Processing of Capped Intron-Containing Pre-mRNA (Homo sapiens)

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ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none nucleoplasmcytosolTRA2BXAB2Mature IntronlessTranscript DerivedmRNA:eIF4E ComplexCstFpost exon ligationcomplexU4 ATAC snRNPATAC C Complex withlariat containing5'-end cleaved mRNANXF1,2:NXT1SUGP1ALYREF, FYTTD1,LUZP4Cleavage andPolyadenylationComplexSNRNP27EIF4A3SARNPMature IntronlessTranscript DerivedHistonemRNA:TAP:Aly/RefComplexCHTOPHNRNPDCWC27ZRSR2DDX5PiAQRNPC:NXF1:NXT1:EJC:CBC:mRNADHX38SNW1RBM22SRSF1NCBP2capped, methylatedpre-mRNP:CBCcomplexU6 ATAC snRNPcapped, methylatedpre-mRNA:CBCComplexELAVL1Nucleoplasmic matureintronless derivedmRNA:TAP:Aly/RefcomplexHNRNPA2B1DHX16CWC27NXF1Spliceosomal EComplexCHTOPU12 snRNPMature intronlessderived mRNAcomplexELAVL2CstFPPWD1SRRM1:SRRM2SF3BNXF1NCBP1ALYREF, FYTTD1,LUZP4BUD31SF1SF3APTBP1U4 ATAC:U5:U6 ATACComplexHNRNPUL1PPILHNRNPH1PRPF40AHNRNPUCASC3CWC25DHX9ALYREFSpliceosomal ActiveC (B*) ComplexFUSTHO complexPABPN1NXF1,2:NXT1::polyadenylated, capped mRNA:CBC:EJC:TREX:SRSF proteinsSRSF4HNRNPA1Mature intronlesstranscript derivedHistonepre-mRNA:CBCcomplexATPSRSF11SRSF10USP39SRSF9CPSFCPSFPCBP1LSM2-8 complexmRNA 3'-end cleavagefactorSRRTmRNA:CBC:EJC:POLDIP3ISY1GPKOWSpliceosomalIntermediate C(Bact) Complexpre-EJC:SpliceosomalC:pre-mRNP:CBCPPIEMatureIntronlesstranscriptderivedHistonemRNA:SLBP:CBP80:CBP20PAPOLA3' end cleaved,ligated exoncontaining complexU2AF1,U2AF1L4ALYREFNXF1HNRNPLSART1CF IU4 snRNPRNApolymeraseII(phosphorylated):TFIIF complexSpliceosomal AComplexU5 snRNPATPNuclear Pore Complex(NPC)ALYREFHNRNPKPRP19-CDC5L complexGLE1PRCCCRNKL1EIF4EWBP4Spliced mRNPU2 snRNPintron-containingcomplexDNAJC8U4:U5:U6 tri-snRNPcomplexCF IIZC3H11ASpliceosomal activeC complex withlariat containing,5'-end cleavedpre-mRNP:CBCcomplexCD2BP2Mature IntronlessTranscript DerivedHistonemRNA:TAP:Aly/RefcomplexRBMXMature intronlesstranscript derivedHistonemRNA:SLBP:eIF4EComplexNPC:NXF1,2:NXT1:EJC:CBC:mRNASARNPMature SLBPindependent HistonemRNA:eIF4E complexATAC B ComplexMatureintronlesstranscriptderivedHistonemRNA:SLBP:TAP:Aly/Ref complexHNRNPA3NXF1,2:NXT1U2AF2HNRNPH2CDC40Mature intronlessderivedmRNA:TAP:Aly/RefcomplexUPF3BhSLU7CWC22RNPS1NXF1cappedpre-mRNA:CBC:RNAPol II(phosphorylated)complexMatureintronlesstranscriptderivedHistonemRNA:SLBP:TAP:Aly/Ref complexhSLU7HNRNPMMagoh-Y14 complexHNRNPCYBX1HNRNPRSRSF2HNRNPFHNRNPA0THO complexRBM5SRSF7PABPN1ATAC A ComplexSRSF3ATAC C ComplexPRPF38ASplicedmRNA:CBC:EJC:TREXZC3H11ASRSF5PAPOLANuclear Pore Complex(NPC)Nuclear Pore Complex(NPC)U11 snRNPCCAR1CF IIU1 snRNPSRSF6POLDIP3DDX39B:ADPDDX39A,BEIF4Epolyadenylated,cappedmRNA:CBC:EJC:TREX:SRSF proteinsCap Binding Complex(CBC)CPSFPCBP2CF ImRNA(N6-adenosine)-methyltransferaseSpliceosomal BComplexSYF2POLR2HZRSR2GTF2F1capped, methylated pre-mRNAPOLR2GPOLR2BPOLR2CNCBP1POLR2JPOLR2DSRSF6POLR2KGTF2F2POLR2FPOLR2LSRSF2mRNA with spliced exonsPOLR2ESRSF1SRSF7POLR2IPOLR2ANCBP2FUSNCBP2CF I - 68 kDa subunitMe2-R108,R112-SNRPNGPKOWFIP1L1HNRNPA3SRSF9SRSF11Me2-R108,R112-SNRPBSRSF3PPIECSTF1AQRGTF2F1UPF3BU2 snRNASNRPA1PPWD1DDX5CF I - 72 kDa subunitHNRNPUPOLR2JTRA2BSNRNP200SF3B5CWC25PPIL1ISY1SRSF7CPSF4SF3B4CD2BP2U6 snRNAHNRNPA2B1CPSF1HNRNPDSF3A1CDC5LEFTUD2SYF2CLP1PRPF6CWC22DHX38DHX9SNRPGGTF2F2BUD31U2AF1L4SRSF6POLR2EBCAS2EIF4A3CSTF2TWBP11PRPF8RBM5PCBP2PAPOLACPSF7SF3B2SRSF1HNRNPFCHERPDHX15HSPA8PRPF19SF3B6U2AF1SRRTPPIL4NHP2L1p-S5-POLR2ADHX16SYMPKHNRNPLPPIL6PCF11U2SURPU2AF2DDX23SNRNP40RBM17XAB2POLR2DYBX1POLR2GCPSF2PCBP1WDR33CSTF3HNRNPCSRSF2SRRM1SRSF5NCBP1RBM8AELAVL1RBMXLSM2SNRPD2CDC40HNRNPRALYREFPOLR2BCSTF2RNPS1HNRNPA0SRSF4SF3A3SNRPEMAGOHBPTBP1CWC15lariat containing 5'-end cleaved mRNAPUF60POLR2FHNRNPH2HNRNPUL1PLRG1NUDT21U5 snRNAPHF5APOLR2LSNRPB22xMe-SNRPD3SF3A2CTNNBL1PQBP1SRRM2POLR2CSF3B1SNRPFTXNL4APOLR2ISUGP1ELAVL2HNRNPMDDX42POLR2KRBM22PPIL3SNW1SF3B3PABPN1HNRNPKHNRNPA1HNRNPH12xMe-SNRPD1CCAR1DDX46CPSF3SMNDC1CRNKL1DNAJC8PRCCPOLR2HMAGOHU5 snRNAMe2-R108,R112-SNRPBSNRNP40DDX23PRPF8TXNL4ASNRPD2EFTUD2SNRPENHP2L12xMe-SNRPD1LSM2PRPF6SNRNP200SNRPF2xMe-SNRPD3SNRPGNCBP1NCBP2NUP98-3SEH1L-1SEH1L-2POM121CNUP54NUP160NUP37SEC13NUP155NUP85NUP188NUP43NUP98-4NUP107NUP88NUP214RAE1NUP133NUP93NUP35AAASNUP153NUP210NUP50POM121NDC1NUP58-2NUP58-1NUP98-5RANBP2NUP62TPRNUPL2NUP205CLP1PCF11THOC2U2AF1L4DDX39BU2AF1MAGOHSRSF5WDR33DHX38ZC3H11APABPN1NCBP2FYTTD1POLDIP3CPSF4MAGOHBTHOC6hSLU7SARNPSRSF1FIP1L1LUZP4THOC1UPF3BSRSF4SRRM1SRSF11RNPS1RBM8APAPOLASRSF3CASC3CHTOPCDC40ALYREFSRSF2DDX39ATHOC5CPSF1SRSF7ATPNCBP1SRSF9U2AF2CPSF3THOC3SRSF6SYMPK3'-end cleaved mRNA with spliced exonsCPSF2EIF4A3THOC7NXF1ALYREFMature intronless transcript derived mRNACLP1PCF11SNRPGDDX42SF3B6Me2-R108,R112-SNRPBSNRPD2RNPC3U12 snRNASNRPFZCRB1SF3B52xMe-SNRPD3ZMAT5SF3B2SF3B4SF3B3SNRPE2xMe-SNRPD1SF3B1EIF4EMature intronless transcript derived Histone mRNAPPIL3PPIL1PPIL4PPIL6Mature intronless transcript derived mRNAFIP1L1CPSF4SYMPKNCBP2NCBP1CPSF1WDR33CPSF3CPSF2EIF4A3RNPS1NCBP1ALYREFNCBP2RBM8AmRNAPOLDIP3MAGOHCASC3UPF3BMAGOHBSRRM1SNRPD2SNRPESNRPF2xMe-SNRPD32xMe-SNRPD1Me2-R108,R112-SNRPBSNRPGU6 ATAC snRNACDC40LUZP4MAGOHBCSTF2SRSF6SRSF11U2AF2THOC3UPF3BSRSF2THOC1SRSF7SRSF3SRSF5RNPS1CPSF7WDR33CSTF3PCF11U2AF1L4NCBP1U2AF1DHX38THOC6hTra2CPSF1RBM8ACHTOPCSTF1CPSF3ZC3H11AmRNA with spliced exonsALYREFFYTTD1CLP1PAPOLANUDT21MAGOHCASC3CF I - 72 kDa subunitTHOC5FIP1L1DDX39BPABPN1SRSF1NCBP2SRRM1SRSF9SARNPCPSF4CPSF2ATPSYMPKTHOC2CSTF2TCF I - 68 kDa subunitSRSF4THOC7hSLU7DDX39APOLDIP3EIF4A3THOC1THOC2THOC6THOC3THOC5THOC7POLR2GPOLR2BPOLR2Kp-S5-POLR2APOLR2JPOLR2HGTF2F1POLR2Ecapped pre-mRNANCBP2POLR2DPOLR2CPOLR2FGTF2F2POLR2LNCBP1POLR2ISNRNP48POLR2HPRPF8SF3B4SF3B6SNRPFSRSF6U6 ATAC snRNASNRNP40POLR2FPOLR2CGTF2F2U11 snRNASNRPGSF3B1NCBP1SNRPD2LSM2U5 snRNASRSF2POLR2ASF3B2PRPF6SNRPERNPC32xMe-SNRPD3SRSF7Me2-R108,R112-SNRPBSNRNP35PDCD7EFTUD2SF3B3POLR2Jcapped, methylated pre-mRNADDX42SNRNP200U4atac snRNAPOLR2ISNRNP25NHP2L1POLR2LU12 snRNA2xMe-SNRPD1ZRSR2POLR2KPOLR2GYBX1POLR2BSF3B5POLR2EZCRB1ZMAT5SRSF1TXNL4AGTF2F1DDX23POLR2DNCBP2CPSF7CF I - 68 kDa subunitPCF11NUDT21CF I - 72 kDa subunitCLP1SNRPD2SNRPGSNRPE2xMe-SNRPD3SNRNP70SNRPF2xMe-SNRPD1U1 snRNASNRPCMe2-R108,R112-SNRPBSNRPAPOLR2GPOLR2HPOLR2BPOLR2EPOLR2CPOLR2JGTF2F2POLR2DPOLR2FPOLR2IPOLR2KPOLR2Acapped, methylated pre-mRNANCBP2POLR2LGTF2F1NCBP1DDX39ADDX39BDHX15SNRPGDDX42SNRPD2SNRPA1SMNDC1SF3B3RBM17SF3A3Me2-R108,R112-SNRPBSF3B5U2SURPSF3B6PUF60U2 snRNA2xMe-SNRPD12xMe-SNRPD3SNRPEMe2-R108,R112-SNRPNSNRPFSF3B1SF3A1SF3A2CHERPPHF5ADDX46SNRPB2SF3B2SF3B4SRRM2SRRM1SRSF3HNRNPMHNRNPH2SNRPD2SUGP1SRSF7HNRNPUPOLR2FGTF2F2SRSF1YBX12xMe-SNRPD1RNPS1RBM5HNRNPKALYREFSF1SRSF6capped, methylated pre-mRNASNRPCPOLR2DSRRM1U2AF2POLR2ESRRTGTF2F1SNRPGCD2BP2POLR2ASRRM2U2AF1L4POLR2GFUSDDX5RBMXU1 snRNASNRPAHNRNPRNCBP1SNRPEPOLR2JPOLR2KHNRNPA3POLR2LSRSF5PTBP1Me2-R108,R112-SNRPBSNRPFHNRNPH1POLR2B2xMe-SNRPD3HNRNPA1SRSF2HNRNPCHNRNPLSNRNP70HNRNPA2B1DHX9U2AF1CCAR1HNRNPA0PRPF40APOLR2IPCBP1POLR2HSRSF9HNRNPDNCBP2POLR2CPCBP2HNRNPUL1HNRNPFSRSF6HNRNPCU2AF2Me2-R108,R112-SNRPBNCBP2PPIL1WBP11SRSF11PRPF19PPIL4ISY1GTF2F1U2AF1L4RBMXHNRNPA3POLR2ISNW1ELAVL2POLR2JU2AF1HNRNPKDHX16DHX9SNRPB2HNRNPA0NCBP1CD2BP2PRPF6PRPF8EFTUD2LSM2POLR2DCPSF2HNRNPA1CF I - 68 kDa subunitSRSF7DDX42HNRNPDGTF2F2HNRNPUL1SF3B3hTra2NHP2L1CRNKL1SRSF5CSTF1RBM17PTBP1PCF11NUDT21SNRPGPOLR2KSRSF1PPIEHNRNPA2B1SF3B1PCBP1CSTF2FIP1L1CSTF3CHERPPUF60DDX46ELAVL1CWC27Me2-R108,R112-SNRPNSNRNP402xMe-SNRPD1POLR2HDDX23SF3B4POLR2ESRSF2ALYREFCSTF2TPOLR2BHNRNPFHNRNPH2U5 snRNADHX15POLR2CPABPN1TXNL4ACWC15POLR2ASRRM2U2 snRNASF3A1SRSF3PAPOLASNRPA1CCAR1XAB2HNRNPRU2SURPHNRNPUSMNDC1FUSSNRPEWDR33DDX5PHF5ACPSF3POLR2GU6 snRNARBM22CPSF1RNPS1SNRNP200CPSF7capped, methylated pre-mRNASYMPKCWC22SRRTSRSF9SNRPD2CDC5LSRRM1SNRPFHNRNPMCF I - 72 kDa subunitAQRPOLR2FSF3A2PCBP2GPKOW2xMe-SNRPD3PPIL6DHX38CTNNBL1PRCCPOLR2LPPIL3EIF4A3PLRG1BCAS2SUGP1SF3B6YBX1SF3A3CDC40CPSF4HSPA8PQBP1SF3B5BUD31RBM5SF3B2HNRNPH1DNAJC8HNRNPLCLP1SRSF4CWC25FIP1L1CLP1PCF11CPSF3CF I - 72 kDa subunitCPSF1WDR33NUDT21CSTF2CSTF1CPSF4CPSF7PABPN1CSTF2TPAPOLACSTF3CPSF2SYMPKCF I - 68 kDa subunitALYREFFYTTD1LUZP4Mature Intronless transcript derived Histone mRNASLBPALYREFNXF1RANBP2NUP50RAE1NXF1AAASNDC1NUP205NUPL2NUP58-1SEC13NUP98-4RNPS1NUP153SRRM1NUP35NUP88NXF2NUP188NUP107NCBP2NUP210NUP98-3NUP54NUP133SEH1L-2POM121NUP37SEH1L-1NUP155CASC3NUP214UPF3BNUP62NUP93TPRNUP58-2MAGOHBALYREFNUP85EIF4A3NUP43NCBP1POLDIP3MAGOHNUP98-5NXT1mRNAPOM121CNUP160RBM8AU2AF1L4U2AF1THOC2THOC6THOC1THOC5THOC3THOC7Mature Intronless transcript derived Histone mRNANCBP1NCBP2TPRMAGOHNUP54NUP160AAASUPF3BNDC1NUP155NXF2NUP214NUP85NUP98-3NUP133NUP37NCBP2NUP43SRRM1SEH1L-2NUP58-1EIF4A3NUP98-5SEC13NUP353'-polyadenylated, capped pre-mRNANUPL2NUP205NUP50RAE1RNPS1NUP107NUP98-4NXF1NCBP1CASC3NUP210NXT1NUP88NUP93POM121NUP188POM121CNUP153SEH1L-1MAGOHBNUP58-2NUP62RANBP2POLDIP3RBM8AALYREFDDX39BADPDDX39ANUDT21CPSF7CF I - 72 kDa subunitCF I - 68 kDa subunitNXF1ALYREFMature Intronless transcript derived Histone mRNANCBP2SLBPMature Intronless transcript derived Histone mRNANCBP1NUP133NUP160NUP153NUP85NUP62NUP205POM121CNUP50NUP210TPRNUP214NUP54NUP88NUP98-3NUP37SEH1L-1NUP188AAASNUP58-2NUP93NDC1RAE1NUP155SEC13SEH1L-2RANBP2POM121NUP98-5NUP107NUPL2NUP35NUP98-4NUP58-1NUP43NXF1NXT1NXF2NUDT21CF I - 72 kDa subunitCPSF7CF I - 68 kDa subunitHNRNPA2B1SUGP1CPSF4PRPF6CPSF7SYMPKSRRTPQBP1BCAS2CSTF1DHX38SRSF4U2 snRNASNRPD2SRSF3HNRNPH1DHX16BUD31CPSF2PPIL1SRRM2TXNL4AHNRNPA1DDX42POLR2AU2AF1U2AF2CF I - 72 kDa subunitGTF2F2HNRNPCRNPS1POLR2IRBM22SF3B2DDX46SRRM1PPIEPOLR2CHNRNPMELAVL1DDX5DHX9CDC5LALYREFDDX23CF I - 68 kDa subunitSRSF1POLR2DDNAJC8SRSF5NCBP2SNRPA1HNRNPKHNRNPLU2SURP2xMe-SNRPD1PPIL4PAPOLACLP1Me2-R108,R112-SNRPNFUSPLRG1NUDT21PRPF19PRPF8PABPN1WBP11NHP2L1HNRNPDHNRNPUL1CRNKL1EIF4A3POLR2HCDC40POLR2LSF3A1CCAR1Me2-R108,R112-SNRPBSF3A2PHF5ARBM5PPIL3SRSF9LSM2SRSF6SNRPEWDR33SNRPB2CWC22CWC25AQRSRSF7POLR2FPUF60GPKOWNCBP1POLR2Kcapped, methylated pre-mRNASNW1SF3A3SRSF11CWC15HNRNPREFTUD2ISY1POLR2EhTra2SF3B3CPSF3RBMXPCBP1U6 snRNAHNRNPFPOLR2GU5 snRNAXAB2POLR2BRBM17SRSF2SNRNP40HNRNPA3PRCCGTF2F1CSTF2DHX15ELAVL2SF3B1HSPA8U2AF1L4CD2BP2SNRNP200PTBP1CSTF3YBX1CHERPPOLR2JCPSF1HNRNPA0FIP1L1SF3B4CSTF2TSF3B5SNRPFPPIL6PCBP2SNRPGSMNDC1HNRNPH2PCF11SF3B6HNRNPUCTNNBL12xMe-SNRPD3Mature intronless transcript derived Histone mRNAEIF4ESLBPPQBP1HSPA8PRPF19PLRG1CWC15CDC5LCTNNBL1BCAS2WBP11GTF2F1PRPF6POLR2GPOLR2LPPIHSNRPD2SRSF6POLR2JSRRTHNRNPMSRSF5SRRM2CDC40HNRNPDSMNDC1DDX42HNRNPRPRPF31CRNKL1PRPF38ALSM3PHF5AYBX1PTBP1PUF60U4 snRNALSM2U2AF1L4POLR2FXAB2SNRNP27Me2-R108,R112-SNRPNCD2BP2RBM22SF3A3NCBP2POLR2DSF3A2HNRNPFLSM4SART1SNRNP40U1 snRNAPOLR2EHNRNPUL1HNRNPA3SF3B2SF3B5PPIESNRPA1POLR2Acapped, methylated pre-mRNADDX46PRPF19DNAJC8HNRNPH1SNRPGHSPA8Me2-R108,R112-SNRPBPPIL1LSM6PRPF8AQRU2SURPHNRNPA2B1SF3B4FUSELAVL2DDX23U5 snRNAHNRNPUPLRG1PPIL62xMe-SNRPD1DHX38SF3B3SNRPAU2AF1LSM7SRSF4ISY1RNPS1U2 snRNAPRCCSNRNP70CDC5LPCBP1SRSF7PRPF4RBM5POLR2KCWC22SRSF9HNRNPKPRPF3POLR2CWBP11CHERPALYREFCWC15HNRNPCSNW1HNRNPA0NCBP1SNRPB2SF3B6TXNL4ALSM8GTF2F2BCAS2PCBP2SNRPCSRSF22xMe-SNRPD3POLR2HDHX15POLR2IRBM17RBMXSNRPFLSM5HNRNPA1DDX5SNRNP200PPIL3SF3B1ELAVL1EFTUD2BUD31HNRNPLSNRPEU6 snRNASRSF1SUGP1CTNNBL1PQBP1CCAR1SF3A1PPIL4HNRNPH2SRRM1SRSF3NHP2L1WBP4POLR2BU2AF2DHX9USP39SRSF11Me2-R108,R112-SNRPBSNRNP40DDX23LSM2SNRPFPRPF6NHP2L12xMe-SNRPD1SNRPD2SNRPEU6 ATAC snRNASNRPGTXNL4APRPF82xMe-SNRPD3U5 snRNAU4atac snRNAEFTUD2SNRNP200SF3A3SF3A1SF3A2U2AF1CF I - 68 kDa subunitEIF4A3SRRM1SRSF5CPSF7SRSF6NCBP2PAPOLACPSF2MAGOHBSRSF11CSTF2TCDC40SRSF4U2AF2SRSF2CLP1SYMPKU2AF1L4PABPN1NUDT21PCF11WDR33SRSF7UPF3BSRSF1RBM8ASRSF3ALYREFSRSF9CSTF2CPSF4hSLU7CPSF3CSTF1hTra2FIP1L1MAGOHRNPS1DHX38CSTF3CASC3CPSF1mRNA with spliced exonsNCBP1CF I - 72 kDa subunitU11 snRNAYBX1SNRNP482xMe-SNRPD3Me2-R108,R112-SNRPBSNRNP252xMe-SNRPD1SNRPESNRPD2SNRPGSNRPFSNRNP35PDCD72xMe-SNRPD1SNRPFSNRPD2NHP2L1Me2-R108,R112-SNRPBPRPF31PRPF4SNRPE2xMe-SNRPD3SNRPGU4 snRNAPPIHPRPF3LSM2LSM5LSM8LSM7LSM6LSM4LSM3ZRSR2U12 snRNAPOLR2DGTF2F1SRSF7NCBP1NCBP2POLR2BPOLR2KDDX42SRSF6POLR2FSNRNP25SRSF2POLR2CPOLR2APOLR2ESNRNP48SRSF1SF3B3SNRPD2RNPC3PDCD7SNRPGSF3B5Me2-R108,R112-SNRPBGTF2F2SF3B1U11 snRNAPOLR2GPOLR2LSNRPEZMAT52xMe-SNRPD32xMe-SNRPD1SNRPFPOLR2Jcapped, methylated pre-mRNASF3B4ZCRB1YBX1POLR2ISF3B2POLR2HSNRNP35SF3B6NXF1Mature intronless transcript derived Histone mRNAALYREFSF3B6SF3B4DDX42SF3B1SF3B3SF3B2SF3B5SNRNP200U5 snRNALSM5DDX23U6 snRNAPPIHSNRNP40PRPF82xMe-SNRPD1PRPF6SNRPGEFTUD2U4 snRNAPRPF3PRPF4TXNL4ASNRPD2LSM3NHP2L1Me2-R108,R112-SNRPBPRPF31SART1SNRPFSNRPELSM7USP39LSM8LSM4LSM22xMe-SNRPD3LSM6SNRNP27CSTF3CSTF2TCSTF1CSTF2NXF2NXT1NXF1WTAPMETTL3METTL14SLBPMature intronless transcript derived Histone mRNANXF1ALYREFALYREFNXF1Mature intronless derived mRNAU2AF1THOC2SRSF7SRSF11CASC3U2AF2DHX38NCBP2POLDIP3THOC5SRSF9RBM8ASRSF1SRSF2SRSF3ATPDDX39AUPF3BSARNPU2AF1L4SRSF5ALYREFNCBP1SRSF6THOC1FYTTD1hSLU7CHTOPZC3H11ATHOC7SRSF4MAGOHBSRRM1LUZP4EIF4A3CDC40RNPS1DDX39BTHOC63'-polyadenylated, capped pre-mRNAMAGOHTHOC3SRSF2LUZP4hSLU7NCBP1ZC3H11AU2AF2THOC1UPF3BRNPS1SRSF4THOC7SRSF9DHX38SRSF5U2AF1L4SARNPTHOC53'-polyadenylated, capped pre-mRNANCBP2MAGOHTHOC3ALYREFTHOC6POLDIP3SRSF7NXT1FYTTD1SRSF11MAGOHBCDC40U2AF1THOC2CASC3SRSF6NXF2SRSF3CHTOPEIF4A3NXF1SRRM1SRSF1RBM8AMAGOHBMAGOHRBM8ASF3B4SUGP1SF3B3HNRNPFPOLR2BSRRM1DNAJC8PCF11PLRG1POLR2GSF3A2NUDT21SRSF1LSM2POLR2CNCBP1HNRNPUISY1AQRSRRTSF3B1SRSF9SNRPD2SMNDC1p-S5-POLR2ARBM22WDR33SNRNP40CDC40SNW1POLR2IDHX15POLR2JDDX5ELAVL1SF3A3PPIESF3A1lariat containing 5'-end cleaved mRNAPOLR2ESNRPGSYMPKPCBP2PQBP1EIF4A3DHX9SF3B5PAPOLACF I - 68 kDa subunitHNRNPK2xMe-SNRPD3CRNKL1CCAR1CPSF3PRPF19YBX1DDX42FIP1L1U2AF1L4CSTF2U2SURPXAB2CWC15SRSF5CDC5LDHX38U5 snRNARBMXU2AF1NHP2L1SRSF6HNRNPUL1TRA2BGTF2F2CPSF4CWC25SYF2POLR2HHNRNPA1PCBP1HNRNPLSRSF11HNRNPH1BCAS2Me2-R108,R112-SNRPNSNRPB2RBM5CSTF2THNRNPA3ALYREFRNPS1DDX46HNRNPDPPIL3DDX23PRCCCF I - 72 kDa subunitHNRNPRSRSF2EFTUD2PRPF6PPIL6HNRNPMSRRM2SRSF7HSPA8HNRNPA2B1PHF5AHNRNPH2POLR2LPPIL42xMe-SNRPD1PUF60NCBP2POLR2DGTF2F1RBM17CHERPPPIL1GPKOWMe2-R108,R112-SNRPBPRPF8CTNNBL1CSTF3FUSSNRNP200POLR2FSF3B2PTBP1POLR2KBUD31SNRPEPABPN1CWC22U2 snRNASF3B6UPF3BSRSF3CSTF1PPWD1ELAVL2SNRPA1CPSF1CPSF2CPSF7CLP1WBP11DHX16SRSF4U6 snRNAHNRNPCCD2BP2SNRPFTXNL4AU2AF2HNRNPA0CSTF1CSTF2CSTF3CSTF2TPTBP1U5 snRNASNRPB2AQRWBP11SUGP1SNRNP200TXNL4AGPKOWRBM5SMNDC1FUSRBM17Me2-R108,R112-SNRPNPPIL3excised intronPQBP1PRCCSNRNP40EFTUD2CDC5LGCFC2PLRG1PPIL1PRPF6HNRNPUHSPA8SKIV2L2PHF5AHNRNPUL1YBX1CRNKL1CWC15PUF60RBM22DHX9BCAS2ISY1SNRPA1CHERPDDX46DNAJC8BUD31U6 snRNALSM2U2SURPPRPF8SNRPGPPIL4PPIL6U2 snRNATFIP11CCAR1SNRPENHP2L12xMe-SNRPD3HNRNPA2B1SNRPFCD2BP2DDX23DHX15PPIESNW1Me2-R108,R112-SNRPBCTNNBL1SNRPD22xMe-SNRPD1XAB2DHX16PRPF19NUP205NUP155SEH1L-2NUP188NUP98-4TPRNUPL2NUP210NUP98-5NUP98-3NUP88NDC1NUP58-1NUP62SEC13NUP160RANBP2NUP54POM121NUP85NUP43NUP133NUP58-2RAE1POM121CNUP107NUP37NUP214NUP153NUP35NUP50AAASNUP93SEH1L-1ALYREFFYTTD1LUZP4CPSF2CPSF4WDR33CPSF3SYMPKCPSF1FIP1L1SMNDC1DDX46SRSF5POLR2Acapped, methylated pre-mRNACCAR1ELAVL1CWC15SF3B3HNRNPH2HNRNPA3SF3B5DDX5HNRNPMSF3A1U2AF1SRSF1SF3A2Me2-R108,R112-SNRPBDHX15PTBP1POLR2GHSPA8POLR2DSRSF11Me2-R108,R112-SNRPNRBM17SRRTPLRG1PRPF40ARBMXPRPF19NCBP2ALYREFCTNNBL1SNRPADNAJC8POLR2HSF3B4U2SURPSUGP1SRSF7GTF2F2RBM5PUF60SRSF3WBP11HNRNPDSNRPGHNRNPA2B1DDX42DHX38ELAVL2SF3B2SRSF2GTF2F1HNRNPFSF3A3HNRNPA12xMe-SNRPD1CDC40PCBP12xMe-SNRPD3RNPS1POLR2BHNRNPLSNRPD2HNRNPUHNRNPCSNRPCSRSF9HNRNPRSNRPESNRPFPOLR2JCDC5LHNRNPA0SRSF6POLR2FSF3B1SNRPB2HNRNPUL1PQBP1NCBP1CHERPU1 snRNADHX9POLR2LPOLR2CBCAS2SNRNP70CD2BP2U2AF2SRRM2HNRNPKSRSF4POLR2EPCBP2SNRPA1CWC22WBP4POLR2KU2 snRNASRRM1U2AF1L4PHF5ASF3B6POLR2IFUSYBX1HNRNPH1GTF2F2POLR2IPOLR2JPOLR2BPOLR2CPOLR2GPOLR2HPOLR2EPOLR2LGTF2F1p-S5-POLR2APOLR2DPOLR2FPOLR2KNCBP1GTF2F2U5 snRNASNRNP402xMe-SNRPD3PRPF6DDX23capped, methylated pre-mRNASRSF1SF3B22xMe-SNRPD1RNPC3SF3B5Me2-R108,R112-SNRPBNCBP2LSM2SNRNP200U11 snRNAYBX1U12 snRNAZMAT5POLR2ASNRNP25SNRPESNRPD2NHP2L1PRPF8POLR2GPOLR2JPOLR2IPOLR2FGTF2F1ZRSR2EFTUD2ZCRB1SNRPFSNRNP48SRSF7POLR2KSF3B3SNRPGSF3B1U6 ATAC snRNAPOLR2ESNRNP35PDCD7POLR2LPOLR2CPOLR2DSF3B4SRSF2SRSF6POLR2HPOLR2BSF3B6TXNL4ADDX42CPSF1WDR33SYMPKFIP1L1CPSF4CPSF3CPSF2Mature intronless derived mRNAEIF4EHNRNPLPOLR2EHNRNPCHNRNPFHNRNPUHNRNPH1HNRNPKPOLR2BHNRNPA1POLR2JHNRNPDHNRNPA3PCBP1POLR2HNCBP1POLR2IPOLR2DRBMXGTF2F2NCBP2HNRNPA2B1POLR2CPOLR2FHNRNPRPTBP1POLR2Lcapped, methylated pre-mRNAPOLR2APCBP2POLR2KHNRNPMHNRNPA0GTF2F1HNRNPH2POLR2GSNRPE2xMe-SNRPD3SNRPFU4atac snRNA2xMe-SNRPD1SNRPGMe2-R108,R112-SNRPBSNRPD2FIP1L1SYMPKCPSF2CPSF1WDR33CPSF3CPSF4LSM2SNRPEZRSR2NHP2L12xMe-SNRPD3PRPF6SNRNP40SNRNP35SF3B4POLR2KPOLR2LPOLR2HSNRPFPDCD7SRSF6SF3B3Me2-R108,R112-SNRPBU6 ATAC snRNATXNL4APOLR2EPOLR2DSRSF7POLR2FPOLR2CU5 snRNAPOLR2GZMAT5NCBP1GTF2F2SNRPG2xMe-SNRPD1YBX1POLR2BPOLR2IGTF2F1SF3B5RNPC3ZCRB1POLR2AU12 snRNAU11 snRNANCBP2DDX42SNRPD2SF3B2SNRNP48POLR2JPRPF8SNRNP25capped, methylated pre-mRNADDX23SRSF1SNRNP200SF3B1SRSF2SF3B6EFTUD2Name: Processing of Capped Intron-Containing Pre-mRNAOrganism: Homo sapiens


Description

Co-transcriptional pre-mRNA splicing is not obligatory. Pre-mRNA splicing begins co-transcriptionally and often continues post-transcriptionally. Human genes contain an average of nine introns per gene, which cannot serve as splicing substrates until both 5' and 3' ends of each intron are synthesized. Thus the time that it takes for pol II to synthesize each intron defines a minimal time and distance along the gene in which splicing factors can be recruited. The time that it takes for pol II to reach the end of the gene defines the maximal time in which splicing could occur co-transcriptionally. Thus, the kinetics of transcription can affect the kinetics of splicing.Any covalent change in a primary (nascent) mRNA transcript is mRNA Processing. For successful gene expression, the primary mRNA transcript needs to be converted to a mature mRNA prior to its translation into polypeptide. Eucaryotic mRNAs undergo a series of complex processing reactions; these begin on nascent transcripts as soon as a few ribonucleotides have been synthesized during transcription by RNA Polymerase II, through the export of the mature mRNA to the cytoplasm, and culminate with mRNA turnover in the cytoplasm. View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 72203
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Carmichael, Gordon G, Hammarskjold, Marie-Louise, Hastings, Michelle L, Krainer, Adrian R, Marzluff, William F, Wahle, Elmar, Zhang, Z

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Quality Tags

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Ontology Terms

Pathway Ontology : disease pathway
 

Bibliography

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  51. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC Scholia
  52. Erkmann JA, Kutay U.; ''Nuclear export of mRNA: from the site of transcription to the cytoplasm.''; PubMed Europe PMC Scholia
  53. Kang Y, Bogerd HP, Yang J, Cullen BR.; ''Analysis of the RNA binding specificity of the human tap protein, a constitutive transport element-specific nuclear RNA export factor.''; PubMed Europe PMC Scholia
  54. Watkins JL, Murphy R, Emtage JL, Wente SR.; ''The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export.''; PubMed Europe PMC Scholia
  55. Schönemann L, Kühn U, Martin G, Schäfer P, Gruber AR, Keller W, Zavolan M, Wahle E.; ''Reconstitution of CPSF active in polyadenylation: recognition of the polyadenylation signal by WDR33.''; PubMed Europe PMC Scholia
  56. Meinel DM, Burkert-Kautzsch C, Kieser A, O'Duibhir E, Siebert M, Mayer A, Cramer P, Söding J, Holstege FC, Sträßer K.; ''Recruitment of TREX to the transcription machinery by its direct binding to the phospho-CTD of RNA polymerase II.''; PubMed Europe PMC Scholia
  57. Lin-Moshier Y, Sebastian PJ, Higgins L, Sampson ND, Hewitt JE, Marchant JS.; ''Re-evaluation of the role of calcium homeostasis endoplasmic reticulum protein (CHERP) in cellular calcium signaling.''; PubMed Europe PMC Scholia
  58. Viphakone N, Cumberbatch MG, Livingstone MJ, Heath PR, Dickman MJ, Catto JW, Wilson SA.; ''Luzp4 defines a new mRNA export pathway in cancer cells.''; PubMed Europe PMC Scholia
  59. Valadkhan S, Mohammadi A, Wachtel C, Manley JL.; ''Protein-free spliceosomal snRNAs catalyze a reaction that resembles the first step of splicing.''; PubMed Europe PMC Scholia
  60. Neubauer G, King A, Rappsilber J, Calvio C, Watson M, Ajuh P, Sleeman J, Lamond A, Mann M.; ''Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex.''; PubMed Europe PMC Scholia
  61. Kang Y, Cullen BR.; ''The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences.''; PubMed Europe PMC Scholia
  62. Madan V, Kanojia D, Li J, Okamoto R, Sato-Otsubo A, Kohlmann A, Sanada M, Grossmann V, Sundaresan J, Shiraishi Y, Miyano S, Thol F, Ganser A, Yang H, Haferlach T, Ogawa S, Koeffler HP.; ''Aberrant splicing of U12-type introns is the hallmark of ZRSR2 mutant myelodysplastic syndrome.''; PubMed Europe PMC Scholia
  63. Folco EG, Lee CS, Dufu K, Yamazaki T, Reed R.; ''The proteins PDIP3 and ZC11A associate with the human TREX complex in an ATP-dependent manner and function in mRNA export.''; PubMed Europe PMC Scholia
  64. Hautbergue GM, Hung ML, Golovanov AP, Lian LY, Wilson SA.; ''Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP.''; PubMed Europe PMC Scholia
  65. Hastings ML, Krainer AR.; ''Functions of SR proteins in the U12-dependent AT-AC pre-mRNA splicing pathway.''; PubMed Europe PMC Scholia
  66. Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA.; ''The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA.''; PubMed Europe PMC Scholia
  67. Deckert J, Hartmuth K, Boehringer D, Behzadnia N, Will CL, Kastner B, Stark H, Urlaub H, Lührmann R.; ''Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions.''; PubMed Europe PMC Scholia
  68. Yoshimoto R, Kataoka N, Okawa K, Ohno M.; ''Isolation and characterization of post-splicing lariat-intron complexes.''; PubMed Europe PMC Scholia
  69. Box JA, Bunch JT, Tang W, Baumann P.; ''Spliceosomal cleavage generates the 3' end of telomerase RNA.''; PubMed Europe PMC Scholia
  70. Johnson SA, Kim H, Erickson B, Bentley DL.; ''The export factor Yra1 modulates mRNA 3' end processing.''; PubMed Europe PMC Scholia
  71. Bachi A, Braun IC, Rodrigues JP, Panté N, Ribbeck K, von Kobbe C, Kutay U, Wilm M, Görlich D, Carmo-Fonseca M, Izaurralde E.; ''The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.''; PubMed Europe PMC Scholia
  72. Strässer K, Masuda S, Mason P, Pfannstiel J, Oppizzi M, Rodriguez-Navarro S, Rondón AG, Aguilera A, Struhl K, Reed R, Hurt E.; ''TREX is a conserved complex coupling transcription with messenger RNA export.''; PubMed Europe PMC Scholia
  73. Chang CT, Hautbergue GM, Walsh MJ, Viphakone N, van Dijk TB, Philipsen S, Wilson SA.; ''Chtop is a component of the dynamic TREX mRNA export complex.''; PubMed Europe PMC Scholia
  74. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC Scholia
  75. Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ.; ''Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.''; PubMed Europe PMC Scholia
  76. Crisci A, Raleff F, Bagdiul I, Raabe M, Urlaub H, Rain JC, Krämer A.; ''Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.''; PubMed Europe PMC Scholia
  77. Shi Y, Di Giammartino DC, Taylor D, Sarkeshik A, Rice WJ, Yates JR, Frank J, Manley JL.; ''Molecular architecture of the human pre-mRNA 3' processing complex.''; PubMed Europe PMC Scholia
  78. Takagaki Y, Manley JL.; ''Complex protein interactions within the human polyadenylation machinery identify a novel component.''; PubMed Europe PMC Scholia
  79. Kreivi JP, Lamond AI.; ''RNA splicing: unexpected spliceosome diversity.''; PubMed Europe PMC Scholia
  80. Katahira J.; ''Nuclear export of messenger RNA.''; PubMed Europe PMC Scholia
  81. Rougemaille M, Dieppois G, Kisseleva-Romanova E, Gudipati RK, Lemoine S, Blugeon C, Boulay J, Jensen TH, Stutz F, Devaux F, Libri D.; ''THO/Sub2p functions to coordinate 3'-end processing with gene-nuclear pore association.''; PubMed Europe PMC Scholia
  82. Luna R, Rondón AG, Aguilera A.; ''New clues to understand the role of THO and other functionally related factors in mRNP biogenesis.''; PubMed Europe PMC Scholia
  83. Zaric B, Chami M, Rémigy H, Engel A, Ballmer-Hofer K, Winkler FK, Kambach C.; ''Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function.''; PubMed Europe PMC Scholia
  84. Zhao J, Hyman L, Moore C.; ''Formation of mRNA 3' ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis.''; PubMed Europe PMC Scholia
  85. Lejeune F, Ishigaki Y, Li X, Maquat LE.; ''The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling.''; PubMed Europe PMC Scholia
  86. Degot S, Le Hir H, Alpy F, Kedinger V, Stoll I, Wendling C, Seraphin B, Rio MC, Tomasetto C.; ''Association of the breast cancer protein MLN51 with the exon junction complex via its speckle localizer and RNA binding module.''; PubMed Europe PMC Scholia
  87. Daguenet E, Baguet A, Degot S, Schmidt U, Alpy F, Wendling C, Spiegelhalter C, Kessler P, Rio MC, Le Hir H, Bertrand E, Tomasetto C.; ''Perispeckles are major assembly sites for the exon junction core complex.''; PubMed Europe PMC Scholia
  88. Braun IC, Herold A, Rode M, Conti E, Izaurralde E.; ''Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export.''; PubMed Europe PMC Scholia
  89. Masuda S, Das R, Cheng H, Hurt E, Dorman N, Reed R.; ''Recruitment of the human TREX complex to mRNA during splicing.''; PubMed Europe PMC Scholia
  90. Harris ME, Böhni R, Schneiderman MH, Ramamurthy L, Schümperli D, Marzluff WF.; ''Regulation of histone mRNA in the unperturbed cell cycle: evidence suggesting control at two posttranscriptional steps.''; PubMed Europe PMC Scholia
  91. Hautbergue GM, Hung ML, Walsh MJ, Snijders AP, Chang CT, Jones R, Ponting CP, Dickman MJ, Wilson SA.; ''UIF, a New mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA.''; PubMed Europe PMC Scholia
  92. Guzik BW, Levesque L, Prasad S, Bor YC, Black BE, Paschal BM, Rekosh D, Hammarskjöld ML.; ''NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells.''; PubMed Europe PMC Scholia
  93. von Moeller H, Lerner R, Ricciardi A, Basquin C, Marzluff WF, Conti E.; ''Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.''; PubMed Europe PMC Scholia
  94. Dreyfuss G, Matunis MJ, Piñol-Roma S, Burd CG.; ''hnRNP proteins and the biogenesis of mRNA.''; PubMed Europe PMC Scholia
  95. Rondón AG, Jimeno S, García-Rubio M, Aguilera A.; ''Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation.''; PubMed Europe PMC Scholia
  96. Steckelberg AL, Boehm V, Gromadzka AM, Gehring NH.; ''CWC22 connects pre-mRNA splicing and exon junction complex assembly.''; PubMed Europe PMC Scholia
  97. Gencheva M, Kato M, Newo AN, Lin RJ.; ''Contribution of DEAH-box protein DHX16 in human pre-mRNA splicing.''; PubMed Europe PMC Scholia
  98. Dufu K, Livingstone MJ, Seebacher J, Gygi SP, Wilson SA, Reed R.; ''ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex.''; PubMed Europe PMC Scholia
  99. Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMed Europe PMC Scholia
  100. Hartmuth K, Urlaub H, Vornlocher HP, Will CL, Gentzel M, Wilm M, Lührmann R.; ''Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method.''; PubMed Europe PMC Scholia
  101. Grzybowska EA.; ''Human intronless genes: functional groups, associated diseases, evolution, and mRNA processing in absence of splicing.''; PubMed Europe PMC Scholia
  102. Yao C, Choi EA, Weng L, Xie X, Wan J, Xing Y, Moresco JJ, Tu PG, Yates JR, Shi Y.; ''Overlapping and distinct functions of CstF64 and CstF64Ï„ in mammalian mRNA 3' processing.''; PubMed Europe PMC Scholia
  103. Reichert VL, Le Hir H, Jurica MS, Moore MJ.; ''5' exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly.''; PubMed Europe PMC Scholia
  104. Katahira J, Strässer K, Podtelejnikov A, Mann M, Jung JU, Hurt E.; ''The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human.''; PubMed Europe PMC Scholia
  105. Kaufmann I, Martin G, Friedlein A, Langen H, Keller W.; ''Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase.''; PubMed Europe PMC Scholia
  106. Wente SR, Rout MP.; ''The nuclear pore complex and nuclear transport.''; PubMed Europe PMC Scholia
  107. Viphakone N, Hautbergue GM, Walsh M, Chang CT, Holland A, Folco EG, Reed R, Wilson SA.; ''TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.''; PubMed Europe PMC Scholia
  108. Will CL, Schneider C, Hossbach M, Urlaub H, Rauhut R, Elbashir S, Tuschl T, Lührmann R.; ''The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome.''; PubMed Europe PMC Scholia
  109. Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
  110. Behzadnia N, Golas MM, Hartmuth K, Sander B, Kastner B, Deckert J, Dube P, Will CL, Urlaub H, Stark H, Lührmann R.; ''Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes.''; PubMed Europe PMC Scholia
  111. Herold A, Suyama M, Rodrigues JP, Braun IC, Kutay U, Carmo-Fonseca M, Bork P, Izaurralde E.; ''TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture.''; PubMed Europe PMC Scholia
  112. Taniguchi I, Ohno M.; ''ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56.''; PubMed Europe PMC Scholia
  113. Kota KP, Wagner SR, Huerta E, Underwood JM, Nickerson JA.; ''Binding of ATP to UAP56 is necessary for mRNA export.''; PubMed Europe PMC Scholia
  114. Padgett RA, Konarska MM, Grabowski PJ, Hardy SF, Sharp PA.; ''Lariat RNA's as intermediates and products in the splicing of messenger RNA precursors.''; PubMed Europe PMC Scholia
  115. Shen H, Zheng X, Luecke S, Green MR.; ''The U2AF35-related protein Urp contacts the 3' splice site to promote U12-type intron splicing and the second step of U2-type intron splicing.''; PubMed Europe PMC Scholia
  116. Wahle E, Rüegsegger U.; ''3'-End processing of pre-mRNA in eukaryotes.''; PubMed Europe PMC Scholia
  117. Grüter P, Tabernero C, von Kobbe C, Schmitt C, Saavedra C, Bachi A, Wilm M, Felber BK, Izaurralde E.; ''TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus.''; PubMed Europe PMC Scholia
  118. Bessonov S, Anokhina M, Will CL, Urlaub H, Lührmann R.; ''Isolation of an active step I spliceosome and composition of its RNP core.''; PubMed Europe PMC Scholia
  119. Singh J, Sikand K, Conrad H, Will CL, Komar AA, Shukla GC.; ''U6atac snRNA stem-loop interacts with U12 p65 RNA binding protein and is functionally interchangeable with the U12 apical stem-loop III.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
115088
Reactome
view17:03, 25 January 2021ReactomeTeamReactome version 75
113530view12:00, 2 November 2020ReactomeTeamReactome version 74
112728view16:13, 9 October 2020ReactomeTeamReactome version 73
101644view11:51, 1 November 2018ReactomeTeamreactome version 66
101180view21:38, 31 October 2018ReactomeTeamreactome version 65
100706view20:10, 31 October 2018ReactomeTeamreactome version 64
100256view16:56, 31 October 2018ReactomeTeamreactome version 63
99809view15:20, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93917view13:44, 16 August 2017ReactomeTeamreactome version 61
93494view11:25, 9 August 2017ReactomeTeamreactome version 61
88115view10:05, 26 July 2016RyanmillerOntology Term : 'regulatory pathway' added !
86590view09:21, 11 July 2016ReactomeTeamreactome version 56
83367view11:01, 18 November 2015ReactomeTeamVersion54
81532view13:04, 21 August 2015ReactomeTeamVersion53
77003view08:29, 17 July 2014ReactomeTeamFixed remaining interactions
76708view12:07, 16 July 2014ReactomeTeamFixed remaining interactions
76034view10:09, 11 June 2014ReactomeTeamRe-fixing comment source
75743view11:23, 10 June 2014ReactomeTeamReactome 48 Update
75093view14:04, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74829view10:05, 30 April 2014ReactomeTeamReactome46
74740view08:49, 30 April 2014ReactomeTeamReactome46
42105view21:57, 4 March 2011MaintBotAutomatic update
39915view05:56, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
Name  â†“Type  â†“Database reference  â†“Comment  â†“
2xMe-SNRPD1 ProteinP62314 (Uniprot-TrEMBL)
2xMe-SNRPD3 ProteinP62318 (Uniprot-TrEMBL)
3' end cleaved,

ligated exon

containing complex		ComplexR-HSA-72177 (Reactome)
3'-end cleaved mRNA with spliced exons R-ALL-71998 (Reactome)
3'-polyadenylated, capped pre-mRNA R-ALL-72184 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
ADP MetaboliteCHEBI:456216 (ChEBI)
ALYREF ProteinQ86V81 (Uniprot-TrEMBL)
ALYREF, FYTTD1, LUZP4ComplexR-HSA-8852182 (Reactome)
ALYREFProteinQ86V81 (Uniprot-TrEMBL)
AQR ProteinO60306 (Uniprot-TrEMBL)
AQRProteinO60306 (Uniprot-TrEMBL)
ATAC A ComplexComplexR-HSA-77463 (Reactome)
ATAC B ComplexComplexR-HSA-77470 (Reactome)
ATAC C Complex with

lariat containing

5'-end cleaved mRNA		ComplexR-HSA-77475 (Reactome)
ATAC C ComplexComplexR-HSA-77473 (Reactome)
ATP MetaboliteCHEBI:30616 (ChEBI)
ATPMetaboliteCHEBI:30616 (ChEBI)
BCAS2 ProteinO75934 (Uniprot-TrEMBL)
BUD31 ProteinP41223 (Uniprot-TrEMBL)
BUD31ProteinP41223 (Uniprot-TrEMBL)
CASC3 ProteinO15234 (Uniprot-TrEMBL)
CASC3ProteinO15234 (Uniprot-TrEMBL)
CCAR1 ProteinQ8IX12 (Uniprot-TrEMBL)
CCAR1ProteinQ8IX12 (Uniprot-TrEMBL)
CD2BP2 ProteinO95400 (Uniprot-TrEMBL)
CD2BP2ProteinO95400 (Uniprot-TrEMBL)
CDC40 ProteinO60508 (Uniprot-TrEMBL)
CDC40ProteinO60508 (Uniprot-TrEMBL)
CDC5L ProteinQ99459 (Uniprot-TrEMBL)
CF I - 68 kDa subunit R-HSA-72013 (Reactome)
CF I - 72 kDa subunit R-HSA-72014 (Reactome)
CF IIComplexR-HSA-72020 (Reactome)
CF IComplexR-HSA-72015 (Reactome)
CHERP ProteinQ8IWX8 (Uniprot-TrEMBL)
CHTOP ProteinQ9Y3Y2 (Uniprot-TrEMBL)
CHTOPProteinQ9Y3Y2 (Uniprot-TrEMBL)
CLP1 ProteinQ92989 (Uniprot-TrEMBL)
CPSF1 ProteinQ10570 (Uniprot-TrEMBL)
CPSF2 ProteinQ9P2I0 (Uniprot-TrEMBL)
CPSF3 ProteinQ9UKF6 (Uniprot-TrEMBL)
CPSF4 ProteinO95639 (Uniprot-TrEMBL)
CPSF7 ProteinQ8N684 (Uniprot-TrEMBL)
CPSFComplexR-HSA-71995 (Reactome)
CRNKL1 ProteinQ9BZJ0 (Uniprot-TrEMBL)
CRNKL1ProteinQ9BZJ0 (Uniprot-TrEMBL)
CSTF1 ProteinQ05048 (Uniprot-TrEMBL)
CSTF2 ProteinP33240 (Uniprot-TrEMBL)
CSTF2T ProteinQ9H0L4 (Uniprot-TrEMBL)
CSTF3 ProteinQ12996 (Uniprot-TrEMBL)
CTNNBL1 ProteinQ8WYA6 (Uniprot-TrEMBL)
CWC15 ProteinQ9P013 (Uniprot-TrEMBL)
CWC22 ProteinQ9HCG8 (Uniprot-TrEMBL)
CWC22ProteinQ9HCG8 (Uniprot-TrEMBL)
CWC25 ProteinQ9NXE8 (Uniprot-TrEMBL)
CWC25ProteinQ9NXE8 (Uniprot-TrEMBL)
CWC27 ProteinQ6UX04 (Uniprot-TrEMBL)
CWC27ProteinQ6UX04 (Uniprot-TrEMBL)
Cap Binding Complex (CBC)ComplexR-HSA-77088 (Reactome)
Cleavage and

Polyadenylation

Complex		ComplexR-HSA-72021 (Reactome)
CstFComplexR-HSA-72006 (Reactome)
DDX23 ProteinQ9BUQ8 (Uniprot-TrEMBL)
DDX39A ProteinO00148 (Uniprot-TrEMBL)
DDX39A,BComplexR-HSA-8852231 (Reactome)
DDX39B ProteinQ13838 (Uniprot-TrEMBL)
DDX39B:ADPComplexR-HSA-8849115 (Reactome)
DDX42 ProteinQ86XP3 (Uniprot-TrEMBL)
DDX46 ProteinQ7L014 (Uniprot-TrEMBL)
DDX5 ProteinP17844 (Uniprot-TrEMBL)
DDX5ProteinP17844 (Uniprot-TrEMBL)
DHX15 ProteinO43143 (Uniprot-TrEMBL)
DHX16 ProteinO60231 (Uniprot-TrEMBL)
DHX16ProteinO60231 (Uniprot-TrEMBL)
DHX38 ProteinQ92620 (Uniprot-TrEMBL)
DHX38ProteinQ92620 (Uniprot-TrEMBL)
DHX9 ProteinQ08211 (Uniprot-TrEMBL)
DHX9ProteinQ08211 (Uniprot-TrEMBL)
DNAJC8 ProteinO75937 (Uniprot-TrEMBL)
DNAJC8ProteinO75937 (Uniprot-TrEMBL)
EFTUD2 ProteinQ15029 (Uniprot-TrEMBL)
EIF4A3 ProteinP38919 (Uniprot-TrEMBL)
EIF4A3ProteinP38919 (Uniprot-TrEMBL)
EIF4E ProteinP06730 (Uniprot-TrEMBL)
EIF4EProteinP06730 (Uniprot-TrEMBL)
ELAVL1 ProteinQ15717 (Uniprot-TrEMBL)
ELAVL1ProteinQ15717 (Uniprot-TrEMBL)
ELAVL2 ProteinQ12926 (Uniprot-TrEMBL)
ELAVL2ProteinQ12926 (Uniprot-TrEMBL)
FIP1L1 ProteinQ6UN15 (Uniprot-TrEMBL)
FUS ProteinP35637 (Uniprot-TrEMBL)
FUSProteinP35637 (Uniprot-TrEMBL)
FYTTD1 ProteinQ96QD9 (Uniprot-TrEMBL)
GCFC2 ProteinP16383 (Uniprot-TrEMBL)
GLE1ProteinQ53GS7 (Uniprot-TrEMBL)
GPKOW ProteinQ92917 (Uniprot-TrEMBL)
GPKOWProteinQ92917 (Uniprot-TrEMBL)
GTF2F1 ProteinP35269 (Uniprot-TrEMBL)
GTF2F2 ProteinP13984 (Uniprot-TrEMBL)
HNRNPA0 ProteinQ13151 (Uniprot-TrEMBL)
HNRNPA0ProteinQ13151 (Uniprot-TrEMBL)
HNRNPA1 ProteinP09651 (Uniprot-TrEMBL)
HNRNPA1ProteinP09651 (Uniprot-TrEMBL)
HNRNPA2B1 ProteinP22626 (Uniprot-TrEMBL)
HNRNPA2B1ProteinP22626 (Uniprot-TrEMBL)
HNRNPA3 ProteinP51991 (Uniprot-TrEMBL)
HNRNPA3ProteinP51991 (Uniprot-TrEMBL)
HNRNPC ProteinP07910 (Uniprot-TrEMBL)
HNRNPCProteinP07910 (Uniprot-TrEMBL)
HNRNPD ProteinQ14103 (Uniprot-TrEMBL)
HNRNPDProteinQ14103 (Uniprot-TrEMBL)
HNRNPF ProteinP52597 (Uniprot-TrEMBL)
HNRNPFProteinP52597 (Uniprot-TrEMBL)
HNRNPH1 ProteinP31943 (Uniprot-TrEMBL)
HNRNPH1ProteinP31943 (Uniprot-TrEMBL)
HNRNPH2 ProteinP55795 (Uniprot-TrEMBL)
HNRNPH2ProteinP55795 (Uniprot-TrEMBL)
HNRNPK ProteinP61978 (Uniprot-TrEMBL)
HNRNPKProteinP61978 (Uniprot-TrEMBL)
HNRNPL ProteinP14866 (Uniprot-TrEMBL)
HNRNPLProteinP14866 (Uniprot-TrEMBL)
HNRNPM ProteinP52272 (Uniprot-TrEMBL)
HNRNPMProteinP52272 (Uniprot-TrEMBL)
HNRNPR ProteinO43390 (Uniprot-TrEMBL)
HNRNPRProteinO43390 (Uniprot-TrEMBL)
HNRNPU ProteinQ00839 (Uniprot-TrEMBL)
HNRNPUL1 ProteinQ9BUJ2 (Uniprot-TrEMBL)
HNRNPUL1ProteinQ9BUJ2 (Uniprot-TrEMBL)
HNRNPUProteinQ00839 (Uniprot-TrEMBL)
HSPA8 ProteinP11142 (Uniprot-TrEMBL)
ISY1 ProteinQ9ULR0 (Uniprot-TrEMBL)
ISY1ProteinQ9ULR0 (Uniprot-TrEMBL)
LSM2 ProteinQ9Y333 (Uniprot-TrEMBL)
LSM2-8 complexComplexR-HSA-6806791 (Reactome)
LSM3 ProteinP62310 (Uniprot-TrEMBL)
LSM4 ProteinQ9Y4Z0 (Uniprot-TrEMBL)
LSM5 ProteinQ9Y4Y9 (Uniprot-TrEMBL)
LSM6 ProteinP62312 (Uniprot-TrEMBL)
LSM7 ProteinQ9UK45 (Uniprot-TrEMBL)
LSM8 ProteinO95777 (Uniprot-TrEMBL)
LUZP4 ProteinQ9P127 (Uniprot-TrEMBL)
MAGOH ProteinP61326 (Uniprot-TrEMBL)
MAGOHB ProteinQ96A72 (Uniprot-TrEMBL)
METTL14 ProteinQ9HCE5 (Uniprot-TrEMBL)
METTL3 ProteinQ86U44 (Uniprot-TrEMBL)
Magoh-Y14 complexComplexR-HSA-156657 (Reactome)
Mature

Intronless transcript derived Histone

mRNA:SLBP:CBP80:CBP20		ComplexR-HSA-111682 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		ComplexR-HSA-159045 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		ComplexR-HSA-159047 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

Complex		ComplexR-HSA-158480 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

complex		ComplexR-HSA-158479 (Reactome)
Mature Intronless

Transcript Derived

mRNA:eIF4E Complex		ComplexR-HSA-113818 (Reactome)
Mature Intronless transcript derived Histone mRNA R-ALL-111676 (Reactome)
Mature SLBP

independent Histone

mRNA:eIF4E complex		ComplexR-HSA-158501 (Reactome)
Mature intronless

derived mRNA:TAP:Aly/Ref

complex		ComplexR-HSA-158442 (Reactome)
Mature intronless

derived mRNA

complex		ComplexR-HSA-112167 (Reactome)
Mature intronless

transcript derived Histone mRNA:SLBP:eIF4E

Complex		ComplexR-HSA-141614 (Reactome)
Mature intronless

transcript derived Histone pre-mRNA:CBC

complex		ComplexR-HSA-156959 (Reactome)
Mature intronless derived mRNA R-ALL-158443 (Reactome) A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript.
Mature intronless transcript derived Histone mRNA R-ALL-113820 (Reactome)
Mature intronless transcript derived mRNA R-ALL-158444 (Reactome) A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript.
Me2-R108,R112-SNRPB ProteinP14678 (Uniprot-TrEMBL)
Me2-R108,R112-SNRPN ProteinP63162 (Uniprot-TrEMBL)
NCBP1 ProteinQ09161 (Uniprot-TrEMBL)
NCBP1ProteinQ09161 (Uniprot-TrEMBL)
NCBP2 ProteinP52298 (Uniprot-TrEMBL)
NCBP2ProteinP52298 (Uniprot-TrEMBL)
NDC1 ProteinQ9BTX1 (Uniprot-TrEMBL)
NHP2L1 ProteinP55769 (Uniprot-TrEMBL)
NPC:NXF1,2:NXT1:EJC:CBC:mRNAComplexR-HSA-113815 (Reactome)
NPC:NXF1:NXT1:EJC:CBC:mRNAComplexR-HSA-159259 (Reactome)
NUDT21 ProteinO43809 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP58-1 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUP58-2 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
NXF1 ProteinQ9UBU9 (Uniprot-TrEMBL)
NXF1,2:NXT1::polyadenylated, capped mRNA:CBC:EJC:TREX:SRSF proteinsComplexR-HSA-159100 (Reactome)
NXF1,2:NXT1ComplexR-HSA-8849118 (Reactome)
NXF1,2:NXT1ComplexR-HSA-8849140 (Reactome)
NXF1ProteinQ9UBU9 (Uniprot-TrEMBL)
NXF2 ProteinQ9GZY0 (Uniprot-TrEMBL)
NXT1 ProteinQ9UKK6 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
Nucleoplasmic mature

intronless derived mRNA:TAP:Aly/Ref

complex		ComplexR-HSA-158446 (Reactome)
PABPN1 ProteinQ86U42 (Uniprot-TrEMBL)
PABPN1ProteinQ86U42 (Uniprot-TrEMBL)
PAPOLA ProteinP51003 (Uniprot-TrEMBL)
PAPOLAProteinP51003 (Uniprot-TrEMBL)
PCBP1 ProteinQ15365 (Uniprot-TrEMBL)
PCBP1ProteinQ15365 (Uniprot-TrEMBL)
PCBP2 ProteinQ15366 (Uniprot-TrEMBL)
PCBP2ProteinQ15366 (Uniprot-TrEMBL)
PCF11 ProteinO94913 (Uniprot-TrEMBL)
PDCD7 ProteinQ8N8D1 (Uniprot-TrEMBL)
PHF5A ProteinQ7RTV0 (Uniprot-TrEMBL)
PLRG1 ProteinO43660 (Uniprot-TrEMBL)
POLDIP3 ProteinQ9BY77 (Uniprot-TrEMBL)
POLDIP3ProteinQ9BY77 (Uniprot-TrEMBL)
POLR2A ProteinP24928 (Uniprot-TrEMBL)
POLR2B ProteinP30876 (Uniprot-TrEMBL)
POLR2C ProteinP19387 (Uniprot-TrEMBL)
POLR2D ProteinO15514 (Uniprot-TrEMBL)
POLR2E ProteinP19388 (Uniprot-TrEMBL)
POLR2F ProteinP61218 (Uniprot-TrEMBL)
POLR2G ProteinP62487 (Uniprot-TrEMBL)
POLR2H ProteinP52434 (Uniprot-TrEMBL)
POLR2I ProteinP36954 (Uniprot-TrEMBL)
POLR2J ProteinP52435 (Uniprot-TrEMBL)
POLR2K ProteinP53803 (Uniprot-TrEMBL)
POLR2L ProteinP62875 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
PPIE ProteinQ9UNP9 (Uniprot-TrEMBL)
PPIEProteinQ9UNP9 (Uniprot-TrEMBL)
PPIH ProteinO43447 (Uniprot-TrEMBL)
PPIL1 ProteinQ9Y3C6 (Uniprot-TrEMBL)
PPIL3 ProteinQ9H2H8 (Uniprot-TrEMBL)
PPIL4 ProteinQ8WUA2 (Uniprot-TrEMBL)
PPIL6 ProteinQ8IXY8 (Uniprot-TrEMBL)
PPILComplexR-HSA-8952109 (Reactome)
PPWD1 ProteinQ96BP3 (Uniprot-TrEMBL)
PPWD1ProteinQ96BP3 (Uniprot-TrEMBL)
PQBP1 ProteinO60828 (Uniprot-TrEMBL)
PRCC ProteinQ92733 (Uniprot-TrEMBL)
PRCCProteinQ92733 (Uniprot-TrEMBL)
PRP19-CDC5L complexComplexR-HSA-5420896 (Reactome)
PRPF19 ProteinQ9UMS4 (Uniprot-TrEMBL)
PRPF3 ProteinO43395 (Uniprot-TrEMBL)
PRPF31 ProteinQ8WWY3 (Uniprot-TrEMBL)
PRPF38A ProteinQ8NAV1 (Uniprot-TrEMBL)
PRPF38AProteinQ8NAV1 (Uniprot-TrEMBL)
PRPF4 ProteinO43172 (Uniprot-TrEMBL)
PRPF40A ProteinO75400 (Uniprot-TrEMBL)
PRPF40AProteinO75400 (Uniprot-TrEMBL)
PRPF6 ProteinO94906 (Uniprot-TrEMBL)
PRPF8 ProteinQ6P2Q9 (Uniprot-TrEMBL)
PTBP1 ProteinP26599 (Uniprot-TrEMBL)
PTBP1ProteinP26599 (Uniprot-TrEMBL)
PUF60 ProteinQ9UHX1 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:43474 (ChEBI)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RBM17 ProteinQ96I25 (Uniprot-TrEMBL)
RBM22 ProteinQ9NW64 (Uniprot-TrEMBL)
RBM22ProteinQ9NW64 (Uniprot-TrEMBL)
RBM5 ProteinP52756 (Uniprot-TrEMBL)
RBM5ProteinP52756 (Uniprot-TrEMBL)
RBM8A ProteinQ9Y5S9 (Uniprot-TrEMBL)
RBMX ProteinP38159 (Uniprot-TrEMBL)
RBMXProteinP38159 (Uniprot-TrEMBL)
RNA

polymerase II

(phosphorylated):TFIIF complex		ComplexR-HSA-113404 (Reactome)
RNPC3 ProteinQ96LT9 (Uniprot-TrEMBL)
RNPS1 ProteinQ15287 (Uniprot-TrEMBL)
RNPS1ProteinQ15287 (Uniprot-TrEMBL)
SARNP ProteinP82979 (Uniprot-TrEMBL)
SARNPProteinP82979 (Uniprot-TrEMBL)
SART1 ProteinO43290 (Uniprot-TrEMBL)
SART1ProteinO43290 (Uniprot-TrEMBL)
SEC13 ProteinP55735 (Uniprot-TrEMBL)
SEH1L-1 ProteinQ96EE3-1 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SF1 ProteinQ15637 (Uniprot-TrEMBL)
SF1ProteinQ15637 (Uniprot-TrEMBL)
SF3A1 ProteinQ15459 (Uniprot-TrEMBL)
SF3A2 ProteinQ15428 (Uniprot-TrEMBL)
SF3A3 ProteinQ12874 (Uniprot-TrEMBL)
SF3AComplexR-HSA-71967 (Reactome)
SF3B1 ProteinO75533 (Uniprot-TrEMBL)
SF3B2 ProteinQ13435 (Uniprot-TrEMBL)
SF3B3 ProteinQ15393 (Uniprot-TrEMBL)
SF3B4 ProteinQ15427 (Uniprot-TrEMBL)
SF3B5 ProteinQ9BWJ5 (Uniprot-TrEMBL)
SF3B6 ProteinQ9Y3B4 (Uniprot-TrEMBL)
SF3BComplexR-HSA-71976 (Reactome)
SKIV2L2 ProteinP42285 (Uniprot-TrEMBL)
SLBP ProteinQ14493 (Uniprot-TrEMBL)
SMNDC1 ProteinO75940 (Uniprot-TrEMBL)
SNRNP200 ProteinO75643 (Uniprot-TrEMBL)
SNRNP25 ProteinQ9BV90 (Uniprot-TrEMBL)
SNRNP27 ProteinQ8WVK2 (Uniprot-TrEMBL)
SNRNP27ProteinQ8WVK2 (Uniprot-TrEMBL)
SNRNP35 ProteinQ16560 (Uniprot-TrEMBL)
SNRNP40 ProteinQ96DI7 (Uniprot-TrEMBL)
SNRNP48 ProteinQ6IEG0 (Uniprot-TrEMBL)
SNRNP70 ProteinP08621 (Uniprot-TrEMBL)
SNRPA ProteinP09012 (Uniprot-TrEMBL)
SNRPA1 ProteinP09661 (Uniprot-TrEMBL)
SNRPB2 ProteinP08579 (Uniprot-TrEMBL)
SNRPC ProteinP09234 (Uniprot-TrEMBL)
SNRPD2 ProteinP62316 (Uniprot-TrEMBL)
SNRPE ProteinP62304 (Uniprot-TrEMBL)
SNRPF ProteinP62306 (Uniprot-TrEMBL)
SNRPG ProteinP62308 (Uniprot-TrEMBL)
SNW1 ProteinQ13573 (Uniprot-TrEMBL)
SNW1ProteinQ13573 (Uniprot-TrEMBL)
SRRM1 ProteinQ8IYB3 (Uniprot-TrEMBL)
SRRM1:SRRM2ComplexR-HSA-8865911 (Reactome)
SRRM2 ProteinQ9UQ35 (Uniprot-TrEMBL)
SRRT ProteinQ9BXP5 (Uniprot-TrEMBL)
SRRTProteinQ9BXP5 (Uniprot-TrEMBL)
SRSF1 ProteinQ07955 (Uniprot-TrEMBL)
SRSF10ProteinO75494 (Uniprot-TrEMBL)
SRSF11 ProteinQ05519 (Uniprot-TrEMBL)
SRSF11ProteinQ05519 (Uniprot-TrEMBL)
SRSF1ProteinQ07955 (Uniprot-TrEMBL)
SRSF2 ProteinQ01130 (Uniprot-TrEMBL)
SRSF2ProteinQ01130 (Uniprot-TrEMBL)
SRSF3 ProteinP84103 (Uniprot-TrEMBL)
SRSF3ProteinP84103 (Uniprot-TrEMBL)
SRSF4 ProteinQ08170 (Uniprot-TrEMBL)
SRSF4ProteinQ08170 (Uniprot-TrEMBL)
SRSF5 ProteinQ13243 (Uniprot-TrEMBL)
SRSF5ProteinQ13243 (Uniprot-TrEMBL)
SRSF6 ProteinQ13247 (Uniprot-TrEMBL)
SRSF6ProteinQ13247 (Uniprot-TrEMBL)
SRSF7 ProteinQ16629 (Uniprot-TrEMBL)
SRSF7ProteinQ16629 (Uniprot-TrEMBL)
SRSF9 ProteinQ13242 (Uniprot-TrEMBL)
SRSF9ProteinQ13242 (Uniprot-TrEMBL)
SUGP1 ProteinQ8IWZ8 (Uniprot-TrEMBL)
SUGP1ProteinQ8IWZ8 (Uniprot-TrEMBL)
SYF2 ProteinO95926 (Uniprot-TrEMBL)
SYF2ProteinO95926 (Uniprot-TrEMBL)
SYMPK ProteinQ92797 (Uniprot-TrEMBL)
Spliced mRNA:CBC:EJC:TREXComplexR-HSA-8850671 (Reactome)
Spliced mRNPComplexR-HSA-72157 (Reactome)
Spliceosomal

Intermediate C

(Bact) Complex		ComplexR-HSA-72074 (Reactome)
Spliceosomal A ComplexComplexR-HSA-72068 (Reactome)
Spliceosomal Active C (B*) ComplexComplexR-HSA-72022 (Reactome)
Spliceosomal B ComplexComplexR-HSA-72069 (Reactome)
Spliceosomal E ComplexComplexR-HSA-72057 (Reactome)
Spliceosomal active

C complex with lariat containing, 5'-end cleaved pre-mRNP:CBC

complex		ComplexR-HSA-77505 (Reactome)
TFIP11 ProteinQ9UBB9 (Uniprot-TrEMBL)
THO complexComplexR-HSA-8849128 (Reactome)
THOC1 ProteinQ96FV9 (Uniprot-TrEMBL)
THOC2 ProteinQ8NI27 (Uniprot-TrEMBL)
THOC3 ProteinQ96J01 (Uniprot-TrEMBL)
THOC5 ProteinQ13769 (Uniprot-TrEMBL)
THOC6 ProteinQ86W42 (Uniprot-TrEMBL)
THOC7 ProteinQ6I9Y2 (Uniprot-TrEMBL)
TPR ProteinP12270 (Uniprot-TrEMBL)
TRA2B ProteinP62995 (Uniprot-TrEMBL)
TRA2BProteinP62995 (Uniprot-TrEMBL)
TXNL4A ProteinP83876 (Uniprot-TrEMBL)
U1 snRNA ProteinV00590 (EMBL)
U1 snRNPComplexR-HSA-71917 (Reactome) The U1 snRNP is a particle consisting of the U1 snRNA and Sm core plus unique snRNP polypeptides. The U1-specific polypeptides are 70K, A, and C. The Sm core polypeptides are B, B', D1, D2, D3, E, F, G. The Sm core is a heteroheptamer in the shape of a donut, containing either B or B', which are almost identical to each other.
U11 snRNA ProteinENST00000387069 (Ensembl)
U11 snRNPComplexR-HSA-77462 (Reactome)
U12 snRNA ProteinENST00000362512 (Ensembl)
U12 snRNPComplexR-HSA-77472 (Reactome)
U2 snRNA ProteinX59360 (EMBL)
U2 snRNPComplexR-HSA-71980 (Reactome)
U2AF1 ProteinQ01081 (Uniprot-TrEMBL)
U2AF1,U2AF1L4ComplexR-HSA-8865886 (Reactome)
U2AF1L4 ProteinQ8WU68 (Uniprot-TrEMBL)
U2AF2 ProteinP26368 (Uniprot-TrEMBL)
U2AF2ProteinP26368 (Uniprot-TrEMBL)
U2SURP ProteinO15042 (Uniprot-TrEMBL)
U4 ATAC snRNPComplexR-HSA-77465 (Reactome)
U4 ATAC:U5:U6 ATAC ComplexComplexR-HSA-77469 (Reactome)
U4 snRNA ProteinX59361 (EMBL)
U4 snRNPComplexR-HSA-71891 (Reactome)
U4:U5:U6 tri-snRNP complexComplexR-HSA-77506 (Reactome)
U4atac snRNA ProteinENST00000580972 (Ensembl)
U5 snRNA ProteinX04293 (EMBL)
U5 snRNPComplexR-HSA-71981 (Reactome)
U6 ATAC snRNA R-ALL-77466 (Reactome)
U6 ATAC snRNPComplexR-HSA-77467 (Reactome)
U6 snRNA ProteinX59362 (EMBL)
UPF3B ProteinQ9BZI7 (Uniprot-TrEMBL)
UPF3BProteinQ9BZI7 (Uniprot-TrEMBL)
USP39 ProteinQ53GS9 (Uniprot-TrEMBL)
USP39ProteinQ53GS9 (Uniprot-TrEMBL)
WBP11 ProteinQ9Y2W2 (Uniprot-TrEMBL)
WBP4 ProteinO75554 (Uniprot-TrEMBL)
WBP4ProteinO75554 (Uniprot-TrEMBL)
WDR33 ProteinQ9C0J8 (Uniprot-TrEMBL)
WTAP ProteinQ15007 (Uniprot-TrEMBL)
XAB2 ProteinQ9HCS7 (Uniprot-TrEMBL)
XAB2ProteinQ9HCS7 (Uniprot-TrEMBL)
YBX1 ProteinP67809 (Uniprot-TrEMBL)
YBX1ProteinP67809 (Uniprot-TrEMBL)
ZC3H11A ProteinO75152 (Uniprot-TrEMBL)
ZC3H11AProteinO75152 (Uniprot-TrEMBL)
ZCRB1 ProteinQ8TBF4 (Uniprot-TrEMBL)
ZMAT5 ProteinQ9UDW3 (Uniprot-TrEMBL)
ZRSR2 ProteinQ15696 (Uniprot-TrEMBL)
ZRSR2ProteinQ15696 (Uniprot-TrEMBL)
capped

pre-mRNA:CBC:RNA Pol II (phosphorylated)

complex		ComplexR-HSA-77089 (Reactome)
capped pre-mRNA R-ALL-72085 (Reactome)
capped, methylated

pre-mRNA:CBC

Complex		ComplexR-HSA-71954 (Reactome)
capped, methylated

pre-mRNP:CBC

complex		ComplexR-HSA-71955 (Reactome)
capped, methylated pre-mRNA R-ALL-77507 (Reactome)
excised intron R-ALL-72158 (Reactome)
hSLU7 ProteinO95391 (Uniprot-TrEMBL)
hSLU7ProteinO95391 (Uniprot-TrEMBL)
hTra2 R-HSA-72063 (Reactome)
intron-containing complexComplexR-HSA-72159 (Reactome)
lariat containing 5'-end cleaved mRNA R-ALL-156756 (Reactome)
mRNA (N6-adenosine)-methyltransferaseComplexR-HSA-72093 (Reactome)
mRNA 3'-end cleavage factorComplexR-HSA-72075 (Reactome)
mRNA R-HSA-72323 (Reactome)
mRNA with spliced exons R-ALL-72156 (Reactome)
mRNA:CBC:EJC:POLDIP3ComplexR-HSA-159329 (Reactome)
p-S5-POLR2A ProteinP24928 (Uniprot-TrEMBL)
polyadenylated,

capped

mRNA:CBC:EJC:TREX:SRSF proteins		ComplexR-HSA-156769 (Reactome)
post exon ligation complexComplexR-HSA-156556 (Reactome)
pre-EJC:Spliceosomal C:pre-mRNP:CBCComplexR-HSA-156656 (Reactome)

Annotated Interactions

View all...
Source  â†“Target  â†“Type  â†“Database reference  â†“Comment  â†“
3' end cleaved,

ligated exon

containing complex		ArrowR-HSA-72180 (Reactome)
3' end cleaved,

ligated exon

containing complex		R-HSA-72185 (Reactome)
ALYREF, FYTTD1, LUZP4ArrowR-HSA-75096 (Reactome)
ALYREF, FYTTD1, LUZP4R-HSA-8849157 (Reactome)
ALYREFArrowR-HSA-158447 (Reactome)
ALYREFArrowR-HSA-158484 (Reactome)
ALYREFArrowR-HSA-159050 (Reactome)
ALYREFR-HSA-111439 (Reactome)
ALYREFR-HSA-72107 (Reactome)
ALYREFR-HSA-77587 (Reactome)
ALYREFR-HSA-77594 (Reactome)
AQRR-HSA-72127 (Reactome)
ATAC A ComplexArrowR-HSA-75080 (Reactome)
ATAC A ComplexR-HSA-75081 (Reactome)
ATAC B ComplexArrowR-HSA-75081 (Reactome)
ATAC B ComplexR-HSA-75079 (Reactome)
ATAC C Complex with

lariat containing

5'-end cleaved mRNA		ArrowR-HSA-75082 (Reactome)
ATAC C Complex with

lariat containing

5'-end cleaved mRNA		R-HSA-75083 (Reactome)
ATAC C ComplexArrowR-HSA-75079 (Reactome)
ATAC C ComplexR-HSA-75082 (Reactome)
ATPR-HSA-72185 (Reactome)
ATPR-HSA-8849157 (Reactome)
BUD31R-HSA-72127 (Reactome)
CASC3R-HSA-72160 (Reactome)
CCAR1R-HSA-72107 (Reactome)
CD2BP2R-HSA-72107 (Reactome)
CDC40ArrowR-HSA-75096 (Reactome)
CDC40R-HSA-72124 (Reactome)
CF IArrowR-HSA-72180 (Reactome)
CF IIArrowR-HSA-72180 (Reactome)
CF IIR-HSA-72231 (Reactome)
CF IR-HSA-72231 (Reactome)
CHTOPArrowR-HSA-75096 (Reactome)
CHTOPR-HSA-8849157 (Reactome)
CPSFArrowR-HSA-72185 (Reactome)
CPSFArrowR-HSA-77594 (Reactome)
CPSFR-HSA-72231 (Reactome)
CRNKL1R-HSA-72127 (Reactome)
CWC22R-HSA-72124 (Reactome)
CWC25R-HSA-72130 (Reactome)
CWC27ArrowR-HSA-72139 (Reactome)
CWC27R-HSA-72130 (Reactome)
Cap Binding Complex (CBC)ArrowR-HSA-111439 (Reactome)
Cap Binding Complex (CBC)ArrowR-HSA-77594 (Reactome)
Cleavage and

Polyadenylation

Complex		ArrowR-HSA-72231 (Reactome)
Cleavage and

Polyadenylation

Complex		R-HSA-72130 (Reactome)
CstFArrowR-HSA-72180 (Reactome)
CstFR-HSA-72231 (Reactome)
DDX39A,BR-HSA-8849157 (Reactome)
DDX39B:ADPArrowR-HSA-159101 (Reactome)
DDX5R-HSA-72107 (Reactome)
DHX16R-HSA-72130 (Reactome)
DHX38ArrowR-HSA-75096 (Reactome)
DHX38R-HSA-72124 (Reactome)
DHX9R-HSA-72107 (Reactome)
DNAJC8R-HSA-72124 (Reactome)
EIF4A3R-HSA-72130 (Reactome)
EIF4ER-HSA-158447 (Reactome)
EIF4ER-HSA-158484 (Reactome)
EIF4ER-HSA-159050 (Reactome)
ELAVL1R-HSA-72124 (Reactome)
ELAVL2R-HSA-72124 (Reactome)
FUSR-HSA-72107 (Reactome)
GLE1ArrowR-HSA-75097 (Reactome)
GPKOWR-HSA-72130 (Reactome)
HNRNPA0ArrowR-HSA-72160 (Reactome)
HNRNPA0R-HSA-72103 (Reactome)
HNRNPA1ArrowR-HSA-72160 (Reactome)
HNRNPA1R-HSA-72103 (Reactome)
HNRNPA2B1R-HSA-72103 (Reactome)
HNRNPA3ArrowR-HSA-72160 (Reactome)
HNRNPA3R-HSA-72103 (Reactome)
HNRNPCArrowR-HSA-72160 (Reactome)
HNRNPCR-HSA-72103 (Reactome)
HNRNPDArrowR-HSA-72160 (Reactome)
HNRNPDR-HSA-72103 (Reactome)
HNRNPFArrowR-HSA-72160 (Reactome)
HNRNPFR-HSA-72103 (Reactome)
HNRNPH1ArrowR-HSA-72160 (Reactome)
HNRNPH1R-HSA-72103 (Reactome)
HNRNPH2ArrowR-HSA-72160 (Reactome)
HNRNPH2R-HSA-72103 (Reactome)
HNRNPKArrowR-HSA-72160 (Reactome)
HNRNPKR-HSA-72103 (Reactome)
HNRNPLArrowR-HSA-72160 (Reactome)
HNRNPLR-HSA-72103 (Reactome)
HNRNPMArrowR-HSA-72160 (Reactome)
HNRNPMR-HSA-72103 (Reactome)
HNRNPRArrowR-HSA-72160 (Reactome)
HNRNPRR-HSA-72103 (Reactome)
HNRNPUL1R-HSA-72107 (Reactome)
HNRNPUR-HSA-72103 (Reactome)
ISY1R-HSA-72127 (Reactome)
LSM2-8 complexArrowR-HSA-72130 (Reactome)
Magoh-Y14 complexR-HSA-156661 (Reactome)
Mature

Intronless transcript derived Histone

mRNA:SLBP:CBP80:CBP20		R-HSA-77587 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		ArrowR-HSA-159046 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		ArrowR-HSA-77587 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		R-HSA-159046 (Reactome)
Mature

intronless transcript derived Histone

mRNA:SLBP:TAP:Aly/Ref complex		R-HSA-159050 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

Complex		ArrowR-HSA-158481 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

Complex		R-HSA-158484 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

complex		ArrowR-HSA-111439 (Reactome)
Mature Intronless

Transcript Derived Histone mRNA:TAP:Aly/Ref

complex		R-HSA-158481 (Reactome)
Mature Intronless

Transcript Derived

mRNA:eIF4E Complex		ArrowR-HSA-158447 (Reactome)
Mature SLBP

independent Histone

mRNA:eIF4E complex		ArrowR-HSA-158484 (Reactome)
Mature intronless

derived mRNA:TAP:Aly/Ref

complex		ArrowR-HSA-158441 (Reactome)
Mature intronless

derived mRNA:TAP:Aly/Ref

complex		R-HSA-158447 (Reactome)
Mature intronless

derived mRNA

complex		R-HSA-77594 (Reactome)
Mature intronless

transcript derived Histone mRNA:SLBP:eIF4E

Complex		ArrowR-HSA-159050 (Reactome)
Mature intronless

transcript derived Histone pre-mRNA:CBC

complex		R-HSA-111439 (Reactome)
NCBP1ArrowR-HSA-77587 (Reactome)
NCBP2ArrowR-HSA-77587 (Reactome)
NPC:NXF1,2:NXT1:EJC:CBC:mRNAArrowR-HSA-75096 (Reactome)
NPC:NXF1,2:NXT1:EJC:CBC:mRNAR-HSA-75097 (Reactome)
NPC:NXF1:NXT1:EJC:CBC:mRNAArrowR-HSA-75097 (Reactome)
NPC:NXF1:NXT1:EJC:CBC:mRNAR-HSA-75098 (Reactome)
NXF1,2:NXT1::polyadenylated, capped mRNA:CBC:EJC:TREX:SRSF proteinsArrowR-HSA-159101 (Reactome)
NXF1,2:NXT1::polyadenylated, capped mRNA:CBC:EJC:TREX:SRSF proteinsR-HSA-75096 (Reactome)
NXF1,2:NXT1ArrowR-HSA-75098 (Reactome)
NXF1,2:NXT1R-HSA-159101 (Reactome)
NXF1ArrowR-HSA-158447 (Reactome)
NXF1ArrowR-HSA-158484 (Reactome)
NXF1ArrowR-HSA-159050 (Reactome)
NXF1R-HSA-111439 (Reactome)
NXF1R-HSA-77587 (Reactome)
NXF1R-HSA-77594 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-111439 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-158441 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-158447 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-158481 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-158484 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-159046 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-159050 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-75096 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-75097 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-75098 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-77587 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-77594 (Reactome)
Nuclear Pore Complex (NPC)R-HSA-75096 (Reactome)
Nucleoplasmic mature

intronless derived mRNA:TAP:Aly/Ref

complex		ArrowR-HSA-77594 (Reactome)
Nucleoplasmic mature

intronless derived mRNA:TAP:Aly/Ref

complex		R-HSA-158441 (Reactome)
PABPN1ArrowR-HSA-72185 (Reactome)
PABPN1R-HSA-72231 (Reactome)
PAPOLAArrowR-HSA-72185 (Reactome)
PAPOLAR-HSA-72231 (Reactome)
PAPOLAmim-catalysisR-HSA-72185 (Reactome)
PCBP1ArrowR-HSA-72160 (Reactome)
PCBP1R-HSA-72103 (Reactome)
PCBP2ArrowR-HSA-72160 (Reactome)
PCBP2R-HSA-72103 (Reactome)
POLDIP3R-HSA-8849157 (Reactome)
PPIER-HSA-72127 (Reactome)
PPILR-HSA-72127 (Reactome)
PPWD1R-HSA-72143 (Reactome)
PRCCR-HSA-72127 (Reactome)
PRP19-CDC5L complexR-HSA-72124 (Reactome)
PRPF38AArrowR-HSA-72130 (Reactome)
PRPF38AR-HSA-72127 (Reactome)
PRPF40AArrowR-HSA-72127 (Reactome)
PRPF40AR-HSA-72107 (Reactome)
PTBP1R-HSA-72103 (Reactome)
PiArrowR-HSA-159101 (Reactome)
R-HSA-111439 (Reactome) Histone mRNAs are exported by a mechanism that requires TAP, the key factor required for transport of polyadenylated mRNAs. How TAP is recruited to the histone mRNAs is not known, but it is clear that transport can occur in the absence of either the stemloop or of SLBP. The mature transcript docks at the NPC. In the course of transport, CBC is lost from the mRNA cap, and remain in the nucleous.
R-HSA-156661 (Reactome) At the beginning of this reaction, 1 molecule of 'Magoh-Y14 complex', and 1 molecule of 'Spliceosomal active C complex with lariat containing, 5'-end cleaved pre-mRNP:CBC complex' are present. At the end of this reaction, 1 molecule of 'Exon Junction Complex' is present.

This reaction takes place in the 'nucleoplasm'.

R-HSA-158441 (Reactome) The nucleoplasmic 3' polyadenylated, capped intronless mRNA and TAP are transported through the NPC to the cyotplasmic side of the pore.
R-HSA-158447 (Reactome) The cytoplasmic 3' polyadenylated, capped intronless mRNA and TAP are released from the NPC into the cytosol. Cytosolic TAP will be recycled to the nucleous, while the 3' polyadenylated, capped intronless mRNA is bound by eIF4E and destined for translation (Carmody and Wente 2009, Wente and Rout 2010, Hetten and Kehlenbach 2007).
R-HSA-158481 (Reactome) The mature SLBP independent intronless histone mRNA is transported through the nucler pore to the cytoplasmic side (von Moeller et al.2013). This is a black box event since there is not physical evidence about how exactly occurs this transport.
R-HSA-158484 (Reactome) At some point eIF4E binds the mature mRNA. While TAP and Aly/Ref are released and will be reycled back to the nucleoplasm (Hung et al.2010, Lindtner et al. 2002).
R-HSA-159046 (Reactome) Once the transport complex is fully assembled the mature mRNA can be translocated from the nucleoplasm to the cytoplasm. The assembled complex starts at the nucleoplasmic basket, travels through the pore, and ends it journey at the cytoplasmic face of the nuclear pore complex.
R-HSA-159050 (Reactome) At some point eIF4E binds the mature mRNA. While TAP and Aly/Ref are released and will be reycled back to the nucleoplasm (Hung et al.2010, Lindtner et al. 2002).
R-HSA-159101 (Reactome) The mRNA is transferred from ALYREF of the TREX complex to NXF1 (TAP) of the NXF1:NXT1 export complex (Hautbergue et al. 2008). Interaction between the TREX complex and NXF1 exposes the arginine-rich RNA-binding domain of NXF1 (Viphakone et al. 2012). Methylation of arginine residues on ALYREF also appears to be necessary for dissociation of mRNA from ALYREF during the transfer (Hung et al. 2010). The interaction between ALYREF and NXF1 occurs in the vicinity of nuclear speckles (Teng and Wilson 2013). DDX39B (UAP56) binds (Kota et al. 2008) and hydrolyzes ATP (Taniguchi and Ohno 2008). UAP56 is believed to hydrolyze ATP and UAP56:ADP is believed to dissociate at some point during the transfer of the mRNA to NXF1 (Taniguchi and Ohno 2008, Chang et al. 2013).
R-HSA-72095 (Reactome) In addition to the methylation of the 5'-cap, there is methylation of internal nucleotides in the mRNA. This methylation can occur in translated and untranslated regions. One to three methyl groups have been seen per mRNA molecule, but methylation is non-stoichiometric. The most frequent methylation observed is at the N6 position of adenosine. The function of mRNA internal methylation, if any, is unknown.
R-HSA-72103 (Reactome) After the nascent pre-mRNA undergoes the initial capping and methylation reactions, it gets associated with numerous factors, including the various heterogeneous nuclear ribonucleoproteins (hnRNPS), the nuclear Cap-Binding Complex, and many splicing factors that make the pre-mRNA a substrate for splicing, 3'-end processing, and in some cases editing.
R-HSA-72107 (Reactome) Pre-mRNA transcripts become rapidly associated with many RNA-binding proteins, including hnRNP proteins, cap-binding proteins, SR proteins, etc; in the test tube this binding does not require splice sites or ATP. The E complex, or early complex, is the first detectable functional intermediate in spliceosome assembly in vitro. It is an ATP-independent complex. When a functional 5' splice site is present, it is bound by the U1 snRNP. The splicing factor U2AF (65 and 35 kDa subunits) binds to the polypyrimidine tract (Y)n and the AG dinucleotide at the 3' splice site, respectively. SF1/mBBP binds to the branch site. Binding of many of these factors is cooperative; e.g., SR proteins and U2AF apparently interact with each other, facilitating their binding to the pre-mRNA. In the presence of ATP, the E complex is converted to the first ATP-dependent spliceosomal complex, namely the A complex.
R-HSA-72124 (Reactome) The A complex is the first ATP-dependent complex in spliceosome assembly. U2AF recruits the U2 snRNP to bind to the branch site in the E complex in an ATP-dependent fashion, to form the A complex. The U2 snRNA base-pairs with the branch site, causing the branch-site adenosine to bulge out, which later positions it for nucleophilic attack at the 5' splice site. The A complex serves as a substrate for formation of the B complex.
R-HSA-72127 (Reactome) The formation of the B complex is ATP-dependent, and both the 5' and 3' splice sites are essential for B complex assembly. The U4 and U6 snRNPS are extensively base-paired, and this U4:U6 complex associates with the U5 snRNP to form a tri-snRNP particle. This tri-snRNP particle then binds to the spliceosomal A complex, to form the spliceosomal B complex.
R-HSA-72130 (Reactome) The intermediate spliceosomal C complex (also called the Bact or B(act) complex) is a very short-lived intermediate; the splicing intermediates are rapidly converted to splicing products. Also, the spliced products are released very rapidly, and no complex containing both the splicing products has been isolated. Conversion of the spliceosomal B complex to the spliceosomal C complex requires ATP. The extensive base-pairing between the U4 and U6 snRNAs is disrupted during the formation of the C complex, which is thought to require helicase-type activity associated with the DEAD box factors. The U4 snRNP and U1 snRNP dissociate from the complex and the LSM2-6 complex of the U6 snRNP is lost, apparently allowing the U6 snRNA to then base-pair with the U2 snRNA and the 5' end of the splice site on the mRNA (Bessonov et al. 2010).
R-HSA-72139 (Reactome) The active C complex is formed due to a conformational change in the intermediate C complex. After formation of the active C complex, the splicing reactions occur very rapidly.
R-HSA-72143 (Reactome) In the first catalytic step of mRNA splicing, the 2' OH group of the bulged A at the branch site performs a nucleophilic attack on the 5' splice site phosphodiester bond, resulting in cleavage of the bond between the 5' exon and the 5' end of the intron, and formation of a new bond between the 5' end of the intron and the branch site A. This results in a lariat-shaped intermediate, with the intron still attached to the 3' exon. The branch site A has a 2'-5' phosphodiester bond with the G at the beginning of the intron, in addition to the usual 5'-3' and 3'-5'phosphodiester bonds.
R-HSA-72160 (Reactome) The second step of the splicing reaction results in cleavage of the transcript at the 3'splice site, and results in ligation of the two exons and excision of the intron.
R-HSA-72180 (Reactome) Endonucleolytic cleavage separates the pre-mRNA into an upstream fragment destined to become the mature mRNA, and a downstream fragment that is rapidly degraded. Cleavage depends on two signals in the RNA, a highly conserved hexanucleotide, AAUAAA, 10 to 30 nucleotides upstream of the cleavage site, and a poorly conserved GU- or U-rich downstream element. Additional sequences, often upstream of AAUAAA, can enhance the efficiency of the reaction. Cleavage occurs most often after a CA dinucleotide. A single gene can have more than one 3' processing site.

Cleavage is preceded by the assembly of a large processing complex, the composition of which is poorly defined. ATP, but not its hydrolysis, is required for assembly. Cleavage at the 3'-end of mRNAs depends on a number of protein factors. CPSF, a heterotetramer, binds specifically to the AAUAAA sequence. The heterotrimer CstF binds the downstream element. CF I, which appears to be composed of two subunits, one of several related larger polypeptides and a common smaller one, also binds RNA, but with unknown specificity. RNA recognition by these proteins is cooperative. Cleavage also requires CF II, composed of at least two subunits, and poly(A) polymerase, the enzyme synthesizing the poly(A) tail in the second step of the reaction. The polypeptide catalyzing the hydrolysis of the phosphodiester bond remains to be identified.

Cleavage produces a 3'-OH on the upstream fragment and a 5'-phosphate on the downstream fragment. At some unknown point after cleavage, the downstream RNA fragment, CstF, CF I and CF II are thought to be released, whereas CPSF and poly(A) polymerase remain to carry out polyadenylation.

R-HSA-72185 (Reactome) The upstream fragment generated by 3' cleavage of the pre-mRNA receives a poly(A) tail of approximately 250 AMP residues in a reaction depending on the AAUAAA sequence 10 to 30 nucleotides upstream of the 3' end. Polyadenylation is carried out by three proteins: Poly(A) polymerase carries the catalytic activity. The enzyme has no specificity for any particular RNA sequence, and it also has a very low affinity for the RNA.

Under physiological conditions, the activity of poly(A) polymerase thus depends on two auxiliary factors, both of which bind to specific RNA sequences and recruit the enzyme by a direct contact. One of these proteins is the heterotetrameric CPSF, which binds the AAUAAA sequence and is also essential for 3' cleavage. The second is the nuclear poly(A) binding protein (PABPN1), which binds the growing poly(A) tails once this has reached a length of about ten nucleotides. Stimulation of poly(A) polymerase by both proteins is synergistic and results in processive elongation of the RNA, i.e. the polymerase adds AMP residues without dissociating from the RNA. The processive reaction is terminated when the tail has reached a length of about 250 nucleotides.

R-HSA-72231 (Reactome) The cleavage and polyadenylation complex includes proteins that recognize the polyA addition signal of the nascent mRNA as well as the endonulcease that cleaves the RNA and other RNA binding elements (Charlesworth et al. 2013).
R-HSA-75079 (Reactome) At the beginning of this reaction, 1 molecule of 'ATAC B Complex' is present. At the end of this reaction, 1 molecule of 'U4 ATAC snRNP', and 1 molecule of 'ATAC C Complex' are present.

This reaction takes place in the 'nucleus' (Pikielny et al.1989, Kreivi et al. 1996).

R-HSA-75080 (Reactome) U12-type AT-AC introns are distinguished from the major U2-type introns by the consensus sequences of their highly conserved splicing signals. U12 introns have the 5' ss consensus sequence (G/A)TATCCTTT, the branchpoint sequence TTTCCTTAACT and the 3' ss (C/T)AG. Initial recognition of AT-AC introns involves interaction of U12 snRNP with the branch-point sequence and U11 with the 5' ss. Unlike the major splicing pathway, U11 and U12 are in a complex and interact with the pre-mRNA simultaneously, binding in an ATP-dependent manner as a di-snRNP complex and likely bridging the 5' ss and 3' ss region.

Twenty proteins have been identified in the U11/U12 di-snRNP complex including the snRNP Sm proteins B’, B, D3, D2, D1, E, F, and G which are identical to the major splicing pathway Sm proteins. A U2 snRNP core protein complex, SF3b is also found in the U11/U12 di-snRNP, including p14, a protein that interacts with the branchpoint adenosine.

SR proteins are required for formation of A complex in AT-AC splicing. The same SR proteins involved in splicing of the major introns are also active in splicing of AT-AC introns, though, as in the major pathway, there is substrate specificity.

R-HSA-75081 (Reactome) The U4atac/U6atac enters the spliceosome and U6atac snRNA forms base pairing interactions with the 5' ss and also forms base pairing interactions with U12 and U4atac is partially displaced. U5 snRNP, the only snRNP common to both the major and minor splicing pathways, also joins the spliceosome to form the B complex and interacts with nucleotides within the 3' end of the exon flanking the 5' ss (Singh et al.2016, Wu and Krainer 1999).
R-HSA-75082 (Reactome) At the beginning of this reaction, 1 molecule of 'ATAC C Complex' is present. At the end of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present.

This reaction takes place in the 'nucleus' (Valadkhan and Manley 2001, Valadkhan et al. 2007).

R-HSA-75083 (Reactome) At the beginning of this reaction, 1 molecule of 'ATAC C Complex with lariat containing 5'-end cleaved mRNA' is present. At the end of this reaction, 1 molecule of 'U6 ATAC snRNP', 1 molecule of 'post exon ligation complex', 1 molecule of 'U12 snRNP', 1 molecule of 'U11 snRNP', and 1 molecule of 'U5 snRNP' are present.

This reaction takes place in the 'nucleus'.

R-HSA-75096 (Reactome) At the beginning of this reaction, 1 molecule of 'TAP:3'-polyadenylated, capped mRNA complex' is present. At the end of this reaction, 1 molecule of 'SRp55', 1 molecule of 'U2AF 65 kDa subunit', 1 molecule of 'SR9 / SRp30', 1 molecule of 'hTra2', 1 molecule of 'hPrp16', 1 molecule of 'SR 11/ p54', 1 molecule of 'hPrp22', 1 molecule of 'SRp40', 1 molecule of 'hPrp17', 1 molecule of 'SF2/ASF/SFRS1', 1 molecule of 'hSLU7', 1 molecule of 'Export Receptor bound mature mRNA Complex', 1 molecule of 'U2AF 35 kDa subunit', 1 molecule of 'SR2 / SC35', 1 molecule of 'hPrp43', 1 molecule of 'SRp20', 1 molecule of 'SR7/ 9G8 protein', 1 molecule of 'hPrp18', and 1 molecule of 'SR4 / SRp75' are present.

This reaction takes place in the 'nucleoplasm'.

R-HSA-75097 (Reactome) In this reaction, 1 molecule of 'Export Receptor bound mature mRNA Complex' is translocated from nucleoplasm to cytosol.

This reaction takes place in the 'nuclear envelope'.

R-HSA-75098 (Reactome) At the beginning of this reaction, 1 molecule of and 1 molecule of 'Export Receptor bound mature mRNA Complex' are present. At the end of this reaction, 1 molecule of 'THOC4(Aly/Ref)', 1 molecule of 'Mature mRNP Complex', 1 molecule of 'SRm160', and 1 molecule of 'TAP' are present.

This reaction takes place in the 'cytoplasm'.

R-HSA-77587 (Reactome) Histone mRNAs are exported by a mechanism that requires TAP, the key factor requires for transport of polyadenylated mRNAs. How TAP is recruited to the histone mRNAs is not known, but it is clear that transport can occur in the absence of either the stemloop or of SLBP. The stemloop and SLBP enhance the rate of transport of histone mRNAs in Xenopus oocytes, but are not essential for transport
R-HSA-77594 (Reactome) The polyadenylated, capped transcript and TAP dock at the nucleoplasmic side of the NPC. The Cap Binding Complex (CBC) and CPSF complexes are released back into the nucleoplasm (Zhou et al. 2000).
R-HSA-8849157 (Reactome) The THO subcomplex of the TREX complex initially interacts with the serine-2,5 phosphorylated C-terminal domain of RNA polymerase II (Strasser et al. 2002, Inferred from yeast in Meinel et al. 2013) then with CBP80 of the cap binding complex (Cheng et al. 2006, Dufu et al. 2010, Chi et al. 2013). A TREX complex binds spliced mRNA near the cap during transcription (Cheng et al. 2006). Recruitment is dependent on splicing of the mRNA (Masuda et al. 2005). THO/TREX is required for efficient mRNP biogenesis and export (reviewed in Luna et al 2012). In yeast, components of the THO/TREX complex also affect transcription and 3' processing of mRNA, (Rondon et al. 2003, Rougemaille et al. 2008, Johnson et al. 2011, reviewed in Katahira 2015), however the human TREX complex does not appear to affect transcription (Masuda et al. 2005). The AREX complex, which contains DDX39A (UHR49) rather than DDX39B (UAP56) appears to perform the same function as TREX in mRNA export, but acts on a different subset of mRNAs (Yamazaki et al. 2010).
RBM22R-HSA-72127 (Reactome)
RBM5R-HSA-72107 (Reactome)
RBMXArrowR-HSA-72160 (Reactome)
RBMXR-HSA-72103 (Reactome)
RNA

polymerase II

(phosphorylated):TFIIF complex		ArrowR-HSA-72160 (Reactome)
RNPS1R-HSA-72107 (Reactome)
SARNPArrowR-HSA-75096 (Reactome)
SARNPR-HSA-8849157 (Reactome)
SART1ArrowR-HSA-72130 (Reactome)
SF1ArrowR-HSA-72124 (Reactome)
SF1R-HSA-72107 (Reactome)
SF3AArrowR-HSA-72160 (Reactome)
SF3BArrowR-HSA-72160 (Reactome)
SNRNP27ArrowR-HSA-72130 (Reactome)
SNW1R-HSA-72127 (Reactome)
SRRM1:SRRM2R-HSA-72107 (Reactome)
SRRTR-HSA-72107 (Reactome)
SRSF10TBarR-HSA-72107 (Reactome)
SRSF11ArrowR-HSA-75096 (Reactome)
SRSF11R-HSA-72124 (Reactome)
SRSF1ArrowR-HSA-75096 (Reactome)
SRSF1R-HSA-72107 (Reactome)
SRSF1R-HSA-75080 (Reactome)
SRSF2ArrowR-HSA-75096 (Reactome)
SRSF2R-HSA-72107 (Reactome)
SRSF2R-HSA-75080 (Reactome)
SRSF3ArrowR-HSA-75096 (Reactome)
SRSF3R-HSA-72107 (Reactome)
SRSF4ArrowR-HSA-75096 (Reactome)
SRSF4R-HSA-72124 (Reactome)
SRSF5ArrowR-HSA-75096 (Reactome)
SRSF5R-HSA-72107 (Reactome)
SRSF6ArrowR-HSA-75096 (Reactome)
SRSF6R-HSA-72107 (Reactome)
SRSF6R-HSA-75080 (Reactome)
SRSF7ArrowR-HSA-75096 (Reactome)
SRSF7R-HSA-72107 (Reactome)
SRSF7R-HSA-75080 (Reactome)
SRSF9ArrowR-HSA-75096 (Reactome)
SRSF9R-HSA-72107 (Reactome)
SUGP1R-HSA-72107 (Reactome)
SYF2R-HSA-72143 (Reactome)
Spliced mRNA:CBC:EJC:TREXArrowR-HSA-8849157 (Reactome)
Spliced mRNA:CBC:EJC:TREXR-HSA-72180 (Reactome)
Spliced mRNPArrowR-HSA-72160 (Reactome)
Spliced mRNPR-HSA-8849157 (Reactome)
Spliceosomal

Intermediate C

(Bact) Complex		ArrowR-HSA-72130 (Reactome)
Spliceosomal

Intermediate C

(Bact) Complex		R-HSA-72139 (Reactome)
Spliceosomal

Intermediate C

(Bact) Complex		mim-catalysisR-HSA-72139 (Reactome)
Spliceosomal A ComplexArrowR-HSA-72124 (Reactome)
Spliceosomal A ComplexR-HSA-72127 (Reactome)
Spliceosomal Active C (B*) ComplexArrowR-HSA-72139 (Reactome)
Spliceosomal Active C (B*) ComplexR-HSA-72143 (Reactome)
Spliceosomal B ComplexArrowR-HSA-72127 (Reactome)
Spliceosomal B ComplexR-HSA-72130 (Reactome)
Spliceosomal E ComplexArrowR-HSA-72107 (Reactome)
Spliceosomal E ComplexR-HSA-72124 (Reactome)
Spliceosomal active

C complex with lariat containing, 5'-end cleaved pre-mRNP:CBC

complex		ArrowR-HSA-72143 (Reactome)
Spliceosomal active

C complex with lariat containing, 5'-end cleaved pre-mRNP:CBC

complex		R-HSA-156661 (Reactome)
THO complexArrowR-HSA-75096 (Reactome)
THO complexR-HSA-8849157 (Reactome)
TRA2BR-HSA-72143 (Reactome)
U1 snRNPArrowR-HSA-72130 (Reactome)
U1 snRNPR-HSA-72107 (Reactome)
U11 snRNPArrowR-HSA-75083 (Reactome)
U11 snRNPR-HSA-75080 (Reactome)
U12 snRNPArrowR-HSA-75083 (Reactome)
U12 snRNPR-HSA-75080 (Reactome)
U2 snRNPR-HSA-72124 (Reactome)
U2AF1,U2AF1L4ArrowR-HSA-75096 (Reactome)
U2AF1,U2AF1L4R-HSA-72107 (Reactome)
U2AF2ArrowR-HSA-75096 (Reactome)
U2AF2R-HSA-72107 (Reactome)
U4 ATAC snRNPArrowR-HSA-75079 (Reactome)
U4 ATAC:U5:U6 ATAC ComplexR-HSA-75081 (Reactome)
U4 snRNPArrowR-HSA-72130 (Reactome)
U4:U5:U6 tri-snRNP complexR-HSA-72127 (Reactome)
U5 snRNPArrowR-HSA-75083 (Reactome)
U6 ATAC snRNPArrowR-HSA-75083 (Reactome)
UPF3BR-HSA-72143 (Reactome)
USP39ArrowR-HSA-72130 (Reactome)
WBP4ArrowR-HSA-72130 (Reactome)
WBP4R-HSA-72124 (Reactome)
XAB2R-HSA-72127 (Reactome)
YBX1R-HSA-72107 (Reactome)
ZC3H11AArrowR-HSA-75096 (Reactome)
ZC3H11AR-HSA-8849157 (Reactome)
ZRSR2R-HSA-75080 (Reactome)
capped

pre-mRNA:CBC:RNA Pol II (phosphorylated)

complex		R-HSA-72095 (Reactome)
capped, methylated

pre-mRNA:CBC

Complex		ArrowR-HSA-72095 (Reactome)
capped, methylated

pre-mRNA:CBC

Complex		R-HSA-72103 (Reactome)
capped, methylated

pre-mRNA:CBC

Complex		R-HSA-75080 (Reactome)
capped, methylated

pre-mRNP:CBC

complex		ArrowR-HSA-72103 (Reactome)
capped, methylated

pre-mRNP:CBC

complex		R-HSA-72107 (Reactome)
hSLU7ArrowR-HSA-75096 (Reactome)
hSLU7R-HSA-72160 (Reactome)
intron-containing complexArrowR-HSA-72160 (Reactome)
mRNA (N6-adenosine)-methyltransferasemim-catalysisR-HSA-72095 (Reactome)
mRNA 3'-end cleavage factormim-catalysisR-HSA-72180 (Reactome)
mRNA:CBC:EJC:POLDIP3ArrowR-HSA-75098 (Reactome)
polyadenylated,

capped

mRNA:CBC:EJC:TREX:SRSF proteins		ArrowR-HSA-72185 (Reactome)
polyadenylated,

capped

mRNA:CBC:EJC:TREX:SRSF proteins		R-HSA-159101 (Reactome)
polyadenylated,

capped

mRNA:CBC:EJC:TREX:SRSF proteins		mim-catalysisR-HSA-159101 (Reactome)
post exon ligation complexArrowR-HSA-75083 (Reactome)
pre-EJC:Spliceosomal C:pre-mRNP:CBCArrowR-HSA-156661 (Reactome)
pre-EJC:Spliceosomal C:pre-mRNP:CBCR-HSA-72160 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP1889"
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