNCTION IN REGULATION OF CELL MIGRATIONPHOSPHORYLATION AT TYR-407; TYR-397 AND TYR-576Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53.INTERACTION WITH P53/TP53SUBCELLULAR LOCATIONMicrotubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase.FUNCTION IN FOCAL ADHESION DISASSEMBLYVascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells.INTERACTION WITH FLT4Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Expression of FAK-related non-kinase (FRNK) coincides with morphological change in the early stage of cell adhesion.ALTERNATIVE PROMOTER USAGEIDENTIFICATION OF ISOFORM 6DEVELOPMENTAL STAGE (ISOFORM 6)A probability-based approach for high-throughput protein phosphorylation analysis and site localization.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Therapeutic efficacy of a novel focal adhesion kinase inhibitor TAE226 in ovarian carcinoma.ACTIVITY REGULATIONROLE IN DISEASEPHOSPHORYLATION AT TYR-397 AND TYR-861Cellular characterization of a novel focal adhesion kinase inhibitor.FUNCTIONACTIVITY REGULATIONROLE IN DISEASEPHOSPHORYLATION AT TYR-397Activation of FAK is necessary for the osteogenic differentiation of human mesenchymal stem cells on laminin-5.FUNCTION IN OSTEOBLAST DIFFERENTIATIONInhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo.FUNCTIONACTIVITY REGULATIONROLE IN DISEASEPHOSPHORYLATION AT TYR-397The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription.FUNCTIONINTERACTION WITH LPXNEtk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways.FUNCTIONINTERACTION WITH BMXA novel Cas family member, HEPL, regulates FAK and cell spreading.FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH CASS4Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation.FUNCTION IN REGULATION OF P53/TP53 LEVELS; CELL PROLIFERATION AND CELL SURVIVALSUBCELLULAR LOCATIONRegulation of estrogen rapid signaling through arginine methylation by PRMT1.INTERACTION WITH ESR1; PIK3R1 AND/OR PIK3R2 AND SRCKinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-887 AND SER-910IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A quantitative atlas of mitotic phosphorylation.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes.PHOSPHORYLATION AT TYR-397; TYR-576; TYR-577; SER-722; TYR-861 AND TYR-925IDENTIFICATION IN A COMPLEX WITH CTTN AND FERPaxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion.FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXNSTEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells.INTERACTION WITH STEAP4Functional consequences of interactions between FAK and epithelial membrane protein 2 (EMP2).INTERACTION WITH EMP2Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling.FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF BCAR1ROLE IN DISEASEEphA1 interacts with integrin-linked kinase and regulates cell morphology and motility.INTERACTION WITH EPHA1Large-scale proteomics analysis of the human kinome.ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5; THR-13; SER-29; TYR-397; TYR-570; SER-580 AND SER-910CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models.ROLE IN DISEASEACTIVITY REGULATIONLIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin.INTERACTION WITH LPXNDownregulation of FAK-related non-kinase mediates the migratory phenotype of human fibrotic lung fibroblasts.FUNCTION (ISOFORM 6)TISSUE SPECIFICITYZF21 protein regulates cell adhesion and motility.INTERACTION WITH ZFYVE21DEPHOSPHORYLATION AT TYR-397Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.INTERACTION WITH TNS1CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer.INTERACTION WITH CD36Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND THR-914IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism.INTERACTION WITH RETFUNCTION IN RET PHOSPHORYLATIONPHOSPHORYLATION AT TYR-576 AND TYR-577Toward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-843 AND SER-910IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis.INTERACTION WITH CIB1 ISOFORM 2Signaling through focal adhesion kinase.REVIEW ON SIGNALING AND ON DIRECT PTK2/FAK1 SUBSTRATESNetrin-integrin signaling in epithelial morphogenesis, axon guidance and vascular patterning.REVIEW ON FUNCTION IN NETRIN SIGNALINGIntegrin-regulated FAK-Src signaling in normal and cancer cells.REVIEW ON FUNCTION IN CELL MIGRATION; FOCAL ADHESION TURNOVER AND ACTIVATION OF SIGNALING PATHWAYSROLE IN DISEASEFocal adhesion kinase: an essential kinase in the regulation of cardiovascular functions.FUNCTIONFERM control of FAK function: implications for cancer therapy.REVIEW ON ROLE IN INTEGRIN SIGNALING AND IN REGULATION OF P53/TP53 ACTIVITIESROLE IN DISEASEACTIVITY REGULATIONFocal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility.REVIEW ON FUNCTION IN REGULATION OF RHO FAMILY GTPASE ACTIVITYFocal adhesion kinase and cancer.REVIEW ON EXPRESSION IN CANCERROLE IN DISEASEFocal adhesion kinase and p53 signal transduction pathways in cancer.REVIEW ON FUNCTION IN REGULATION OF P53/TP53The role of focal adhesion kinase in early development.REVIEW ON ROLE IN DEVELOPMENTIntegrin signaling through FAK in the regulation of mammary stem cells and breast cancer.REVIEW ON FUNCTION IN INTEGRIN SIGNALING AND ACTIVATION OF DOWNSTREAM SIGNALING PATHWAYSCellular functions of FAK kinases: insight into molecular mechanisms and novel functions.FUNCTIONSIGNALINGFocal adhesion kinase: exploring Fak structure to gain insight into function.REVIEW ON FUNCTION; SUBUNIT; PHOSPHORYLATION; ACTIVITY REGULATION AND ROLE IN DISEASEMISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression.INTERACTION WITH MISPThe Intracranial Aneurysm Gene THSD1 Connects Endosome Dynamics to Nascent Focal Adhesion Assembly.SUBUNITDe Novo Mutations in FOXJ1 Result in a Motile Ciliopathy with Hydrocephalus and Randomization of Left/Right Body Asymmetry.SUBCELLULAR LOCATIONTISSUE SPECIFICITYThe structural basis of localization and signaling by the focal adhesion targeting domain.X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 891-1052IDENTIFICATION BY MASS SPECTROMETRYStructures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography.X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 411-686 IN COMPLEX WITH ATPMolecular recognition of paxillin LD motifs by the focal adhesion targeting domain.X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 892-1052 IN COMPLEX WITH PXNINTERACTION WITH PXNAntitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271.X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 414-689 IN COMPLEX WITH INHIBITORCATALYTIC ACTIVITYAUTOPHOSPHORYLATIONStructural basis for the interaction between focal adhesion kinase and CD4.X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 891-1052 IN COMPLEX WITH CD4SUBCELLULAR LOCATIONINTERACTION WITH CD4Patterns of somatic mutation in human cancer genomes.VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.Isoform 6Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271.Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, and CASS4. Interacts with NEDD9 (via SH3 domain) (PubMed:9360983). Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (PubMed:29069646). Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 (By similarity). Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (PubMed:19494199). Interacts with DSCAM (By similarity). Interacts with AMBRA1 (By similarity). Interacts (when tyrosine-phosphorylated) with tensin TNS1; the interaction is increased by phosphorylation of TNS1 (PubMed:20798394).Q05397P56945false2Q05397P46108false3Q05397P00533false7Q05397P29317false3Q05397P06241false3Q05397P62993false4Q05397Q14451false3Q05397P08631-2false2Q05397P16144false7Q05397Q92569false3Q05397P25105false2Q05397Q9H3S7false4Q05397P29350-3false3Q05397Q9Y3E5false2Q05397P49023false18Q05397Q9NP31false3Q05397P12931false9Q05397Q96SB4false2Q05397P42224false3Q05397O43294false3Q05397Q68CZ2false3Q05397P04637false13Q05397Q824H6true3Q05397P05480true5Q05397Q62219true3Cell junctionFocal adhesionCell membranePeripheral membrane proteinCytoplasmic sideCytoplasmPerinuclear regionCytoplasmCell cortexCytoplasmCytoskeletonCytoplasmCytoskeletonMicrotubule organizing centerCentrosomeNucleusCytoplasmCytoskeletonCilium basal bodyCytoplasmConstituent of focal adhesions. Detected at microtubules.Q05397-11Q05397-22Q05397-33Q05397-44Q05397-55Q05397-66FRNKQ05397-77Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous. Expressed in epithelial cells (at protein level) (PubMed:31630787).Isoform 6Detected in cultured cells, immediately after seeding and before formation of focal adhesions (at protein level).The Pro-rich regions interact with the SH3 domain of CAS family members, such as BCAR1 and NEDD9, and with the GTPase activating protein ARHGAP26.The C-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-925, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-925 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21. Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity).Sumoylated; this enhances autophosphorylation.Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.Isoform 6Produced by alternative promoter usage.Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.3D-structureAcetylationAlternative promoter usageAlternative splicingAngiogenesisATP-bindingCell junctionCell membraneCell projectionCytoplasmCytoskeletonDevelopmental proteinDirect protein sequencingIsopeptide bondKinaseMembraneNucleotide-bindingNucleusPhosphoproteinReference proteomeTransferaseTyrosine-protein kinaseUbl conjugationATPATPATPEMRGNALEMSDYWVVGAACHYTSLHWNWCRYISDPNVDACPDPRNAEASKGKGKKSGSTILEEEKAQQEERMRMESRRQATVSWDSGFQNPAQMLPASGRLPNQPCPERENYSFATFDGKEEKNWAERNKKPWRHPHQVADEKEYFVGLSRLLIPSMAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
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