SARS-CoV-2 Infection (Homo sapiens)

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41, 1651332410626, 52, 84, 8913915269211403, 36, 39, 73, 1378, 101, 10437, 115, 138, 15813915, 20, 66, 1501127, 79, 92, 94, 123...6, 12, 23, 59, 71...33991816037, 1497, 55, 6069528, 34, 58, 97, 136...1, 42, 82, 90, 96...601464113949, 11014728, 46, 64, 12737, 62, 95, 1182, 77, 81, 96, 100...41, 90, 1571, 9, 18, 42, 61...1052, 10, 30, 153, 1611393, 144, 14715243, 12586, 88, 91, 13510, 16, 29, 30, 35...87, 144, 1478, 10485, 999918, 105131, 15214815, 20, 45152107, 1591406963, 155147211072127, 79, 92, 94, 123...1527615, 20, 45, 111, 1501071521091393, 1035611344, 75112, 12457, 69131649919139412214014813216214, 43, 12577982469383112027, 79, 92, 94, 123...17, 41, 42, 65, 67...114139102132endocytic vesicle lumendouble membrane vesicle viral factory outer membraneexocytic vesicleendoplasmic reticulum membraneendoplasmic reticulum-Golgi intermediate compartment membraneautophagosomenucleolusGolgi lumencytosolGolgi membranecomplex N-glycan-PALM-Spike S1 Fragment pp1a-nsp7 H+Ncapfully glycosylated Spike GTPnsp7:nsp8:nsp12:nsp14:nsp10:nsp13:nsp15phospho-p-S177-NcapSARS-CoV-2 genomicRNA (plus strand)pp1ab-nsp8 S3:M:E:encapsidated SARS-CoV-2 genomicRNA:O-glycosyl 3atetramermRNA4 CHMP6 pp1ab-nsp12 mRNA3 minus strand UVRAG pp1ab-nsp8fully glycosylated Spike pp1ab-nsp10 pp1a-nsp8 pp1ab-nsp6 pp1a-nsp8 pp1a-nsp1 pp1ab-nsp10 pp1ab-nsp12 pp1ab-nsp5 M high-mannoseN-glycan unfoldedSpikemRNA5 pp1a-3CL MGAT1pp1a-nsp3 MGAT2N-glycan pp1ab-nsp3 TMPRSS2 nsp16:VHLTMPRSS2N-glycan pp1a-nsp3 pp1ab-nsp4 pp1ab-nsp12 CHMP4C pp1ab-nsp16 pp1a-nsp7m7GpppA-cappedSARS-CoV-2 genomicRNA (plus strand)pp1a-nsp3 S1:S2:M:E:7a:O-glycosyl 3atetramerUBB(153-228) UBC(1-76) pp1ab-nsp7 mRNA5 minus strand pp1ab-nsp7 m7G(5')pppAm-mRNA4 phospho-SUMO1-K62-ADPr-p-S177-Ncap phospho-SUMO1-K62-ADPr-p-S177-Ncap mRNA6 fully glycosylatedSpike trimerATPpp1a-nsp10 S-adenosyl-L-methionineADPpp1ab-nsp15 O-glycosyl 3atetramerphospho-SUMO1-K62-ADPr-p-S177-Ncap NMPCHMP4A m7G(5')pppAm-capped,polyadenylated mRNA7 UBC(305-380) PRKCSH m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1a-nsp7 M m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) H2Opp1ab-nsp7STT3A PPiZCRB1S3:M:E:encapsidatedSARS-CoV-2genomicRNA:7a:O-glycosyl3atetramer:glycosylated-ACE2pp1a-nsp10 PIK3R4 Cathepsin L1mRNA9 m7G(5')pppAm-capped,polyadenylatedSARS-CoV-2subgenomic mRNAs(plus strand)ST6GALNAC3 pp1a-nsp10PARP9 phospho-SUMO1-K62-ADPr-p-S177-Ncap m7G(5')pppAm-mRNA7 NAD+pp1ab-nsp15 pp1ab-nsp4 7a pp1ab-nsp6 m7G(5')pppAm-capped SARS-CoV-2 genomic RNA complement (minus strand) CHMP7 N-glycan M pp1ab-nsp9pp1ab-nsp15 phospho-ADPr-p-S177-Ncappp1ab-nsp14 m7GpppA-mRNA2 PPiPimRNA2 GTPbeta-D-glucosepp1a-nsp6 pp1ab-nsp3 pp1ab-nsp3 RNA primer m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) mRNA7b pp1ab-nsp7 pp1a-nsp6 pp1a-nsp4 pp1a-nsp4 CQ, HCQpp1ab-nsp6 pp1ab-nsp13 NTPpp1ab-nsp8 nucleoside5'-diphosphate(3−)pp1a-nsp3 pp1ab-nsp13 H2OUBC(609-684) Ncap tetramerUVRAG complexm7G(5')pppAm-capped,polyadenylated mRNA8 pp1ab-nsp6 pp1a-nsp3 pp1ab-nsp13 N-glycan pp1a-nsp4 PRKCSH pp1a-nsp6 M O-glycosyl 3a S-adenosyl-L-homocysteineH2OTMPRSS2:TMPRSS2inhibitorsnucleoside5'-diphosphate(3-)pp1a-nsp7 Ub-3xPalmC-E pp1ab-nsp9 S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerpp1ab-nsp6 pp1ab-nsp10 SARS-CoV-2gRNA:RTC:RNAprimer:RTCinhibitorsnsp7:nsp8:nsp12phospho-SUMO1-K62-ADPr-p-S177-Ncap UBA52(1-76) 3xPalmC-EMGAT4A(1-535) m7G(5')pppAm-mRNA6 O-glycosyl 3aST3GAL2 pp1ab-nsp13nsp9pp1ab-nsp1-4m7G(5')pppAm-capped,polyadenylated mRNA3pp1ab-nsp3 N-glycan nsp3Ub-3xPalmC-ENTPH2Opp1ab-nsp6PIK3C3 nsp4GSK3BSUMO1-C93-UBE2I pp1a-nsp8 pp1ab-nsp7 H2Opp1ab-nsp15 7a nucleotide-sugarpp1ab-nsp8 fully glycosylated Spike pp1ab-nsp15pp1ab-nsp12 m7G(5')pppAm-mRNA5 pp1ab-nsp5 pp1ab-nsp15 pp1ab-nsp4 nsp15:RB1SARS-CoV-2 plusstrand subgenomicmRNAspp1a-nsp7 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) GANAB RPN2 DDOST 7a pp1ab-nsp12m7G(5')pppAm-capped,polyadenylatedSARS-CoV-2 genomicRNA (plus strand)PPiRPN1 pp1a-nsp3 pp1a-nsp9 H+pp1a-nsp4 SARS-CoV-2 gRNAcomplement (minusstrand):RTC:RTCinhibitorsm7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1ab-nsp4 mRNA6 minus strand Ub-3xPalmC-E DDX5pp1ab-nsp4 pp1ab-nsp14 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) N-glycan MPPiphospho-SUMO1-K62-ADPr-p-S177-Ncap pp1ab-nsp6 pp1ab-nsp8 N-glycan pp1a-nsp3-4 nsp15 hexamerpp1ab-nsp13 pp1ab-nsp5pp1ab-nsp8 pp1ab-nsp8 di-antennary N-glycan-PALM-Spike pp1a-nsp8 high-mannose N-glycan-PALM-Spike nsp2pp1a-nsp7 pp1ab-nsp7 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1ab-nsp12 pp1ab-nsp7 mRNA7b minus strand pp1ab-nsp4 Ncap tetramerM pp1a-nsp4 fully glycosylated Spike N-glycan nsp3-4pp1a-nsp3 pp1a-nsp1-4pp1ab-nsp8 nsp5nsp16:nsp10N-glycan M m7G(5')pppAm-capped,polyadenylated mRNA3 CQ2+, HCQ2+pp1ab-nsp14 O-glycosyl 3a pp1a-nsp8 UBE2IH+pp1ab-nsp4 pp1a-nsp8 phospho-SUMO1-K62-ADPr-p-S177-Ncap S3:M:E:encapsidatedSARS-CoV-2 genomicRNA: 7a:O-glycosyl3a tetramerpp1ab-nsp12 pp1ab-nsp4 m7G(5')pppAm-capped,polyadenylatedSARS-CoV-2 genomicRNA (plus strand)ST3GAL3 pp1ab-nsp14 O-glycosyl 3atetramerphospho-SUMO1-K62-ADPr-p-S177-Ncap PPim7G(5')pppAm-capped,polyadenylated-mRNA9 pp1ab-nsp10 7a pp1a-nsp10 nsp7:nsp8ZCRB1:m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand)pp1ab-nsp7 N-glycan Mpp1ab-nsp15 O-glycosyl 3a CMP-Neu5AcADPphospho-SUMO1-K62-ADPr-p-S177-Ncap TMPRSS2pp1ab-nsp16 pp1a-nsp6 FUT8nsp8:MAP1LC3Bpp1ab-nsp6 phospho-p-S177,S181,S185,S187,S189,S191,S195,T199,S203,S207-NNcap tetramernsp8VHLCHMP2A pp1a-nsp3 SARS coronavirusgRNA:RTC:nascentRNA minus strandwith mismatchednucleotidepp1ab-nsp15 Ub-3xPalmC-E pp1a-nsp4 pp1ab-nsp10 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) N-glycan nsp414-sugar N-glycanunfolded SpikeMGAT4C PARPspp1a-nsp8 Host Derived Lipid Bilayer Membrane UDPUb-3xPalmC-E PARP16 Ub-3xPalmC-E pp1ab-nsp16 pp1ab-nsp3 ST6GAL1 pp1a-nsp6pp1ab-nsp14 S3:M:E:encapsidatedSARS-CoV-2 genomicRNA: 7a:O-glycosyl3a tetramerpp1ab-nsp8 RPS27A(1-76) M sialyltransferasesnsp1m7GpppA-mRNA5 M nucleoside5'-diphosphate(3−)UDP-GalNAcpp1a-nsp4 Pim7GpppA-mRNA9 CMPnsp10:nsp14pp1ab-nsp10 PiACE2pp1ab-nsp3 mRNA7a minus strand pp1a-nsp4 CTSL(114-288) N-glycan M pp1ab-nsp10 ST6GALNAC2 ST3GAL1 UBC(77-152) NcapSARS-CoV-2 genomicRNA complement(minus strand)GalNAc-O-3aMGAT5m7G(5')pppAm-capped,polyadenylated mRNA4NAMZCRB1 pp1ab-nsp13 pp1ab-nsp15 MOGS H2Opp1ab-nsp10 a nucleotide sugarUbm7GpppA-mRNA3 Ub-3xPalmC-E pp1a palmitoyl-CoAmRNA7a NTPpp1ab-nsp7 pp1a-nsp7 M pp1a-nsp10 UBB(1-76) pp1a-nsp4 pp1ab-nsp6 pp1ab-nsp8 pp1a-nsp9 pp1ab-nsp13 H+S-adenosyl-L-methionineUBC(153-228) di-antennaryN-glycan-PALM-SpiketrimerMAN1B1,EDEM2pp1ab-nsp6 pp1ab-nsp7 nsp3:nsp4:nsp6pp1ab-nsp13 O-glycosyl 3atetramerphospho-SUMO1-K62-ADPr-p-S177-Ncap m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) m7G(5')pppAm-capped,polyadenylated mRNA4 pp1ab-nsp4 TUSC3(1-348) S3:M:E:encapsidatedSARS-CoV-2genomicRNA:7a:O-glycosyl3atetramer:glycosylated-ACE2phospho-SUMO1-K62-ADPr-p-S177-Ncap pp1a-nsp7 DDX5 pp1ab-nsp8 N-glycan M NSARS coronavirusgRNA with secondarystructure:RTCpp1ab-nsp15 pp1a-nsp2 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1a-nsp6 RB1 pp1a-nsp4 PARP4 N-glycan M high-mannoseN-glycan-PALM-Spike7a pp1a-nsp10 SARS-CoV-2 nascent genomic RNA complement (minus strand) with mismatched 3' nucleotide pp1a-nsp3 pp1ab-nsp16 O-glycosyl 3a N-glycan M PARP8 pp1ab-nsp7 RB1nascent Ephospho-SUMO1-K62-ADPr-p-S177-Ncap pp1a-nsp6 pp1ab-nsp7 pp1ab-nsp16 OST complexPPiSARS-CoV-2gRNA:RTC:nascentRNA minus strandmRNA9 minus strand encapsidatedSARS-CoV-2 genomicRNANTPERalpha-glucosidasesm7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) high-mannoseN-glycan-PALM-SpiketrimerCoA-SHpp1ab-nsp4 m7GpppA-mRNA7 phospho-SUMO1-K62-ADPr-p-S177-NcapSARS-CoV-2gRNA:RTC:RNA primerMS-adenosyl-L-homocysteinemRNA3 pp1a-nsp8 ER-alphaglucosidases:ER-alpha glucosidase inhibitorsVCPpp1a-nsp8N-glycan Epp1ab-nsp3 pp1ab-nsp16 pp1a-nsp7 pp1ab-nsp12 pp1a-nsp3 pp1ab-nsp6 M pp1a dimerpp1a-nsp3 pp1a-nsp7 pp1a-nsp7 glycosylated-ACE2 pp1ab-nsp15 GSKim7G(5')pppAm-capped,polyadenylated mRNA5 pp1a-nsp3-4 pp1a-nsp4 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) M O-glycosyl 3a Host Derived LipidBilayer Membranem7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) 3CLp dimerMAN1B1 pp1ab-nsp13 CTSL(292-333) 3aUBB(77-152) pp1ab-nsp8 nsp6pp1ab-nsp16 m7GpppA-mRNA8 mRNA8 N-glycan pp1ab-nsp4 pp1ab-nsp3 N-glycan pp1ab-nsp3-4 PPipp1ab-nsp12 M pp1a-nsp6 MAP1LC3B m7G(5')pppAm-mRNA3 nsp7pp1a-nsp8 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) SUMO1:C93-UBE2Ipp1a-nsp8 S-adenosyl-L-homocysteinecomplex N-glycan-PALM-Spike S2 Fragment mRNA8 minus strand m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) CHMP3 nsp6CANXH2Ocomplex N-glycan-PALM-Spike S2 Fragment Ub-3xPalmC-E pp1ab-nsp14H+pp1ab-nsp6 O-glycosyl 3a Ub-3xPalmC-E pp1a-nsp8 pp1ab-nsp16 high-mannoseN-glycan foldedSpikepp1a-nsp6 pp1ab-nsp14 fully glycosylated Spike pp1ab-nsp10 CHMP4B pp1ab-nsp6 pp1ab-nsp12 O-glycosyl 3a m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1a-nsp10 high-mannoseN-glycan-PALM-Spiketrimerpp1a-nsp4 PARP10 pp1a-nsp10 nascent Spikepp1ab-nsp10SARS-CoV-2 nascent genomic RNA complement (minus strand) pp1a-nsp10 complex N-glycan-PALM-Spike S1 Fragment pp1ab-nsp8 pp1a-nsp10 pp1a-nsp10 pp1a-nsp7 pp1a-3CL pp1a-nsp6 CTSL(114-288) pp1ab-nsp7 O-glycosyl 3a N-glycan nsp3MAP1LC3Bnsp13:DDX5Ub-3xPalmC-E H2Opp1ab-nsp15 GSK3B:GSKim7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) pp1ab-nsp3-4 pp1ab-nsp14 complex N-glycan-PALM-Spike S2 Fragment MAGT1 pp1a-nsp10 nsp3pp1ab-nsp10 GSK3B pp1ab-nsp7 N-glycan pp1ab-nsp3 N-glycan M m7G(5')pppAm-capped,polyadenylated mRNA2 pp1ab-nsp3 S1:S2:M lattice:Eproteinpp1ab-nsp16 S3:M:E:encapsidated SARS-CoV-2 genomicRNA:7a:O-glycosyl3a tetramerpp1ab-nsp7 FURINnsp10Ncap tetramerpp1ab-nsp15 pp1ab-nsp2 pp1a-nsp10 N-glycan M nucleoside5'-diphosphate(3-)phospho-SUMO1-K62-ADPr-p-S177-Ncap RTCEDEM2 pp1a-nsp1-4 m7G(5')pppAm-capped,polyadenylated mRNA6 Ub-3xPalmC-Epentamerpp1ab-nsp3 nsp7:nsp8:nsp12:nsp14:nsp10:nsp13MGAT4B pp1ab-nsp16 pp1a-nsp3 O-glycosyl 3a O-glycosyl 3a UBE2I-G97-SUMO1 UBC(229-304) 3ansp7:nsp8:nsp12:nsp14:nsp10pp1a-nsp8 SARS-CoV-2 gRNAcomplement (minusstrand):RTCm7G(5')pppAm-capped,polyadenylated mRNA2complex N-glycan-PALM-Spike S1 Fragment N-glycanpp1ab-nsp3-4ESCRT-IIIpp1a-nsp6 α-KetoamidesGSK3A pp1ab-nsp16pp1a-nsp7 VHL 7app1ab-nsp12 pp1ab-nsp13 MAP1LC3BH2Oglycosylated-ACE2 Ub-3xPalmC-E fully glycosylated Spike pp1a-nsp11pp1a-nsp10 ATPpp1ab-nsp10 pp1a-nsp4 pp1abpp1a-nsp7 CQ, HCQpp1ab-nsp1-4 DAD1 pp1a-nsp8 Ncap tetramerm7G(5')pppAm-SARS-CoV-2 plus strand subgenomic mRNAsO-glycosyl 3a H+pp1ab-nsp12 H+pp1ab-nsp4 tri-antennaryN-glycan-PALM-SpiketrimerRTC inhibitorspp1a-nsp9pp1a-nsp10 pp1ab-nsp8 pp1ab-nsp8 pp1ab-nsp7 H2Ofully glycosylatedSpike trimerpp1ab-nsp4 Ub-3xPalmC-E O-glycosyl 3am7G(5')pppAm-mRNA8 pp1a-nsp8 RNA primer pp1a-nsp8 pp1ab-nsp8 nsp1-4O-glycosyl 3a N-glycan M pp1aM H+phospho-SUMO1-K62-ADPr-p-S177-Ncap NTPphospho-SUMO1-K62-ADPr-p-S177-Ncap high-mannose N-glycan-PALM-Spike ATPER-alpha-glucosidaseinhibitorspp1a-nsp6 nsp8nsp3:nsp4pp1ab-nsp13 m7GpppA-mRNA4 NST6GALNAC4 pp1ab-nsp14 pp1a-3CLSARS-CoV-2 nascent genomic RNA complement (minus strand) SARS-CoV-2 gRNA:RTCpp1ab-nsp14 M SARS-CoV-2gRNA:RTC:nascentRNA minusstrand:RTCinhibitorsMlattice:Eprotein:encapsidated SARS-CoV-2 genomic RNAm7GpppA-SARS-CoV-2plus strandsubgenomic mRNAsRTC inhibitorsBECN1 glycosylated-ACE2pp1ab-nsp12 GALNT1Man(9) N-glycanunfolded Spikepp1ab-nsp13 S-adenosyl-L-methionineS3:M:E:encapsidatedSARS-CoV-2 genomicRNA: 7a:O-glycosyl3a tetramerCTSL:CTSL inhibitorsa nucleotide sugarpp1a-nsp6 phospho-SUMO1-K62-ADPr-p-S177-Ncap N-glycan pp1a-nsp3 pp1ab-nsp13 CTSL(292-333) fully glycosylated Spike ST3GAL4 pp1ab-nsp3 GSK3pp1ab-nsp9 pp1a-nsp8 nsp3-4pp1a-nsp8 MOGSm7GpppA-cappedSARS-CoV-2 genomicRNA complement(minus strand)3CLpdimer:α-Ketoamidesm7G(5')pppAm-capped,polyadenylated-mRNA9m7G(5')pppAm-mRNA9 tri-antennary N-glycan-PALM-Spike pp1ab-nsp15 H2OPiUb-3xPalmC-EpentamerUBC(457-532) pp1a-nsp8 pp1a-nsp10 pp1ab-nsp8 Ub-3xPalmC-E MOGS pp1ab-nsp13 7a N-glycan M phospho-SUMO1-K62-ADPr-p-S177-Ncap mRNA4 minus strand pp1ab-nsp16 ADPPARP14 3a:membranousstructureglycosylated-ACE2pp1ab-nsp12 M latticepp1ab-nsp12 UBC(381-456) pp1a-nsp4 pp1a-nsp3 7a DOLPCTSL inhibitorsnascent Mfully glycosylated Spike pp1ab-nsp3 TMPRSS2 inhibitorsPARP6 pp1a-nsp6-11ATPm7G(5')pppAm-cappedSARS-CoV-2 genomicRNA (plus strand)glycosylated-ACE2pp1ab-nsp7 m7G(5')pppAm-capped SARS-CoV-2 genomic RNA complement (minus strand) pp1ab-nsp14 m7G(5')pppAm-cappedSARS-CoV-2 genomicRNA complement(minus strand)GANAB pp1ab-nsp14 pp1ab-nsp3 Ncap tetramerGTPSUMO-p-Ncapdimer:SARS-CoV-2genomic RNApp1ab-nsp10 UBC(533-608) fully glycosylated Spike Ub-3xPalmC-E encapsidatedSARS-CoV-2 genomicRNA (plus strand)pp1ab-nsp14 pp1ab-nsp8 pp1ab-nsp10 9bpp1ab-nsp1 mRNA2 minus strand pp1a-nsp7 CHMP2B pp1a-nsp3 pp1a-nsp7 N-glycan M pp1ab-nsp16 pp1ab-nsp14 nsp9 dimerpp1ab-nsp4 nucleotide-sugarm7GpppA-mRNA6 pp1a-nsp7 SARS-CoV-2 minusstrand subgenomicmRNAsATPpp1ab-nsp10 m7G(5')pppAm-mRNA2 pp1ab-nsp6 phospho-SUMO1-K62-ADPr-p-S177-Ncap pp1ab-nsp8 N-glycan M pp1a-nsp6 pp1ab-nsp3 PPim7G(5')pppAm-capped,polyadenylated mRNA5pp1ab-nsp10 m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) PPiMGAT4s(Glc)3 (GlcNAc)2(Man)9 (PP-Dol)17a pp1a-nsp10 pp1ab-nsp14 MAN2A1pp1ab-nsp10 5, 25, 53, 74, 119...2121561607416014816215221160120781521521602121321522132561521201601521481481521481605, 25, 53, 74, 119...5651, 74148148148215, 25, 53, 74, 119...2138, 54, 70, 83, 116...148148141148215, 25, 53, 74, 119...241601521601486816085, 9914814815215214815232160148561521521605, 25, 53, 74, 119...5, 25, 53, 74, 119...383298211071481521481201609321107242141529316456148321481522156160


Description

This pathway, SARS-CoV-2 infection of human cells (COVID-19), was initially generated via electronic inference from the manually curated and reviewed Reactome SARS-CoV-1 (Human SARS coronavirus) infection pathway. The inference process created SARS-CoV-2 events corresponding to each event in the SARS-CoV-1 pathway and populated those events with SARS-CoV-2 protein-containing physical entities based on orthology to SARS-CoV-1 proteins (https://reactome.org/documentation/inferred-events). All of these computationally created events and entities have been reviewed by Reactome curators and modified as appropriate where recently published experimental data indicate the existences of differences between the molecular details of the SARS-CoV-1 and SARS-CoV-2 infection pathways.

SARS‑CoV‑2 infection begins with the binding of viral S (spike) protein to cell surface angiotensin converting enzyme 2 (ACE2) and endocytosis of the bound virion. Within the endocytic vesicle, host proteases mediate cleavage of S protein into S1 and S2 fragments, leading to S2‑mediated fusion of the viral and host endosome membranes and release of the viral capsid into the host cell cytosol. The capsid is uncoated to free the viral genomic RNA, whose cap‑dependent translation produces polyprotein pp1a and, by means of a 1‑base frameshift, polyprotein pp1ab. Autoproteolytic cleavage of pp1a and pp1ab generates 15 or 16 nonstructural proteins (nsps) with various functions. Importantly, the RNA dependent RNA polymerase (RdRP) activity is encoded in nsp12. Nsp3, 4, and 6 induce rearrangement of the cellular endoplasmic reticulum membrane to form cytosolic double membrane vesicles (DMVs) where the viral replication transcription complex is assembled and anchored. With viral genomic RNA as a template, viral replicase‑transcriptase synthesizes a full length negative sense antigenome, which in turn serves as a template for the synthesis of new genomic RNA. The replicase‑transcriptase can also switch template during discontinuous transcription of the genome at transcription regulated sequences to produce a nested set of negative‑sense subgenomic (sg) RNAs, which are used as templates for the synthesis of positive‑sense sgRNAs that are translated to generate viral proteins. Finally, viral particle assembly occurs in the ER Golgi intermediate compartment (ERGIC). Viral M protein provides the scaffold for virion morphogenesis (Hartenian et al. 2020; Fung & Liu 2019; Masters 2006). View original pathway at Reactome.

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Reactome-Converter 
Pathway is converted from Reactome ID: 9694516
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Gillespie, Marc E

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Bibliography

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  1. de Haan CA, Vennema H, Rottier PJ.; ''Assembly of the coronavirus envelope: homotypic interactions between the M proteins.''; PubMed Europe PMC Scholia
  2. Neuman BW, Adair BD, Yoshioka C, Quispe JD, Orca G, Kuhn P, Milligan RA, Yeager M, Buchmeier MJ.; ''Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.''; PubMed Europe PMC Scholia
  3. Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Müller MA, Drosten C, Pöhlmann S.; ''SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor.''; PubMed Europe PMC Scholia
  4. Zhao X, Guo F, Comunale MA, Mehta A, Sehgal M, Jain P, Cuconati A, Lin H, Block TM, Chang J, Guo JT.; ''Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2.''; PubMed Europe PMC Scholia
  5. Han DP, Lohani M, Cho MW.; ''Specific asparagine-linked glycosylation sites are critical for DC-SIGN- and L-SIGN-mediated severe acute respiratory syndrome coronavirus entry.''; PubMed Europe PMC Scholia
  6. Yang N, Shen HM.; ''Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19.''; PubMed Europe PMC Scholia
  7. Shu T, Huang M, Wu D, Ren Y, Zhang X, Han Y, Mu J, Wang R, Qiu Y, Zhang DY, Zhou X.; ''SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts.''; PubMed Europe PMC Scholia
  8. Tan YJ, Teng E, Shen S, Tan TH, Goh PY, Fielding BC, Ooi EE, Tan HC, Lim SG, Hong W.; ''A novel severe acute respiratory syndrome coronavirus protein, U274, is transported to the cell surface and undergoes endocytosis.''; PubMed Europe PMC Scholia
  9. Tseng YT, Wang SM, Huang KJ, Lee AI, Chiang CC, Wang CT.; ''Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.''; PubMed Europe PMC Scholia
  10. Chang CK, Chen CM, Chiang MH, Hsu YL, Huang TH.; ''Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.''; PubMed Europe PMC Scholia
  11. Littler DR, Gully BS, Colson RN, Rossjohn J.; ''Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9.''; PubMed Europe PMC Scholia
  12. Colson P, Rolain JM, Lagier JC, Brouqui P, Raoult D.; ''Chloroquine and hydroxychloroquine as available weapons to fight COVID-19.''; PubMed Europe PMC Scholia
  13. Fan K, Wei P, Feng Q, Chen S, Huang C, Ma L, Lai B, Pei J, Liu Y, Chen J, Lai L.; ''Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase.''; PubMed Europe PMC Scholia
  14. Hsu MF, Kuo CJ, Chang KT, Chang HC, Chou CC, Ko TP, Shr HL, Chang GG, Wang AH, Liang PH.; ''Mechanism of the maturation process of SARS-CoV 3CL protease.''; PubMed Europe PMC Scholia
  15. Xia S, Lan Q, Su S, Wang X, Xu W, Liu Z, Zhu Y, Wang Q, Lu L, Jiang S.; ''The role of furin cleavage site in SARS-CoV-2 spike protein-mediated membrane fusion in the presence or absence of trypsin.''; PubMed Europe PMC Scholia
  16. Peng TY, Lee KR, Tarn WY.; ''Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization.''; PubMed Europe PMC Scholia
  17. Chen SC, Lo SY, Ma HC, Li HC.; ''Expression and membrane integration of SARS-CoV E protein and its interaction with M protein.''; PubMed Europe PMC Scholia
  18. Voss D, Pfefferle S, Drosten C, Stevermann L, Traggiai E, Lanzavecchia A, Becker S.; ''Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein.''; PubMed Europe PMC Scholia
  19. Chinappi M, Via A, Marcatili P, Tramontano A.; ''On the mechanism of chloroquine resistance in Plasmodium falciparum.''; PubMed Europe PMC Scholia
  20. Shulla A, Heald-Sargent T, Subramanya G, Zhao J, Perlman S, Gallagher T.; ''A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry.''; PubMed Europe PMC Scholia
  21. Oostra M, de Haan CA, de Groot RJ, Rottier PJ.; ''Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.''; PubMed Europe PMC Scholia
  22. Wong HH, Kumar P, Tay FP, Moreau D, Liu DX, Bard F.; ''Genome-Wide Screen Reveals Valosin-Containing Protein Requirement for Coronavirus Exit from Endosomes.''; PubMed Europe PMC Scholia
  23. Vincent MJ, Bergeron E, Benjannet S, Erickson BR, Rollin PE, Ksiazek TG, Seidah NG, Nichol ST.; ''Chloroquine is a potent inhibitor of SARS coronavirus infection and spread.''; PubMed Europe PMC Scholia
  24. Wu CH, Yeh SH, Tsay YG, Shieh YH, Kao CL, Chen YS, Wang SH, Kuo TJ, Chen DS, Chen PJ.; ''Glycogen synthase kinase-3 regulates the phosphorylation of severe acute respiratory syndrome coronavirus nucleocapsid protein and viral replication.''; PubMed Europe PMC Scholia
  25. Zeng R, Ruan HQ, Jiang XS, Zhou H, Shi L, Zhang L, Sheng QH, Tu Q, Xia QC, Wu JR.; ''Proteomic analysis of SARS associated coronavirus using two-dimensional liquid chromatography mass spectrometry and one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by mass spectroemtric analysis.''; PubMed Europe PMC Scholia
  26. Cottam EM, Maier HJ, Manifava M, Vaux LC, Chandra-Schoenfelder P, Gerner W, Britton P, Ktistakis NT, Wileman T.; ''Coronavirus nsp6 proteins generate autophagosomes from the endoplasmic reticulum via an omegasome intermediate.''; PubMed Europe PMC Scholia
  27. Brown AJ, Won JJ, Graham RL, Dinnon KH, Sims AC, Feng JY, Cihlar T, Denison MR, Baric RS, Sheahan TP.; ''Broad spectrum antiviral remdesivir inhibits human endemic and zoonotic deltacoronaviruses with a highly divergent RNA dependent RNA polymerase.''; PubMed Europe PMC Scholia
  28. Kumar S, Dare L, Vasko-Moser JA, James IE, Blake SM, Rickard DJ, Hwang SM, Tomaszek T, Yamashita DS, Marquis RW, Oh H, Jeong JU, Veber DF, Gowen M, Lark MW, Stroup G.; ''A highly potent inhibitor of cathepsin K (relacatib) reduces biomarkers of bone resorption both in vitro and in an acute model of elevated bone turnover in vivo in monkeys.''; PubMed Europe PMC Scholia
  29. Luo H, Chen J, Chen K, Shen X, Jiang H.; ''Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization.''; PubMed Europe PMC Scholia
  30. Chen CY, Chang CK, Chang YW, Sue SC, Bai HI, Riang L, Hsiao CD, Huang TH.; ''Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA.''; PubMed Europe PMC Scholia
  31. Fukushi M, Yoshinaka Y, Matsuoka Y, Hatakeyama S, Ishizaka Y, Kirikae T, Sasazuki T, Miyoshi-Akiyama T.; ''Monitoring of S protein maturation in the endoplasmic reticulum by calnexin is important for the infectivity of severe acute respiratory syndrome coronavirus.''; PubMed Europe PMC Scholia
  32. Towler P, Staker B, Prasad SG, Menon S, Tang J, Parsons T, Ryan D, Fisher M, Williams D, Dales NA, Patane MA, Pantoliano MW.; ''ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.''; PubMed Europe PMC Scholia
  33. Chen IY, Moriyama M, Chang MF, Ichinohe T.; ''Severe Acute Respiratory Syndrome Coronavirus Viroporin 3a Activates the NLRP3 Inflammasome.''; PubMed Europe PMC Scholia
  34. Lu W, Zheng BJ, Xu K, Schwarz W, Du L, Wong CK, Chen J, Duan S, Deubel V, Sun B.; ''Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release.''; PubMed Europe PMC Scholia
  35. Yu IM, Gustafson CL, Diao J, Burgner JW, Li Z, Zhang J, Chen J.; ''Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.''; PubMed Europe PMC Scholia
  36. Kawase M, Shirato K, van der Hoek L, Taguchi F, Matsuyama S.; ''Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry.''; PubMed Europe PMC Scholia
  37. Belouzard S, Millet JK, Licitra BN, Whittaker GR.; ''Mechanisms of coronavirus cell entry mediated by the viral spike protein.''; PubMed Europe PMC Scholia
  38. Bhardwaj K, Liu P, Leibowitz JL, Kao CC.; ''The coronavirus endoribonuclease Nsp15 interacts with retinoblastoma tumor suppressor protein.''; PubMed Europe PMC Scholia
  39. Yamamoto M, Matsuyama S, Li X, Takeda M, Kawaguchi Y, Inoue JI, Matsuda Z.; ''Identification of Nafamostat as a Potent Inhibitor of Middle East Respiratory Syndrome Coronavirus S Protein-Mediated Membrane Fusion Using the Split-Protein-Based Cell-Cell Fusion Assay.''; PubMed Europe PMC Scholia
  40. Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang WL, Lin CH, Huang TH.; ''Modular organization of SARS coronavirus nucleocapsid protein.''; PubMed Europe PMC Scholia
  41. Fung TS, Liu DX.; ''Human Coronavirus: Host-Pathogen Interaction.''; PubMed Europe PMC Scholia
  42. Hsieh PK, Chang SC, Huang CC, Lee TT, Hsiao CW, Kou YH, Chen IY, Chang CK, Huang TH, Chang MF.; ''Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent.''; PubMed Europe PMC Scholia
  43. Chen S, Jonas F, Shen C, Hilgenfeld R.; ''Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode.''; PubMed Europe PMC Scholia
  44. Zhang L, Lin D, Kusov Y, Nian Y, Ma Q, Wang J, von Brunn A, Leyssen P, Lanko K, Neyts J, de Wilde A, Snijder EJ, Liu H, Hilgenfeld R.; ''α-Ketoamides as Broad-Spectrum Inhibitors of Coronavirus and Enterovirus Replication: Structure-Based Design, Synthesis, and Activity Assessment.''; PubMed Europe PMC Scholia
  45. Hoffmann M, Kleine-Weber H, Pöhlmann S.; ''A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells.''; PubMed Europe PMC Scholia
  46. Baron SA, Devaux C, Colson P, Raoult D, Rolain JM.; ''Teicoplanin: an alternative drug for the treatment of COVID-19?''; PubMed Europe PMC Scholia
  47. Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang CF, Huang TH.; ''The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure.''; PubMed Europe PMC Scholia
  48. Surjit M, Lal SK.; ''The SARS-CoV nucleocapsid protein: a protein with multifarious activities.''; PubMed Europe PMC Scholia
  49. Veit M.; ''Palmitoylation of virus proteins.''; PubMed Europe PMC Scholia
  50. Huang Q, Yu L, Petros AM, Gunasekera A, Liu Z, Xu N, Hajduk P, Mack J, Fesik SW, Olejniczak ET.; ''Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.''; PubMed Europe PMC Scholia
  51. Arnesen T, Anderson D, Baldersheim C, Lanotte M, Varhaug JE, Lillehaug JR.; ''Identification and characterization of the human ARD1-NATH protein acetyltransferase complex.''; PubMed Europe PMC Scholia
  52. Prentice E, McAuliffe J, Lu X, Subbarao K, Denison MR.; ''Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins.''; PubMed Europe PMC Scholia
  53. Chakraborti S, Prabakaran P, Xiao X, Dimitrov DS.; ''The SARS coronavirus S glycoprotein receptor binding domain: fine mapping and functional characterization.''; PubMed Europe PMC Scholia
  54. Joseph JS, Saikatendu KS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P.; ''Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch.''; PubMed Europe PMC Scholia
  55. Ji D, Juhas M, Tsang CM, Kwok CK, Li Y, Zhang Y.; ''Discovery of G-quadruplex-forming sequences in SARS-CoV-2.''; PubMed Europe PMC Scholia
  56. Herrera NG, Morano NC, Celikgil A, Georgiev GI, Malonis RJ, Lee JH, Tong K, Vergnolle O, Massimi AB, Yen LY, Noble AJ, Kopylov M, Bonanno JB, Garrett-Thomson SC, Hayes DB, Bortz RH, Wirchnianski AS, Florez C, Laudermilch E, Haslwanter D, Fels JM, Dieterle ME, Jangra RK, Barnhill J, Mengotto A, Kimmel D, Daily JP, Pirofski LA, Chandran K, Brenowitz M, Garforth SJ, Eng ET, Lai JR, Almo SC.; ''Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis.''; PubMed Europe PMC Scholia
  57. Thiel V, Ivanov KA, Putics Á, Hertzig T, Schelle B, Bayer S, Weißbrich B, Snijder EJ, Rabenau H, Doerr HW, Gorbalenya AE, Ziebuhr J.; ''Mechanisms and enzymes involved in SARS coronavirus genome expression.''; PubMed Europe PMC Scholia
  58. Shen S, Lin PS, Chao YC, Zhang A, Yang X, Lim SG, Hong W, Tan YJ.; ''The severe acute respiratory syndrome coronavirus 3a is a novel structural protein.''; PubMed Europe PMC Scholia
  59. Foley M, Tilley L.; ''Quinoline antimalarials: mechanisms of action and resistance and prospects for new agents.''; PubMed Europe PMC Scholia
  60. Chen J, Malone B, Llewellyn E, Grasso M, Shelton PMM, Olinares PDB, Maruthi K, Eng E, Vatandaslar H, Chait BT, Kapoor T, Darst SA, Campbell EA.; ''Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex.''; PubMed Europe PMC Scholia
  61. Tseng YT, Chang CH, Wang SM, Huang KJ, Wang CT.; ''Identifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly.''; PubMed Europe PMC Scholia
  62. Simmons G, Reeves JD, Rennekamp AJ, Amberg SM, Piefer AJ, Bates P.; ''Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry.''; PubMed Europe PMC Scholia
  63. Nieto-Torres JL, Dediego ML, Alvarez E, Jiménez-Guardeño JM, Regla-Nava JA, Llorente M, Kremer L, Shuo S, Enjuanes L.; ''Subcellular location and topology of severe acute respiratory syndrome coronavirus envelope protein.''; PubMed Europe PMC Scholia
  64. Kamboj RC, Raghav N, Mittal A, Khurana S, Sadana R, Singh H.; ''Effects of some antituberculous and anti-leprotic drugs on cathepsins B, H and L.''; PubMed Europe PMC Scholia
  65. Liu DX, Yuan Q, Liao Y.; ''Coronavirus envelope protein: a small membrane protein with multiple functions.''; PubMed Europe PMC Scholia
  66. Matsuyama S, Nagata N, Shirato K, Kawase M, Takeda M, Taguchi F.; ''Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2.''; PubMed Europe PMC Scholia
  67. Torres J, Wang J, Parthasarathy K, Liu DX.; ''The transmembrane oligomers of coronavirus protein E.''; PubMed Europe PMC Scholia
  68. Yuan Q, Liao Y, Torres J, Tam JP, Liu DX.; ''Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells.''; PubMed Europe PMC Scholia
  69. Harcourt BH, Jukneliene D, Kanjanahaluethai A, Bechill J, Severson KM, Smith CM, Rota PA, Baker SC.; ''Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity.''; PubMed Europe PMC Scholia
  70. Bhardwaj K, Palaninathan S, Alcantara JM, Yi LL, Guarino L, Sacchettini JC, Kao CC.; ''Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15.''; PubMed Europe PMC Scholia
  71. Al-Bari MAA.; ''Targeting endosomal acidification by chloroquine analogs as a promising strategy for the treatment of emerging viral diseases.''; PubMed Europe PMC Scholia
  72. Chen Y, Shi L, Zhang L, Li R, Liang J, Yu W, Sun L, Yang X, Wang Y, Zhang Y, Shang Y.; ''The molecular mechanism governing the oncogenic potential of SOX2 in breast cancer.''; PubMed Europe PMC Scholia
  73. Pászti-Gere E, Czimmermann E, Ujhelyi G, Balla P, Maiwald A, Steinmetzer T.; ''In vitro characterization of TMPRSS2 inhibition in IPEC-J2 cells.''; PubMed Europe PMC Scholia
  74. Krokhin O, Li Y, Andonov A, Feldmann H, Flick R, Jones S, Stroeher U, Bastien N, Dasuri KV, Cheng K, Simonsen JN, Perreault H, Wilkins J, Ens W, Plummer F, Standing KG.; ''Mass spectrometric characterization of proteins from the SARS virus: a preliminary report.''; PubMed Europe PMC Scholia
  75. Chen S, Chen L, Tan J, Chen J, Du L, Sun T, Shen J, Chen K, Jiang H, Shen X.; ''Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations.''; PubMed Europe PMC Scholia
  76. Liao Y, Lescar J, Tam JP, Liu DX.; ''Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability.''; PubMed Europe PMC Scholia
  77. McBride CE, Machamer CE.; ''Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein.''; PubMed Europe PMC Scholia
  78. Surjit M, Liu B, Kumar P, Chow VT, Lal SK.; ''The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain.''; PubMed Europe PMC Scholia
  79. Sheahan TP, Sims AC, Zhou S, Graham RL, Pruijssers AJ, Agostini ML, Leist SR, Schäfer A, Dinnon KH, Stevens LJ, Chappell JD, Lu X, Hughes TM, George AS, Hill CS, Montgomery SA, Brown AJ, Bluemling GR, Natchus MG, Saindane M, Kolykhalov AA, Painter G, Harcourt J, Tamin A, Thornburg NJ, Swanstrom R, Denison MR, Baric RS.; ''An orally bioavailable broad-spectrum antiviral inhibits SARS-CoV-2 in human airway epithelial cell cultures and multiple coronaviruses in mice.''; PubMed Europe PMC Scholia
  80. He R, Dobie F, Ballantine M, Leeson A, Li Y, Bastien N, Cutts T, Andonov A, Cao J, Booth TF, Plummer FA, Tyler S, Baker L, Li X.; ''Analysis of multimerization of the SARS coronavirus nucleocapsid protein.''; PubMed Europe PMC Scholia
  81. Ujike M, Huang C, Shirato K, Makino S, Taguchi F.; ''The contribution of the cytoplasmic retrieval signal of severe acute respiratory syndrome coronavirus to intracellular accumulation of S proteins and incorporation of S protein into virus-like particles.''; PubMed Europe PMC Scholia
  82. Schoeman D, Fielding BC.; ''Coronavirus envelope protein: current knowledge.''; PubMed Europe PMC Scholia
  83. Ricagno S, Egloff MP, Ulferts R, Coutard B, Nurizzo D, Campanacci V, Cambillau C, Ziebuhr J, Canard B.; ''Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family.''; PubMed Europe PMC Scholia
  84. Shi CS, Qi HY, Boularan C, Huang NN, Abu-Asab M, Shelhamer JH, Kehrl JH.; ''SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome.''; PubMed Europe PMC Scholia
  85. Rosas-Lemus M, Minasov G, Shuvalova L, Inniss NL, Kiryukhina O, Wiersum G, Kim Y, Jedrzejczak R, Maltseva NI, Endres M, Jaroszewski L, Godzik A, Joachimiak A, Satchell KJF.; ''The crystal structure of nsp10-nsp16 heterodimer from SARS-CoV-2 in complex with S-adenosylmethionine.''; PubMed Europe PMC Scholia
  86. Reggiori F, Monastyrska I, Verheije MH, Calì T, Ulasli M, Bianchi S, Bernasconi R, de Haan CA, Molinari M.; ''Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication.''; PubMed Europe PMC Scholia
  87. Wang Q, Wu J, Wang H, Gao Y, Liu Q, Mu A, Ji W, Yan L, Zhu Y, Zhu C, Fang X, Yang X, Huang Y, Gao H, Liu F, Ge J, Sun Q, Yang X, Xu W, Liu Z, Yang H, Lou Z, Jiang B, Guddat LW, Gong P, Rao Z.; ''Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase.''; PubMed Europe PMC Scholia
  88. Cottam EM, Whelband MC, Wileman T.; ''Coronavirus NSP6 restricts autophagosome expansion.''; PubMed Europe PMC Scholia
  89. Shi CS, Nabar NR, Huang NN, Kehrl JH.; ''SARS-Coronavirus Open Reading Frame-8b triggers intracellular stress pathways and activates NLRP3 inflammasomes.''; PubMed Europe PMC Scholia
  90. Masters PS.; ''The molecular biology of coronaviruses.''; PubMed Europe PMC Scholia
  91. Angelini MM, Akhlaghpour M, Neuman BW, Buchmeier MJ.; ''Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles.''; PubMed Europe PMC Scholia
  92. Gordon CJ, Tchesnokov EP, Feng JY, Porter DP, Götte M.; ''The antiviral compound remdesivir potently inhibits RNA-dependent RNA polymerase from Middle East respiratory syndrome coronavirus.''; PubMed Europe PMC Scholia
  93. Gao Y, Yan L, Huang Y, Liu F, Zhao Y, Cao L, Wang T, Sun Q, Ming Z, Zhang L, Ge J, Zheng L, Zhang Y, Wang H, Zhu Y, Zhu C, Hu T, Hua T, Zhang B, Yang X, Li J, Yang H, Liu Z, Xu W, Guddat LW, Wang Q, Lou Z, Rao Z.; ''Structure of the RNA-dependent RNA polymerase from COVID-19 virus.''; PubMed Europe PMC Scholia
  94. Gordon CJ, Tchesnokov EP, Woolner E, Perry JK, Feng JY, Porter DP, Götte M.; ''Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency.''; PubMed Europe PMC Scholia
  95. Yang ZY, Huang Y, Ganesh L, Leung K, Kong WP, Schwartz O, Subbarao K, Nabel GJ.; ''pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN.''; PubMed Europe PMC Scholia
  96. Hsieh YC, Li HC, Chen SC, Lo SY.; ''Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.''; PubMed Europe PMC Scholia
  97. McBride R, Fielding BC.; ''The role of severe acute respiratory syndrome (SARS)-coronavirus accessory proteins in virus pathogenesis.''; PubMed Europe PMC Scholia
  98. Chen JY, Chen WN, Poon KM, Zheng BJ, Lin X, Wang YX, Wen YM.; ''Interaction between SARS-CoV helicase and a multifunctional cellular protein (Ddx5) revealed by yeast and mammalian cell two-hybrid systems.''; PubMed Europe PMC Scholia
  99. Viswanathan T, Arya S, Chan SH, Qi S, Dai N, Misra A, Park JG, Oladunni F, Kovalskyy D, Hromas RA, Martinez-Sobrido L, Gupta YK.; ''Structural basis of RNA cap modification by SARS-CoV-2.''; PubMed Europe PMC Scholia
  100. McBride CE, Machamer CE.; ''A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein.''; PubMed Europe PMC Scholia
  101. Wong SL, Chen Y, Chan CM, Chan CS, Chan PK, Chui YL, Fung KP, Waye MM, Tsui SK, Chan HY.; ''In vivo functional characterization of the SARS-Coronavirus 3a protein in Drosophila.''; PubMed Europe PMC Scholia
  102. Tan YW, Hong W, Liu DX.; ''Binding of the 5'-untranslated region of coronavirus RNA to zinc finger CCHC-type and RNA-binding motif 1 enhances viral replication and transcription.''; PubMed Europe PMC Scholia
  103. Konkolova E, Klima M, Nencka R, Boura E.; ''Structural analysis of the putative SARS-CoV-2 primase complex.''; PubMed Europe PMC Scholia
  104. Chan CM, Tsoi H, Chan WM, Zhai S, Wong CO, Yao X, Chan WY, Tsui SK, Chan HY.; ''The ion channel activity of the SARS-coronavirus 3a protein is linked to its pro-apoptotic function.''; PubMed Europe PMC Scholia
  105. Zhang L, Lin D, Sun X, Curth U, Drosten C, Sauerhering L, Becker S, Rox K, Hilgenfeld R.; ''Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors.''; PubMed Europe PMC Scholia
  106. Alvarez E, DeDiego ML, Nieto-Torres JL, Jiménez-Guardeño JM, Marcos-Villar L, Enjuanes L.; ''The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated.''; PubMed Europe PMC Scholia
  107. Kim D, Lee JY, Yang JS, Kim JW, Kim VN, Chang H.; ''The Architecture of SARS-CoV-2 Transcriptome.''; PubMed Europe PMC Scholia
  108. Huang Y, Yang ZY, Kong WP, Nabel GJ.; ''Generation of synthetic severe acute respiratory syndrome coronavirus pseudoparticles: implications for assembly and vaccine production.''; PubMed Europe PMC Scholia
  109. Huang C, Narayanan K, Ito N, Peters CJ, Makino S.; ''Severe acute respiratory syndrome coronavirus 3a protein is released in membranous structures from 3a protein-expressing cells and infected cells.''; PubMed Europe PMC Scholia
  110. Liao Y, Yuan Q, Torres J, Tam JP, Liu DX.; ''Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.''; PubMed Europe PMC Scholia
  111. Mortola E, Roy P.; ''Efficient assembly and release of SARS coronavirus-like particles by a heterologous expression system.''; PubMed Europe PMC Scholia
  112. Grunewald ME, Fehr AR, Athmer J, Perlman S.; ''The coronavirus nucleocapsid protein is ADP-ribosylated.''; PubMed Europe PMC Scholia
  113. Kim Y, Jedrzejczak R, Maltseva NI, Wilamowski M, Endres M, Godzik A, Michalska K, Joachimiak A.; ''Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.''; PubMed Europe PMC Scholia
  114. Stertz S, Reichelt M, Spiegel M, Kuri T, Martínez-Sobrido L, García-Sastre A, Weber F, Kochs G.; ''The intracellular sites of early replication and budding of SARS-coronavirus.''; PubMed Europe PMC Scholia
  115. Zhang H, Penninger JM, Li Y, Zhong N, Slutsky AS.; ''Angiotensin-converting enzyme 2 (ACE2) as a SARS-CoV-2 receptor: molecular mechanisms and potential therapeutic target.''; PubMed Europe PMC Scholia
  116. Guarino LA, Bhardwaj K, Dong W, Sun J, Holzenburg A, Kao C.; ''Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.''; PubMed Europe PMC Scholia
  117. McBride CE, Li J, Machamer CE.; ''The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein.''; PubMed Europe PMC Scholia
  118. Hofmann H, Hattermann K, Marzi A, Gramberg T, Geier M, Krumbiegel M, Kuate S, Uberla K, Niedrig M, Pöhlmann S.; ''S protein of severe acute respiratory syndrome-associated coronavirus mediates entry into hepatoma cell lines and is targeted by neutralizing antibodies in infected patients.''; PubMed Europe PMC Scholia
  119. Ying W, Hao Y, Zhang Y, Peng W, Qin E, Cai Y, Wei K, Wang J, Chang G, Sun W, Dai S, Li X, Zhu Y, Li J, Wu S, Guo L, Dai J, Wang J, Wan P, Chen T, Du C, Li D, Wan J, Kuai X, Li W, Shi R, Wei H, Cao C, Yu M, Liu H, Dong F, Wang D, Zhang X, Qian X, Zhu Q, He F.; ''Proteomic analysis on structural proteins of Severe Acute Respiratory Syndrome coronavirus.''; PubMed Europe PMC Scholia
  120. Ye Q, West AMV, Silletti S, Corbett KD.; ''Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein.''; PubMed Europe PMC Scholia
  121. Luo H, Wu D, Shen C, Chen K, Shen X, Jiang H.; ''Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.''; PubMed Europe PMC Scholia
  122. Ho Y, Lin PH, Liu CY, Lee SP, Chao YC.; ''Assembly of human severe acute respiratory syndrome coronavirus-like particles.''; PubMed Europe PMC Scholia
  123. Agostini ML, Andres EL, Sims AC, Graham RL, Sheahan TP, Lu X, Smith EC, Case JB, Feng JY, Jordan R, Ray AS, Cihlar T, Siegel D, Mackman RL, Clarke MO, Baric RS, Denison MR.; ''Coronavirus Susceptibility to the Antiviral Remdesivir (GS-5734) Is Mediated by the Viral Polymerase and the Proofreading Exoribonuclease.''; PubMed Europe PMC Scholia
  124. Fehr AR, Singh SA, Kerr CM, Mukai S, Higashi H, Aikawa M.; ''The impact of PARPs and ADP-ribosylation on inflammation and host-pathogen interactions.''; PubMed Europe PMC Scholia
  125. Muramatsu T, Takemoto C, Kim YT, Wang H, Nishii W, Terada T, Shirouzu M, Yokoyama S.; ''SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity.''; PubMed Europe PMC Scholia
  126. Bhardwaj K, Sun J, Holzenburg A, Guarino LA, Kao CC.; ''RNA recognition and cleavage by the SARS coronavirus endoribonuclease.''; PubMed Europe PMC Scholia
  127. Zhou N, Pan T, Zhang J, Li Q, Zhang X, Bai C, Huang F, Peng T, Zhang J, Liu C, Tao L, Zhang H.; ''Glycopeptide Antibiotics Potently Inhibit Cathepsin L in the Late Endosome/Lysosome and Block the Entry of Ebola Virus, Middle East Respiratory Syndrome Coronavirus (MERS-CoV), and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV).''; PubMed Europe PMC Scholia
  128. Ujike M, Huang C, Shirato K, Matsuyama S, Makino S, Taguchi F.; ''Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization.''; PubMed Europe PMC Scholia
  129. de Haan CA, Kuo L, Masters PS, Vennema H, Rottier PJ.; ''Coronavirus particle assembly: primary structure requirements of the membrane protein.''; PubMed Europe PMC Scholia
  130. Hatakeyama S, Matsuoka Y, Ueshiba H, Komatsu N, Itoh K, Shichijo S, Kanai T, Fukushi M, Ishida I, Kirikae T, Sasazuki T, Miyoshi-Akiyama T.; ''Dissection and identification of regions required to form pseudoparticles by the interaction between the nucleocapsid (N) and membrane (M) proteins of SARS coronavirus.''; PubMed Europe PMC Scholia
  131. Zhou D, Tian X, Qi R, Peng C, Zhang W.; ''Identification of 22 N-glycosites on spike glycoprotein of SARS-CoV-2 and accessible surface glycopeptide motifs: implications for vaccination and antibody therapeutics.''; PubMed Europe PMC Scholia
  132. Baranov PV, Henderson CM, Anderson CB, Gesteland RF, Atkins JF, Howard MT.; ''Programmed ribosomal frameshifting in decoding the SARS-CoV genome.''; PubMed Europe PMC Scholia
  133. Ritchie G, Harvey DJ, Feldmann F, Stroeher U, Feldmann H, Royle L, Dwek RA, Rudd PM.; ''Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein.''; PubMed Europe PMC Scholia
  134. Siu YL, Teoh KT, Lo J, Chan CM, Kien F, Escriou N, Tsao SW, Nicholls JM, Altmeyer R, Peiris JS, Bruzzone R, Nal B.; ''The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.''; PubMed Europe PMC Scholia
  135. Sakai Y, Kawachi K, Terada Y, Omori H, Matsuura Y, Kamitani W.; ''Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.''; PubMed Europe PMC Scholia
  136. Tohge T, Nishiyama Y, Hirai MY, Yano M, Nakajima J, Awazuhara M, Inoue E, Takahashi H, Goodenowe DB, Kitayama M, Noji M, Yamazaki M, Saito K.; ''Functional genomics by integrated analysis of metabolome and transcriptome of Arabidopsis plants over-expressing an MYB transcription factor.''; PubMed Europe PMC Scholia
  137. Heurich A, Hofmann-Winkler H, Gierer S, Liepold T, Jahn O, Pöhlmann S.; ''TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein.''; PubMed Europe PMC Scholia
  138. Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA, Somasundaran M, Sullivan JL, Luzuriaga K, Greenough TC, Choe H, Farzan M.; ''Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.''; PubMed Europe PMC Scholia
  139. Wu F, Zhao S, Yu B, Chen YM, Wang W, Song ZG, Hu Y, Tao ZW, Tian JH, Pei YY, Yuan ML, Zhang YL, Dai FH, Liu Y, Wang QM, Zheng JJ, Xu L, Holmes EC, Zhang YZ.; ''A new coronavirus associated with human respiratory disease in China.''; PubMed Europe PMC Scholia
  140. Surjit M, Kumar R, Mishra RN, Reddy MK, Chow VT, Lal SK.; ''The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.''; PubMed Europe PMC Scholia
  141. Leduc R, Molloy SS, Thorne BA, Thomas G.; ''Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage.''; PubMed Europe PMC Scholia
  142. Al-Bari MA.; ''Chloroquine analogues in drug discovery: new directions of uses, mechanisms of actions and toxic manifestations from malaria to multifarious diseases.''; PubMed Europe PMC Scholia
  143. Takeda M, Chang CK, Ikeya T, Güntert P, Chang YH, Hsu YL, Huang TH, Kainosho M.; ''Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method.''; PubMed Europe PMC Scholia
  144. Hillen HS, Kokic G, Farnung L, Dienemann C, Tegunov D, Cramer P.; ''Structure of replicating SARS-CoV-2 polymerase.''; PubMed Europe PMC Scholia
  145. He R, Leeson A, Ballantine M, Andonov A, Baker L, Dobie F, Li Y, Bastien N, Feldmann H, Strocher U, Theriault S, Cutts T, Cao J, Booth TF, Plummer FA, Tyler S, Li X.; ''Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus.''; PubMed Europe PMC Scholia
  146. Taylor DL, Kang MS, Brennan TM, Bridges CG, Sunkara PS, Tyms AS.; ''Inhibition of alpha-glucosidase I of the glycoprotein-processing enzymes by 6-O-butanoyl castanospermine (MDL 28,574) and its consequences in human immunodeficiency virus-infected T cells.''; PubMed Europe PMC Scholia
  147. Yin W, Mao C, Luan X, Shen DD, Shen Q, Su H, Wang X, Zhou F, Zhao W, Gao M, Chang S, Xie YC, Tian G, Jiang HW, Tao SC, Shen J, Jiang Y, Jiang H, Xu Y, Zhang S, Zhang Y, Xu HE.; ''Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir.''; PubMed Europe PMC Scholia
  148. Li FQ, Xiao H, Tam JP, Liu DX.; ''Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus.''; PubMed Europe PMC Scholia
  149. Belouzard S, Chu VC, Whittaker GR.; ''Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.''; PubMed Europe PMC Scholia
  150. Glowacka I, Bertram S, Müller MA, Allen P, Soilleux E, Pfefferle S, Steffen I, Tsegaye TS, He Y, Gnirss K, Niemeyer D, Schneider H, Drosten C, Pöhlmann S.; ''Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response.''; PubMed Europe PMC Scholia
  151. Locker JK, Opstelten DJ, Ericsson M, Horzinek MC, Rottier PJ.; ''Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention.''; PubMed Europe PMC Scholia
  152. Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M.; ''Site-specific glycan analysis of the SARS-CoV-2 spike.''; PubMed Europe PMC Scholia
  153. Saikatendu KS, Joseph JS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P.; ''Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein.''; PubMed Europe PMC Scholia
  154. Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH.; ''Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging.''; PubMed Europe PMC Scholia
  155. Cohen JR, Lin LD, Machamer CE.; ''Identification of a Golgi complex-targeting signal in the cytoplasmic tail of the severe acute respiratory syndrome coronavirus envelope protein.''; PubMed Europe PMC Scholia
  156. Amirian ES, Levy JK.; ''Current knowledge about the antivirals remdesivir (GS-5734) and GS-441524 as therapeutic options for coronaviruses.''; PubMed Europe PMC Scholia
  157. Ujike M, Taguchi F.; ''Incorporation of spike and membrane glycoproteins into coronavirus virions.''; PubMed Europe PMC Scholia
  158. Li F, Li W, Farzan M, Harrison SC.; ''Structure of SARS coronavirus spike receptor-binding domain complexed with receptor.''; PubMed Europe PMC Scholia
  159. Ravindra NG, Alfajaro MM, Gasque V, Wei J, Filler RB, Huston NC, Wan H, Szigeti-Buck K, Wang B, Montgomery RR, Eisenbarth SC, Williams A, Pyle AM, Iwasaki A, Horvath TL, Foxman EF, van Dijk D, Wilen CB.; ''Single-cell longitudinal analysis of SARS-CoV-2 infection in human bronchial epithelial cells.''; PubMed Europe PMC Scholia
  160. Oostra M, te Lintelo EG, Deijs M, Verheije MH, Rottier PJ, de Haan CA.; ''Localization and membrane topology of coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication.''; PubMed Europe PMC Scholia
  161. Chang CK, Hou MH, Chang CF, Hsiao CD, Huang TH.; ''The SARS coronavirus nucleocapsid protein--forms and functions.''; PubMed Europe PMC Scholia
  162. Yu X, Chen S, Hou P, Wang M, Chen Y, Guo D.; ''VHL negatively regulates SARS coronavirus replication by modulating nsp16 ubiquitination and stability.''; PubMed Europe PMC Scholia
  163. Toots M, Yoon JJ, Cox RM, Hart M, Sticher ZM, Makhsous N, Plesker R, Barrena AH, Reddy PG, Mitchell DG, Shean RC, Bluemling GR, Kolykhalov AA, Greninger AL, Natchus MG, Painter GR, Plemper RK.; ''Characterization of orally efficacious influenza drug with high resistance barrier in ferrets and human airway epithelia.''; PubMed Europe PMC Scholia
  164. Voss D, Kern A, Traggiai E, Eickmann M, Stadler K, Lanzavecchia A, Becker S.; ''Characterization of severe acute respiratory syndrome coronavirus membrane protein.''; PubMed Europe PMC Scholia
  165. Marra MA, Jones SJ, Astell CR, Holt RA, Brooks-Wilson A, Butterfield YS, Khattra J, Asano JK, Barber SA, Chan SY, Cloutier A, Coughlin SM, Freeman D, Girn N, Griffith OL, Leach SR, Mayo M, McDonald H, Montgomery SB, Pandoh PK, Petrescu AS, Robertson AG, Schein JE, Siddiqui A, Smailus DE, Stott JM, Yang GS, Plummer F, Andonov A, Artsob H, Bastien N, Bernard K, Booth TF, Bowness D, Czub M, Drebot M, Fernando L, Flick R, Garbutt M, Gray M, Grolla A, Jones S, Feldmann H, Meyers A, Kabani A, Li Y, Normand S, Stroher U, Tipples GA, Tyler S, Vogrig R, Ward D, Watson B, Brunham RC, Krajden M, Petric M, Skowronski DM, Upton C, Roper RL.; ''The Genome sequence of the SARS-associated coronavirus.''; PubMed Europe PMC Scholia
  166. Huang C, Ito N, Tseng CT, Makino S.; ''Severe acute respiratory syndrome coronavirus 7a accessory protein is a viral structural protein.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114788view16:28, 25 January 2021ReactomeTeamReactome version 75
113563view13:18, 2 November 2020DeSlOntology Term : 'viral infectious disease' added !
113562view13:18, 2 November 2020DeSlOntology Term : 'severe acute respiratory syndrome' added !
113551view12:47, 2 November 2020DeSlOntology Term : 'infectious disease pathway' added !
113550view12:46, 2 November 2020DeSlOntology Term : 'disease pathway' added !
113549view12:42, 2 November 2020DeSlRemoved empty complex drawing at top left corner.
113548view12:38, 2 November 2020DeSlChanged layout for several complexes (included at least one small DataNode at top left corner, stretching the whole complex visually).
113542view12:02, 2 November 2020ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
(Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1MetaboliteCHEBI:53019 (ChEBI)
1-deoxynojirimycin
14-sugar N-glycan unfolded SpikeProteinP0DTC2 (Uniprot-TrEMBL)
3CLp dimer:α-KetoamidesComplexR-COV-9694375 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
3CLp dimerComplexR-COV-9694407 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
3a:membranous structureComplexR-COV-9694475 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
3aProteinP0DTC3 (Uniprot-TrEMBL)
3xPalmC-EProteinP0DTC4 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
7a ProteinP0DTC7 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
7aProteinP0DTC7 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
9bProteinP0DTD2 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
ACE2ProteinQ9BYF1 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:456216 (ChEBI)
ATPMetaboliteCHEBI:30616 (ChEBI)
BECN1 ProteinQ14457 (Uniprot-TrEMBL)
CANXProteinP27824 (Uniprot-TrEMBL)
CHMP2A ProteinO43633 (Uniprot-TrEMBL)
CHMP2B ProteinQ9UQN3 (Uniprot-TrEMBL)
CHMP3 ProteinQ9Y3E7 (Uniprot-TrEMBL)
CHMP4A ProteinQ9BY43 (Uniprot-TrEMBL)
CHMP4B ProteinQ9H444 (Uniprot-TrEMBL)
CHMP4C ProteinQ96CF2 (Uniprot-TrEMBL)
CHMP6 ProteinQ96FZ7 (Uniprot-TrEMBL)
CHMP7 ProteinQ8WUX9 (Uniprot-TrEMBL)
CMP-Neu5AcMetaboliteCHEBI:16556 (ChEBI)
CMPMetaboliteCHEBI:17361 (ChEBI)
CQ, HCQComplexR-ALL-9685610 (Reactome)
CQ, HCQComplexR-ALL-9685614 (Reactome)
CQ2+
CQ2+, HCQ2+ComplexR-ALL-9685618 (Reactome)
CTSL inhibitorsComplexR-ALL-9693170 (Reactome)
CTSL(114-288) ProteinP07711 (Uniprot-TrEMBL)
CTSL(292-333) ProteinP07711 (Uniprot-TrEMBL)
CTSL:CTSL inhibitorsComplexR-HSA-9683316 (Reactome)
Cathepsin L1ComplexR-HSA-9686717 (Reactome)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
DAD1 ProteinP61803 (Uniprot-TrEMBL)
DDOST ProteinP39656 (Uniprot-TrEMBL)
DDX5 ProteinP17844 (Uniprot-TrEMBL)
DDX5ProteinP17844 (Uniprot-TrEMBL)
DOLPMetaboliteCHEBI:16214 (ChEBI)
EDEM2 ProteinQ9BV94 (Uniprot-TrEMBL)
ER alpha-glucosidasesComplexR-HSA-9682983 (Reactome)
ER-alpha glucosidases:ER-alpha glucosidase inhibitorsComplexR-HSA-9686842 (Reactome)
ER-alpha-glucosidase inhibitorsComplexR-ALL-9686811 (Reactome)
ESCRT-IIIComplexR-HSA-917723 (Reactome)
FURINProteinP09958 (Uniprot-TrEMBL)
FUT8ProteinQ9BYC5 (Uniprot-TrEMBL)
GALNT1ProteinQ10472 (Uniprot-TrEMBL)
GANAB ProteinQ14697 (Uniprot-TrEMBL)
GSK3A ProteinP49840 (Uniprot-TrEMBL)
GSK3B ProteinP49841 (Uniprot-TrEMBL)
GSK3B:GSKiComplexR-HSA-9687663 (Reactome)
GSK3BProteinP49841 (Uniprot-TrEMBL)
GSK3ComplexR-HSA-198358 (Reactome)
GSKiComplexR-ALL-9687688 (Reactome)
GTPMetaboliteCHEBI:15996 (ChEBI)
GalNAc-O-3aProteinP0DTC3 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCQ
Host Derived Lipid Bilayer MembraneR-ALL-9685933 (Reactome)
Host Derived Lipid Bilayer Membrane R-ALL-9685947 (Reactome)
Li+
M

lattice:E

protein:encapsidated SARS-CoV-2 genomic RNA
ComplexR-COV-9694491 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
M ProteinP0DTC5 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
M latticeComplexR-COV-9694371 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
MAGT1 ProteinQ9H0U3 (Uniprot-TrEMBL)
MAN1B1 ProteinQ9UKM7 (Uniprot-TrEMBL)
MAN1B1,EDEM2ComplexR-HSA-6782581 (Reactome)
MAN2A1ProteinQ16706 (Uniprot-TrEMBL)
MAP1LC3B ProteinQ9GZQ8 (Uniprot-TrEMBL)
MAP1LC3BProteinQ9GZQ8 (Uniprot-TrEMBL)
MGAT1ProteinP26572 (Uniprot-TrEMBL)
MGAT2ProteinQ10469 (Uniprot-TrEMBL)
MGAT4A(1-535) ProteinQ9UM21 (Uniprot-TrEMBL)
MGAT4B ProteinQ9UQ53 (Uniprot-TrEMBL)
MGAT4C ProteinQ9UBM8 (Uniprot-TrEMBL)
MGAT4sComplexR-HSA-975913 (Reactome)
MGAT5ProteinQ09328 (Uniprot-TrEMBL)
MOGS ProteinQ13724 (Uniprot-TrEMBL)
MOGSProteinQ13724 (Uniprot-TrEMBL)
MProteinP0DTC5 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
Man(9) N-glycan unfolded SpikeProteinP0DTC2 (Uniprot-TrEMBL)
N-glycan pp1ab-nsp3-4ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan EProteinP0DTC4 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan M ProteinP0DTC5 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan MProteinP0DTC5 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan nsp3-4ComplexR-COV-9694479 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
N-glycan nsp3ComplexR-COV-9694735 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
N-glycan nsp4ComplexR-COV-9694569 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
N-glycan pp1a-nsp3 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan pp1a-nsp3-4 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan pp1a-nsp4 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan pp1ab-nsp3 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan pp1ab-nsp3-4 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
N-glycan pp1ab-nsp4 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
NAD+MetaboliteCHEBI:57540 (ChEBI)
NAMMetaboliteCHEBI:17154 (ChEBI)
NHC
NMPMetaboliteCHEBI:26558 (ChEBI)
NProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
NTPMetaboliteCHEBI:17326 (ChEBI)
Ncap tetramerComplexR-COV-9694464 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
Ncap tetramerComplexR-COV-9694573 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
Ncap tetramerComplexR-COV-9694659 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
Ncap tetramerComplexR-COV-9694702 (Reactome)
NcapProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
O-glycosyl 3a tetramerComplexR-COV-9694306 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
O-glycosyl 3a tetramerComplexR-COV-9694598 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
O-glycosyl 3a tetramerComplexR-COV-9694781 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
O-glycosyl 3a ProteinP0DTC3 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
O-glycosyl 3aProteinP0DTC3 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
OST complexComplexR-HSA-532516 (Reactome)
PARP10 ProteinQ53GL7 (Uniprot-TrEMBL)
PARP14 ProteinQ460N5 (Uniprot-TrEMBL)
PARP16 ProteinQ8N5Y8 (Uniprot-TrEMBL)
PARP4 ProteinQ9UKK3 (Uniprot-TrEMBL)
PARP6 ProteinQ2NL67 (Uniprot-TrEMBL)
PARP8 ProteinQ8N3A8 (Uniprot-TrEMBL)
PARP9 ProteinQ8IXQ6 (Uniprot-TrEMBL)
PARPsComplexR-HSA-8938273 (Reactome)
PIK3C3 ProteinQ8NEB9 (Uniprot-TrEMBL)
PIK3R4 ProteinQ99570 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
PRKCSH ProteinP14314 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:43474 (ChEBI)
RB1 ProteinP06400 (Uniprot-TrEMBL)
RB1ProteinP06400 (Uniprot-TrEMBL)
RNA primer R-ALL-9681661 (Reactome)
RPN1 ProteinP04843 (Uniprot-TrEMBL)
RPN2 ProteinP04844 (Uniprot-TrEMBL)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
RTC inhibitorsComplexR-ALL-9687408 (Reactome)
RTCComplexR-COV-9694302 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S-adenosyl-L-homocysteineMetaboliteCHEBI:16680 (ChEBI)
S-adenosyl-L-methionineMetaboliteCHEBI:15414 (ChEBI)
S1:S2:M lattice:E proteinComplexR-COV-9698997 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S1:S2:M:E:

7a:O-glycosyl 3a

tetramer
ComplexR-COV-9694534 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerComplexR-COV-9694585 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
ComplexR-HSA-9694785 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
ComplexR-HSA-9694758 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl

3a tetramer
ComplexR-COV-9694500 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:7a:O-glycosyl

3a tetramer
ComplexR-COV-9694324 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:O-glycosyl 3a

tetramer
ComplexR-COV-9694321 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS coronavirus

gRNA with secondary

structure:RTC
ComplexR-COV-9694731 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS coronavirus

gRNA:RTC:nascent RNA minus strand with mismatched

nucleotide
ComplexR-COV-9694269 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2

gRNA:RTC:RNA primer:RTC

inhibitors
ComplexR-COV-9694255 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 gRNA:RTC:RNA primerComplexR-COV-9694725 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2

gRNA:RTC:nascent RNA minus strand:RTC

inhibitors
ComplexR-COV-9694327 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
ComplexR-COV-9694618 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 gRNA

complement (minus strand):RTC:RTC

inhibitors
ComplexR-COV-9694690 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 gRNA

complement (minus

strand):RTC
ComplexR-COV-9694404 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 gRNA:RTCComplexR-COV-9694458 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 genomic RNA (plus strand)RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
SARS-CoV-2 genomic

RNA complement

(minus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
SARS-CoV-2 minus

strand subgenomic

mRNAs
ComplexR-COV-9694501 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SARS-CoV-2 nascent genomic RNA complement (minus strand) ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
SARS-CoV-2 nascent genomic RNA complement (minus strand) with mismatched 3' nucleotide ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
SARS-CoV-2 plus

strand subgenomic

mRNAs
ComplexR-COV-9694701 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
ST3GAL1 ProteinQ11201 (Uniprot-TrEMBL)
ST3GAL2 ProteinQ16842 (Uniprot-TrEMBL)
ST3GAL3 ProteinQ11203 (Uniprot-TrEMBL)
ST3GAL4 ProteinQ11206 (Uniprot-TrEMBL)
ST6GAL1 ProteinP15907 (Uniprot-TrEMBL)
ST6GALNAC2 ProteinQ9UJ37 (Uniprot-TrEMBL)
ST6GALNAC3 ProteinQ8NDV1 (Uniprot-TrEMBL)
ST6GALNAC4 ProteinQ9H4F1 (Uniprot-TrEMBL)
STT3A ProteinP46977 (Uniprot-TrEMBL)
SUMO-p-Ncap

dimer:SARS-CoV-2

genomic RNA
ComplexR-COV-9694402 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1:C93-UBE2IComplexR-HSA-4656922 (Reactome)
TMPRSS2 ProteinO15393 (Uniprot-TrEMBL)
TMPRSS2 inhibitorsComplexR-ALL-9682035 (Reactome)
TMPRSS2:TMPRSS2 inhibitorsComplexR-HSA-9681532 (Reactome)
TMPRSS2ProteinO15393 (Uniprot-TrEMBL)
TUSC3(1-348) ProteinQ13454 (Uniprot-TrEMBL)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
UBE2I-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
UBE2IProteinP63279 (Uniprot-TrEMBL)
UDP-GalNAcMetaboliteCHEBI:16846 (ChEBI)
UDPMetaboliteCHEBI:17659 (ChEBI)
UVRAG ProteinQ9P2Y5 (Uniprot-TrEMBL)
UVRAG complexComplexR-HSA-5683632 (Reactome) The PIK3C3-containing Beclin-1 complex consists of PIK3C3 (Vps34), BECN1 (Beclin-1, Atg6), PIK3R4 (p150, Vps15) and ATG14 (Barkor) (Matsunaga et al. 2009, Zhong et al. 2009). A similar complex where ATG14 is replaced by UVRAG functions later in autophagosome maturation and endocytic traffic (Itakura et al. 2008, Liang et al. 2008). Binding of KIAA0226 to this complex negatively regulates the maturation process (Matsunaga et al. 2009).
Ub-3xPalmC-E pentamerComplexR-COV-9694408 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
Ub-3xPalmC-E pentamerComplexR-COV-9694787 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
Ub-3xPalmC-E ProteinP0DTC4 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
Ub-3xPalmC-EProteinP0DTC4 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
UbComplexR-HSA-8943136 (Reactome)
VCPProteinP55072 (Uniprot-TrEMBL)
VHL ProteinP40337 (Uniprot-TrEMBL)
VHLProteinP40337 (Uniprot-TrEMBL)
ZCRB1 ProteinQ8TBF4 (Uniprot-TrEMBL)
ZCRB1:m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand)ComplexR-HSA-9698376 (Reactome)
ZCRB1ProteinQ8TBF4 (Uniprot-TrEMBL)
a nucleotide sugarMetaboliteCHEBI:25609 (ChEBI)
beta-D-glucoseMetaboliteCHEBI:15903 (ChEBI)
camostat
complex N-glycan-PALM-Spike S1 Fragment ProteinP0DTC2 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
complex N-glycan-PALM-Spike S2 Fragment ProteinP0DTC2 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
compound 11r
di-antennary

N-glycan-PALM-Spike

trimer
ComplexR-COV-9697195 (Reactome)
di-antennary N-glycan-PALM-Spike ProteinP0DTC2 (Uniprot-TrEMBL)
encapsidated

SARS-CoV-2 genomic

RNA (plus strand)
ComplexR-COV-9694461 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
encapsidated

SARS-CoV-2 genomic

RNA
ComplexR-COV-9694612 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
fully glycosylated Spike trimerComplexR-COV-9697197 (Reactome)
fully glycosylated Spike trimerComplexR-COV-9698334 (Reactome)
fully glycosylated Spike ProteinP0DTC2 (Uniprot-TrEMBL)
glycosylated-ACE2 ProteinQ9BYF1 (Uniprot-TrEMBL)
glycosylated-ACE2ProteinQ9BYF1 (Uniprot-TrEMBL)
high-mannose

N-glycan folded

Spike
ProteinP0DTC2 (Uniprot-TrEMBL)
high-mannose

N-glycan unfolded

Spike
ProteinP0DTC2 (Uniprot-TrEMBL)
high-mannose

N-glycan-PALM-Spike

trimer
ComplexR-COV-9696883 (Reactome)
high-mannose

N-glycan-PALM-Spike

trimer
ComplexR-COV-9696901 (Reactome)
high-mannose N-glycan-PALM-SpikeProteinP0DTC2 (Uniprot-TrEMBL)
high-mannose N-glycan-PALM-Spike ProteinP0DTC2 (Uniprot-TrEMBL)
m7G(5')pppAm-SARS-CoV-2 plus strand subgenomic mRNAsComplexR-COV-9694259 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
m7G(5')pppAm-capped

SARS-CoV-2 genomic

RNA (plus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped SARS-CoV-2 genomic RNA complement (minus strand) ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 subgenomic mRNAs

(plus strand)
ComplexR-COV-9694561 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand) ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA2 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA2RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA3 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA3RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA4 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA4RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA5 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA5RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA6 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA7 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated mRNA8 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated-mRNA9 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-capped,polyadenylated-mRNA9RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA2 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA3 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA4 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA5 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA6 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA7 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA8 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7G(5')pppAm-mRNA9 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-SARS-CoV-2

plus strand

subgenomic mRNAs
ComplexR-COV-9694711 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
m7GpppA-capped

SARS-CoV-2 genomic

RNA (plus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
RnaMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA2 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA3 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA4 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA5 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA6 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA7 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA8 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
m7GpppA-mRNA9 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA2 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA2 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA3 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA3 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA4 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA4 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA5 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA5 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA6 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA6 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA7a ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA7a minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA7b ProteinMN908947.3 (NCBI Protein)
mRNA7b minus strand ProteinMN908947.3 (NCBI Protein)
mRNA8 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA8 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA9 ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
mRNA9 minus strand ProteinMN908947.3 (NCBI Protein) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
nascent EProteinP0DTC4 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
nascent MProteinP0DTC5 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
nascent SpikeProteinP0DTC2 (Uniprot-TrEMBL)
nsp1-4ComplexR-COV-9694784 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp10:nsp14ComplexR-COV-9694688 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp10ComplexR-COV-9694358 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp13:DDX5ComplexR-HSA-9694692 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp15 hexamerComplexR-COV-9694570 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp15:RB1ComplexR-HSA-9694258 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp16:VHLComplexR-HSA-9694398 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp16:nsp10ComplexR-COV-9694416 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp1ComplexR-COV-9694741 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp2ComplexR-COV-9694760 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp3-4ComplexR-COV-9694554 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp3:nsp4:nsp6ComplexR-COV-9694728 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp3:nsp4ComplexR-COV-9694366 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp3ComplexR-COV-9694428 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp4ComplexR-COV-9694577 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp5ComplexR-COV-9694748 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp6ComplexR-COV-9694361 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp6ComplexR-COV-9694770 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13:nsp15ComplexR-COV-9694740 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13ComplexR-COV-9694717 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp7:nsp8:nsp12:nsp14:nsp10ComplexR-COV-9694597 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp7:nsp8:nsp12ComplexR-COV-9691364 (Reactome)
nsp7:nsp8ComplexR-COV-9691348 (Reactome)
nsp7ComplexR-COV-9691334 (Reactome)
nsp8:MAP1LC3BComplexR-HSA-9694566 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp8ComplexR-COV-9691351 (Reactome)
nsp9 dimerComplexR-COV-9694286 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nsp9ComplexR-COV-9694383 (Reactome) This COVID-19 DefinedSet instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
nucleoside 5'-diphosphate(3-)MetaboliteCHEBI:57930 (ChEBI)
nucleoside 5'-diphosphate(3−)R-ALL-9683046 (Reactome)
nucleotide-sugarR-ALL-9683033 (Reactome)
palmitoyl-CoAMetaboliteCHEBI:15525 (ChEBI)
phospho-ADPr-p-S177-NcapProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
phospho-SUMO1-K62-ADPr-p-S177-Ncap ProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
phospho-SUMO1-K62-ADPr-p-S177-NcapProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
phospho-p-S177,S181,S185,S187,S189,S191,S195,T199,S203,S207-NProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
phospho-p-S177-NcapProteinP0DTC9 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a dimerComplexR-COV-9694743 (Reactome) This COVID-19 Complex instance was generated via electronic inference from a curated CoV-1 (Human SARS coronavirus) Reactome instance. In Reactome, inference is the process used to automatically create orthologous Pathways, Reactions and PhysicalEntities from our expertly curated data (https://reactome.org/documentation/inferred-events).
pp1a-3CL ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-3CLProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp1 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp1-4 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp1-4ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp10 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp10ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp11ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp2 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp3 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp3-4 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp4 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp6 ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp6-11ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp6ProteinP0DTC1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1a-nsp7 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp7ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp8 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp8ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp9 ProteinP0DTC1 (Uniprot-TrEMBL)
pp1a-nsp9ProteinP0DTC1 (Uniprot-TrEMBL)
pp1aProteinP0DTC1 (Uniprot-TrEMBL)
pp1ab-nsp1 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp1-4 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp1-4ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp10 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp10ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp12 ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp12ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp13 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp13ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp14 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp14ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp15 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp15ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp16 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp16ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp2 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp3 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp3-4 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp4 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp5 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp5ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp6 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp6ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp7 ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp7ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp8 ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp8ProteinP0DTD1 (Uniprot-TrEMBL)
pp1ab-nsp9 ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1ab-nsp9ProteinP0DTD1-1 (Uniprot-TrEMBL) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
pp1abProteinP0DTD1 (Uniprot-TrEMBL)
sialyltransferasesComplexR-HSA-9683042 (Reactome)
teicoplanin
tri-antennary

N-glycan-PALM-Spike

trimer
ComplexR-COV-9697194 (Reactome)
tri-antennary N-glycan-PALM-Spike ProteinP0DTC2 (Uniprot-TrEMBL)
α-KetoamidesComplexR-ALL-9682022 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
(Glc)3 (GlcNAc)2 (Man)9 (PP-Dol)1R-HSA-9694793 (Reactome)
14-sugar N-glycan unfolded SpikeArrowR-HSA-9694793 (Reactome)
14-sugar N-glycan unfolded SpikeR-HSA-9694364 (Reactome)
3CLp dimer:α-KetoamidesArrowR-HSA-9694592 (Reactome)
3CLp dimer:α-KetoamidesTBarR-HSA-9694441 (Reactome)
3CLp dimer:α-KetoamidesTBarR-HSA-9694551 (Reactome)
3CLp dimer:α-KetoamidesTBarR-HSA-9694732 (Reactome)
3CLp dimerArrowR-HSA-9694333 (Reactome)
3CLp dimerR-HSA-9694592 (Reactome)
3CLp dimermim-catalysisR-HSA-9694441 (Reactome)
3CLp dimermim-catalysisR-HSA-9694551 (Reactome)
3CLp dimermim-catalysisR-HSA-9694732 (Reactome)
3a:membranous structureArrowR-HSA-9694308 (Reactome)
3aArrowR-HSA-9694392 (Reactome)
3aArrowR-HSA-9694794 (Reactome)
3aR-HSA-9694392 (Reactome)
3aR-HSA-9694438 (Reactome)
3xPalmC-EArrowR-HSA-9694401 (Reactome)
3xPalmC-ER-HSA-9694529 (Reactome)
7aR-HSA-9694528 (Reactome)
9bArrowR-HSA-9698265 (Reactome)
ACE2ArrowR-HSA-9694661 (Reactome)
ACE2ArrowR-HSA-9699007 (Reactome)
ADPArrowR-HSA-9694265 (Reactome)
ADPArrowR-HSA-9694293 (Reactome)
ADPArrowR-HSA-9694620 (Reactome)
ATPR-HSA-9694265 (Reactome)
ATPR-HSA-9694293 (Reactome)
ATPR-HSA-9694471 (Reactome)
ATPR-HSA-9694620 (Reactome)
ATPR-HSA-9694733 (Reactome)
CANXmim-catalysisR-HSA-9694337 (Reactome)
CMP-Neu5AcR-HSA-9694718 (Reactome)
CMPArrowR-HSA-9694718 (Reactome)
CQ, HCQArrowR-HSA-9683478 (Reactome)
CQ, HCQR-HSA-9683467 (Reactome)
CQ, HCQR-HSA-9683478 (Reactome)
CQ2+, HCQ2+ArrowR-HSA-9683467 (Reactome)
CTSL inhibitorsR-HSA-9685655 (Reactome)
CTSL:CTSL inhibitorsArrowR-HSA-9685655 (Reactome)
CTSL:CTSL inhibitorsTBarR-HSA-9694287 (Reactome)
Cathepsin L1R-HSA-9685655 (Reactome)
Cathepsin L1mim-catalysisR-HSA-9694287 (Reactome)
CoA-SHArrowR-HSA-9694341 (Reactome)
CoA-SHArrowR-HSA-9694401 (Reactome)
DDX5R-HSA-9694406 (Reactome)
DOLPArrowR-HSA-9694793 (Reactome)
ER alpha-glucosidasesR-HSA-9686790 (Reactome)
ER alpha-glucosidasesmim-catalysisR-HSA-9694364 (Reactome)
ER-alpha glucosidases:ER-alpha glucosidase inhibitorsArrowR-HSA-9686790 (Reactome)
ER-alpha glucosidases:ER-alpha glucosidase inhibitorsTBarR-HSA-9694364 (Reactome)
ER-alpha-glucosidase inhibitorsR-HSA-9686790 (Reactome)
ESCRT-IIIArrowR-HSA-9698265 (Reactome)
FURINArrowR-HSA-9698988 (Reactome)
FURINmim-catalysisR-HSA-9699007 (Reactome)
FUT8mim-catalysisR-HSA-9696980 (Reactome)
GALNT1mim-catalysisR-HSA-9694438 (Reactome)
GSK3B:GSKiArrowR-HSA-9687724 (Reactome)
GSK3B:GSKiTBarR-HSA-9694293 (Reactome)
GSK3BR-HSA-9687724 (Reactome)
GSK3Bmim-catalysisR-HSA-9694293 (Reactome)
GSK3mim-catalysisR-HSA-9694620 (Reactome)
GSKiR-HSA-9687724 (Reactome)
GTPR-HSA-9694476 (Reactome)
GTPR-HSA-9694492 (Reactome)
GTPR-HSA-9694737 (Reactome)
GalNAc-O-3aArrowR-HSA-9694438 (Reactome)
GalNAc-O-3aR-HSA-9694718 (Reactome)
H+ArrowR-HSA-9694293 (Reactome)
H+ArrowR-HSA-9694331 (Reactome)
H+ArrowR-HSA-9694389 (Reactome)
H+ArrowR-HSA-9694438 (Reactome)
H+ArrowR-HSA-9694525 (Reactome)
H+ArrowR-HSA-9694611 (Reactome)
H+ArrowR-HSA-9694773 (Reactome)
H+ArrowR-HSA-9694790 (Reactome)
H+R-HSA-9683467 (Reactome)
H2OR-HSA-9694338 (Reactome)
H2OR-HSA-9694364 (Reactome)
H2OR-HSA-9694377 (Reactome)
H2OR-HSA-9694441 (Reactome)
H2OR-HSA-9694476 (Reactome)
H2OR-HSA-9694492 (Reactome)
H2OR-HSA-9694551 (Reactome)
H2OR-HSA-9694601 (Reactome)
H2OR-HSA-9694625 (Reactome)
H2OR-HSA-9694632 (Reactome)
H2OR-HSA-9694732 (Reactome)
H2OR-HSA-9694737 (Reactome)
Host Derived Lipid Bilayer MembraneR-HSA-9694308 (Reactome)
M

lattice:E

protein:encapsidated SARS-CoV-2 genomic RNA
ArrowR-HSA-9694444 (Reactome)
M

lattice:E

protein:encapsidated SARS-CoV-2 genomic RNA
R-HSA-9694553 (Reactome)
M latticeArrowR-HSA-9694487 (Reactome)
M latticeR-HSA-9694444 (Reactome)
MAN1B1,EDEM2mim-catalysisR-HSA-9696807 (Reactome)
MAN2A1mim-catalysisR-HSA-9694656 (Reactome)
MAP1LC3BArrowR-HSA-9698265 (Reactome)
MAP1LC3BR-HSA-9694580 (Reactome)
MAP1LC3BR-HSA-9698265 (Reactome)
MArrowR-HSA-9694555 (Reactome)
MGAT1mim-catalysisR-HSA-9694656 (Reactome)
MGAT2mim-catalysisR-HSA-9694656 (Reactome)
MGAT4smim-catalysisR-HSA-9696980 (Reactome)
MGAT5mim-catalysisR-HSA-9696980 (Reactome)
MOGSmim-catalysisR-HSA-9694364 (Reactome)
MR-HSA-9694487 (Reactome)
Man(9) N-glycan unfolded SpikeArrowR-HSA-9694364 (Reactome)
Man(9) N-glycan unfolded SpikeR-HSA-9696807 (Reactome)
N-glycan pp1ab-nsp3-4mim-catalysisR-HSA-9694601 (Reactome)
N-glycan EArrowR-HSA-9694790 (Reactome)
N-glycan MArrowR-HSA-9694367 (Reactome)
N-glycan MArrowR-HSA-9694525 (Reactome)
N-glycan MR-HSA-9694367 (Reactome)
N-glycan MR-HSA-9694487 (Reactome)
N-glycan nsp3-4ArrowR-HSA-9694331 (Reactome)
N-glycan nsp3ArrowR-HSA-9694389 (Reactome)
N-glycan nsp3R-HSA-9694317 (Reactome)
N-glycan nsp3mim-catalysisR-HSA-9694625 (Reactome)
N-glycan nsp4ArrowR-HSA-9694611 (Reactome)
N-glycan nsp4R-HSA-9694317 (Reactome)
NAD+R-HSA-9694773 (Reactome)
NAMArrowR-HSA-9694773 (Reactome)
NArrowR-HSA-9694344 (Reactome)
NMPArrowR-HSA-9694632 (Reactome)
NR-HSA-9694620 (Reactome)
NTPR-HSA-9694277 (Reactome)
NTPR-HSA-9694344 (Reactome)
NTPR-HSA-9694506 (Reactome)
NTPR-HSA-9694549 (Reactome)
NTPR-HSA-9694581 (Reactome)
NTPR-HSA-9694605 (Reactome)
NTPR-HSA-9694792 (Reactome)
Ncap tetramerArrowR-HSA-9694345 (Reactome)
Ncap tetramerArrowR-HSA-9694363 (Reactome)
Ncap tetramerArrowR-HSA-9694568 (Reactome)
Ncap tetramerArrowR-HSA-9694575 (Reactome)
Ncap tetramerArrowR-HSA-9694723 (Reactome)
Ncap tetramerR-HSA-9694281 (Reactome)
Ncap tetramerR-HSA-9694345 (Reactome)
Ncap tetramerR-HSA-9694455 (Reactome)
Ncap tetramerR-HSA-9694568 (Reactome)
Ncap tetramerR-HSA-9694575 (Reactome)
NcapArrowR-HSA-9694370 (Reactome)
NcapArrowR-HSA-9694373 (Reactome)
NcapR-HSA-9694293 (Reactome)
NcapR-HSA-9694373 (Reactome)
O-glycosyl 3a tetramerArrowR-HSA-9694662 (Reactome)
O-glycosyl 3a tetramerArrowR-HSA-9694727 (Reactome)
O-glycosyl 3a tetramerR-HSA-9694308 (Reactome)
O-glycosyl 3a tetramerR-HSA-9694528 (Reactome)
O-glycosyl 3a tetramerR-HSA-9694572 (Reactome)
O-glycosyl 3a tetramerR-HSA-9694727 (Reactome)
O-glycosyl 3aArrowR-HSA-9694572 (Reactome)
O-glycosyl 3aArrowR-HSA-9694718 (Reactome)
O-glycosyl 3aR-HSA-9694662 (Reactome)
OST complexmim-catalysisR-HSA-9694793 (Reactome)
PARPsmim-catalysisR-HSA-9694773 (Reactome)
PPiArrowR-HSA-9694277 (Reactome)
PPiArrowR-HSA-9694344 (Reactome)
PPiArrowR-HSA-9694471 (Reactome)
PPiArrowR-HSA-9694476 (Reactome)
PPiArrowR-HSA-9694492 (Reactome)
PPiArrowR-HSA-9694506 (Reactome)
PPiArrowR-HSA-9694549 (Reactome)
PPiArrowR-HSA-9694581 (Reactome)
PPiArrowR-HSA-9694605 (Reactome)
PPiArrowR-HSA-9694733 (Reactome)
PPiArrowR-HSA-9694737 (Reactome)
PPiArrowR-HSA-9694792 (Reactome)
PiArrowR-HSA-9694265 (Reactome)
PiArrowR-HSA-9694476 (Reactome)
PiArrowR-HSA-9694492 (Reactome)
PiArrowR-HSA-9694737 (Reactome)
R-HSA-9681514 (Reactome) Entry of influenza, parainfluenza and coronaviruses into airway epithelial cells requires binding of a viral spike protein to a host cell receptor, followed by cleavage and activation of the viral spike protein mediated by the host cell. Without this cleavage, fusion of the viral and host cell membranes is blocked. The primary receptor for the human SARS-CoV-1 virus is angiotensin converting enzyme 2 (ACE2) (Li et al. 2003). The resultant complex is cleaved by the protease transmembrane protease serine 2 (TMPRSS2) (Shulla et al. 2011, Heurich et al. 2014). Therefore, active site inhibitors of these airway proteases could have broad therapeutic applicability against multiple respiratory viruses (Laporte & Naesens 2017). The approved drug camostat is a protease inhibitor that may block SARS-CoV-2 entry into cells by inhibiting the actions of TMPRSS2 (Kawase et al. 2012, Hoffmann et al. 2020). Nafamostat, another serine protease inhibitor, was found to be a potent inhibitor of S-mediated membrane fusion and blocked MERS-CoV infection in vitro (Yamamoto et al. 2016).

Otamixaban (FXV673), an anticoagulant, is a potent and selective direct inhibitor of coagulation factor Xa. Virtual docking studies suggest that otamixaban may bind to the serine protease TMPRSS2 (Rensi et al. 2020, preprint). Inhibition of TMPRSS2 is being examined for antiviral activity but its inhibitory potential and/or antiviral activity have not yet been determined so it is annotated here as a candidate drug. I-432 is another inhibitor of TMPRSS2 under investigation for anti viral potential (Pászti-Gere et al. 2016).
R-HSA-9683467 (Reactome) Chloroquine (CQ) and hydroxychloroquine (HCQ) are diprotic weak bases that can exist in both protonated and unprotonated forms. Unprotonated CQ or HCQ can diffuse freely and rapidly across the membranes of cells and organelles to acidic cytoplasmic vesicles (late endosomes and lysosomes). Agents that have this ability are known as lysosomotropic agents. Once protonated, CQ2+ or HCQ2+ are trapped in the acidic lumen of these vesicles. This leads to an irreversible accumulation of CQ or HCQ in acidic vesicles to concentrations as much as 100 fold over cytosolic ones and to an elevation of vesicle pH due to trapping of H+ ions by CQ or HCQ. Thus, CQ analogues interfere with endosomal and lysosomal acidification, which in turn inhibits proteolysis, chemotaxis, phagocytosis and antigen presentation. As a result, cells are not able to proceed with endocytosis, exosome release and phagolysosomal fusion in an orderly manner (Foley & Tilley 1998, Yang & Shen 2020). In vitro, these endosomal acidification fusion inhibitors block cellular infection by a clinical isolate of SARS-CoV-2 (Wang et al. 2020, Hu et al. 2020).
R-HSA-9683478 (Reactome) Unprotonated chloroquine (CQ) and hydroxychloroquine (HCQ) can both diffuse freely and rapidly across the membranes of cells and organelles (Chinappi et al. 2010).
R-HSA-9685655 (Reactome) Lysosomes play critical roles in human biology receiving, trafficking, processing, and degrading biological molecules from cellular processes such as endocytosis, phagocytosis, autophagy and secretion. Lysosomes house around sixty proteolytic enzymes, among them cathepsins. Cathepsins are involved in many processes involving cell death, protein degradation, post-translational modifications of proteins, extracellular matrix (ECM) remodeling, autophagy, and immune signaling. The early stages of the viral life cycle involve the cleavage of the viral spike protein by cathepsin L (CTSL) in late endosomes, facilitating viral RNA release to continue viral replication. Teicoplanin, a glycopeptide antibiotic used to treat Gram-positive bacterial infection, especially in Staphylococcal infections, was shown to have efficacy in vitro against Ebola Virus, MERS and SARS-CoV-1 (Zhou et al. 2016).

Teicoplanin is thought to inhibit the low pH cleavage of the viral spike protein by CTSL in late endosomes thereby preventing the release of genomic viral RNA and the continuation of virus replication cycle (Baron et al. 2020). The target sequence that serve as the cleavage site for CTSL is conserved in the SARS-CoV-2 spike protein (Zhou et al. 2020 [preprint]). Further investigation is required to determine the therapeutic potential of teicoplanin in COVID-19 patients.

Relacatib is an investigational drug trialed for the treatment of osteoporosis (Duong et al. 2016). It is a potent CTSK inhibitor but also shows activity against CTSL (Kumar et al. 2007) so could potentially be investigated for Covid-19 patients. The antileprotic drug clofazimine and the antituberculous drugs rifampicin and isoniazid have been shown to inhibit cathepsins B, H and L from purified goat and bovine brains (Kamboj et al. 2003).
R-HSA-9686790 (Reactome) Inhibition of host cellular functions required for viral replication is considered another host-targeting antiviral strategy. Extensive pharmacological studies have validated ER glucosidases as valuable host antiviral targets against many enveloped viruses (Chang et al. 2013). Most known ER glucosidase inhibitors are imino sugars like 1-deoxynojirimycin (DNJ) and castanopermine (CAST) derivatives (Taylor et al. 1994).

It is generally believed that inhibition of ER glucosidase I and/or II prevents the removal of the terminal glucose moieties on N-linked glycans and results in misfolding and retention of glycoproteins in the ER and ultimate degradation via the ER-associated degradation (ERAD) pathway (Simsek et al. 2005, Alonzi et al. 2013). As a consequence of the abnormal trafficking and degradation of viral glycoproteins, virion assembly and secretion are inhibited (Chang et al. 2009, Taylor et al. 1998).

Long-term suppression of ER glucosidases I and/or II with more potent inhibitors may cause significant side effects, particularly in nerve and immune systems (Sadat et al. 2014).
R-HSA-9687724 (Reactome) Many GSK-3β inhibitors (GSKi) have been identified. They are known to induce apoptosis in leukemia and pancreatic cancer cells, and can destabilize p53, which may promote cellular death in response to DNA damaging agents (Wang et al, 2008; Beurel et al, 2009). Administration of GSKi inhibited cochlear destruction in cisplatin-injected mice (Park et al, 2009).

Li is a selective ATP competitive inhibitor of GSK-3 (Ryves and Harwood, 2001). Lithium carbonate has been and continously is in clinical trials with bipolar disorder patients (Moore et al, 2009). LY2090314 has been in clinical trials for metastatic pancreatic cancer and acute leukemia ([NCT01632306], [NCT01287520], [NCT01214603]). Clinical trials of GSKi for Alzheimer's disease were unsuccessful.

The use of GSKi remains controversial because of their possibly oncogenic properties. Evaluation of GSKi in clinical trials has been hampered by the fear that inhibition of GSK-3 may stimulate or aid in malignant transformation as GSK-3 can phosphorylate pro-oncogenic factors such as beta-catenin, c-Jun and c-Myc which targets them for degradation (Patel & Woodgett, 2008). However, no studies have been reported suggesting that treatment of mice with GSKi resulted in an increase in cancer incidence. In fact, many patients with bi-polar disorder have been treated with lithium for prolonged periods of time. There does not appear to be any evidence that these patients have increased incidences of cancer (McCubrey et al, 2014).

The GSKi kenpaullone and lithium chloride were found to reduce viral Nucleoprotein phosphorylation in the severe acute respiratory syndrome CoV-infected VeroE6 cells and decrease the viral titer and cytopathic symptoms. Effect of GSK-3 inhibition were reproduced in another coronavirus, the neurotropic JHM strain of mouse hepatitis virus (Wu et al, 2009).
R-HSA-9691335 (Reactome) SARS-CoV-2 nonstructural proteins nsp7 and nsp8 form a heterodimer (Gao et al. 2020, Li et al. 2020). A dimer of dimers has also been observed and it has been proposed that this heterotetramer forms a putative RNA-binding site (Konkolova et al. 2020).
R-HSA-9691363 (Reactome) The nsp7:nsp8 heterodimer binds to the RNA-directed RNA polymerase (nsp12) of the SARS-CoV-2 (Gao et al. 2020, Li et al. 2020, Hillen et al. 2020). The second subunit of nsp8, not bound to nsp7, interacts with a different region of nsp12 (Gao et al. 2020, Yin et al. 2020), as previously found in SARS-CoV-1 (Kirchdoerfer and Ward 2019).
R-HSA-9694261 (Reactome) Nonstructural protein 9 from SARS-Cov-2 is an obligate homodimer, comprising a unique fold that associates via an unusual α-helical GxxxG interaction motif. The integrity of this motif is considered important for viral replication (Littler et al, 2020; Miknis et al, 2009).
R-HSA-9694265 (Reactome) nsp13 of SARS-CoV-2 possesses the nucleoside triphosphate hydrolase (NTPase) activity (Chen et al. 2020, Shu et al. 2020), and functions as an NTP-dependent RNA helicase that can unwind RNA helices (Shu et al. 2020). Several G-quadruplex structures were confirmed in SARS-CoV-2 RNA and found to directly interact with nsp13, which may act to melt these structures (Ji et al. 2020).

nsp13 of SARS-CoV-1 is an ATP-dependent helicase that functions in the 5'-3' direction to unwind double stranded RNAs that have a 5' single strand overhang at least 20 nucleotides long. nsp13 can also act on double strand DNA in vitro, but dsRNA is thought to be its physiological substrate. The catalytic activity of SARS-CoV-1 nsp13 is increased in the presence of nsp12, the viral RNA-dependent RNA polymerase. nsp13 is needed for the replication of SARS-CoV-1 and is thought to act by melting secondary structures in the genomic RNA template during replication, and also to be involved in unwinding of RNA duplexes during transcription of viral genes. nsp13 is a promising target for experimental anti-SARS-CoV-1 drugs (Tanner et al. 2003, Ivanov et al. 2004, Bernini et al. 2006, Chen et al. 2009, Lee et al. 2010, Adedeji et al. 2012).
R-HSA-9694274 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

In about 15% of translation attempts of the genomic viral mRNA1 in the host cell cytosol, a -1 frameshift happens after the nsp10 gene that leads to translation of the full pp1ab polyprotein (Baranov et al, 2005).
R-HSA-9694277 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

nsp8 functions as an RNA-dependent RNA polymerase (RdRp) that serves as the primase for nsp12, the main RdRp of the SARS coronavirus 1 (SARS-CoV-1) (Imbert et al. 2006), as it is capable of de novo RNA synthesis (te Velthuis et al. 2011). nsp8 synthesizes short oligonucleotides (less than 6 bases long) using genomic RNA as a template. nsp8 requires at least one cytidine residue in the template sequence for its activity. Activity is dependent on manganese ions (Imbert et al. 2006). nsp8 can also extend primers but is 20-fold less efficient than nsp12 (te Velthuis et al. 2011).
R-HSA-9694280 (Reactome) SARS-CoV-2 mRNA4 has a length of 228 nt and encodes the 75 aa Envelope small membrane protein (Wu et al, 2020).
R-HSA-9694281 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Based on studies in other coronaviruses, the final SARS-COV-2 ribonucleoprotein complex is predicted to be a hollow helical structure with an approximate diameter of 9-16nm, with the C-terminal domain of N protein forming the inner core and the N-terminal domain forming the outer surface (Neuman et al, 2006; Chen et al, 2007). Oliomerization of the N protein capsid coat is likely nucleated through both protein-RNA and protein-protein interactions by the first few N-protein dimers on the genomic RNA (Saikatendu et al, 2007; Chang et al, 2013; reviewed in Chang et al, 2014). Each N dimer may make contact with up to 7 bases of the RNA (reviewed in Chang et al, 2014).
R-HSA-9694287 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Within the host cell endocytic vesicle, SARS-CoV-2 Spike (S) protein is cleaved between residues 797 and 798 by cathepsin L1 (CTSL) (Huang et al. 2006). The roles of S protein in viral binding to the host cell membrane and fusion of viral and host cell membranes and thus the central role of S protein in determining the host range and tissue tropisms of the virus are reviewed by Belouzard et al. (2012).
R-HSA-9694293 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The majority of nucleoprotein is serine-phosphorylated in the cytosol and, possibly, in the nucleus where it gets immediately transported to the cytosol. Phosphorylation is catalyzed by glycogen synthase kinase 3 (GSK3) and several other host cell kinases (Surjit et al, 2005; Wu et al. 2009)
R-HSA-9694294 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Both a predicted beta-hairpin motif and the N-terminal part of protein E are sufficient for its localization to the Golgi membrane. Although porin activity has been shown for protein E it cannot be detected in the plasma membrane of infected cells (Liao et al, 2006; Cohen et al, 2011; Nieto-Torres, 2011).
R-HSA-9694304 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Non-structural protein 14 (nsp14) of the human SARS coronavirus is a bifunctional enzyme bearing 3'-5 exoribonuclease activity involved in replication fidelity and RNA cap N7-guanine methyltransferase activity involved in 5'-RNA capping. nsp14 binds to the minimal replication and transcription complex (RTC), composed of nsp7, nsp8, and nsp12, by directly binding to nsp12 (the main RNA-dependent RNA polymerase). Binding of nsp14 does not affect the processivity of the RTC (Minskaia et al. 2006, Subissi et al. 2014).
R-HSA-9694308 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Membranous structures containing protein 3a are being shedded from the cell membrane (Huang et al, 2006)
R-HSA-9694317 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

nsp3 and nsp4 alone caused considerable ER membrane deformation, producing a perinuclear double-walled maze-like body (MLB), and the nsp3–nsp4 interaction was shown to be absolutely necessary for such membrane rearrangement. Further necessary factors are nsp6 and unidentified host factors (Angelini et al 2013, Sakai et al 2017). nsp6 by itself can form Atg5 and LC3II-positive vesicles classically observed in autophagy (Cottam et al, 2014). However, in mouse hepatitis virus (MHV) infections, EDEM1 and OS9 of the ER-associated degradation system have been shown to be necessary co-factors (Reggiori et al, 2010)
R-HSA-9694331 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

To process the nsp3/4 cleavage site, PL-PRO and, presumably, nsp3-4 need to be glycosylated and localized to a membrane (Harcourt et al, 2004)
R-HSA-9694333 (Reactome) SARS-Cov-2 main protease forms a tight dimer. Dimerization of the enzyme is necessary for catalytic activity (Zhang et al, 2020).
R-HSA-9694334 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

In most translation attempts the genomic viral mRNA1 in the cytosol is translated to a shortened polyprotein, pp1a, that does not contain genome replication enzymes (Baranov et al, 2005).
R-HSA-9694337 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Calnexin transiently binds the unfolded spike protein and prevents its aggregation and premature degradation, ensuring its correct folding (Fukushi et al, 2012).
R-HSA-9694338 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The papain-like protease domain of the nsp1-4 fragment alone is sufficient for processing the nsp1/2 and nsp2/3 cleavage sites (Harcourt et al, 2004).
R-HSA-9694341 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Two of the four cysteine-rich clusters of the viral spike protein are modified by palmitoylation. This is required for the protein's partitioning into detergent-resistant membranes and for cell–cell fusion. In general, palmitoylation is usually non-enzymatic (Petit et al, 2007; McBride and Machamer, 2010; Veit, 2012).
R-HSA-9694344 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

SARS-CoV-1 encodes eight subgenomic RNAs, mRNA2 to mRNA9. mRNA1 corresponds to the genomic RNA. The 5' and 3' ends of subgenomic RNAs are identical, in accordance with the template switch model of coronavirus RNA transcription (Snijder et al. 2003, Thiel et al. 2003, Yount et al. 2003). Therefore, consistent with this and the studies of the murine hepatitis virus (MHV), which is closely related to SARS-CoV-1, genomic positive strand RNA is first transcribed into negative sense (minus strand) subgenomic mRNAs, that subsequently serve as templates for the synthesis of positive strand subgenomic mRNAs. Negative-sense virus RNAs are present in much smaller amounts than positive-sense RNAs (Irigoyen et al. 2016). Each subgenomic RNA contains a leader transcription regulatory sequence (leader TRS) that is identical to the leader of the genome, appended via polymerase “jumping� during negative strand synthesis to the body transcription regulatory sequence (body TRS), a short, AU-rich motif of about 10 nucleotides found upstream of each ORF that is destined to become 5' proximal in one of the subgenome-length mRNAs. The 3' and 5'UTRs may interact through RNA–RNA and/or RNA–protein plus protein–protein interactions to promote circularization of the coronavirus genome, placing the elongating minus strand in a favorable topology for leader-body joining. The host protein PABP was found to bind to the coronavirus 3' poly(A) tail and to interact with the host protein eIF-4G, a component of the three-subunit complex that binds to mRNA cap structures, which may promote the circularization of the coronavirus genome. Two viral proteins that bind to the coronavirus 5'UTR, the N protein and nsp1, may play a role in template switching. The poly(A) tail is necessary for the initiation of minus-strand RNA synthesis at the 3' end of genomic RNA. For review, please refer to Sawicki et al. 2007 and Yang and Leibowitz 2015.
R-HSA-9694345 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

A certain part of the nucleoprotein can be found in the nucleolus. This localisation seems to depend on the protein's sumoylation (Li et al, 2005)
R-HSA-9694363 (Reactome) Nucleoprotein of SARS-Cov-2 forms dimers which in solution predominantly assemble to homotetramers (Ye et al, 2002).
R-HSA-9694364 (Reactome) N-glycan side chains on the unfolded SARS-CoV-2 spike protein get their terminal glucose moieties cleaved by ER glucosidases I and II, before folding. (Watanabe et al, 2020, Völker et al, 2002, Pelletier et al, 2000).
R-HSA-9694367 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein M accumulates in the Golgi complex and recruits Spike protein to the sites of virus assembly and budding in the ERGIC (Voss et al, 2009).
R-HSA-9694370 (Reactome) SARS-CoV-2 mRNA9a has a length of 1,260 nt and encodes the 419 aa nucleoprotein (Wu et al, 2020).
R-HSA-9694373 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Significant amounts of the unphosphorylated N protein are associated with the cell membrane (Surjit et al, 2005)
R-HSA-9694377 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The crucial step of autocleavage of pp1a involves the formation of an "intermediate" pp1a dimer which has weak protease activity. This "embedded" 3CLp liberates itself by cleaving the ends off its monomer in trans. Only after that occurs does the cleaved 3CLp form a dimer, the most efficient form of the enzyme (Hsu et al, 2005; Chen et al, 2010; Muramatsu et al, 2016)
R-HSA-9694389 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

To process the nsp3/4 cleavage site, PL-PRO and, presumably, nsp3-4 need to be glycosylated and localized to a membrane (Harcourt et al, 2004)
R-HSA-9694390 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Human SARS coronavirus 1 (SARS-CoV-1) non-structural protein 15 (nsp15) contains the LXCXE/D motif characteristic of proteins that bind to the retinoblastoma protein RB1. Binding to human RB1 increases the endonuclease activity of nsp15 but is not required for it. RB1 bound to nsp15 is retained in the cytosol. Interaction of nsp15 with RB1 likely affects the cell cycle of infected cells and probably modulates cytotoxicity of SARS-CoV-1 (Bhardwaj et al. 2012).
R-HSA-9694392 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Viral protein 3a translocates from the cytosol to the ERGIC (endoplasmic reticulum Golgi intermediate compartment) (Oostra et al. 2006)
R-HSA-9694401 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Viral E protein is modified by palmitoylation at all three cysteine residues. In general, palmitoylation is usually non-enzymatic (Liao et al, 2006, Veit, 2012).
R-HSA-9694406 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

nsp13, the helicase of the human SARS coronavirus 1 (SARS-CoV-1) binds to DDX5, a host protein implicated in transcription, pre-mRNA processing, RNA degradation, RNA export, ribosome assembly and translation. DDX5 knockdown inhibits viral replication (Chen et al. 2009).
R-HSA-9694419 (Reactome) Remdesivir (GS-5734) is an investigational nucleotide analogue drug that was developed for its broad spectrum antiviral potential against Ebola and Marburg virus activity (Siegel et al. 2017). It targets and inhibitis viral RNA-dependent RNA polymerase (nsp12, RdRP), the key component of the replication transcription complex (RTC) (Agostini et al. 2018, Brown et al. 2019, Gordon et al. 2020). Remdesivir is being investigated for potential antiviral activity against SARS-CoV-2 by targeting viral replication (Agostini et al. 2018). Gordon et al. demonstrate remdesivir possesses broad antiviral activity against RNA viruses, including SARS-CoV, MERS-CoV and SARS-CoV-2 in-vitro (Gordon et al. 2020b). It could prevent asymptomatic, mild or moderate Covid-19 cases from progressing to severe disease (clinical trials NCT04252664, NCT04257656) but results so far in infected people have been mixed.

EIDD-2801, is an isopropylester prodrug of the ribonucleoside analogue N4-hydroxycytidine (NHC, EIDD-1931) that shows broad spectrum antiviral activity against various RNA viruses including Ebola, Influenza and CoV (Toots et al. 2019). NHC acts as a competitive alternative substrate for virally encoded RNA-dependent RNA polymerases. NHC was shown to inhibit multiple genetically-distinct Bat-CoV viruses in human primary epithelial cells without affecting cell viability. Prophylactic/therapeutic oral administration of NHC reduced lung titers and prevented acute lung failure in C57B/6 mice infected with CoV. The potency of NHC against multiple coronaviruses, its therapeutic efficacy, and oral bioavailability in vivo, all highlight its potential as an effective antiviral against SARS-CoV-2 in Covid-19 infections and other future zoonotic coronaviruses (Sheahan et al. 2020).
R-HSA-9694436 (Reactome) nsp15 of SARS-CoV-2 shares 88% sequence identity and 95% sequence similarity with nsp15 of SARS-CoV-1. Similar to its SARS-CoV-1 orthologue, nsp15 of SARS-CoV-2 forms a hexamerthat consists of a dimer of trimers. Hexamer formation is necessary for the endonuclease activity of nsp15. nsp15 preferentially cleaves 3' of uridines, generating 2'-3' cyclic phosphates after cleavage. nsp15 requires Mn2+ ions for catalytic activity. C-terminal domain contains the active site, which faces away from the center of the hexamer and contains the extreme C-terminal residues (Kim et al. 2020).
R-HSA-9694438 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

A sialyltransferase adds a terminal sialic acid moiety to protein 3a with an O-linked glycosyl side chain. This glycosylated form later is associated with the virion (Oostra et al, 2006)
R-HSA-9694441 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Main protease cleaves all cleavage sites of pp1a and ppa1b starting with nsp4/5, thus cleaving itself, and all the cytosolic RTC proteins (Fan et al, 2004)
R-HSA-9694444 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The ribonucleoprotein complex is recruited to the assembling virion through interactions with the M C-terminal tail, and appears to be independent of viral RNA (Hsieh et al, 2008; Hatakeyama et al, 2008; He et al, 2004; Luo et al, 2006; reviewed in Ujike and Taguchi, 2015). How much of this is fully conserved in SARS-COV-2 remains to be experimentally verified.
R-HSA-9694445 (Reactome) The interaction between the non-structural proteins nsp16 and nsp10 is conserved in SARS-CoV-2 virus (Li et al. 2020, Viswanathan et al. 2020, Rosas-Lemus et al. 2020).

In SARS-CoV-1, nsp16 was identified as an AdoMet-dependent (nucleoside-2'O)-methyltransferase involved in capping of viral RNAs. nsp16 binds to nsp10, which serves as a cofactor for nsp16 (Bouvet et al. 2010, Lugari et al. 2010). Nsp16 alone is unstable and exhibits 2'-O-methyltransferase activity only in complex with nsp10 (Debarnot et al, 2011; Decroly et al, 2011). nsp10-mediated activation of nsp16 catalytic activity is conserved in all coronaviruses (Wang et al. 2015). The same binding surface of nsp10 interacts with nsp14 and nsp16, suggesting that binding of nsp14 and nsp16 to nsp10 is mutually exclusive. However, as nsp10 is produced in a higher number of copies than nsp14 and nsp16, and as nsp14 and nsp16 act coordinately in RNA capping, it is most likely that nsp14:nsp10 and nsp16:nsp10 complexes co-exist within the viral replication-transcription complex (RTC) (Bouvet et al. 2012, Bouvet et al. 2014). One structural study reported that nsp10 forms dodecamers (Su et al. 2006), which would potentially allow simultaneous binding of nsp14 and nsp16 to nsp10 homomeric complexes, but it is not certain if such homomeric complexes of nsp10 exist in vivo, and if the structure of the nsp10 dodecamer would be permissive for nsp16 binding (Chen et al. 2011). nsp10 contains two zinc fingers which are thought to be involved in RNA binding (Su et al. 2006, Joseph et al. 2006).
R-HSA-9694447 (Reactome) SARS-CoV-2 mRNA2 has a length of 3,822 nt and encodes the 1,273 aa spike preprotein (Wu et al, 2020).
R-HSA-9694452 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein E forms a pentamer of monomers without disulfide bonds (Parthasarathy et al, 2012)
R-HSA-9694454 (Reactome) The cryo-electron microscopy (cryoEM) structure of the SARS-CoV-2 replication transcription complex (RTC) components nsp7, nsp8 and nsp12, bound to more than two turns of RNA template-product duplex, indicates that the active cleft of nsp12 binds to the first turn of RNA, while two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged "sliding poles". These sliding poles may confer processivity to the RTC (Hillen et al. 2020). Binding of nsp12 to the template RNA is markedly increased by the presence of nsp7 and nsp8 (Yin et al. 2020). Notable structural rearrangements occur in nsp12, nsp8 and nsp7 to accommodate the RNA (Wang et al. 2020).

Based on studies in SARS-CoV-1, the RTC binds to the 3' end of the viral plus strand genomic RNA to initiate synthesis of the complementary minus strand. A 36 nucleotide sequence from the 3’-UTR of the plus strand, predicted to form a stable stem-loop structure, seems to be the minimal cis-acting RNA element required for the viral RNA-directed RNA polymerase (nsp12) to initiate RNA synthesis. The polyA tail also seems to play a role in the initiation of replication of viral genomic RNA (Ahn et al. 2012).
R-HSA-9694455 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Binding of the genomic RNA to one or a small number of N-N dimers may be the initiating event in nucleocapsid formation. Both the NTD and the CTD of N have been shown to have RNA-binding activity (Huang et al, 2004a; Huang et al, 2004b; Chen et al, 2007; Chang et al, 2009; Takeda et al, 2008), and the IDRs seem likely to also contribute (Chang et al, 2009). These initial binding events may nucleate nucleocapsid formation through further recruitment of N protein dimers (reviewed in Chang et al, 2014).
R-HSA-9694463 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

N protein is sumoylated at a lysine residue. Abolition of sumoylation of nucleoprotein significantly decreases homo-oligomerisation of the protein (Li et al, 2005)
R-HSA-9694467 (Reactome) The SARS-Cov spike protein forms a homotrimer, both in solution and on membranes (Herrera et al, 2020).
R-HSA-9694471 (Reactome) SARS-CoV-2 plus strand genomic RNA (gRNA), like genomic RNAs of SARS-CoV-1 and other coronaviruses, is polyadenylated. The poly(A) tail of gRNA is longer than the poly(A) tail of subgenomic SARS-CoV-2 RNAs (Kim et al. 2020). Coronavirus plus strand gRNAs possess a polyadenylation signal in their 3'UTR and are polyadenylated by an undetermined viral RNA polymerase, possibly nsp8 or nsp12 (Spagnolo and Hogue 2000, Peng et al. 2016, Tvarogova et al. 2019).
R-HSA-9694476 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The genomic and subgenomic (sg) mRNAs of SARS-CoV-1 coronavirus are presumed to be capped at their 5′ end, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). Non-structural protein 14 (nsp14) acts as an RNA guanine-N7-methyltransferase (N7-MTase) that completes the synthesis of the cap-0 on SARS-CoV-1 mRNAs. The cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage, and is also known as m7G cap or m7Gppp cap. The N7-MTase domain maps to the carboxy-terminal part of nsp14 (Chen et al. 2009). Cap-0 formation requires three sequential reactions catalyzed by RNA triphosphatase (TPase), guanylyltransferase (GTase), and N7-MTase. There is no evidence that nsp14 possesses TPase and GTase activities, and no other SARS-CoV-1 proteins with these activities have been identified, so the identities of the enzymes that mediate these required steps remain unknown. Based on the study of the human coronavirus 229E, non-structural protein 13 (nsp13) may have a TPase activity in addition to its established helicase activity (Ivanov and Ziebuhr 2004).
R-HSA-9694487 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Despite its importance, expression of M alone is not sufficient to drive formation of a mature virus (reviewed in Masters, 2006). Protein-protein interactions between M and S, N and E, among other components, are required for assembly of a mature virus and for membrane curvature. Many studies have examined the minimal system required for release of viral like particles (VLPs) with sometimes contradictory results, but interactions between M, N and E are sufficient to promote release of significant numbers of VLPs (Ho et al, 2004; Huang et al, 2004; Mortola and Roy, 2004; Hsieh et al, 2005; Siu et al, 2008; Hatakeyama et al, 2008; Tseng et al, 2013; reviewed in Masters, 2006)
R-HSA-9694492 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The genomic and subgenomic mRNAs of SARS-CoV-1 coronavirus, including the minus strand genomic RNA complement, are presumed to be capped at their 5′ end, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). The non-structural protein 14 (nsp14) acts as an RNA guanine-N7-methyltransferase (N7-MTase) that completes the synthesis of the cap-0 on SARS-CoV-1 minus strand genomic RNA. The cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage, and is also known as m7G cap or m7Gppp cap. The N7-MTase domain maps to the carboxy-terminal part of nsp14 (Chen et al. 2009). Cap-0 formation requires three sequential reactions catalyzed by RNA triphosphatase (TPase), guanylyltransferase (GTase), and N7-MTase. There is no evidence that nsp14 possesses TPase and GTase activities, and no other SARS-CoV-1 proteins with these activities have been identified, so the identities of the enzymes that mediate these required steps remain unknown. Based on the study of the human coronavirus 229E, non-structural protein 13 (nsp13) may have a TPase activity in addition to its established helicase activity (Ivanov and Ziebuhr 2004).
R-HSA-9694495 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

After synthesizing the complementary minus RNA of the plus strand viral genomic RNA, SARS-CoV-1 replication-transcription complex (RTC) associates with the minus strand to initiate plus strand synthesis and to initiate transcription of subgenomic (sg) mRNAs (Ahn et al. 2012).
R-HSA-9694499 (Reactome) The function of the non-structural protein nsp16 as a 2'O-methyltransferase that acts in complex with its co-activator nsp10 is conserved in SARS-CoV-2 (Viswanathan et al. 2020).

The subgenomic mRNAs of SARS-CoV-2 coronavirus are presumed to be capped at their 5′ ends, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). The non-structural protein 16 (nsp16) acts as a 2'O-methyltransferase that converts coronavirus cap-0 to cap-1, which was first demonstrated with nsp16 cloned from the feline coronavirus (FCV) (Decroly et al. 2008). Cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage (also known as m7G cap or m7Gppp cap). Cap-1 is generated by an additional methylation on the 2′O position of the initiating nucleotide, and is also known as m7GpppNm. The non-structural protein 10 (nsp10) acts as an activator of nsp16 and is necessary for cap-1 synthesis (Bouvet et al. 2010, Decroly et al. 2011). Coronavirus RNAs with cap-1 are protected from IFIT-mediated interferon response, as IFITs recognize unmethylated 2'-O RNAs. IFITs are interferon-induced proteins with tetratricopeptide repeats that recognize unmethylated 2'-O RNAs and act to inhibit expression of virally encoded mRNAs (Menachery et al. 2014).
R-HSA-9694506 (Reactome) SARS-CoV-2 produces nine subgenomic RNAs (sgRNAs). N protein-encoding mRNA (mRNA9) is most abundantly expressed, followed by mRNAs encoding proteins S (mRNA2), 7a (mRNA7a), 3a (mRNA3), 8 (mRNA8), M (mRNA5), E (mRNA4), 6 (mRNA6) and 7b (mRNA7b) (Kim et al. 2020).

SARS-CoV-1 encodes eight subgenomic RNAs, mRNA2 to mRNA9. mRNA1 corresponds to the genomic RNA. mRNA2 encodes the S protein. mRNA3 is bicistronic and encodes proteins 3a and 3b. mRNA4 encodes the E protein. mRNA5 encodes the M protein. mRNA6 encodes the protein 6. mRNA7, mRNA8 and mRNA9 are bicistronic, with mRNA7 encoding proteins 7a and 7b, mRNA8 encoding proteins 8a and 8b, and mRNA 9 encoding proteins 9a and N. The 5' and 3' ends of subgenomic RNAs are identical, in accordance with the template switch model of coronavirus RNA transcription (Snijder et al. 2003, Thiel et al. 2003, Yount et al. 2003). Based on studies of the murine hepatitis virus (MHV), which is closely related to SARS-CoV-1, positive-sense virus mRNAs are present at much higher amounts than negative-sense mRNAs (Irigoyen et al. 2016).
R-HSA-9694520 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Human von Hippel Lindau (VHL) protein, a tumor suppressor that acts as a component of an E3 ubiquitin ligase complex, interacts with the non-structural protein 16 (nsp16) of the human SARS coronavirus 1 (SARS-CoV-1) and the mouse hepatitis virus, also a coronavirus. VHL negatively regulates SARS-CoV-1 replication, but the exact mechanism is not known (Yu et al. 2015).
R-HSA-9694521 (Reactome) The function of the non-structural protein nsp16 as a 2'O-methyltransferase that acts in complex with its co-activator nsp10 is conserved in SARS-CoV-2 (Viswanathan et al. 2020).

The genomic and subgenomic mRNAs of SARS-CoV-2 coronavirus, including the minus strand genomic RNA, are presumed to be capped at their 5′ end, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). Non-structural protein 16 (nsp16) acts as a 2'O-methyltransferase that converts coronavirus cap-0 to cap-1, which was first demonstrated with nsp16 cloned from the feline coronavirus (FCV) (Decroly et al. 2008). Cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage (also known as m7G cap or m7Gppp cap). Cap-1 is generated by an additional methylation on the 2′O position of the initiating nucleotide, and is also known as m7GpppNm. Non-structural protein 10 (nsp10) acts as an activator of nsp16 and is necessary for cap-1 synthesis (Bouvet et al. 2010, Decroly et al. 2011). Coronavirus RNAs with cap-1 are protected from IFIT-mediated interferon response. IFITs are interferon-induced proteins with tetratricopeptide repeats that recognize unmethylated 2'-O RNAs and act to inhibit expression of virally encoded mRNAs (Menachery et al. 2014).
R-HSA-9694524 (Reactome) nsp13, which functions as the viral helicase, is as a part of the SARS coronavirus 2 (SARS-CoV-2) replication-transcription complex (RTC). Two molecules of SARS-CoV-2 nsp13 are found in the RTC complex. N-terminal domains of each nsp13 interact with N-terminal extensions of each copy of nsp8, while nsp13 molecule interacts with the thumb region of nsp12, the viral RNA-dependent RNA polymerase. One nsp13 molecule of SARS-CoV-2 is tightly bound to the RTC, while the other nsp13 molecule is dissociable (Chen et al. 2020). In SARS-CoV-1, nsp13 has been reported to directly interact with nsp12, and nsp12 was shown to increase the helicase activity of nsp13 (von Brunn et al. 2007, Adedeji et al. 2012, Jia et al. 2019).
R-HSA-9694525 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein M is exclusively N-glycosylated at one asparagine by an unknown glycosyltransferase. However, further processing of N-linked glycans is prevented in infected cells. Both the glycosylated and nonglycosylated M is incorporated into the virion. In summary, glycosylation of M is neither a prerequisite for intra-cellular transport nor for recruitment into the virion (Voss et al, 2006).
R-HSA-9694528 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

In addition to the main structural proteins and the nucleocapsid, the mature virion may also contain low proportions of accessory proteins, including protein 3a and 7a (reviewed in McBride and Fielding, 2012). Protein 3a has been shown to interact with E, M, S and protein 7a and is estimated to be present in the virion at 2/3 the molar ratio of E protein (Ito et al, 2005; Shen et al, 2005; Tan et al, 2004). Although 3a tetramers are predicted to act as ion channels in the host plasma membrane, increasing cell permeability, the role of 3a in the mature virion is not clear (Lu et al, 2006; reviewed in McBride and Fielding, 2012). Protein 7a is type 1 transmembrane protein that interacts with M, E, S and protein 3a and may be incorporated into the mature virion. What functional role protein 7a may play in the assembled virion is unclear (Huang et al, 2006; Fielding et al, 2004; Tan et al, 2004).
R-HSA-9694529 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Viral E protein is ubiquitinated both in vitro and in cells (Alvarez et al, 2011).
R-HSA-9694539 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Nonstructural protein 15 (nsp15) of the SARS coronavirus (SARS-CoV-1) binds to the replication-transcription complex (RTC) through interaction with nsp8 (Imbert et al. 2008). This interaction appears to be conserved in other coronaviruses, such as mouse hepatitis virus (MHV) (Athmer et al. 2017). nsp15 is an endonuclease characteristic for the order Nidovirales that includes the family Coronaviridae. nsp15 preferentially cleaves 3' of uridines, generating 2'-3' cyclic phosphates after cleavage. nsp15 requires Mn2+ ions for catalytic activity. Functional nsp15 is needed for production of viable virions and for viral transcription (Guarino et al. 2005, Ricagno et al. 2006, Bhardwaj et al. 2006, Joseph et al. 2007, Bhardwaj et al. 2008, Bhardwaj et al. 2012). The biological role of nsp15 has not been elucidated. It may degrade host mRNAs to shut down host translation, but so far no human or viral RNA targets have been identified.
R-HSA-9694541 (Reactome) Remdesivir (GS-5734) is an investigational nucleotide analogue drug that was developed for its broad spectrum antiviral potential against Ebola and Marburg virus activity (Siegel et al. 2017). It targets and inhibitis viral RNA-dependent RNA polymerase (nsp12, RdRP), the key component of the replication transcription complex (RTC) (Agostini et al. 2018, Brown et al. 2019, Gordon et al. 2020). Remdesivir is being investigated for potential antiviral activity against SARS-CoV-2 by targeting viral replication (Agostini et al. 2018). Gordon et al. demonstrate remdesivir possesses broad antiviral activity against RNA viruses, including SARS-CoV, MERS-CoV and SARS-CoV-2 in-vitro (Gordon et al. 2020b). It could prevent asymptomatic, mild or moderate COVID-19 cases from progressing to severe disease (clinical trials NCT04252664, NCT04257656) but results so far in infected people have been mixed.

EIDD-2801, is an isopropylester prodrug of the ribonucleoside analogue N4-hydroxycytidine (NHC, EIDD-1931) that shows broad spectrum antiviral activity against various RNA viruses including Ebola, Influenza and CoV (Toots et al. 2019). NHC acts as a competitive alternative substrate for virally encoded RNA-dependent RNA polymerases. NHC was shown to inhibit multiple genetically-distinct Bat-CoV viruses in human primary epithelial cells without affecting cell viability. Prophylactic/therapeutic oral administration of NHC reduced lung titers and prevented acute lung failure in C57B/6 mice infected with CoV. The potency of NHC against multiple coronaviruses, its therapeutic efficacy, and oral bioavailability in vivo, all highlight its potential as an effective antiviral against SARS-CoV-2 and other future zoonotic coronaviruses (Sheahan et al. 2020).
R-HSA-9694542 (Reactome) The interaction between nsp10 and nsp14 is conserved in SARS-CoV-2 virus (Li et al. 2020). In SARS-CoV-1, nsp10 was shown to form a stable complex with nsp14 (Bouvet et al. 2012) and serve as a co-factor for nsp14, stimulating its 3'->5' exonuclease activity (Bouvet et al. 2012, Subissi et al. 2014, Bouvet et al. 2014).
R-HSA-9694549 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The replication-transcription complex (RTC) completes synthesis of the genomic RNA complement (minus strand). The complex of nsp7 and nsp8 confers processivity to nsp12, the virally encoded RNA-dependent RNA polymerase that replicates the viral genomic RNA, enabling the RTC to complete the RNA synthesis with a very low dissociation rate. nsp7 plays a crucial role in maintaining binding of the RTC to the RNA. nsp14 subunit of the RTC does not affect the processivity (Subissi et al. 2014).
R-HSA-9694551 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Main protease cleaves all cleavage sites of pp1a and ppa1b starting with nsp4/5, thus cleaving itself, and all the cytosolic RTC proteins (Fan et al, 2004)
R-HSA-9694553 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Based on studies in other coronaviruses, SARS-COV-2 S trimers are presumed to be recruited to the assembling virion through interaction with M protein (reviewed in Ujike and Taguchi, 2015). Multiple regions of M contribute to the recruitment of S, with a single tyrosine residue in the C-terminal domain of M playing a critical role (McBride et al, 2010a; Hsieh et al, 2008). Interaction with M is aided by a dibasic motif in the C-terminus of S, which promotes retrieval of the spike protein from the cell surface by binding the COPI coat (McBride et al, 2007; Ujike et al, 2016). Palmitoylation of the C-terminus of S appears dispensible for the interaction with M in SARS-COV-1, unlike the case in other coronaviruses; whether this is also true for SARS-COV-2 remains to be determined (Ujike et al, 2012; McBride 2010b; reviewed in Ujike and Taguchi, 2015). Size estimates and modelling suggest the mature virion has approximately 300 S trimers (Neuman et al, 2006; reviewed in Chang et al, 2014).
R-HSA-9694555 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein M accumulates in the Golgi complex and recruits Spike protein to the sites of virus assembly and budding in the ERGIC (Voss et al, 2009).
R-HSA-9694567 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

In the host cell cytosol the pp1a polyprotein spontaneously dimerizes. This temporary dimer has weak protease activity (Chen et al, 2010)
R-HSA-9694568 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

As early as 3 hours post-infection, cytoplasmic accumulations of N are formed in infected cells, they colocalize with viral RNA. From 5 hours post-infection on, N can be detected in the Golgi, the budding site (Stertz et al, 2007)
R-HSA-9694572 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

As it contains cargo sorting motifs in its cytoplasmic domain, protein 3a gets localized by the cell's protein transport system to the cell membrane where it functions as an ion channel (Tan et al, 2004). This ion channel function is necessary for the protein's pro-apoptotic function (Chan et al, 2009)
R-HSA-9694575 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Some phosphorylated N is found to associate with the cell membrane (Surjit et al, 2005).
R-HSA-9694576 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

On the final assembly, proteomics data suggest that the NAB−βSM−TM1 domains of nsp3 can interact with nsp7 − 8, as well as nsps 12–16, and the domain Y1 plus CoV-Y interacts with nsp9 and nsp12 (Imbert et al., 2008). Also a PL2pro−NAB−βSM−TM1 construct of Nsp3 can bind Nsp4 and Nsp12, while the region from TM1 to the end of Nsp3 only binds Nsp8 (Pan et al., 2008).
R-HSA-9694579 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

SARS-CoV-2 spike (S3a) protein, as a component of the S3:M:E:encapsidated SARS coronavirus genomic RNA: 7a:O-glycosyl 3a tetramer complex, binds to glycosylated angiotensin converting enzyme 2 (ACE2) associated with the human host cell plasma membrane. Structural studies of the interaction between human ACE2 protein and the receptor-binding domain of S3a protein have identified key amino acid residues in both proteins responsible for their high-affinity interaction. These residues may be a key factor determining severity (and possibly human-to-human transmission) of SARS-CoV-2 (Li et al. 2003, 2005). The roles of S protein in viral binding to the host cell membrane and fusion of viral and host cell membranes and thus the central role of S protein in determining the host range and tissue tropisms of the virus are reviewed by Belouzard et al. (2012).
R-HSA-9694580 (Reactome) This COVID‑19 event has been created by a combination of computational inference from SARS-CoV-1 data (https://reactome.org/documentation/inferred-events) and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The replicase polyprotein 1a of the human severe acute respiratory syndrome coronavirus is post-translationally cleaved by virally encoded proteases to generate non-structural proteins (nsps). Viral nsps induce the formation of ER-bound double membrane vesicles (DMV) in host cells post infection. These DMVs are decorated with host microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) proteins that are involved in autophagosome formation. However, there is no evidence that DMVs are recruited to the autophagy machinery. Immunofluorescence studies show that nsp8 colocalizes with MAP1LC3B suggesting a binding event (Prentice E. et al 2004).
R-HSA-9694581 (Reactome) After synthesizing the complementary minus RNA of the plus strand viral genomic RNA, virally encoded RNA-dependent RNA polymerase (nsp12, also known as RdRP) uses the minus strand as a template to generate viral genomic RNA that can be packaged into virions. SARS-CoV-2-derived nsp12, in complex with nsp7 and nsp8, was shown to have RNA polymerization activity on a poly-U template (Yin et al. 2020). Details of SARS-CoV-2 replication have not yet been elucidated and are inferred from SARS-CoV-1. Purified SARS-CoV-1 nsp12 shows both primer dependent and primer-independent RNA synthesis activity in vitro. nsp12 is able to initiate RNA synthesis with as little as 37 nucleotides of RNA from the 3’ end of the minus strand viral RNA (complementary to the 5’-UTR of the plus strand genomic RNA - c5’-UTR). Similar to the 3'-UTR of the plus strand, the 3' end of the minus strand (c5’-UTR) is predicted to form a stable stem-loop structure and seems to be the minimal cis-acting RNA element required for nsp12 to initiate RNA synthesis using the minus strand as a template (Ahn et al. 2012). It is unclear if replication of the minus strand is primer-dependent. The complex of nsp7 and nsp8 confers processivity to nsp12 (Subissi et al. 2014).
R-HSA-9694592 (Reactome) The rep proteases that are essential for viral polyprotein processing by the coronaviruses and enteroviruses exhibit a strong preference for substrates containing Gln at P1 position, and share an active-site conformation that engages the substrate's P1 residue. Compound 11r and compound 13b are peptidomimetic α-ketoamides that function as high-affinity non-cleavable substrate analogues and thus exhibit antiviral activity against dimeric 3C-like proteinases (C3Lp dimer) of coronaviruses and enteroviruses (Chen et al. 2005, Zhang et al. 2020). The clinical safety and efficacy of α-ketoamides in Covid-19 are under investigation.
R-HSA-9694601 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

To process the nsp3/4 cleavage site, PL-PRO and, presumably, nsp3-4 need to be glycosylated and localized to a membrane (Harcourt et al, 2004).
R-HSA-9694605 (Reactome) Virally encoded RNA-dependent RNA polymerase (nsp12, also known as RdRP) is the key component of the replication transcription complex (RTC). SARS-CoV-2-derived nsp12, in complex with nsp7 and nsp8, was shown to have RNA polymerization activity on a poly-U template (Yin et al. 2020). Details of SARS-CoV-2 replication have not yet been elucidated and are inferred from SARS-CoV-1. As SARS-CoV-2 and SARS-CoV-1 are plus strand RNA viruses, nsp12 first synthesizes the complementary minus RNA strand. The purified SARS-CoV-1 nsp12 shows both primer dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. The catalytic activity of nsp12 is strictly dependent on manganese ions (Mn2+) and primers when the template is a viral-genome-derived RNA representing part of the 3’-UTR of the plus strand with a polyA tail. A 36 nucleotide sequence from the 3’-UTR, predicted to form a stable stem-loop structure, seems to be the minimal cis-acting RNA element required for nsp12 to initiate RNA synthesis (Ahn et al. 2012). The complex of nsp7 and nsp8 confers processivity to nsp12 (Subissi et al. 2014).
R-HSA-9694611 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Part of nsp4 protein becomes N-glycosylated and gets recruited to the replication complexes in infected cells (Oostra et al, 2007).
R-HSA-9694620 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Human glycogen synthase kinases GSK3A and GSK3B phosphorylate SARS-CoV-1 coronavirus N (nucleocapsid) protein on multiple serine and threonine residues. GSK3-mediated phosphorylation of the N protein is needed for efficient replication of viral genomic RNA (Wu et al. 2009).
R-HSA-9694625 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Glycosylated nsp3 (papain-like protease) cleaves the N-proximal polyprotein regions at three sites (Thiel et al, 2003; Harcourt et al, 2004).
R-HSA-9694630 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The SARS-CoV nsp3 was shown to bind ORF7a and Nsp6 by using proteomics analysis (Neuman et al, 2008)
R-HSA-9694632 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

nsp14 acts as 3'-5' exonuclease (Minskaia et al. 2006, Chen et al. 2007) that preferentially excises mismatched nucleotides from double stranded RNA (Minskaia et al. 2006, Bouvet et al. 2012). Binding to nsp10 increases the exonuclease activity of nsp14 (Bouvet et al. 2012, Subissi et al. 2014, Bouvet et al. 2014). nsp14 increases the fidelity of human SARS coronavirus 1 (SARS-CoV-1) replication by the nsp12 RNA-dependent RNA polymerase by 21-fold (Eckerle et al. 2010).
R-HSA-9694633 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Interaction of the ribonucleocapsid and the structural proteins of SARS-COV-2 in the ERGIC membrane is presumed to promote the formation of virions by budding into to the ERGIC lumen, as is the case for other coronaviruses (reviewed in Masters, 2006). Coronavirus membrane curvature is driven by M lattice formation, interaction with the nucleocapsid and by E protein (de Haan et al, 1998; de Haan et al, 2000; Hsieh et al, 2005; Hsieh et al, 2008; reviewed in Masters, 2006; Ujike and Taguchi, 2015; Schoeman and Fielding 2019).
R-HSA-9694641 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Similar to other coronaviruses, SARS-CoV-2 virions are released from the host cell by exocytosis in smooth-walled vesicles (reviewed in Ujike and Taguchi, 2015; Masters, 2006; Fung and Liu, 2019). The nature and details of this export remain to be elucidated.
R-HSA-9694656 (Reactome) Of the 22 glycosylated asparagine residues on the Spike protein 14 are further processed to get complex N-glycan sidechains (Watanabe et al, 2020).
R-HSA-9694661 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Transmembrane protease serine 2 (TMPRSS2), associated with the plasma membrane of the host cell, mediates the hydrolytic cleavage of SARS-CoV-2 Spike (S) protein component of the viral membrane-associate S3:M:E:encapsidated SARS coronavirus genomic RNA: 7a:O-glycosyl 3a tetramer complex associated with ACE2 (Matsuyama et al. 2010; Glowacka et al. 2011; Shulla et al. 2011).
R-HSA-9694662 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein 3a can form homodimers and tetramers. The homotetramer shows typical patterns of ion channels. Transport of potassium ions through this channel is effective (Lu et al, 2006). Potassium efflux by protein 3a is important for 3a-induced NLRP3 inflammasome activation (Chen et al, 2019)
R-HSA-9694665 (Reactome) Remdesivir (GS-5734) is an investigational nucleotide analogue drug that was developed for its broad spectrum antiviral potential against Ebola and Marburg virus activity (Siegel et al. 2017). It targets and inhibitis viral RNA-dependent RNA polymerase (nsp12, RdRP), the key component of the replication transcription complex (RTC) (Agostini et al. 2018, Brown et al. 2019, Gordon et al. 2020). Remdesivir is being investigated for potential antiviral activity against SARS-CoV-2 by targeting viral replication (Agostini et al. 2018). Gordon et al. demonstrate remdesivir possesses broad antiviral activity against RNA viruses, including SARS-CoV, MERS-CoV and SARS-CoV-2 in-vitro (Gordon et al. 2020b). It could prevent asymptomatic, mild or moderate Covid-19 cases from progressing to severe disease (clinical trials NCT04252664, NCT04257656) but results so far in infected people have been mixed.

EIDD-2801, is an isopropylester prodrug of the ribonucleoside analogue N4-hydroxycytidine (NHC, EIDD-1931) that shows broad spectrum antiviral activity against various RNA viruses including Ebola, Influenza and CoV (Toots et al. 2019). NHC acts as a competitive alternative substrate for virally encoded RNA-dependent RNA polymerases. NHC was shown to inhibit multiple genetically-distinct Bat-CoV viruses in human primary epithelial cells without affecting cell viability. Prophylactic/therapeutic oral administration of NHC reduced lung titers and prevented acute lung failure in C57B/6 mice infected with CoV. The potency of NHC against multiple coronaviruses, its therapeutic efficacy, and oral bioavailability in vivo, all highlight its potential as an effective antiviral against SARS-CoV-2 and other future zoonotic coronaviruses (Sheahan et al. 2020).
R-HSA-9694677 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Human zinc finger CCHC-type and RNA-binding motif-containing protein 1 (ZCRB1, also known as MADP1) binds to the 5'UTR of the plus strand genomic RNA of the SARS-CoV-1, as well as other coronaviruses, infectious bronchitis virus (IBV) and human coronavirus OC43. ZCRB1 normally localizes to the nucleus, where it is a component of the U12-type spliceosome. Upon infection with a coronavirus, ZCRB1 appears in the cytosol. Binding of ZCRB1 to the 5'UTR stem of coronavirus genomic RNA is thought to be necessary for efficient transcription of viral genes (Tan et al. 2012).
R-HSA-9694681 (Reactome) SARS-CoV-2 mRNA5 has a length of 669 nt and encodes the 222 aa M protein (Wu et al, 2020).
R-HSA-9694689 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The SARS-CoV-2 nucleocapsid is released from the host cell endosome into the cytosol. Molecular details of this step are not well worked out. Studies of the infection of the human cultured cells with HCoV-229E coronavirus established a requirement for VCP (transitional endoplasmic reticulum ATPase) protein function for release to occur (Wong et al. 2015). A similar requirement for VCP involvement in SARS-CoV-2 nucleocapsid release is inferred here.
R-HSA-9694718 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

A sialyltransferase adds a terminal sialic acid moiety to protein 3a with an O-linked glycosyl side chain. This glycosylated form later is associated with the virion (Oostra et al, 2006)
R-HSA-9694721 (Reactome) The function of the non-structural protein nsp16 as a 2'O-methyltransferase that acts in complex with its co-activator nsp10 is conserved in SARS-CoV-2 (Viswanathan et al. 2020).

The genomic and subgenomic mRNAs of SARS-CoV-2 coronavirus, including the plus strand genomic RNA, are presumed to be capped at their 5′ end, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). The non-structural protein 16 (nsp16) acts as a 2'O-methyltransferase that converts coronavirus cap-0 to cap-1, which was first demonstrated with nsp16 cloned from the feline coronavirus (FCV) (Decroly et al. 2008). Cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage (also known as m7G cap or m7Gppp cap). Cap-1 is generated by an additional methylation on the 2′O position of the initiating nucleotide, and is also known as m7GpppNm. Non-structural protein 10 (nsp10) acts as an activator of nsp16 and is necessary for cap-1 synthesis (Bouvet et al. 2010, Decroly et al. 2011). Coronavirus RNAs with cap-1 are protected from IFIT-mediated interferon response, as IFITs recognize unmethylated 2'-O RNAs. IFITs are interferon-induced proteins with tetratricopeptide repeats that recognize unmethylated 2'-O RNAs and act to inhibit expression of virally encoded mRNAs (Menachery et al. 2014).
R-HSA-9694723 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The viral nucleocapsid complex, released into the host cell cytosol, dissociates to release the viral RNA genome (Fung & Liu 2019).
R-HSA-9694727 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Protein 3a is rapidly internalized into cells by endocytosis. It contains a Yxxφ motif and also diacidic motifs which are typically found in internalized membrane proteins (Tan et al, 2004). The ability to be internalized is necessary for the protein's pro-apoptotic function (Wong et al, 2006; Chan et al, 2009)
R-HSA-9694732 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Main protease cleaves all cleavage sites of pp1a and ppa1b starting with nsp4/5, thus cleaving itself, and all the cytosolic RTC proteins (Fan et al, 2004)
R-HSA-9694733 (Reactome) SARS-CoV-2 transcripts are polyadenylated (Ravindra et al. 2020, Kim et al. 2020), similar to their SARS-CoV-1 counterparts. SARS-CoV-2 subgenomic RNAs (sgRNAs) carry poly(A) tails of the meadian lenght of 47 nucleotides. The poly(A) tails of sgRNAs of SARS-CoV-2 are shorter than the poly(A) tails of the full-length SARS-CoV-2 genomic RNA (Kim et al. 2020).

SARS-CoV-1 plus strand sgRNAs share a 3'UTR with the plus strand genomic RNA, and as this 3'UTR possesses a polyadenylation signal, they undergo polyadenylation by an undetermined viral RNA polymerase, possibly nsp8 or nsp12 (Spagnolo and Hogue 2000, Peng et al. 2016, Tvarogova et al. 2019).
R-HSA-9694737 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The genomic and subgenomic mRNAs of SARS-CoV-1 coronavirus, including the plus strand genomic RNA, are presumed to be capped at their 5′ end, based on studies of the mouse hepatitis virus (MHV) (Lai and Stohlman 1981) and the equine torovirus (van Vliet et al. 2002). Non-structural protein 14 (nsp14) acts as an RNA guanine-N7-methyltransferase (N7-MTase) that completes the synthesis of the cap-0 on the SARS-CoV-1 plus strand genomic RNA. Cap-0 represents N7-methyl guanosine connected to the 5′ nucleotide through a 5′ to 5′ triphosphate linkage, and is also known as m7G cap or m7Gppp cap. The N7-MTase domain maps to the carboxy-terminal part of nsp14 (Chen et al. 2009). Cap-0 formation requires three sequential reactions catalyzed by RNA triphosphatase (TPase), guanylyltransferase (GTase), and N7-MTase. There is no evidence that nsp14 possesses TPase and GTase activities, and no other SARS-CoV-1 proteins with these activities have been identified, so the identities of the enzymes that mediate these required steps remain unknown. Based on the study of the human coronavirus 229E, non-structural protein 13 (nsp13) may have a TPase activity in addition to its established helicase activity (Ivanov and Ziebuhr 2004).
R-HSA-9694773 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Nucleoprotein (N) is ADP-ribosylated. The modification is maintained both in the cell and in virions (Grunewald et al, 2018). Members of the protein mono-ADP-ribosyltransferase (PARP) enzyme family are thought to catalyze this reaction (Fehr et al. 2020)
R-HSA-9694780 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

Trimmed palmitoylated Spike protein trimers become associated with the ERGIC (ER-Golgi Intermediate Compartment) (Fung & Liu 2019)
R-HSA-9694790 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

A minor proportion of the E protein is modified by N-linked glycosylation. This variant appears to be more likely to form multimers, and it shows a different membrane topology than the main variant (Yuan et al, 2006).
R-HSA-9694792 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

In the presence of functional nsp14, which acts as a 3'-to-5' exonuclease, the mutation rate during human SARS coronavirus 1 (SARS-CoV-1) replication is 9 x 10^-7 (9E-7) per nucleotide per replication cycle or 2.2 x 10^-5 (2.2E-5) non-redundant substitutions per nucleotide, which translates into 2-3 nucleotide substitutions for each replicated SARS-CoV-1 genome. When nsp14 is defective, the mutation rate during SARS-CoV-1 replication increases to 1.2 x 10^-5 (1.2E-5) mutations per nucleotide per replication cycle or 3.34 x 10^-4 (3.34E-4) non-redundant substitutions per nucleotide, which translates into 12-23 nucleotide substitutions for each replicated SARS-CoV-1 genome (Eckerle et al. 2010). Here the process is annotated in two steps, nsp12- mediated misincorporation of a base (this reaction) and nsp14-mediated detection and removal of that base (next reaction).
R-HSA-9694793 (Reactome) Glycosyltransferases in the endoplasmatic reticulum are responsible for the attachment of numerous high-mannose N-glycans on the SARS-CoV-2 spike protein. After virion assembly and release these glycosidations are required for fusion with host cells (Watanabe et al, 2020, Breuer et al, 2001).
R-HSA-9694794 (Reactome) SARS-CoV-2 mRNA3 has a length of 828 nt and encodes the 275 aa protein 3a (Wu et al, 2020).
R-HSA-9696807 (Reactome) Except for position 234, all Man(9)-N-glycan modifications on SARS-Cov-2 Spike are further trimmed to yield high-mannose N-glycan groups containing 5-8 mannose sugars. This reaction is mainly catalyzed by human MAN1B1 glycosdase (Watanabe et al, 2020; Avezov et al, 2008).
R-HSA-9696980 (Reactome) Nearly all di-antennary N-glycan sidechains of Spike get further extended to tri-antennary configuration by addition of fucose and further N-acetylglucosamine moieties. Asn-1158 is probably an exception, it stays di-antennary (Watanabe et al, 2020).
R-HSA-9697018 (Reactome) Glycosyl sidechains at Asn-1158 and Asn-1194 are sialylated, presumably by the cell's sialyltransferases (Watanabe et al, 2020).
R-HSA-9697423 (Reactome) Based on SARS-CoV-1 experiments, SARS-CoV-2 virions attached to the host cell surface via a complex involving viral spike (S) protein and host angiotensin-converting enzyme 2 (ACE2) are inferred to undergo endocytosis. In the case of SARS-CoV-1, studies with pseudoviruses have established that S protein is necessary and sufficient for mediating viral attachment and entry. Inhibition of this SARS-CoV-1 S protein-mediated transduction by two different classes of lysosomotropic agents in multiple cell lines strongly suggests that acidification of endosomes is needed for viral entry (Hofmann et al. 2004; Simmons et al. 2004; Yang et al. 2004). The roles of S protein in viral binding to the host cell membrane and fusion of viral and host cell membranes and thus the central role of S protein in determining the host range and tissue tropisms of the virus are reviewed by Belouzard et al. (2012).
R-HSA-9698265 (Reactome) This COVID‑19 event has been created by a combination of computational inference from SARS-CoV-1 data (https://reactome.org/documentation/inferred-events) and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

The replicase polyprotein 1a of the human severe acute respiratory syndrome coronavirus (SARS-CoV) is post-translationally cleaved by virally encoded proteases to generate non-structural proteins (nsps). Viral nsps induce the formation of ER-bound double membrane vesicles (DMV) in host cells post infection. These DMVs are decorated with microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) proteins that are involved in autophagosome formation. However, there is no evidence that DMVs are recruited to the autophagy machinery. Immunofluorescence studies show that nsp6 (Cottam E M. et al 2011) and nsp8 (Prentice E. et al 2004) colocalizes with MAP1LC3B suggesting a binding event. In some cell types, expression of sars9b (9b) triggers the formation of autophagosomes and underlying molecular mechanisms are unclear (Shi C S. et al 2014). Studies also show that sars8b (8b) can trigger cellular stress, which results in a calcineurin dependent Transcription Factor EB (TFEB) activation and its target genes. This leads to an increase in autophagic flux (Shi C S. et al 2019).
R-HSA-9698988 (Reactome) SARS-CoV-2 virions attached to the host cell surface via a complex involving viral spike (S) protein and host angiotensin-converting enzyme 2 (ACE2) are inferred to undergo endocytosis. In the case of SARE-CoV-2 it is apparent that the spike protein undergoes cleavage in some cases and fuses directly with the plasma membrane. This cleavage is induced by FURIN or TMPRSS.


The cellular protease furin cleaves the spike protein at the S1/S2 site and that cleavage is essential for S-protein-mediated cell-cell fusion and entry into human lung cells (Hoffman et al. 2020).
Transmembrane protease serine 2 (TMPRSS2), associated with the plasma membrane of the host cell, mediates the hydrolytic cleavage of SARS-CoV-2 Spike (S) protein component of the viral membrane-associate S3:M:E:encapsidated SARS coronavirus genomic RNA: 7a:O-glycosyl 3a tetramer complex associated with ACE2 (Matsuyama et al. 2010; Glowacka et al. 2011; Shulla et al. 2011).

The uncoated virion nucleocapsid is released directly into the cytoplasm.
R-HSA-9699007 (Reactome) This COVID-19 event has been created by a combination of computational inference (see https://reactome.org/documentation/inferred-events) from SARS-CoV-1 data and manual curation, as described in the summation for the overall SARS-CoV-2 infection pathway.

the cellular protease furin cleaves the spike protein at the S1/S2 site and that cleavage is essential for S-protein-mediated cell-cell fusion and entry into human lung cells (Hoffman et al. 2020). Furin is associated with the plasma membrane of the host cell, mediates the hydrolytic cleavage of SARS-CoV-2 Spike (S) protein component of the viral membrane-associate S3:M:E:encapsidated SARS coronavirus genomic RNA: 7a:O-glycosyl 3a tetramer complex associated with ACE2.
RB1R-HSA-9694390 (Reactome)
RTC inhibitorsR-HSA-9694419 (Reactome)
RTC inhibitorsR-HSA-9694541 (Reactome)
RTC inhibitorsR-HSA-9694665 (Reactome)
RTCArrowR-HSA-9694549 (Reactome)
RTCArrowR-HSA-9694576 (Reactome)
RTCArrowR-HSA-9694581 (Reactome)
RTCR-HSA-9694454 (Reactome)
RTCR-HSA-9694495 (Reactome)
RTCmim-catalysisR-HSA-9694476 (Reactome)
RTCmim-catalysisR-HSA-9694492 (Reactome)
RTCmim-catalysisR-HSA-9694499 (Reactome)
RTCmim-catalysisR-HSA-9694506 (Reactome)
RTCmim-catalysisR-HSA-9694521 (Reactome)
RTCmim-catalysisR-HSA-9694721 (Reactome)
RTCmim-catalysisR-HSA-9694737 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694476 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694492 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694499 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694521 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694721 (Reactome)
S-adenosyl-L-homocysteineArrowR-HSA-9694737 (Reactome)
S-adenosyl-L-methionineR-HSA-9694476 (Reactome)
S-adenosyl-L-methionineR-HSA-9694492 (Reactome)
S-adenosyl-L-methionineR-HSA-9694499 (Reactome)
S-adenosyl-L-methionineR-HSA-9694521 (Reactome)
S-adenosyl-L-methionineR-HSA-9694721 (Reactome)
S-adenosyl-L-methionineR-HSA-9694737 (Reactome)
S1:S2:M lattice:E proteinArrowR-HSA-9698988 (Reactome)
S1:S2:M:E:

7a:O-glycosyl 3a

tetramer
ArrowR-HSA-9694689 (Reactome)
S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerArrowR-HSA-9694287 (Reactome)
S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerArrowR-HSA-9694661 (Reactome)
S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerArrowR-HSA-9699007 (Reactome)
S1:S2:M:E:encapsidated SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a tetramerR-HSA-9694689 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
ArrowR-HSA-9694579 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
R-HSA-9694661 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
R-HSA-9697423 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
R-HSA-9698988 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
R-HSA-9699007 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
ArrowR-HSA-9697423 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl 3a

tetramer:glycosylated-ACE2
R-HSA-9694287 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl

3a tetramer
ArrowR-HSA-9694633 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl

3a tetramer
ArrowR-HSA-9694641 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl

3a tetramer
R-HSA-9694579 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA: 7a:O-glycosyl

3a tetramer
R-HSA-9694641 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:7a:O-glycosyl

3a tetramer
ArrowR-HSA-9694528 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:7a:O-glycosyl

3a tetramer
R-HSA-9694633 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:O-glycosyl 3a

tetramer
ArrowR-HSA-9694553 (Reactome)
S3:M:E:encapsidated

SARS-CoV-2 genomic RNA:O-glycosyl 3a

tetramer
R-HSA-9694528 (Reactome)
SARS coronavirus

gRNA with secondary

structure:RTC
ArrowR-HSA-9694454 (Reactome)
SARS coronavirus

gRNA with secondary

structure:RTC
R-HSA-9694265 (Reactome)
SARS coronavirus

gRNA with secondary

structure:RTC
mim-catalysisR-HSA-9694265 (Reactome)
SARS coronavirus

gRNA:RTC:nascent RNA minus strand with mismatched

nucleotide
ArrowR-HSA-9694792 (Reactome)
SARS coronavirus

gRNA:RTC:nascent RNA minus strand with mismatched

nucleotide
R-HSA-9694632 (Reactome)
SARS coronavirus

gRNA:RTC:nascent RNA minus strand with mismatched

nucleotide
mim-catalysisR-HSA-9694632 (Reactome)
SARS-CoV-2

gRNA:RTC:RNA primer:RTC

inhibitors
ArrowR-HSA-9694541 (Reactome)
SARS-CoV-2

gRNA:RTC:RNA primer:RTC

inhibitors
TBarR-HSA-9694605 (Reactome)
SARS-CoV-2

gRNA:RTC:RNA primer:RTC

inhibitors
TBarR-HSA-9694792 (Reactome)
SARS-CoV-2 gRNA:RTC:RNA primerArrowR-HSA-9694277 (Reactome)
SARS-CoV-2 gRNA:RTC:RNA primerR-HSA-9694541 (Reactome)
SARS-CoV-2 gRNA:RTC:RNA primerR-HSA-9694605 (Reactome)
SARS-CoV-2 gRNA:RTC:RNA primermim-catalysisR-HSA-9694605 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent RNA minus strand:RTC

inhibitors
ArrowR-HSA-9694665 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent RNA minus strand:RTC

inhibitors
TBarR-HSA-9694549 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
ArrowR-HSA-9694605 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
ArrowR-HSA-9694632 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
R-HSA-9694549 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
R-HSA-9694665 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
R-HSA-9694792 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
mim-catalysisR-HSA-9694549 (Reactome)
SARS-CoV-2

gRNA:RTC:nascent

RNA minus strand
mim-catalysisR-HSA-9694792 (Reactome)
SARS-CoV-2 gRNA

complement (minus strand):RTC:RTC

inhibitors
ArrowR-HSA-9694419 (Reactome)
SARS-CoV-2 gRNA

complement (minus strand):RTC:RTC

inhibitors
TBarR-HSA-9694581 (Reactome)
SARS-CoV-2 gRNA

complement (minus

strand):RTC
ArrowR-HSA-9694495 (Reactome)
SARS-CoV-2 gRNA

complement (minus

strand):RTC
R-HSA-9694419 (Reactome)
SARS-CoV-2 gRNA

complement (minus

strand):RTC
R-HSA-9694581 (Reactome)
SARS-CoV-2 gRNA

complement (minus

strand):RTC
mim-catalysisR-HSA-9694581 (Reactome)
SARS-CoV-2 gRNA:RTCArrowR-HSA-9694265 (Reactome)
SARS-CoV-2 gRNA:RTCR-HSA-9694277 (Reactome)
SARS-CoV-2 gRNA:RTCR-HSA-9694344 (Reactome)
SARS-CoV-2 gRNA:RTCmim-catalysisR-HSA-9694277 (Reactome)
SARS-CoV-2 gRNA:RTCmim-catalysisR-HSA-9694344 (Reactome)
SARS-CoV-2 genomic RNA (plus strand)ArrowR-HSA-9694581 (Reactome)
SARS-CoV-2 genomic RNA (plus strand)R-HSA-9694737 (Reactome)
SARS-CoV-2 genomic

RNA complement

(minus strand)
ArrowR-HSA-9694549 (Reactome)
SARS-CoV-2 genomic

RNA complement

(minus strand)
R-HSA-9694492 (Reactome)
SARS-CoV-2 minus

strand subgenomic

mRNAs
ArrowR-HSA-9694344 (Reactome)
SARS-CoV-2 minus

strand subgenomic

mRNAs
R-HSA-9694506 (Reactome)
SARS-CoV-2 plus

strand subgenomic

mRNAs
ArrowR-HSA-9694506 (Reactome)
SARS-CoV-2 plus

strand subgenomic

mRNAs
R-HSA-9694476 (Reactome)
SUMO-p-Ncap

dimer:SARS-CoV-2

genomic RNA
ArrowR-HSA-9694455 (Reactome)
SUMO-p-Ncap

dimer:SARS-CoV-2

genomic RNA
R-HSA-9694281 (Reactome)
SUMO1:C93-UBE2IR-HSA-9694463 (Reactome)
TMPRSS2 inhibitorsR-HSA-9681514 (Reactome)
TMPRSS2:TMPRSS2 inhibitorsArrowR-HSA-9681514 (Reactome)
TMPRSS2:TMPRSS2 inhibitorsTBarR-HSA-9694661 (Reactome)
TMPRSS2ArrowR-HSA-9698988 (Reactome)
TMPRSS2R-HSA-9681514 (Reactome)
TMPRSS2mim-catalysisR-HSA-9694661 (Reactome)
UBE2IArrowR-HSA-9694463 (Reactome)
UDP-GalNAcR-HSA-9694438 (Reactome)
UDPArrowR-HSA-9694438 (Reactome)
UVRAG complexArrowR-HSA-9698265 (Reactome)
Ub-3xPalmC-E pentamerArrowR-HSA-9694294 (Reactome)
Ub-3xPalmC-E pentamerArrowR-HSA-9694452 (Reactome)
Ub-3xPalmC-E pentamerR-HSA-9694294 (Reactome)
Ub-3xPalmC-E pentamerR-HSA-9694444 (Reactome)
Ub-3xPalmC-EArrowR-HSA-9694529 (Reactome)
Ub-3xPalmC-ER-HSA-9694452 (Reactome)
UbR-HSA-9694529 (Reactome)
VCPArrowR-HSA-9694689 (Reactome)
VHLR-HSA-9694520 (Reactome)
ZCRB1:m7G(5')pppAm-capped, polyadenylated SARS-CoV-2 genomic RNA (plus strand)ArrowR-HSA-9694677 (Reactome)
ZCRB1R-HSA-9694677 (Reactome)
a nucleotide sugarR-HSA-9694331 (Reactome)
a nucleotide sugarR-HSA-9694389 (Reactome)
a nucleotide sugarR-HSA-9694611 (Reactome)
beta-D-glucoseArrowR-HSA-9694364 (Reactome)
di-antennary

N-glycan-PALM-Spike

trimer
ArrowR-HSA-9694656 (Reactome)
di-antennary

N-glycan-PALM-Spike

trimer
R-HSA-9696980 (Reactome)
encapsidated

SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694689 (Reactome)
encapsidated

SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9698988 (Reactome)
encapsidated

SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694723 (Reactome)
encapsidated

SARS-CoV-2 genomic

RNA
ArrowR-HSA-9694281 (Reactome)
encapsidated

SARS-CoV-2 genomic

RNA
R-HSA-9694444 (Reactome)
fully glycosylated Spike trimerArrowR-HSA-9697018 (Reactome)
fully glycosylated Spike trimerR-HSA-9694553 (Reactome)
glycosylated-ACE2ArrowR-HSA-9694287 (Reactome)
glycosylated-ACE2ArrowR-HSA-9698988 (Reactome)
glycosylated-ACE2R-HSA-9694579 (Reactome)
high-mannose

N-glycan folded

Spike
ArrowR-HSA-9694337 (Reactome)
high-mannose

N-glycan folded

Spike
R-HSA-9694341 (Reactome)
high-mannose

N-glycan unfolded

Spike
ArrowR-HSA-9696807 (Reactome)
high-mannose

N-glycan unfolded

Spike
R-HSA-9694337 (Reactome)
high-mannose

N-glycan-PALM-Spike

trimer
ArrowR-HSA-9694467 (Reactome)
high-mannose

N-glycan-PALM-Spike

trimer
ArrowR-HSA-9694780 (Reactome)
high-mannose

N-glycan-PALM-Spike

trimer
R-HSA-9694656 (Reactome)
high-mannose

N-glycan-PALM-Spike

trimer
R-HSA-9694780 (Reactome)
high-mannose N-glycan-PALM-SpikeArrowR-HSA-9694341 (Reactome)
high-mannose N-glycan-PALM-SpikeR-HSA-9694467 (Reactome)
m7G(5')pppAm-SARS-CoV-2 plus strand subgenomic mRNAsArrowR-HSA-9694499 (Reactome)
m7G(5')pppAm-SARS-CoV-2 plus strand subgenomic mRNAsR-HSA-9694733 (Reactome)
m7G(5')pppAm-capped

SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694721 (Reactome)
m7G(5')pppAm-capped

SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694471 (Reactome)
m7G(5')pppAm-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
ArrowR-HSA-9694521 (Reactome)
m7G(5')pppAm-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
ArrowR-HSA-9694581 (Reactome)
m7G(5')pppAm-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
R-HSA-9694495 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 subgenomic mRNAs

(plus strand)
ArrowR-HSA-9694733 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694471 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694549 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694723 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694274 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694334 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694454 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694455 (Reactome)
m7G(5')pppAm-capped,

polyadenylated SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694677 (Reactome)
m7G(5')pppAm-capped,polyadenylated mRNA2R-HSA-9694447 (Reactome)
m7G(5')pppAm-capped,polyadenylated mRNA3R-HSA-9694794 (Reactome)
m7G(5')pppAm-capped,polyadenylated mRNA4R-HSA-9694280 (Reactome)
m7G(5')pppAm-capped,polyadenylated mRNA5R-HSA-9694681 (Reactome)
m7G(5')pppAm-capped,polyadenylated-mRNA9R-HSA-9694370 (Reactome)
m7GpppA-SARS-CoV-2

plus strand

subgenomic mRNAs
R-HSA-9694499 (Reactome)
m7GpppA-capped

SARS-CoV-2 genomic

RNA (plus strand)
ArrowR-HSA-9694737 (Reactome)
m7GpppA-capped

SARS-CoV-2 genomic

RNA (plus strand)
R-HSA-9694721 (Reactome)
m7GpppA-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
ArrowR-HSA-9694492 (Reactome)
m7GpppA-capped

SARS-CoV-2 genomic RNA complement

(minus strand)
R-HSA-9694521 (Reactome)
nascent EArrowR-HSA-9694280 (Reactome)
nascent ER-HSA-9694401 (Reactome)
nascent ER-HSA-9694790 (Reactome)
nascent MArrowR-HSA-9694681 (Reactome)
nascent MR-HSA-9694525 (Reactome)
nascent MR-HSA-9694555 (Reactome)
nascent SpikeArrowR-HSA-9694447 (Reactome)
nascent SpikeR-HSA-9694793 (Reactome)
nsp1-4R-HSA-9694338 (Reactome)
nsp1-4R-HSA-9694625 (Reactome)
nsp10:nsp14ArrowR-HSA-9694542 (Reactome)
nsp10:nsp14R-HSA-9694304 (Reactome)
nsp10R-HSA-9694445 (Reactome)
nsp10R-HSA-9694542 (Reactome)
nsp13:DDX5ArrowR-HSA-9694406 (Reactome)
nsp15 hexamerArrowR-HSA-9694436 (Reactome)
nsp15 hexamerR-HSA-9694390 (Reactome)
nsp15 hexamerR-HSA-9694539 (Reactome)
nsp15:RB1ArrowR-HSA-9694390 (Reactome)
nsp16:VHLArrowR-HSA-9694520 (Reactome)
nsp16:nsp10ArrowR-HSA-9694445 (Reactome)
nsp16:nsp10R-HSA-9694576 (Reactome)
nsp1ArrowR-HSA-9694338 (Reactome)
nsp1ArrowR-HSA-9694625 (Reactome)
nsp2ArrowR-HSA-9694338 (Reactome)
nsp2ArrowR-HSA-9694625 (Reactome)
nsp3-4ArrowR-HSA-9694338 (Reactome)
nsp3-4R-HSA-9694331 (Reactome)
nsp3-4R-HSA-9694601 (Reactome)
nsp3:nsp4:nsp6ArrowR-HSA-9694630 (Reactome)
nsp3:nsp4:nsp6R-HSA-9694576 (Reactome)
nsp3:nsp4ArrowR-HSA-9694317 (Reactome)
nsp3:nsp4R-HSA-9694630 (Reactome)
nsp3ArrowR-HSA-9694601 (Reactome)
nsp3ArrowR-HSA-9694625 (Reactome)
nsp3R-HSA-9694389 (Reactome)
nsp4ArrowR-HSA-9694601 (Reactome)
nsp4ArrowR-HSA-9694625 (Reactome)
nsp4R-HSA-9694611 (Reactome)
nsp5R-HSA-9694333 (Reactome)
nsp6ArrowR-HSA-9694317 (Reactome)
nsp6R-HSA-9694317 (Reactome)
nsp6R-HSA-9694630 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13:nsp15ArrowR-HSA-9694539 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13:nsp15R-HSA-9694576 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13ArrowR-HSA-9694524 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10:nsp13R-HSA-9694539 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10ArrowR-HSA-9694304 (Reactome)
nsp7:nsp8:nsp12:nsp14:nsp10R-HSA-9694524 (Reactome)
nsp7:nsp8:nsp12ArrowR-HSA-9691363 (Reactome)
nsp7:nsp8:nsp12R-HSA-9694304 (Reactome)
nsp7:nsp8ArrowR-HSA-9691335 (Reactome)
nsp7:nsp8R-HSA-9691363 (Reactome)
nsp7R-HSA-9691335 (Reactome)
nsp8:MAP1LC3BArrowR-HSA-9694580 (Reactome)
nsp8R-HSA-9691335 (Reactome)
nsp8R-HSA-9691363 (Reactome)
nsp8R-HSA-9694580 (Reactome)
nsp9 dimerArrowR-HSA-9694261 (Reactome)
nsp9R-HSA-9694261 (Reactome)
nucleoside 5'-diphosphate(3-)ArrowR-HSA-9694331 (Reactome)
nucleoside 5'-diphosphate(3-)ArrowR-HSA-9694389 (Reactome)
nucleoside 5'-diphosphate(3-)ArrowR-HSA-9694611 (Reactome)
nucleoside 5'-diphosphate(3−)ArrowR-HSA-9694525 (Reactome)
nucleoside 5'-diphosphate(3−)ArrowR-HSA-9694790 (Reactome)
nucleotide-sugarR-HSA-9694525 (Reactome)
nucleotide-sugarR-HSA-9694790 (Reactome)
palmitoyl-CoAR-HSA-9694341 (Reactome)
palmitoyl-CoAR-HSA-9694401 (Reactome)
phospho-ADPr-p-S177-NcapArrowR-HSA-9694773 (Reactome)
phospho-ADPr-p-S177-NcapR-HSA-9694463 (Reactome)
phospho-SUMO1-K62-ADPr-p-S177-NcapArrowR-HSA-9694463 (Reactome)
phospho-SUMO1-K62-ADPr-p-S177-NcapR-HSA-9694363 (Reactome)
phospho-p-S177,S181,S185,S187,S189,S191,S195,T199,S203,S207-NArrowR-HSA-9694620 (Reactome)
phospho-p-S177-NcapArrowR-HSA-9694293 (Reactome)
phospho-p-S177-NcapR-HSA-9694773 (Reactome)
pp1a dimerArrowR-HSA-9694567 (Reactome)
pp1a dimermim-catalysisR-HSA-9694377 (Reactome)
pp1a-3CLArrowR-HSA-9694377 (Reactome)
pp1a-3CLArrowR-HSA-9694441 (Reactome)
pp1a-nsp1-4ArrowR-HSA-9694377 (Reactome)
pp1a-nsp1-4ArrowR-HSA-9694441 (Reactome)
pp1a-nsp1-4mim-catalysisR-HSA-9694338 (Reactome)
pp1a-nsp10ArrowR-HSA-9694551 (Reactome)
pp1a-nsp11ArrowR-HSA-9694551 (Reactome)
pp1a-nsp6-11ArrowR-HSA-9694377 (Reactome)
pp1a-nsp6-11ArrowR-HSA-9694441 (Reactome)
pp1a-nsp6-11ArrowR-HSA-9698265 (Reactome)
pp1a-nsp6-11R-HSA-9694551 (Reactome)
pp1a-nsp6ArrowR-HSA-9694551 (Reactome)
pp1a-nsp7ArrowR-HSA-9694551 (Reactome)
pp1a-nsp8ArrowR-HSA-9694551 (Reactome)
pp1a-nsp9ArrowR-HSA-9694551 (Reactome)
pp1aArrowR-HSA-9694334 (Reactome)
pp1aR-HSA-9694377 (Reactome)
pp1aR-HSA-9694441 (Reactome)
pp1aR-HSA-9694567 (Reactome)
pp1ab-nsp1-4ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp10ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp12ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp12R-HSA-9691363 (Reactome)
pp1ab-nsp13ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp13R-HSA-9694406 (Reactome)
pp1ab-nsp13R-HSA-9694524 (Reactome)
pp1ab-nsp14ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp14R-HSA-9694542 (Reactome)
pp1ab-nsp15ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp15R-HSA-9694436 (Reactome)
pp1ab-nsp16ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp16R-HSA-9694445 (Reactome)
pp1ab-nsp16R-HSA-9694520 (Reactome)
pp1ab-nsp5ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp6ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp7ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp8ArrowR-HSA-9694732 (Reactome)
pp1ab-nsp9ArrowR-HSA-9694732 (Reactome)
pp1abArrowR-HSA-9694274 (Reactome)
pp1abR-HSA-9694732 (Reactome)
sialyltransferasesmim-catalysisR-HSA-9694718 (Reactome)
sialyltransferasesmim-catalysisR-HSA-9697018 (Reactome)
tri-antennary

N-glycan-PALM-Spike

trimer
ArrowR-HSA-9696980 (Reactome)
tri-antennary

N-glycan-PALM-Spike

trimer
R-HSA-9697018 (Reactome)
α-KetoamidesR-HSA-9694592 (Reactome)
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