true2008-02-052024-03-27170SET1B_HUMANRbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via a SPOC domain that is required for cytokine-independent proliferation.Lee J.H.Skalnik D.G.doi:10.1371/journal.pone.00429652012PLoS ONE7E42965NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)INTERACTION WITH RBM15MUTAGENESIS OF LEU-577 AND ASP-579The finished DNA sequence of human chromosome 12.Scherer S.E.Muzny D.M.Buhay C.J.Chen R.Cree A.Ding Y.Dugan-Rocha S.Gill R.Gunaratne P.Harris R.A.Hawes A.C.Hernandez J.Hodgson A.V.Hume J.Jackson A.Khan Z.M.Kovar-Smith C.Lewis L.R.Lozado R.J.Metzker M.L.Milosavljevic A.Miner G.R.Montgomery K.T.Morgan M.B.Nazareth L.V.Scott G.Sodergren E.Song X.-Z.Steffen D.Lovering R.C.Wheeler D.A.Worley K.C.Yuan Y.Zhang Z.Adams C.Q.Ansari-Lari M.A.Ayele M.Brown M.J.Chen G.Chen Z.Clerc-Blankenburg K.P.Davis C.Delgado O.Dinh H.H.Draper H.Gonzalez-Garay M.L.Havlak P.Jackson L.R.Jacob L.S.Kelly S.H.Li L.Li Z.Liu J.Liu W.Lu J.Maheshwari M.Nguyen B.-V.Okwuonu G.O.Pasternak S.Perez L.M.Plopper F.J.H.Santibanez J.Shen H.Tabor P.E.Verduzco D.Waldron L.Wang Q.Williams G.A.Zhang J.Zhou J.Allen C.C.Amin A.G.Anyalebechi V.Bailey M.Barbaria J.A.Bimage K.E.Bryant N.P.Burch P.E.Burkett C.E.Burrell K.L.Calderon E.Cardenas V.Carter K.Casias K.Cavazos I.Cavazos S.R.Ceasar H.Chacko J.Chan S.N.Chavez D.Christopoulos C.Chu J.Cockrell R.Cox C.D.Dang M.Dathorne S.R.David R.Davis C.M.Davy-Carroll L.Deshazo D.R.Donlin J.E.D'Souza L.Eaves K.A.Egan A.Emery-Cohen A.J.Escotto M.Flagg N.Forbes L.D.Gabisi A.M.Garza M.Hamilton C.Henderson N.Hernandez O.Hines S.Hogues M.E.Huang M.Idlebird D.G.Johnson R.Jolivet A.Jones S.Kagan R.King L.M.Leal B.Lebow H.Lee S.LeVan J.M.Lewis L.C.London P.Lorensuhewa L.M.Loulseged H.Lovett D.A.Lucier A.Lucier R.L.Ma J.Madu R.C.Mapua P.Martindale A.D.Martinez E.Massey E.Mawhiney S.Meador M.G.Mendez S.Mercado C.Mercado I.C.Merritt C.E.Miner Z.L.Minja E.Mitchell T.Mohabbat F.Mohabbat K.Montgomery B.Moore N.Morris S.Munidasa M.Ngo R.N.Nguyen N.B.Nickerson E.Nwaokelemeh O.O.Nwokenkwo S.Obregon M.Oguh M.Oragunye N.Oviedo R.J.Parish B.J.Parker D.N.Parrish J.Parks K.L.Paul H.A.Payton B.A.Perez A.Perrin W.Pickens A.Primus E.L.Pu L.-L.Puazo M.Quiles M.M.Quiroz J.B.Rabata D.Reeves K.Ruiz S.J.Shao H.Sisson I.Sonaike T.Sorelle R.P.Sutton A.E.Svatek A.F.Svetz L.A.Tamerisa K.S.Taylor T.R.Teague B.Thomas N.Thorn R.D.Trejos Z.Y.Trevino B.K.Ukegbu O.N.Urban J.B.Vasquez L.I.Vera V.A.Villasana D.M.Wang L.Ward-Moore S.Warren J.T.Wei X.White F.Williamson A.L.Wleczyk R.Wooden H.S.Wooden S.H.Yen J.Yoon L.Yoon V.Zorrilla S.E.Nelson D.Kucherlapati R.Weinstock G.Gibbs R.A.doi:10.1038/nature045692006Nature440346-351NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Prediction 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] OF 1163-1966 (ISOFORM 1/2)BrainIdentification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex.Lee J.-H.Tate C.M.You J.-S.Skalnik D.G.doi:10.1074/jbc.m6098092002007J. Biol. Chem.28213419-13428FUNCTIONCATALYTIC ACTIVITYSUBCELLULAR LOCATIONIDENTIFICATION IN THE SET1 COMPLEXWdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes.Lee J.H.Skalnik D.G.doi:10.1128/mcb.01356-072008Mol. Cell. Biol.28609-618IDENTIFICATION IN SET1 COMPLEXINTERACTION WITH WDR82; ASH2L AND POLR2AMolecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS.Wu M.Wang P.F.Lee J.S.Martin-Brown S.Florens L.Washburn M.Shilatifard A.doi:10.1128/mcb.00976-082008Mol. Cell. Biol.287337-7344IDENTIFICATION IN SET1 COMPLEXA 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.10510762-10767IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaQuantitative 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 SER-1659IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Leukemic T-cellToward 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-986; SER-994 AND SER-1031IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaQuantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes.van Nuland R.Smits A.H.Pallaki P.Jansen P.W.Vermeulen M.Timmers H.T.doi:10.1128/mcb.01742-122013Mol. Cell. Biol.332067-2077IDENTIFICATION IN SET1B COMPLEXAn 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 SER-1335IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverBiochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation.Shinsky S.A.Monteith K.E.Viggiano S.Cosgrove M.S.doi:10.1074/jbc.m114.6276462015J. Biol. Chem.2906361-6375FUNCTIONCATALYTIC ACTIVITYSUBUNITMUTAGENESIS OF ASN-1905A novel de novo frameshift variant in SETD1B causes epilepsy.Den K.Kato M.Yamaguchi T.Miyatake S.Takata A.Mizuguchi T.Miyake N.Mitsuhashi S.Matsumoto N.doi:10.1038/s10038-019-0617-12019J. Hum. Genet.64821-827INVOLVEMENT IN IDDSELDIn Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F).Amin H.M.Szabo B.Abukhairan R.Zeke A.Kardos J.Schad E.Tantos A.doi:10.3390/ijms2422160322023Int. J. Mol. Sci.2416032SUBCELLULAR LOCATIONStructural basis for WDR5 interaction (Win) motif recognition in human SET1 family histone methyltransferases.Dharmarajan V.Lee J.H.Patel A.Skalnik D.G.Cosgrove M.S.doi:10.1074/jbc.m112.3641252012J. Biol. Chem.28727275-27289X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1741-1754 IN COMPLEX WITH WDR5INTERACTION WITH WDR5MOTIF WINThe plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.Zhang P.Lee H.Brunzelle J.S.Couture J.F.doi:10.1093/nar/gkr12352012Nucleic Acids Res.404237-4246X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1745-1755 IN COMPLEX WITH WDR5INTERACTION WITH WDR5MOTIF WINMolecular insight into the SETD1A/B N-terminal region and its interaction with WDR82.Bao S.Xu C.doi:10.1016/j.bbrc.2023.03.0642023Biochem. Biophys. Res. Commun.658136-140X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 102-204INTERACTION WITH WDR82De novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.Hiraide T.Nakashima M.Yamoto K.Fukuda T.Kato M.Ikeda H.Sugie Y.Aoto K.Kaname T.Nakabayashi K.Ogata T.Matsumoto N.Saitsu H.doi:10.1007/s00439-017-1863-y2018Hum. Genet.13795-104VARIANTS IDDSELD TRP-1885 AND CYS-1902INVOLVEMENT IN IDDSELDA genome-wide DNA methylation signature for SETD1B-related syndrome.Krzyzewska I.M.Maas S.M.Henneman P.Lip K.V.D.Venema A.Baranano K.Chassevent A.Aref-Eshghi E.van Essen A.J.Fukuda T.Ikeda H.Jacquemont M.Kim H.G.Labalme A.Lewis S.M.E.Lesca G.Madrigal I.Mahida S.Matsumoto N.Rabionet R.Rajcan-Separovic E.Qiao Y.Sadikovic B.Saitsu H.Sweetser D.A.Alders M.Mannens M.M.A.M.doi:10.1186/s13148-019-0749-32019Clin. Epigenetics11156VARIANTS IDDSELD TRP-1885 AND CYS-1902De novo variants in SETD1B cause intellectual disability, autism spectrum disorder, and epilepsy with myoclonic absences.Hiraide T.Hattori A.Ieda D.Hori I.Saitoh S.Nakashima M.Saitsu H.doi:10.1002/epi4.123392019Epilepsia Open4476-481VARIANT IDDSELD GLY-129SETD1B-associated neurodevelopmental disorder.Roston A.Evans D.Gill H.McKinnon M.Isidor B.Cogne B.Mwenifumbo J.van Karnebeek C.An J.Jones S.J.M.Farrer M.Demos M.Connolly M.Gibson W.T.CAUSES StudyEPGEN Studydoi:10.1136/jmedgenet-2019-1067562021J. Med. Genet.58196-204VARIANTS IDDSELD 978-GLN--ASN-1966 DEL; 1322-GLN--ASN-1966 DEL AND LEU-19452.20B=1745-17551.82C=1741-17541.77A=102-20471Histone-lysine N-methyltransferase complex, SET1B variant201 site, 1 glycan3 sites, 1 O-linked glycan (3 sites)144 antibodies from 26 providershumanSETD1BLow tissue specificitygenephenotypeAutosomal dominant non-syndromic intellectual disabilityEukaryotaPKMTs methylate histone lysinesRUNX1 regulates genes involved in megakaryocyte differentiation and platelet functionFormation of WDR5-containing histone-modifying complexes129 hits in 1180 CRISPR screensTbioProteinExpressed in blood vessel layer and 205 other cell types or tissuesbaseline and differentialRRM_Set1BSET_SETD1SET domainCOMPASS_Set1_N-SETNucleotide-bd_a/b_plait_sfPost-SET_domRBD_domain_sfRRM_domSet1-likeSet1B_RRMSET_domSET_dom_sfSET_SETD1A/BHISTONE-LYSINE N-METHYLTRANSFERASE SETD1HISTONE-LYSINE N-METHYLTRANSFERASE SETD1BN-SETRRM_1SETN-SETPostSETRRMSETRNA-binding domain, RBDSET domainPOST_SETRRMSETHSHistone-lysine N-methyltransferase SETD1B2.1.1.364Lysine N-methyltransferase 2GSET domain-containing protein 1BhSET1BSETD1BKIAA1076KMT2GSET1BHistone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:25561738, PubMed:17355966). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:25561738, PubMed:17355966). Plays an essential role in regulating the transcriptional programming of multipotent hematopoietic progenitor cells and lymphoid lineage specification during hematopoiesis (By similarity).Component of the SET1B/COMPASS complex composed of the catalytic subunit SETD1B, WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1, DPY30 homotrimer and BOD1 (PubMed:23508102, PubMed:17355966, PubMed:18838538). Forms a core complex with the evolutionary conserved subcomplex WRAD composed of WDR5, RBBP5, ASH2L/ASH2 and DPY30 subunits; WRAD differentially stimulates the methyltransferase activity (PubMed:25561738). Interacts with HCFC1 and ASH2L/ASH2 (PubMed:17998332). Interacts (via N-terminal region) with WDR82 (PubMed:37030068, PubMed:17998332). Interacts (via the RRM domain) with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) only in the presence of WDR82 (PubMed:17998332). Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. Interacts with RBM15 (PubMed:22927943). Interacts (via WIN motif) with WDR5 (PubMed:22665483, PubMed:22266653).Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1A, suggesting that SETD1A and SET1B each bind to a unique set of target genes (PubMed:17355966) (Probable). Predominantly nuclear (PubMed:38003223).The disease is caused by variants affecting the gene represented in this entry.Belongs to the class V-like SAM-binding methyltransferase superfamily.Histone-lysine N-methyltransferase SETD1B21280311966RRM93181SET18271944Post-SET1950Disordered26Interaction with WDR826898Disordered235302Disordered357660Disordered675719Disordered9631462Disordered15011541Disordered15551606Disordered16361668Disordered1767180011731204WDR5 interaction motif (WIN)17451750RxxxRR motif17981803Polar residues366382Pro residues431461Basic and acidic residues493525Polar residues527573Pro residues676Basic and acidic residues9981041Polar residues10421064Acidic residues10691088Acidic residues11031141Polar residues11461171Acidic residues11721198Basic and acidic residues12941311Pro residues13131359Pro residues1516Pro residues15781603Basic and acidic residues1655Polar residues17891943Phosphoserine986Phosphoserine994Phosphoserine1031Phosphoserine1265Phosphoserine1283Phosphoserine1335Phosphoserine1659Phosphoserine1663In isoform 2.10431068In isoform 2.1104In IDDSELD.G129In IDDSELD.978In IDDSELD.1322In IDDSELD.W1885In IDDSELD.C1902In IDDSELD.L1945Abolishes interaction with RBM15.A577Abolishes interaction with RBM15.A579Abolishes interaction with S-adenosyl-L-methionine.A19051747false2ASH2L2014-03-19321280336b20f85963131c1e71ec5cd2af519941MENSHPPHHHHQQPPPQPGPSGERRNHHWRSYKLMIDPALKKGHHKLYRYDGQHFSLAMSSNRPVEIVEDPRVVGIWTKNKELELSVPKFKIDEFYVGPVPPKQVTFAKLNDNIRENFLRDMCKKYGEVEEVEILYNPKTKKHLGIAKVVFATVRGAKDAVQHLHSTSVMGNIIHVELDTKGETRMRFYELLVTGRYTPQTLPVGELDAVSPIVNETLQLSDALKRLKDGGLSAGCGSGSSSVTPNSGGTPFSQDTAYSSCRLDTPNSYGQGTPLTPRLGTPFSQDSSYSSRQPTPSYLFSQDPAVTFKARRHESKFTDAYNRRHEHHYVHNSPAVTAVAGATAAFRGSSDLPFGAVGGTGGSSGPPFKAQPQDSATFAHTPPPAQATPAPGFKSAFSPYQTPVAHFPPPPEEPTATAAFGARDSGEFRRAPAPPPLPPAEPLAKEKPGTPPGPPPPDTNSMELGGRPTFGWSPEPCDSPGTPTLESSPAGPEKPHDSLDSRIEMLLKEQRTKLLFLREPDSDTELQMEGSPISSSSSQLSPLAPFGTNSQPGFRGPTPPSSRPSSTGLEDISPTPLPDSDEDEELDLGLGPRPPPEPGPPDPAGLLSQTAEVALDLVGDRTPTSEKMDEGQQSSGEDMEISDDEMPSAPITSADCPKPMVVTPGAAAVAAPSVLAPTLPLPPPPGFPPLPPPPPPPPPQPGFPMPPPLPPPPPPPPPAHPAVTVPPPPLPAPPGVPPPPILPPLPPFPPGLFPVMQVDMSHVLGGQWGGMPMSFQMQTQVLSRLMTGQGACPYPPFMAAAAAAASAGLQFVNLPPYRGPFSLSNSGPGRGQHWPPLPKFDPSVPPPGYMPRQEDPHKATVDGVLLVVLKELKAIMKRDLNRKMVEVVAFRAFDEWWDKKERMAKASLTPVKSGEHKDEDRPKPKDRIASCLLESWGKGEGLGYEGLGLGIGLRGAIRLPSFKVKRKEPPDTTSSGDQKRLRPSTSVDEEDEESERERDRDMADTPCELAKRDPKGVGVRRRPARPLELDSGGEEDEKESLSASSSSSASSSSGSSTTSPSSSASDKEEEQESTEEEEEAEEEEEEEVPRSQLSSSSTSSTSDKDDDDDDSDDRDESENDDEDTALSEASEKDEGDSDEEETVSIVTSKAEATSSSESSESSEFESSSESSPSSSEDEEEVVAREEEEEEEEEEMVAEESMASAGPEDFEQDGEEAALAPGAPAVDSLGMEEEVDIETEAVAPEERPSMLDEPPLPVGVEEPADSREPPEEPGLSQEGAMLLSPEPPAKEVEARPPLSPERAPEHDLEVEPEPPMMLPLPLQPPLPPPRPPRPPSPPPEPETTDASHPSVPPEPLAEDHPPHTPGLCGSLAKSQSTETVPATPGGEPPLSGGSSGLSLSSPQVPGSPFSYPAPSPSLSSGGLPRTPGRDFSFTPTFSEPSGPLLLPVCPLPTGRRDERSGPLASPVLLETGLPLPLPLPLPLPLALPAVLRAQARAPTPLPPLLPAPLASCPPPMKRKPGRPRRSPPSMLSLDGPLVRPPAGAALGRELLLLPGQPQTPVFPSTHDPRTVTLDFRNAGIPAPPPPLPPQPPPPPPPPPVEPTKLPFKELDNQWPSEAIPPGPRGRDEVTEEYMELAKSRGPWRRPPKKRHEDLVPPAGSPELSPPQPLFRPRSEFEEMTILYDIWNGGIDEEDIRFLCVTYERLLQQDNGMDWLNDTLWVYHPSTSLSSAKKKKRDDGIREHVTGCARSEGFYTIDKKDKLRYLNSSRASTDEPPADTQGMSIPAQPHASTRAGSERRSEQRRLLSSFTGSCDSDLLKFNQLKFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLN2MENSHPPHHHHQQPPPQPGPSGERRNHHWRSYKLMIDPALKKGHHKLYRYDGQHFSLAMSSNRPVEIVEDPRVVGIWTKNKELELSVPKFKIDEFYVGPVPPKQVTFAKLNDNIRENFLRDMCKKYGEVEEVEILYNPKTKKHLGIAKVVFATVRGAKDAVQHLHSTSVMGNIIHVELDTKGETRMRFYELLVTGRYTPQTLPVGELDAVSPIVNETLQLSDALKRLKDGGLSAGCGSGSSSVTPNSGGTPFSQDTAYSSCRLDTPNSYGQGTPLTPRLGTPFSQDSSYSSRQPTPSYLFSQDPAVTFKARRHESKFTDAYNRRHEHHYVHNSPAVTAVAGATAAFRGSSDLPFGAVGGTGGSSGPPFKAQPQDSATFAHTPPPAQATPAPGFKSAFSPYQTPVAHFPPPPEEPTATAAFGARDSGEFRRAPAPPPLPPAEPLAKEKPGTPPGPPPPDTNSMELGGRPTFGWSPEPCDSPGTPTLESSPAGPEKPHDSLDSRIEMLLKEQRTKLLFLREPDSDTELQMEGSPISSSSSQLSPLAPFGTNSQPGFRGPTPPSSRPSSTGLEDISPTPLPDSDEDEELDLGLGPRPPPEPGPPDPAGLLSQTAEVALDLVGDRTPTSEKMDEGQQSSGEDMEISDDEMPSAPITSADCPKPMVVTPGAAAVAAPSVLAPTLPLPPPPGFPPLPPPPPPPPPQPGFPMPPPLPPPPPPPPPAHPAVTVPPPPLPAPPGVPPPPILPPLPPFPPGLFPVMQVDMSHVLGGQWGGMPMSFQMQTQVLSRLMTGQGACPYPPFMAAAAAAASAGLQFVNLPPYRGPFSLSNSGPGRGQHWPPLPKFDPSVPPPGYMPRQEDPHKATVDGVLLVVLKELKAIMKRDLNRKMVEVVAFRAFDEWWDKKERMAKASLTPVKSGEHKDEDRPKPKDRIASCLLESWGKGEGLGYEGLGLGIGLRGAIRLPSFKVKRKEPPDTTSSGDQKRLRPSTSVDEEDEESERERDRDMADTPCELAKRDPKGVGVRRRPARPLELDSGGEEDEKESLSEEQESTEEEEEAEEEEEEEDDDDDDSDDRDESENDDEDTALSEASEKDEGDSDEEETVSIVTSKAEATSSSESSESSEFESSSESSPSSSEDEEEVVAREEEEEEEEEEMVAEESMASAGPEDFEQDGEEAALAPGAPAVDSLGMEEEVDIETEAVAPEERPSMLDEPPLPVGVEEPADSREPPEEPGLSQEGAMLLSPEPPAKEVEARPPLSPERAPEHDLEVEPEPPMMLPLPLQPPLPPPRPPRPPSPPPEPETTDASHPSVPPEPLAEDHPPHTPGLCGSLAKSQSTETVPATPGGEPPLSGGSSGLSLSSPQVPGSPFSYPAPSPSLSSGGLPRTPGRDFSFTPTFSEPSGPLLLPVCPLPTGRRDERSGPLASPVLLETGLPLPLPLPLPLPLALPAVLRAQARAPTPLPPLLPAPLASCPPPMKRKPGRPRRSPPSMLSLDGPLVRPPAGAALGRELLLLPGQPQTPVFPSTHDPRTVTLDFRNAGIPAPPPPLPPQPPPPPPPPPVEPTKLPFKELDNQWPSEAIPPGPRGRDEVTEEYMELAKSRGPWRRPPKKRHEDLVPPAGSPELSPPQPLFRPRSEFEEMTILYDIWNGGIDEEDIRFLCVTYERLLQQDNGMDWLNDTLWVYHPSTSLSSAKKKKRDDGIREHVTGCARSEGFYTIDKKDKLRYLNSSRASTDEPPADTQGMSIPAQPHASTRAGSERRSEQRRLLSSFTGSCDSDLLKFNQLKFRKKKLKFCKSHIHDWGLFAMEPIAADEMVIEYVGQNIRQVIADMREKRYEDEGIGSSYMFRVDHDTIIDATKCGNFARFINHSCNPNCYAKVITVESQKKIVIYSKQHINVNEEITYDYKFPIEDVKIPCLCGSENCRGTLNtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue