true2006-10-032024-03-27162AAK1_HUMANA novel AAK1 splice variant functions at multiple steps of the endocytic pathway.Henderson D.M.Conner S.D.doi:10.1091/mbc.e06-09-08312007Mol. Biol. Cell182698-2706NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)FUNCTIONCATALYTIC ACTIVITYACTIVITY REGULATIONINTERACTION WITH CLATHRIN AND AP-2TISSUE SPECIFICITYDOMAINBrainPrediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.Kikuno R.Nagase T.Ishikawa K.Hirosawa M.Miyajima N.Tanaka A.Kotani H.Nomura N.Ohara O.doi:10.1093/dnares/6.3.1971999DNA Res.6197-205NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)VARIANT GLN-509Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W.Graves T.A.Fulton R.S.Fulton L.A.Pepin K.H.Minx P.Wagner-McPherson C.Layman D.Wylie K.Sekhon M.Becker M.C.Fewell G.A.Delehaunty K.D.Miner T.L.Nash W.E.Kremitzki C.Oddy L.Du H.Sun H.Bradshaw-Cordum H.Ali J.Carter J.Cordes M.Harris A.Isak A.van Brunt A.Nguyen C.Du F.Courtney L.Kalicki J.Ozersky P.Abbott S.Armstrong J.Belter E.A.Caruso L.Cedroni M.Cotton M.Davidson T.Desai A.Elliott G.Erb T.Fronick C.Gaige T.Haakenson W.Haglund K.Holmes A.Harkins R.Kim K.Kruchowski S.S.Strong C.M.Grewal N.Goyea E.Hou S.Levy A.Martinka S.Mead K.McLellan M.D.Meyer R.Randall-Maher J.Tomlinson C.Dauphin-Kohlberg S.Kozlowicz-Reilly A.Shah N.Swearengen-Shahid S.Snider J.Strong J.T.Thompson J.Yoakum M.Leonard S.Pearman C.Trani L.Radionenko M.Waligorski J.E.Wang C.Rock S.M.Tin-Wollam A.-M.Maupin R.Latreille P.Wendl M.C.Yang S.-P.Pohl C.Wallis J.W.Spieth J.Bieri T.A.Berkowicz N.Nelson J.O.Osborne J.Ding L.Meyer R.'Sabo A.Shotland Y.Sinha P.Wohldmann P.E.Cook L.L.Hickenbotham M.T.Eldred J.Williams D.Jones T.A.She X.Ciccarelli F.D.Izaurralde E.Taylor J.Schmutz J.Myers R.M.Cox D.R.Huang X.McPherson J.D.Mardis E.R.Clifton S.W.Warren W.C.Chinwalla A.T.Eddy S.R.Marra M.A.Ovcharenko I.Furey T.S.Miller W.Eichler E.E.Bork P.Suyama M.Torrents D.Waterston R.H.Wilson R.K.doi:10.1038/nature034662005Nature434724-731NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)VARIANT GLN-509CerebellumPhosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals.Ricotta D.Conner S.D.Schmid S.L.von Figura K.Honing S.doi:10.1083/jcb.2001110682002J. Cell Biol.156791-795FUNCTIONCATALYTIC ACTIVITYIdentification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis.Conner S.D.Schmid S.L.doi:10.1083/jcb.2001081232002J. Cell Biol.156921-929FUNCTIONCATALYTIC ACTIVITYSUBCELLULAR LOCATIONDifferential requirements for AP-2 in clathrin-mediated endocytosis.Conner S.D.Schmid S.L.doi:10.1083/jcb.2003040692003J. Cell Biol.162773-779FUNCTIONCATALYTIC ACTIVITYINTERACTION WITH AP-2MUTAGENESIS OF LYS-74 AND ASP-176AAK1-mediated micro2 phosphorylation is stimulated by assembled clathrin.Conner S.D.Schroter T.Schmid S.L.doi:10.1046/j.1398-9219.2003.0142.x2003Traffic4885-890FUNCTIONCATALYTIC ACTIVITYACTIVITY REGULATIONINTERACTION WITH CLATHRIN AND AP-2Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V.Blagoev B.Gnad F.Macek B.Kumar C.Mortensen P.Mann M.doi:10.1016/j.cell.2006.09.0262006Cell127635-648IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaA probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A.Villen J.Gerber S.A.Rush J.Gygi S.P.doi:10.1038/nbt12402006Nat. Biotechnol.241285-1292PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T.Yi W.Lu B.Park S.K.Xu T.Lee J.-D.Yates J.R. IIIdoi:10.1021/pr07054412008J. Proteome Res.71346-1351PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.Carrascal M.Ovelleiro D.Casas V.Gay M.Abian J.doi:10.1021/pr800500r2008J. Proteome Res.75167-5176PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]T-cellKinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H.Olsen J.V.Bairlein M.Gnad F.Oppermann F.S.Korner R.Greff Z.Keri G.Stemmann O.Mann M.doi:10.1016/j.molcel.2008.07.0072008Mol. Cell31438-448PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-441; SER-637 AND SER-731IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A quantitative atlas of mitotic phosphorylation.Dephoure N.Zhou C.Villen J.Beausoleil S.A.Bakalarski C.E.Elledge S.J.Gygi S.P.doi:10.1073/pnas.08051391052008Proc. Natl. Acad. Sci. U.S.A.10510762-10767PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234; SER-235; THR-389; THR-606; THR-620; SER-623; SER-624 AND SER-637IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]AAK1 regulates Numb function at an early step in clathrin-mediated endocytosis.Sorensen E.B.Conner S.D.doi:10.1111/j.1600-0854.2008.00790.x2008Traffic91791-1800FUNCTIONCATALYTIC ACTIVITYINTERACTION WITH NUMBMUTAGENESIS OF LYS-74 AND ASP-176Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S.Helbig A.O.Slijper M.Krijgsveld J.Heck A.J.Mohammed S.doi:10.1021/ac90043092009Anal. Chem.814493-4501IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Large-scale proteomics analysis of the human kinome.Oppermann F.S.Gnad F.Olsen J.V.Hornberger R.Greff Z.Keri G.Mann M.Daub H.doi:10.1074/mcp.m800588-mcp2002009Mol. Cell. Proteomics81751-1764PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-354; THR-389; SER-637; SER-650; TYR-687 AND SER-731IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V.Lundgren D.H.Hwang S.-I.Rezaul K.Wu L.Eng J.K.Rodionov V.Han D.K.doi:10.1126/scisignal.20000072009Sci. Signal.2RA46PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-606; SER-637 AND THR-653IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Leukemic T-cellQuantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V.Vermeulen M.Santamaria A.Kumar C.Miller M.L.Jensen L.J.Gnad F.Cox J.Jensen T.S.Nigg E.A.Brunak S.Mann M.doi:10.1126/scisignal.20004752010Sci. Signal.3RA3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620; SER-623; SER-624 AND SER-637IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]The adaptor-associated kinase 1, AAK1, is a positive regulator of the Notch pathway.Gupta-Rossi N.Ortica S.Meas-Yedid V.Heuss S.Moretti J.Olivo-Marin J.C.Israel A.doi:10.1074/jbc.m110.1907692011J. Biol. Chem.28618720-18730FUNCTIONINTERACTION WITH EPS15 AND NOTCH1MUTAGENESIS OF LYS-74 AND 777-ASP--PHE-779System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T.Prokhorova T.A.Akimov V.Henningsen J.Johansen P.T.Kratchmarova I.Kassem M.Mann M.Olsen J.V.Blagoev B.doi:10.1126/scisignal.20015702011Sci. Signal.4RS3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; THR-620; SER-624 AND SER-637IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P.Lasa M.Polevoda B.Gazquez C.Elosegui-Artola A.Kim D.S.De Juan-Pardo E.Demeyer K.Hole K.Larrea E.Timmerman E.Prieto J.Arnesen T.Sherman F.Gevaert K.Aldabe R.doi:10.1073/pnas.12103031092012Proc. Natl. Acad. Sci. U.S.A.10912449-12454ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-606; THR-620 AND SER-637IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y.Song C.Cheng K.Dong M.Wang F.Huang J.Sun D.Wang L.Ye M.Zou H.doi:10.1016/j.jprot.2013.11.0142014J. Proteomics96253-262PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverAP-2-associated protein kinase 1 and cyclin G-associated kinase regulate hepatitis C virus entry and are potential drug targets.Neveu G.Ziv-Av A.Barouch-Bentov R.Berkerman E.Mulholland J.Einav S.doi:10.1128/jvi.02705-142015J. Virol.894387-4404FUNCTION (MICROBIAL INFECTION)Family-wide Structural Analysis of Human Numb-Associated Protein Kinases.Sorrell F.J.Szklarz M.Abdul Azeez K.R.Elkins J.M.Knapp S.doi:10.1016/j.str.2015.12.0152016Structure24401-411X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-345 IN COMPLEX WITH INHIBITORCATALYTIC ACTIVITYCrystal Structure of Adaptor Protein 2 Associated Kinase (AAK1) in complex with BIBF 1120.Counago R.M.Elkins J.M.Arrowsmith C.H.Bountra C.Arruda P.Edwards A.M.Gileadi O.2016-09PDBX-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-365Synthesis and Structure-Activity Relationships of 3,5-Disubstituted-pyrrolo[2,3- b]pyridines as Inhibitors of Adaptor-Associated Kinase 1 with Antiviral Activity.Verdonck S.Pu S.Y.Sorrell F.J.Elkins J.M.Froeyen M.Gao L.J.Prugar L.I.Dorosky D.E.Brannan J.M.Barouch-Bentov R.Knapp S.Dye J.M.Herdewijn P.Einav S.De Jonghe S.doi:10.1021/acs.jmedchem.9b001362019J. Med. Chem.625810-5831X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 27-365CATALYTIC ACTIVITYPatterns of somatic mutation in human cancer genomes.Greenman C.Stephens P.Smith R.Dalgliesh G.L.Hunter C.Bignell G.Davies H.Teague J.Butler A.Stevens C.Edkins S.O'Meara S.Vastrik I.Schmidt E.E.Avis T.Barthorpe S.Bhamra G.Buck G.Choudhury B.Clements J.Cole J.Dicks E.Forbes S.Gray K.Halliday K.Harrison R.Hills K.Hinton J.Jenkinson A.Jones D.Menzies A.Mironenko T.Perry J.Raine K.Richardson D.Shepherd R.Small A.Tofts C.Varian J.Webb T.West S.Widaa S.Yates A.Cahill D.P.Louis D.N.Goldstraw P.Nicholson A.G.Brasseur F.Looijenga L.Weber B.L.Chiew Y.-E.DeFazio A.Greaves M.F.Green A.R.Campbell P.Birney E.Easton D.F.Chenevix-Trench G.Tan M.-H.Khoo S.K.Teh B.T.Yuen S.T.Leung S.Y.Wooster R.Futreal P.A.Stratton M.R.doi:10.1038/nature056102007Nature446153-158VARIANTS [LARGE SCALE ANALYSIS] VAL-59; HIS-533; ALA-603; MET-694; THR-725; ARG-771 AND ASP-835Different initiation.1.95A/B=29-3451.97A/B=27-3651.90A=27-3652.50A/B=26-3302.20A/B=26-33011155Fostamatinib7 sites, 2 glycans11 sites, 2 O-linked glycans (11 sites)399 antibodies from 39 providershumanAAK1Tissue enhanced (parathyroid)geneEukaryotaCargo recognition for clathrin-mediated endocytosisClathrin-mediated endocytosis23 hits in 1189 CRISPR screenshumanTchemProteinExpressed in lateral nuclear group of thalamus and 215 other cell types or tissuesbaseline and differentialSTKc_NAK_likeTransferase(Phosphotransferase) domain 1Kinase-like_dom_sfProt_kinase_domSer/Thr_kinase_ASAP2-ASSOCIATED PROTEIN KINASE 1PROTEIN KINASE DOMAIN-CONTAINING PROTEINPkinaseS_TKcProtein kinase-like (PK-like)PROTEIN_KINASE_DOMPROTEIN_KINASE_STHSAP2-associated protein kinase 12.7.11.1Adaptor-associated kinase 1AAK1KIAA1048Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis (PubMed:17494869, PubMed:11877457, PubMed:11877461, PubMed:12952931, PubMed:14617351, PubMed:25653444). Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1 (PubMed:17494869). Preferentially, may phosphorylate substrates on threonine residues (PubMed:11877457, PubMed:18657069). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (PubMed:12952931). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (PubMed:18657069). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (PubMed:21464124).(Microbial infection) By regulating clathrin-mediated endocytosis, AAK1 plays a role in the entry of hepatitis C virus as well as for the lifecycle of other viruses such as Ebola and Dengue.Stimulated by clathrin.Interacts (via CBD domain) with clathrin (PubMed:17494869, PubMed:14617351). Interacts with AP-2 complex (PubMed:17494869, PubMed:12952931, PubMed:14617351). Interacts with NUMB (PubMed:18657069). Interacts with alpha-adaptin (By similarity). Interacts with EPS15 isoform 2 (PubMed:21464124). Interacts with membrane-bound activated NOTCH1 but not with the inactive full-length form of NOTCH1 (PubMed:21464124). Preferentially interacts with monoubiquitinated activated NOTCH1 compared to the non-ubiquitinated form (PubMed:21464124).Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells.Detected in brain, heart and liver. Isoform 1 is the predominant isoform in brain.Autophosphorylated.By regulating the entry of hepatitis C virus as well as the lifecycle of other viruses such as Ebola and Dengue, AAK1 is a potential drug target for developing antiviral therapies.Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.Extended N-terminus.AP2-associated protein kinase 11038851961Protein kinase46315Disordered25Disordered327493Disordered562632Disordered664701Clathrin-binding domain (CBD)823960Disordered836860Disordered921945Polar residues353382Polar residues399414Pro residues416443Polar residues444Polar residues577Polar residues598627Polar residues843Polar residues929Proton acceptor176526074N-acetylmethioninePhosphoserine14Phosphotyrosine234Phosphoserine235Phosphothreonine354Phosphothreonine389Omega-N-methylarginine391Phosphothreonine441Phosphothreonine606Phosphoserine618Phosphothreonine620Phosphoserine623Phosphoserine624Phosphoserine637Phosphoserine650Phosphothreonine653Phosphotyrosine687Phosphoserine731Phosphoserine846Phosphoserine937Phosphoserine938In isoform 2.GKVIISVSSVMHDMCACFKNDKYLVNQSLGNSPATPEAKAIV59Q509H533A603M694T725R771D835Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1.AInhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization.ADoes not affect interaction with NOTCH1 but abolishes interaction with ESP15.AAA777779313438414455586470788197106113116118120127134139142144148167168170179181182184190192205208210220223225228231242257261264266271284293298300304339344false2ATP13A22010-07-1331038856e5509ded394c629acb1714a5c491f9c1AAK1LMKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL2AAK1SMKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIGKVIISVSSVMHDMCACFKNDKYLVNQSLGNSPATPEAKAItruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue