Influenza Infection (Homo sapiens)
From WikiPathways
Description
The virus particle initially associates with a human host cell by binding to sialic acid-containing receptors on the host cell surface. The bound virus is endocytosed by one of four distinct mechanisms. The low endosomal pH sets in motion a number of steps that lead to viral membrane fusion mediated by the viral hemagglutinin (HA) protein, and the eventual release of the uncoated viral ribonucleoprotein complex into the cytosol of the host cell. The ribonucleoprotein complex is transported through the nuclear pore into the nucleus. Once in the nucleus, the incoming negative-sense viral RNA (vRNA) is transcribed into messenger RNA (mRNA) by a primer-dependent mechanism. Replication occurs via a two step process. A full-length complementary RNA (cRNA), a positive-sense copy of the vRNA, is first made and this in turn is used as a template to produce more vRNA. The viral proteins are expressed and processed and eventually assemble with vRNAs at budding sites within the host cell membrane. The viral protein complexes and ribonucleoproteins are assembled into viral particles and bud from the host cell, enveloped in the host cell's membrane.
This release contains a framework for the further annotation of the viral life-cycle.Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=168255</div>
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- Honda A, Mizumoto K, Ishihama A.; ''Two separate sequences of PB2 subunit constitute the RNA cap-binding site of influenza virus RNA polymerase.''; PubMed Europe PMC Scholia
- Cros JF, García-Sastre A, Palese P.; ''An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein.''; PubMed Europe PMC Scholia
- Lamb RA, Choppin PW, Chanock RM, Lai CJ.; ''Mapping of the two overlapping genes for polypeptides NS1 and NS2 on RNA segment 8 of influenza virus genome.''; PubMed Europe PMC Scholia
- Li Y, Chen ZY, Wang W, Baker CC, Krug RM.; ''The 3'-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo.''; PubMed Europe PMC Scholia
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- Scheiffele P, Roth MG, Simons K.; ''Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain.''; PubMed Europe PMC Scholia
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- Doms RW, Lamb RA, Rose JK, Helenius A.; ''Folding and assembly of viral membrane proteins.''; PubMed Europe PMC Scholia
- Chen Z, Li Y, Krug RM.; ''Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.''; PubMed Europe PMC Scholia
- Molinari M, Helenius A.; ''Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.''; PubMed Europe PMC Scholia
- Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC Scholia
- Alonso-Caplen FV, Nemeroff ME, Qiu Y, Krug RM.; ''Nucleocytoplasmic transport: the influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA.''; PubMed Europe PMC Scholia
- McCown MF, Pekosz A.; ''The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging.''; PubMed Europe PMC Scholia
- Luo GX, Luytjes W, Enami M, Palese P.; ''The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure.''; PubMed Europe PMC Scholia
- Saito T, Taylor G, Webster RG.; ''Steps in maturation of influenza A virus neuraminidase.''; PubMed Europe PMC Scholia
- Hagen M, Chung TD, Butcher JA, Krystal M.; ''Recombinant influenza virus polymerase: requirement of both 5' and 3' viral ends for endonuclease activity.''; PubMed Europe PMC Scholia
- Hausmann J, Kretzschmar E, Garten W, Klenk HD.; ''Biosynthesis, intracellular transport and enzymatic activity of an avian influenza A virus neuraminidase: role of unpaired cysteines and individual oligosaccharides.''; PubMed Europe PMC Scholia
- Wang P, Palese P, O'Neill RE.; ''The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal.''; PubMed Europe PMC Scholia
- Ye Q, Krug RM, Tao YJ.; ''The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA.''; PubMed Europe PMC Scholia
- Stegmann T.; ''Membrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.''; PubMed Europe PMC Scholia
- Shimizu K, Iguchi A, Gomyou R, Ono Y.; ''Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site.''; PubMed Europe PMC Scholia
- Park CJ, Bae SH, Lee MK, Varani G, Choi BS.; ''Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase.''; PubMed Europe PMC Scholia
- Neumann G, Hughes MT, Kawaoka Y.; ''Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1.''; PubMed Europe PMC Scholia
- Barman S, Ali A, Hui EK, Adhikary L, Nayak DP.; ''Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses.''; PubMed Europe PMC Scholia
- Elster C, Fourest E, Baudin F, Larsen K, Cusack S, Ruigrok RW.; ''A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction.''; PubMed Europe PMC Scholia
- O'Neill RE, Jaskunas R, Blobel G, Palese P, Moroianu J.; ''Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import.''; PubMed Europe PMC Scholia
- Daniels R, Kurowski B, Johnson AE, Hebert DN.; ''N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.''; PubMed Europe PMC Scholia
- Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J.; ''The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP.''; PubMed Europe PMC Scholia
- Nayak DP, Hui EK, Barman S.; ''Assembly and budding of influenza virus.''; PubMed Europe PMC Scholia
- Cianci C, Tiley L, Krystal M.; ''Differential activation of the influenza virus polymerase via template RNA binding.''; PubMed Europe PMC Scholia
- Nemergut ME, Lindsay ME, Brownawell AM, Macara IG.; ''Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor.''; PubMed Europe PMC Scholia
- Detjen BM, St Angelo C, Katze MG, Krug RM.; ''The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex.''; PubMed Europe PMC Scholia
- Li ML, Ramirez BC, Krug RM.; ''RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites.''; PubMed Europe PMC Scholia
- Kash JC, Goodman AG, Korth MJ, Katze MG.; ''Hijacking of the host-cell response and translational control during influenza virus infection.''; PubMed Europe PMC Scholia
- Pleschka S, Wolff T, Ehrhardt C, Hobom G, Planz O, Rapp UR, Ludwig S.; ''Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade.''; PubMed Europe PMC Scholia
- Mukaigawa J, Nayak DP.; ''Two signals mediate nuclear localization of influenza virus (A/WSN/33) polymerase basic protein 2.''; PubMed Europe PMC Scholia
- Honda A, Uéda K, Nagata K, Ishihama A.; ''RNA polymerase of influenza virus: role of NP in RNA chain elongation.''; PubMed Europe PMC Scholia
- Brownlee GG, Sharps JL.; ''The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.''; PubMed Europe PMC Scholia
- Crow M, Deng T, Addley M, Brownlee GG.; ''Mutational analysis of the influenza virus cRNA promoter and identification of nucleotides critical for replication.''; PubMed Europe PMC Scholia
- Vreede FT, Jung TE, Brownlee GG.; ''Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates.''; PubMed Europe PMC Scholia
- Krug RM.; ''Priming of influenza viral RNA transcription by capped heterologous RNAs.''; PubMed Europe PMC Scholia
- Bergmann M, Garcia-Sastre A, Carnero E, Pehamberger H, Wolff K, Palese P, Muster T.; ''Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.''; PubMed Europe PMC Scholia
- Yasuda J, Nakada S, Kato A, Toyoda T, Ishihama A.; ''Molecular assembly of influenza virus: association of the NS2 protein with virion matrix.''; PubMed Europe PMC Scholia
- Sugrue RJ, Belshe RB, Hay AJ.; ''Palmitoylation of the influenza A virus M2 protein.''; PubMed Europe PMC Scholia
- Chen W, Calvo PA, Malide D, Gibbs J, Schubert U, Bacik I, Basta S, O'Neill R, Schickli J, Palese P, Henklein P, Bennink JR, Yewdell JW.; ''A novel influenza A virus mitochondrial protein that induces cell death.''; PubMed Europe PMC Scholia
- Luo C, Nobusawa E, Nakajima K.; ''An analysis of the role of neuraminidase in the receptor-binding activity of influenza B virus: the inhibitory effect of Zanamivir on haemadsorption.''; PubMed Europe PMC Scholia
- Marjuki H, Alam MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S.; ''Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling.''; PubMed Europe PMC Scholia
- Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
- Li ML, Rao P, Krug RM.; ''The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.''; PubMed Europe PMC Scholia
- Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY, Krug RM, Julkunen I.; ''Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.''; PubMed Europe PMC Scholia
- Palese P, Compans RW.; ''Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action.''; PubMed Europe PMC Scholia
- Nilsson J, Askjaer P, Kjems J.; ''A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1.''; PubMed Europe PMC Scholia
- Li N, Ren A, Wang X, Fan X, Zhao Y, Gao GF, Cleary P, Wang B.; ''Influenza viral neuraminidase primes bacterial coinfection through TGF-β-mediated expression of host cell receptors.''; PubMed Europe PMC Scholia
- Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
- DONALD HB, ISAACS A.; ''Counts of influenza virus particles.''; PubMed Europe PMC Scholia
- Chanturiya AN, Basañez G, Schubert U, Henklein P, Yewdell JW, Zimmerberg J.; ''PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes.''; PubMed Europe PMC Scholia
- Stegmann T, Morselt HW, Scholma J, Wilschut J.; ''Fusion of influenza virus in an intracellular acidic compartment measured by fluorescence dequenching.''; PubMed Europe PMC Scholia
- Veit M, Klenk HD, Kendal A, Rott R.; ''The M2 protein of influenza A virus is acylated.''; PubMed Europe PMC Scholia
- Enami M, Sharma G, Benham C, Palese P.; ''An influenza virus containing nine different RNA segments.''; PubMed Europe PMC Scholia
- Braam J, Ulmanen I, Krug RM.; ''Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription.''; PubMed Europe PMC Scholia
- Neumann G, Brownlee GG, Fodor E, Kawaoka Y.; ''Orthomyxovirus replication, transcription, and polyadenylation.''; PubMed Europe PMC Scholia
- Garman E, Laver G.; ''Controlling influenza by inhibiting the virus's neuraminidase.''; PubMed Europe PMC Scholia
- Ward AC, Castelli LA, Lucantoni AC, White JF, Azad AA, Macreadie IG.; ''Expression and analysis of the NS2 protein of influenza A virus.''; PubMed Europe PMC Scholia
- Martin K, Helenius A.; ''Transport of incoming influenza virus nucleocapsids into the nucleus.''; PubMed Europe PMC Scholia
- Perez DR, Donis RO.; ''Functional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity.''; PubMed Europe PMC Scholia
- Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM.; ''Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs.''; PubMed Europe PMC Scholia
- Watanabe K, Takizawa N, Katoh M, Hoshida K, Kobayashi N, Nagata K.; ''Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B.''; PubMed Europe PMC Scholia
- Vreede FT, Brownlee GG.; ''Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro.''; PubMed Europe PMC Scholia
- Plotch SJ, Bouloy M, Ulmanen I, Krug RM.; ''A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.''; PubMed Europe PMC Scholia
- Amorim MJ, Read EK, Dalton RM, Medcalf L, Digard P.; ''Nuclear export of influenza A virus mRNAs requires ongoing RNA polymerase II activity.''; PubMed Europe PMC Scholia
- Zhang J, Lamb RA.; ''Characterization of the membrane association of the influenza virus matrix protein in living cells.''; PubMed Europe PMC Scholia
- González S, Zürcher T, Ortín J.; ''Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure.''; PubMed Europe PMC Scholia
- Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-López M, Baudin F, Mattaj IW, Müller CW.; ''Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.''; PubMed Europe PMC Scholia
- Carrasco M, Amorim MJ, Digard P.; ''Lipid raft-dependent targeting of the influenza A virus nucleoprotein to the apical plasma membrane.''; PubMed Europe PMC Scholia
- Mikulásová A, Varecková E, Fodor E.; ''Transcription and replication of the influenza a virus genome.''; PubMed Europe PMC Scholia
- Nakagawa Y, Oda K, Nakada S.; ''The PB1 subunit alone can catalyze cRNA synthesis, and the PA subunit in addition to the PB1 subunit is required for viral RNA synthesis in replication of the influenza virus genome.''; PubMed Europe PMC Scholia
- Veit M, Kretzschmar E, Kuroda K, Garten W, Schmidt MF, Klenk HD, Rott R.; ''Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
- Palese P, Tobita K, Ueda M, Compans RW.; ''Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.''; PubMed Europe PMC Scholia
- Pritlove DC, Fodor E, Seong BL, Brownlee GG.; ''In vitro transcription and polymerase binding studies of the termini of influenza A virus cRNA: evidence for a cRNA panhandle.''; PubMed Europe PMC Scholia
- Schmitt AP, Lamb RA.; ''Escaping from the cell: assembly and budding of negative-strand RNA viruses.''; PubMed Europe PMC Scholia
- Salom D, Hill BR, Lear JD, DeGrado WF.; ''pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus.''; PubMed Europe PMC Scholia
- Deng T, Vreede FT, Brownlee GG.; ''Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.''; PubMed Europe PMC Scholia
- Boulo S, Akarsu H, Ruigrok RW, Baudin F.; ''Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.''; PubMed Europe PMC Scholia
- De Marcos Lousa C, Trézéguet V, Dianoux AC, Brandolin G, Lauquin GJ.; ''The human mitochondrial ADP/ATP carriers: kinetic properties and biogenesis of wild-type and mutant proteins in the yeast S. cerevisiae.''; PubMed Europe PMC Scholia
- Lamb RA, Lai CJ, Choppin PW.; ''Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins.''; PubMed Europe PMC Scholia
- Tatu U, Hammond C, Helenius A.; ''Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.''; PubMed Europe PMC Scholia
- Zheng H, Lee HA, Palese P, García-Sastre A.; ''Influenza A virus RNA polymerase has the ability to stutter at the polyadenylation site of a viral RNA template during RNA replication.''; PubMed Europe PMC Scholia
- Baudin F, Petit I, Weissenhorn W, Ruigrok RW.; ''In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.''; PubMed Europe PMC Scholia
- Fortes P, Beloso A, Ortín J.; ''Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport.''; PubMed Europe PMC Scholia
- Chen Z, Krug RM.; ''Selective nuclear export of viral mRNAs in influenza-virus-infected cells.''; PubMed Europe PMC Scholia
- Donelan NR, Basler CF, García-Sastre A.; ''A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice.''; PubMed Europe PMC Scholia
- Mayer D, Molawi K, Martínez-Sobrido L, Ghanem A, Thomas S, Baginsky S, Grossmann J, García-Sastre A, Schwemmle M.; ''Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches.''; PubMed Europe PMC Scholia
- Fodor E, Pritlove DC, Brownlee GG.; ''The influenza virus panhandle is involved in the initiation of transcription.''; PubMed Europe PMC Scholia
- Bortz E, Westera L, Maamary J, Steel J, Albrecht RA, Manicassamy B, Chase G, Martínez-Sobrido L, Schwemmle M, García-Sastre A.; ''Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.''; PubMed Europe PMC Scholia
- Morris SJ, Price GE, Barnett JM, Hiscox SA, Smith H, Sweet C.; ''Role of neuraminidase in influenza virus-induced apoptosis.''; PubMed Europe PMC Scholia
- Takeda M, Leser GP, Russell CJ, Lamb RA.; ''Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.''; PubMed Europe PMC Scholia
- Veit M, Schmidt MF.; ''Timing of palmitoylation of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
- Son KN, Liang Z, Lipton HL.; ''Double-Stranded RNA Is Detected by Immunofluorescence Analysis in RNA and DNA Virus Infections, Including Those by Negative-Stranded RNA Viruses.''; PubMed Europe PMC Scholia
- Gething MJ, McCammon K, Sambrook J.; ''Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.''; PubMed Europe PMC Scholia
History
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External references
DataNodes
| View all... |
| Name | Type | Database reference | Comment |
|---|---|---|---|
| 18S rRNA [cytosol] | Protein | X03205 (EMBL)  | |
| 28S rRNA [cytosol] | Protein | M11167 (EMBL) | |
| 2xMe-SNRPB [nucleoplasm] | Protein | P14678 (Uniprot-TrEMBL) | |
| 2xMe-SNRPD1 [nucleoplasm] | Protein | P62314 (Uniprot-TrEMBL) | |
| 2xMe-SNRPD3 [nucleoplasm] | Protein | P62318 (Uniprot-TrEMBL) | |
| 5.8S rRNA [cytosol] | Protein | J01866 (EMBL) | |
| 5S rRNA [cytosol] | Protein | V00589 (EMBL) | |
| 7-methylguanosine cap [nucleoplasm] | Metabolite | CHEBI:17825 (ChEBI) | |
| 80S ribosome | Complex | REACT_4330 (Reactome) | |
| AAAS [nuclear envelope] | Protein | Q9NRG9 (Uniprot-TrEMBL) | |
| ALYREF [nucleoplasm] | Protein | Q86V81 (Uniprot-TrEMBL) | |
| Acidified Influenza
A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | Complex | REACT_9103 (Reactome) | |
| Aminoacyl-tRNA | Metabolite | REACT_4792 (Reactome) | |
| CALR | Protein | P27797 (Uniprot-TrEMBL) | |
| CANX | Protein | P27824 (Uniprot-TrEMBL) | |
| CCAR1 [nucleoplasm] | Protein | Q8IX12 (Uniprot-TrEMBL) | |
| CD2BP2 [nucleoplasm] | Protein | O95400 (Uniprot-TrEMBL) | |
| CLTA [plasma membrane] | Protein | P09496 (Uniprot-TrEMBL) | |
| Clathrin | Complex | REACT_9338 (Reactome) | |
| Cleaved HA Influenza A Viral Particle | Complex | REACT_9239 (Reactome) | |
| Crm1:Ran GTPase:GDP | Complex | REACT_6660 (Reactome) | |
| DHX9 [nucleoplasm] | Protein | Q08211 (Uniprot-TrEMBL) | |
| DNAJC3 | Protein | Q13217 (Uniprot-TrEMBL) | |
| Elongated vRNA-mRNA Complex | Complex | REACT_9568 (Reactome) | Capped, synthesized RNA strand complementary to vRNA, plus viral polymerase and template vRNA (Plotch, 1977). |
| FAU [cytosol] | Protein | P62861 (Uniprot-TrEMBL) | |
| FUS [nucleoplasm] | Protein | P35637 (Uniprot-TrEMBL) | |
| GDP [cytosol] | Metabolite | CHEBI:17552 (ChEBI) | |
| GRSF1(?-?) | Protein | Q12849 (Uniprot-TrEMBL) | |
| GTF2F1(2-517) [nucleoplasm] | Protein | P35269 (Uniprot-TrEMBL) | |
| GTF2F2(2-249) [nucleoplasm] | Protein | P13984 (Uniprot-TrEMBL) | |
| GTP [nucleoplasm] | Metabolite | CHEBI:15996 (ChEBI) | |
| Genomic RNA Segment 1 [cytosol] | Protein | AF389115 (EMBL) | |
| Genomic RNA Segment 1 [endosome lumen] | Protein | AF389115 (EMBL) | |
| Genomic RNA Segment
1 [extracellular region] | Protein | AF389115 (EMBL) | |
| Genomic RNA Segment 1 [nucleoplasm] | Protein | AF389115 (EMBL) | |
| Genomic RNA Segment 2 [cytosol] | Protein | AF389116 (EMBL) | |
| Genomic RNA Segment 2 [endosome lumen] | Protein | AF389116 (EMBL) | |
| Genomic RNA Segment
2 [extracellular region] | Protein | AF389116 (EMBL) | |
| Genomic RNA Segment 2 [nucleoplasm] | Protein | AF389116 (EMBL) | |
| Genomic RNA Segment 3 [cytosol] | Protein | AF389117 (EMBL) | |
| Genomic RNA Segment 3 [endosome lumen] | Protein | AF389117 (EMBL) | |
| Genomic RNA Segment
3 [extracellular region] | Protein | AF389117 (EMBL) | |
| Genomic RNA Segment 3 [nucleoplasm] | Protein | AF389117 (EMBL) | |
| Genomic RNA Segment 4 [cytosol] | Protein | AF389118 (EMBL) | |
| Genomic RNA Segment 4 [endosome lumen] | Protein | AF389118 (EMBL) | |
| Genomic RNA Segment
4 [extracellular region] | Protein | AF389118 (EMBL) | |
| Genomic RNA Segment 4 [nucleoplasm] | Protein | AF389118 (EMBL) | |
| Genomic RNA Segment 5 [cytosol] | Protein | AF389119 (EMBL) | |
| Genomic RNA Segment 5 [endosome lumen] | Protein | AF389119 (EMBL) | |
| Genomic RNA Segment
5 [extracellular region] | Protein | AF389119 (EMBL) | |
| Genomic RNA Segment 5 [nucleoplasm] | Protein | AF389119 (EMBL) | |
| Genomic RNA Segment 6 [cytosol] | Protein | AF389120 (EMBL) | |
| Genomic RNA Segment 6 [endosome lumen] | Protein | AF389120 (EMBL) | |
| Genomic RNA Segment
6 [extracellular region] | Protein | AF389120 (EMBL) | |
| Genomic RNA Segment 6 [nucleoplasm] | Protein | AF389120 (EMBL) | |
| Genomic RNA Segment 7 [cytosol] | Protein | AF389121 (EMBL) | |
| Genomic RNA Segment 7 [endosome lumen] | Protein | AF389121 (EMBL) | |
| Genomic RNA Segment
7 [extracellular region] | Protein | AF389121 (EMBL) | |
| Genomic RNA Segment 7 [nucleoplasm] | Protein | AF389121 (EMBL) | |
| Genomic RNA Segment 8 [cytosol] | Protein | AF389122 (EMBL) | |
| Genomic RNA Segment 8 [endosome lumen] | Protein | AF389122 (EMBL) | |
| Genomic RNA Segment
8 [extracellular region] | Protein | AF389122 (EMBL) | |
| Genomic RNA Segment 8 [nucleoplasm] | Protein | AF389122 (EMBL) | |
| Glycosylated NA Tetramer | Complex | REACT_10176 (Reactome) | |
| Glycosylated NA Tetramer | Complex | REACT_10567 (Reactome) | |
| Glycosylated NA Tetramer | Complex | REACT_10972 (Reactome) | |
| Glycosylated NA [Golgi membrane] | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated NA
[endocytic vesicle membrane] | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated NA
[endoplasmic reticulum membrane] | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated NA
[extracellular region] | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated NA [plasma membrane] | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated NA | Protein | P03468 (Uniprot-TrEMBL) | |
| Glycosylated and
folded HA [endoplasmic reticulum membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| Glycosylated and folded HA trimer | Complex | REACT_10412 (Reactome) | |
| Glycosylated and folded HA trimer | Complex | REACT_10554 (Reactome) | |
| Glycosylated and folded HA trimer | Complex | REACT_10717 (Reactome) | |
| Glycosylated and folded HA | Protein | P03452 (Uniprot-TrEMBL) | |
| Glycosylated,
palmitylated and folded HA trimer:Lipid Raft Complex | Complex | REACT_10369 (Reactome) | |
| Glycosylated,
palmitylated and folded HA trimer:Lipid Raft Complex | Complex | REACT_10581 (Reactome) | |
| Glycosylated,
palmitylated and folded HA trimer | Complex | REACT_10197 (Reactome) | |
| Glycosylated,
palmitylated and folded HA trimer | Complex | REACT_10978 (Reactome) | |
| Gycosylated NA Tetramer:Lipid Raft | Complex | REACT_10662 (Reactome) | |
| Gycosylated NA Tetramer:Lipid Raft | Complex | REACT_10954 (Reactome) | |
| Gycosylated NA Tetramer | Complex | REACT_10841 (Reactome) | |
| H+ [endosome lumen] | Metabolite | CHEBI:15378 (ChEBI) | |
| H+ | Metabolite | CHEBI:15378 (ChEBI) | |
| HA folded and
glycosylated [endocytic vesicle membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA folded and
glycosylated [Golgi membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA folded,
glycosylated, and palmitylated [extracellular region] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA folded,
glycosylated, and palmitylated [Golgi membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA folded,
glycosylated, and palmitylated [plasma membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA mRNA [nucleoplasm] | Protein | V01088 (EMBL) | |
| HA1 [endocytic vesicle membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA1 [endosome lumen] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA1 [extracellular region] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA2 [endosome lumen] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA2 [extracellular region] | Protein | P03452 (Uniprot-TrEMBL) | |
| HA | Protein | P03452 (Uniprot-TrEMBL) | |
| HNRNPA0 [nucleoplasm] | Protein | Q13151 (Uniprot-TrEMBL) | |
| HNRNPA1 [nucleoplasm] | Protein | P09651 (Uniprot-TrEMBL) | |
| HNRNPA2B1 [nucleoplasm] | Protein | P22626 (Uniprot-TrEMBL) | |
| HNRNPA3 [nucleoplasm] | Protein | P51991 (Uniprot-TrEMBL) | |
| HNRNPC [nucleoplasm] | Protein | P07910 (Uniprot-TrEMBL) | |
| HNRNPD [nucleoplasm] | Protein | Q14103 (Uniprot-TrEMBL) | |
| HNRNPF(1-415) [nucleoplasm] | Protein | P52597 (Uniprot-TrEMBL) | |
| HNRNPH1(1-449) [nucleoplasm] | Protein | P31943 (Uniprot-TrEMBL) | |
| HNRNPH2 [nucleoplasm] | Protein | P55795 (Uniprot-TrEMBL) | |
| HNRNPK [nucleoplasm] | Protein | P61978 (Uniprot-TrEMBL) | |
| HNRNPL [nucleoplasm] | Protein | P14866 (Uniprot-TrEMBL) | |
| HNRNPM [nucleoplasm] | Protein | P52272 (Uniprot-TrEMBL) | |
| HNRNPR [nucleoplasm] | Protein | O43390 (Uniprot-TrEMBL) | |
| HNRNPU [nucleoplasm] | Protein | Q00839 (Uniprot-TrEMBL) | |
| HNRNPUL1 [nucleoplasm] | Protein | Q9BUJ2 (Uniprot-TrEMBL) | |
| HSP90AA1 | Protein | P07900 (Uniprot-TrEMBL) | |
| HSPA1A(2-641) | Protein | P08107 (Uniprot-TrEMBL) | |
| Host Derived Lipid
Bilayer Membrane Rich In Sphingolipids And Cholesterol | REACT_9200 (Reactome) | ||
| IPO5 | Protein | O00410 (Uniprot-TrEMBL) | |
| Influenza A Viral
Envelope Inserted Into The Endocytic Vesicle Membrane | Complex | REACT_9160 (Reactome) | |
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | Complex | REACT_9315 (Reactome) | |
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane | Complex | REACT_9257 (Reactome) | |
| Influenza A Viral
Particle With A Fusion Competent HA2 | Complex | REACT_9163 (Reactome) | |
| Influenza A Viral Particle | Complex | REACT_10742 (Reactome) | |
| Influenza A Viral Particle | Complex | REACT_9077 (Reactome) | |
| Influenza cRNA (complete) | REACT_9879 (Reactome) | ||
| Initiated cRNA-vRNA Complex | Complex | REACT_9672 (Reactome) | cRNA bound by NP and trimeric polymerase, capable of vRNA synthesis from the cRNA template. |
| Initiated vRNA
Transcription Complex | Complex | REACT_9684 (Reactome) | Viral RNA bound by polymerase PB1-PB2-PA subunits, primed by a 5' end cap cleaved from a host mRNA, and the second ribonucleotide (a G) complementary to a the vRNA second position (a C, Beaton, 1981; Krug, 1981; Li, 2001). |
| Initiated vRNA-cRNA Complex | Complex | REACT_9685 (Reactome) | vRNA bound by NP and trimeric polymerase, capable of complementary RNA synthesis. |
| Inter-Membrane
Spanning HA2 [endocytic vesicle membrane] | Protein | P03452 (Uniprot-TrEMBL) | |
| Intracellular assembly complex | Complex | REACT_10426 (Reactome) | |
| KPNA1 [cytosol] | Protein | P52294 (Uniprot-TrEMBL) | |
| KPNA1 [nucleoplasm] | Protein | P52294 (Uniprot-TrEMBL) | |
| KPNA1 | Protein | P52294 (Uniprot-TrEMBL) | |
| KPNB1 [cytosol] | Protein | Q14974 (Uniprot-TrEMBL) | |
| KPNB1 [nucleoplasm] | Protein | Q14974 (Uniprot-TrEMBL) | |
| KPNB1 | Protein | Q14974 (Uniprot-TrEMBL) | |
| Lipid Raft | REACT_10385 (Reactome) | ||
| M1 [cytosol] | Protein | P03485 (Uniprot-TrEMBL) | |
| M1 [endosome lumen] | Protein | P03485 (Uniprot-TrEMBL) | |
| M1 [extracellular region] | Protein | P03485 (Uniprot-TrEMBL) | |
| M1 [nucleoplasm] | Protein | P03485 (Uniprot-TrEMBL) | |
| M1 mRNA [nucleoplasm] | Protein | AF389121 (EMBL) | |
| M1 mRNA | Rna | AF389121 (EMBL) | |
| M1 | Protein | P03485 (Uniprot-TrEMBL) | |
| M2 Tetramer | Complex | REACT_10281 (Reactome) | |
| M2 Tetramer | Complex | REACT_10501 (Reactome) | |
| M2 Tetramer | Complex | REACT_10683 (Reactome) | |
| M2 [Golgi membrane] | Protein | P06821 (Uniprot-TrEMBL) | |
| M2 [cytosol] | Protein | P06821 (Uniprot-TrEMBL) | |
| M2 [endocytic vesicle membrane] | Protein | P06821 (Uniprot-TrEMBL) | |
| M2 [endoplasmic reticulum membrane] | Protein | P06821 (Uniprot-TrEMBL) | |
| M2 [endosome lumen] | Protein | P06821 (Uniprot-TrEMBL) | |
| M2 mRNA [nucleoplasm] | Protein | AF389121 (EMBL) | |
| M2 mRNA | Rna | AF389121 (EMBL) | |
| M2 | Protein | P06821 (Uniprot-TrEMBL) | |
| Mature intronless
transcript derived mRNA with m7G cap removed | REACT_9723 (Reactome) | A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. The m7G has been removed or snatched. This product was derived from an intronless transcript. | |
| Mature intronless
transcript derived mRNA | REACT_4033 (Reactome) | A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript. | |
| NA [endosome lumen] | Protein | P03468 (Uniprot-TrEMBL) | |
| NA mRNA [nucleoplasm] | Protein | J02146 (EMBL) | |
| NA | Protein | P03468 (Uniprot-TrEMBL) | |
| NCBP1 [nucleoplasm] | Protein | Q09161 (Uniprot-TrEMBL) | |
| NCBP2 [nucleoplasm] | Protein | P52298 (Uniprot-TrEMBL) | |
| NEP/NS2
[extracellular region] | Protein | P03508 (Uniprot-TrEMBL) | |
| NEP/NS2 [nucleoplasm] | Protein | P03508 (Uniprot-TrEMBL) | |
| NEP/NS2 [cytosol] | Protein | P03508 (Uniprot-TrEMBL) | |
| NEP/NS2 [endosome lumen] | Protein | P03508 (Uniprot-TrEMBL) | |
| NEP/NS2 | Protein | P03508 (Uniprot-TrEMBL) | |
| NFX.1 [nucleoplasm] | Protein | O43831 (Uniprot-TrEMBL) | |
| NP [Golgi membrane] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP [cytosol] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP [endosome lumen] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP [extracellular region] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP [nucleoplasm] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP [plasma membrane] | Protein | P03466 (Uniprot-TrEMBL) | |
| NP mRNA [nucleoplasm] | Protein | J02147 (EMBL) | |
| NP:Lipid Raft | Complex | REACT_10315 (Reactome) | |
| NP:Lipid Raft | Complex | REACT_10830 (Reactome) | |
| NP | Protein | P03466 (Uniprot-TrEMBL) | |
| NS1 [cytosol] | Protein | P03496 (Uniprot-TrEMBL) | |
| NS1 mRNA [nucleoplasm] | Protein | J02150 (EMBL) | |
| NS1 mRNA | Rna | J02150 (EMBL) | |
| NS1 | Protein | P03496 (Uniprot-TrEMBL) | |
| NS2 mRNA [nucleoplasm] | Protein | J02150 (EMBL) | |
| NS2 mRNA | Rna | J02150 (EMBL) | |
| NTP | Metabolite | REACT_4491 (Reactome) | |
| NUP107 [nuclear envelope] | Protein | P57740 (Uniprot-TrEMBL) | |
| NUP133 [nuclear envelope] | Protein | Q8WUM0 (Uniprot-TrEMBL) | |
| NUP153 [nucleoplasm] | Protein | P49790 (Uniprot-TrEMBL) | |
| NUP155 [nuclear envelope] | Protein | O75694 (Uniprot-TrEMBL) | |
| NUP160 [nuclear envelope] | Protein | Q12769 (Uniprot-TrEMBL) | |
| NUP188(2-1749) [nuclear envelope] | Protein | Q5SRE5 (Uniprot-TrEMBL) | |
| NUP205(2-2012) [nuclear envelope] | Protein | Q92621 (Uniprot-TrEMBL) | |
| NUP210 [nuclear envelope] | Protein | Q8TEM1 (Uniprot-TrEMBL) | |
| NUP214 [cytosol] | Protein | P35658 (Uniprot-TrEMBL) | |
| NUP35 [nuclear envelope] | Protein | Q8NFH5 (Uniprot-TrEMBL) | |
| NUP37 [nuclear envelope] | Protein | Q8NFH4 (Uniprot-TrEMBL) | |
| NUP43 [nuclear envelope] | Protein | Q8NFH3 (Uniprot-TrEMBL) | |
| NUP50 [nucleoplasm] | Protein | Q9UKX7 (Uniprot-TrEMBL) | |
| NUP54 [nuclear envelope] | Protein | Q7Z3B4 (Uniprot-TrEMBL) | |
| NUP62 [nuclear envelope] | Protein | P37198 (Uniprot-TrEMBL) | |
| NUP85 [nuclear envelope] | Protein | Q9BW27 (Uniprot-TrEMBL) | |
| NUP88 [cytosol] | Protein | Q99567 (Uniprot-TrEMBL) | |
| NUP93 [nuclear envelope] | Protein | Q8N1F7 (Uniprot-TrEMBL) | |
| NUP98-5 [nuclear envelope] | Protein | P52948-5 (Uniprot-TrEMBL) | |
| NUPL1-2 [nuclear envelope] | Protein | Q9BVL2-1 (Uniprot-TrEMBL) | |
| NUPL2 [cytosol] | Protein | O15504 (Uniprot-TrEMBL) | |
| Nuclear Pore Complex (NPC) | Complex | REACT_5542 (Reactome) | |
| Nup45 [nuclear envelope] | Protein | Q9BVL2-2 (Uniprot-TrEMBL) | |
| P1 mRNA [nucleoplasm] | Protein | J02151 (EMBL) | |
| PA [cytosol] | Protein | P03433 (Uniprot-TrEMBL) | |
| PA [endosome lumen] | Protein | P03433 (Uniprot-TrEMBL) | |
| PA [extracellular region] | Protein | P03433 (Uniprot-TrEMBL) | |
| PA [nucleoplasm] | Protein | P03433 (Uniprot-TrEMBL) | |
| PA mRNA [nucleoplasm] | Protein | V01106 (EMBL) | |
| PA | Protein | P03433 (Uniprot-TrEMBL) | |
| PB1 [cytosol] | Protein | P03431 (Uniprot-TrEMBL) | |
| PB1 [endosome lumen] | Protein | P03431 (Uniprot-TrEMBL) | |
| PB1 [extracellular region] | Protein | P03431 (Uniprot-TrEMBL) | |
| PB1 [nucleoplasm] | Protein | P03431 (Uniprot-TrEMBL) | |
| PB1 mRNA | Rna | J02151 (EMBL) | |
| PB1-F2 | Protein | P0C0U1 (Uniprot-TrEMBL) | |
| PB1 | Protein | P03431 (Uniprot-TrEMBL) | |
| PB2 [cytosol] | Protein | P03428 (Uniprot-TrEMBL) | |
| PB2 [endosome lumen] | Protein | P03428 (Uniprot-TrEMBL) | |
| PB2 [extracellular region] | Protein | P03428 (Uniprot-TrEMBL) | |
| PB2 [nucleoplasm] | Protein | P03428 (Uniprot-TrEMBL) | |
| PB2 | Protein | P03428 (Uniprot-TrEMBL) | |
| PCBP1 [nucleoplasm] | Protein | Q15365 (Uniprot-TrEMBL) | |
| PCBP2 [nucleoplasm] | Protein | Q15366 (Uniprot-TrEMBL) | |
| POLR2A [nucleoplasm] | Protein | P24928 (Uniprot-TrEMBL) | |
| POLR2B [nucleoplasm] | Protein | P30876 (Uniprot-TrEMBL) | |
| POLR2C [nucleoplasm] | Protein | P19387 (Uniprot-TrEMBL) | |
| POLR2D(2-142) [nucleoplasm] | Protein | O15514 (Uniprot-TrEMBL) | |
| POLR2E [nucleoplasm] | Protein | P19388 (Uniprot-TrEMBL) | |
| POLR2F(1-127) [nucleoplasm] | Protein | P61218 (Uniprot-TrEMBL) | |
| POLR2G [nucleoplasm] | Protein | P62487 (Uniprot-TrEMBL) | |
| POLR2H [nucleoplasm] | Protein | P52434 (Uniprot-TrEMBL) | |
| POLR2I [nucleoplasm] | Protein | P36954 (Uniprot-TrEMBL) | |
| POLR2J [nucleoplasm] | Protein | P52435 (Uniprot-TrEMBL) | |
| POLR2K [nucleoplasm] | Protein | P53803 (Uniprot-TrEMBL) | |
| POLR2L [nucleoplasm] | Protein | P62875 (Uniprot-TrEMBL) | |
| POM121 [nuclear envelope] | Protein | Q96HA1 (Uniprot-TrEMBL) | |
| PTBP1 [nucleoplasm] | Protein | P26599 (Uniprot-TrEMBL) | |
| Pi | Metabolite | CHEBI:18367 (ChEBI) | |
| RAE1 [nuclear envelope] | Protein | P78406 (Uniprot-TrEMBL) | |
| RAN [cytosol] | Protein | P62826 (Uniprot-TrEMBL) | |
| RAN [nucleoplasm] | Protein | P62826 (Uniprot-TrEMBL) | |
| RANBP2 [cytosol] | Protein | P49792 (Uniprot-TrEMBL) | |
| RBM5 [nucleoplasm] | Protein | P52756 (Uniprot-TrEMBL) | |
| RBMX(1-391) [nucleoplasm] | Protein | P38159 (Uniprot-TrEMBL) | |
| RNA Polymerase II
(phosphorylated):TFIIF:capped pre-mRNA | Complex | REACT_3935 (Reactome) | |
| RNP
Complex:Karyopherin alpha | Complex | REACT_9328 (Reactome) | |
| RNP pre-assembly complex | Complex | REACT_11005 (Reactome) | |
| RNP:Karyopherin
alpha:Karyopherin beta complex | Complex | REACT_9158 (Reactome) | |
| RNP:Karyopherin
alpha:Karyopherin beta complex | Complex | REACT_9341 (Reactome) | |
| RNPS1 [nucleoplasm] | Protein | Q15287 (Uniprot-TrEMBL) | |
| RPL10 [cytosol] | Protein | P27635 (Uniprot-TrEMBL) | |
| RPL10A [cytosol] | Protein | P62906 (Uniprot-TrEMBL) | |
| RPL11 [cytosol] | Protein | P62913 (Uniprot-TrEMBL) | |
| RPL12 [cytosol] | Protein | P30050 (Uniprot-TrEMBL) | |
| RPL13(2-211) [cytosol] | Protein | P26373 (Uniprot-TrEMBL) | |
| RPL13A [cytosol] | Protein | P40429 (Uniprot-TrEMBL) | |
| RPL14 [cytosol] | Protein | P50914 (Uniprot-TrEMBL) | |
| RPL15(2-204) [cytosol] | Protein | P61313 (Uniprot-TrEMBL) | |
| RPL17 [cytosol] | Protein | P18621 (Uniprot-TrEMBL) | |
| RPL18 [cytosol] | Protein | Q07020 (Uniprot-TrEMBL) | |
| RPL18A [cytosol] | Protein | Q02543 (Uniprot-TrEMBL) | |
| RPL19 [cytosol] | Protein | P84098 (Uniprot-TrEMBL) | |
| RPL21 [cytosol] | Protein | P46778 (Uniprot-TrEMBL) | |
| RPL22 [cytosol] | Protein | P35268 (Uniprot-TrEMBL) | |
| RPL23 [cytosol] | Protein | P62829 (Uniprot-TrEMBL) | |
| RPL23A [cytosol] | Protein | P62750 (Uniprot-TrEMBL) | |
| RPL24 [cytosol] | Protein | P83731 (Uniprot-TrEMBL) | |
| RPL26 [cytosol] | Protein | P61254 (Uniprot-TrEMBL) | |
| RPL26L1(2-145) [cytosol] | Protein | Q9UNX3 (Uniprot-TrEMBL) | |
| RPL27(2-136) [cytosol] | Protein | P61353 (Uniprot-TrEMBL) | |
| RPL27A [cytosol] | Protein | P46776 (Uniprot-TrEMBL) | |
| RPL28 [cytosol] | Protein | P46779 (Uniprot-TrEMBL) | |
| RPL29 [cytosol] | Protein | P47914 (Uniprot-TrEMBL) | |
| RPL3 [cytosol] | Protein | P39023 (Uniprot-TrEMBL) | |
| RPL30(2-115) [cytosol] | Protein | P62888 (Uniprot-TrEMBL) | |
| RPL31 [cytosol] | Protein | P62899 (Uniprot-TrEMBL) | |
| RPL32 [cytosol] | Protein | P62910 (Uniprot-TrEMBL) | |
| RPL34 [cytosol] | Protein | P49207 (Uniprot-TrEMBL) | |
| RPL35 [cytosol] | Protein | P42766 (Uniprot-TrEMBL) | |
| RPL35A [cytosol] | Protein | P18077 (Uniprot-TrEMBL) | |
| RPL36 [cytosol] | Protein | Q9Y3U8 (Uniprot-TrEMBL) | |
| RPL36A [cytosol] | Protein | P83881 (Uniprot-TrEMBL) | |
| RPL37 [cytosol] | Protein | P61927 (Uniprot-TrEMBL) | |
| RPL37A [cytosol] | Protein | P61513 (Uniprot-TrEMBL) | |
| RPL38 [cytosol] | Protein | P63173 (Uniprot-TrEMBL) | |
| RPL39 [cytosol] | Protein | P62891 (Uniprot-TrEMBL) | |
| RPL3L(2-407) [cytosol] | Protein | Q92901 (Uniprot-TrEMBL) | |
| RPL4 [cytosol] | Protein | P36578 (Uniprot-TrEMBL) | |
| RPL41 [cytosol] | Protein | P62945 (Uniprot-TrEMBL) | |
| RPL5 [cytosol] | Protein | P46777 (Uniprot-TrEMBL) | |
| RPL6 [cytosol] | Protein | Q02878 (Uniprot-TrEMBL) | |
| RPL7 [cytosol] | Protein | P18124 (Uniprot-TrEMBL) | |
| RPL7A [cytosol] | Protein | P62424 (Uniprot-TrEMBL) | |
| RPL8 [cytosol] | Protein | P62917 (Uniprot-TrEMBL) | |
| RPL9 [cytosol] | Protein | P32969 (Uniprot-TrEMBL) | |
| RPLP0 [cytosol] | Protein | P05388 (Uniprot-TrEMBL) | |
| RPLP1(2-114) [cytosol] | Protein | P05386 (Uniprot-TrEMBL) | |
| RPLP2 [cytosol] | Protein | P05387 (Uniprot-TrEMBL) | |
| RPS10 [cytosol] | Protein | P46783 (Uniprot-TrEMBL) | |
| RPS11 [cytosol] | Protein | P62280 (Uniprot-TrEMBL) | |
| RPS12 [cytosol] | Protein | P25398 (Uniprot-TrEMBL) | |
| RPS13(2-151) [cytosol] | Protein | P62277 (Uniprot-TrEMBL) | |
| RPS14 [cytosol] | Protein | P62263 (Uniprot-TrEMBL) | |
| RPS15 [cytosol] | Protein | P62841 (Uniprot-TrEMBL) | |
| RPS15A [cytosol] | Protein | P62244 (Uniprot-TrEMBL) | |
| RPS16 [cytosol] | Protein | P62249 (Uniprot-TrEMBL) | |
| RPS17 [cytosol] | Protein | P08708 (Uniprot-TrEMBL) | |
| RPS18 [cytosol] | Protein | P62269 (Uniprot-TrEMBL) | |
| RPS19 [cytosol] | Protein | P39019 (Uniprot-TrEMBL) | |
| RPS2(2-293) [cytosol] | Protein | P15880 (Uniprot-TrEMBL) | |
| RPS20 [cytosol] | Protein | P60866 (Uniprot-TrEMBL) | |
| RPS21 [cytosol] | Protein | P63220 (Uniprot-TrEMBL) | |
| RPS23 [cytosol] | Protein | P62266 (Uniprot-TrEMBL) | |
| RPS24 [cytosol] | Protein | P62847 (Uniprot-TrEMBL) | |
| RPS25 [cytosol] | Protein | P62851 (Uniprot-TrEMBL) | |
| RPS26 [cytosol] | Protein | P62854 (Uniprot-TrEMBL) | |
| RPS27 [cytosol] | Protein | P42677 (Uniprot-TrEMBL) | |
| RPS27A(77-156) [cytosol] | Protein | P62979 (Uniprot-TrEMBL) | |
| RPS28 [cytosol] | Protein | P62857 (Uniprot-TrEMBL) | |
| RPS29 [cytosol] | Protein | P62273 (Uniprot-TrEMBL) | |
| RPS3 [cytosol] | Protein | P23396 (Uniprot-TrEMBL) | |
| RPS3A [cytosol] | Protein | P61247 (Uniprot-TrEMBL) | |
| RPS4X [cytosol] | Protein | P62701 (Uniprot-TrEMBL) | |
| RPS4Y1(2-263) [cytosol] | Protein | P22090 (Uniprot-TrEMBL) | |
| RPS5(1-204) [cytosol] | Protein | P46782 (Uniprot-TrEMBL) | |
| RPS6 [cytosol] | Protein | P62753 (Uniprot-TrEMBL) | |
| RPS7 [cytosol] | Protein | P62081 (Uniprot-TrEMBL) | |
| RPS8(2-208) [cytosol] | Protein | P62241 (Uniprot-TrEMBL) | |
| RPS9 [cytosol] | Protein | P46781 (Uniprot-TrEMBL) | |
| RPSA [cytosol] | Protein | P08865 (Uniprot-TrEMBL) | |
| Ran GTPase:GTP | Complex | REACT_6698 (Reactome) | |
| Ribonucleoprotein (RNP) Complex | Complex | REACT_9223 (Reactome) | |
| Ribonucleoprotein (RNP) Complex | Complex | REACT_9227 (Reactome) | |
| SA [plasma membrane] | Metabolite | CHEBI:21622 (ChEBI) | |
| SA | Metabolite | CHEBI:21622 (ChEBI) | |
| SEH1L-2 [nuclear envelope] | Protein | Q96EE3-2 (Uniprot-TrEMBL) | |
| SMC1A [nucleoplasm] | Protein | Q14683 (Uniprot-TrEMBL) | |
| SNRNP70 [nucleoplasm] | Protein | P08621 (Uniprot-TrEMBL) | |
| SNRPA [nucleoplasm] | Protein | P09012 (Uniprot-TrEMBL) | |
| SNRPD2 [nucleoplasm] | Protein | P62316 (Uniprot-TrEMBL) | |
| SNRPE [nucleoplasm] | Protein | P62304 (Uniprot-TrEMBL) | |
| SNRPF [nucleoplasm] | Protein | P62306 (Uniprot-TrEMBL) | |
| SNRPG [nucleoplasm] | Protein | P62308 (Uniprot-TrEMBL) | |
| SRRM1 [nucleoplasm] | Protein | Q8IYB3 (Uniprot-TrEMBL) | |
| SRSF1 [nucleoplasm] | Protein | Q07955 (Uniprot-TrEMBL) | |
| SRSF2 [nucleoplasm] | Protein | Q01130 (Uniprot-TrEMBL) | |
| SRSF3 [nucleoplasm] | Protein | P84103 (Uniprot-TrEMBL) | |
| SRSF5 [nucleoplasm] | Protein | Q13243 (Uniprot-TrEMBL) | |
| SRSF6 [nucleoplasm] | Protein | Q13247 (Uniprot-TrEMBL) | |
| SRSF7 [nucleoplasm] | Protein | Q16629 (Uniprot-TrEMBL) | |
| SRSF9 [nucleoplasm] | Protein | Q13242 (Uniprot-TrEMBL) | |
| SUGP1 [nucleoplasm] | Protein | Q8IWZ8 (Uniprot-TrEMBL) | |
| Segment 1 RNP | Complex | REACT_10624 (Reactome) | |
| Segment 2 RNP | Complex | REACT_10270 (Reactome) | |
| Segment 3 RNP | Complex | REACT_10968 (Reactome) | |
| Segment 4 RNP | Complex | REACT_10933 (Reactome) | |
| Segment 5 RNP | Complex | REACT_10746 (Reactome) | |
| Segment 6 RNP | Complex | REACT_10870 (Reactome) | |
| Segment 7 RNP | Complex | REACT_10503 (Reactome) | |
| Segment 8 RNP | Complex | REACT_10273 (Reactome) | |
| Sialic Acid Bound
Influenza A Viral Particle | Complex | REACT_10492 (Reactome) | |
| Sialic Acid Bound
Influenza A Viral Particle | Complex | REACT_9232 (Reactome) | |
| Spliceosomal E Complex | Complex | REACT_4545 (Reactome) | |
| TPR [nucleoplasm] | Protein | P12270 (Uniprot-TrEMBL) | |
| U1 snRNA [nucleoplasm] | Protein | V00590 (EMBL) | |
| U2AF1 [nucleoplasm] | Protein | Q01081 (Uniprot-TrEMBL) | |
| U2AF2 [nucleoplasm] | Protein | P26368 (Uniprot-TrEMBL) | |
| UBA52(77-128) [cytosol] | Protein | P62987 (Uniprot-TrEMBL) | |
| Viral Polymerase | Complex | REACT_9586 (Reactome) | Heterotrimeric influenza viral polymerase complex consisting of PB1, PB2, and PA; although capable of being imported into the nucleus independently, the three subunits of the influenza polymerase assemble in the nucleus to form a mature ternary polymerase complex that binds viral vRNA or cRNA (reviewed in Buolo et al., 2006). |
| Viral Proteins | Complex | REACT_9572 (Reactome) | |
| XPO1 [cytosol] | Protein | O14980 (Uniprot-TrEMBL) | |
| XPO1 [nucleoplasm] | Protein | O14980 (Uniprot-TrEMBL) | |
| XPO1 | Protein | O14980 (Uniprot-TrEMBL) | |
| YBX1 [nucleoplasm] | Protein | P67809 (Uniprot-TrEMBL) | |
| cRNP | Complex | REACT_9556 (Reactome) | Extended cRNA complexed with viral NP and trimeric polymerase. |
| p-S5-POLR2A [nucleoplasm] | Protein | P24928 (Uniprot-TrEMBL) | |
| palmitylated M2 Tetramer | Complex | REACT_10389 (Reactome) | |
| palmitylated M2 Tetramer | Complex | REACT_10582 (Reactome) | |
| palmitylated M2 [Golgi membrane] | Protein | P06821 (Uniprot-TrEMBL) | |
| palmitylated M2
[extracellular region] | Protein | P06821 (Uniprot-TrEMBL) | |
| palmitylated M2 [plasma membrane] | Protein | P06821 (Uniprot-TrEMBL) | |
| vRNA (Genomic):NP Complex | Complex | REACT_9729 (Reactome) | |
| vRNA (genomic) | Protein | REACT_9646 (Reactome) | |
| vRNA Transcription Complex | Complex | REACT_9896 (Reactome) | The 5' and 3' ends of the vRNA bound to the PB1 subunit of the viral RNA polymerase; PB2 bound to the methylated cap on a host pre-mRNA amino acids (Cianci, 1995; Brownlee, 2002; Honda, 1999). |
| vRNP Export Complex | Complex | REACT_9906 (Reactome) | |
| vRNP destined for Export | Complex | REACT_9574 (Reactome) | |
| vRNP:M1 for Export | Complex | REACT_9769 (Reactome) | |
| vRNP:M1:NEP:NP | Complex | REACT_9710 (Reactome) | |
| vRNP:M1:NEP | Complex | REACT_9569 (Reactome) | |
| vRNP | Complex | REACT_9584 (Reactome) | A three dimensional crystal structure of NP suggests that this molecule forms a trimer that binds viral RNA (Ye et al., 2006). Mutiple NP trimers complex vRNA or cRNA. |
| viral mRNA | Rna | REACT_9782 (Reactome) | |
| viral mRNA | Protein | REACT_9819 (Reactome) |
Annotated Interactions
| View all... |
| Source | Target | Type | Database reference | Comment |
|---|---|---|---|---|
| 80S ribosome | mim-catalysis | REACT_9514 (Reactome) | ||
| 80S ribosome | mim-catalysis | REACT_9524 (Reactome) | ||
| Acidified Influenza
A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | Arrow | REACT_6315 (Reactome) | ||
| Acidified Influenza
A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | REACT_6230 (Reactome) | |||
| Aminoacyl-tRNA | REACT_9514 (Reactome) | |||
| Aminoacyl-tRNA | REACT_9524 (Reactome) | |||
| CALR | Arrow | REACT_6177 (Reactome) | ||
| CANX | Arrow | REACT_6177 (Reactome) | ||
| Clathrin | Arrow | REACT_6262 (Reactome) | ||
| Cleaved HA Influenza A Viral Particle | REACT_6232 (Reactome) | |||
| Crm1:Ran GTPase:GDP | Arrow | REACT_6136 (Reactome) | ||
| DNAJC3 | Arrow | REACT_9514 (Reactome) | ||
| Elongated vRNA-mRNA Complex | Arrow | REACT_6210 (Reactome) | ||
| Elongated vRNA-mRNA Complex | REACT_6264 (Reactome) | |||
| GRSF1(?-?) | Arrow | REACT_9514 (Reactome) | ||
| Glycosylated NA Tetramer | Arrow | REACT_6225 (Reactome) | ||
| Glycosylated NA Tetramer | Arrow | REACT_6231 (Reactome) | ||
| Glycosylated NA Tetramer | Arrow | REACT_6273 (Reactome) | ||
| Glycosylated NA Tetramer | REACT_6225 (Reactome) | |||
| Glycosylated NA Tetramer | REACT_6273 (Reactome) | |||
| Glycosylated NA Tetramer | REACT_9947 (Reactome) | |||
| Glycosylated NA | Arrow | REACT_6181 (Reactome) | ||
| Glycosylated NA | REACT_6231 (Reactome) | |||
| Glycosylated and folded HA trimer | Arrow | REACT_6141 (Reactome) | ||
| Glycosylated and folded HA trimer | Arrow | REACT_6225 (Reactome) | ||
| Glycosylated and folded HA trimer | Arrow | REACT_6273 (Reactome) | ||
| Glycosylated and folded HA trimer | REACT_6187 (Reactome) | |||
| Glycosylated and folded HA trimer | REACT_6225 (Reactome) | |||
| Glycosylated and folded HA trimer | REACT_6273 (Reactome) | |||
| Glycosylated and folded HA | Arrow | REACT_6177 (Reactome) | ||
| Glycosylated and folded HA | REACT_6141 (Reactome) | |||
| Glycosylated,
palmitylated and folded HA trimer:Lipid Raft Complex | Arrow | REACT_10039 (Reactome) | ||
| Glycosylated,
palmitylated and folded HA trimer:Lipid Raft Complex | Arrow | REACT_6146 (Reactome) | ||
| Glycosylated,
palmitylated and folded HA trimer:Lipid Raft Complex | REACT_10039 (Reactome) | |||
| Glycosylated,
palmitylated and folded HA trimer | Arrow | REACT_6187 (Reactome) | ||
| Glycosylated,
palmitylated and folded HA trimer | REACT_10077 (Reactome) | |||
| Glycosylated,
palmitylated and folded HA trimer | REACT_6146 (Reactome) | |||
| Gycosylated NA Tetramer:Lipid Raft | Arrow | REACT_10039 (Reactome) | ||
| Gycosylated NA Tetramer:Lipid Raft | Arrow | REACT_9947 (Reactome) | ||
| Gycosylated NA Tetramer:Lipid Raft | REACT_10039 (Reactome) | |||
| Gycosylated NA Tetramer | REACT_10077 (Reactome) | |||
| H+ | Arrow | REACT_6230 (Reactome) | ||
| H+ | REACT_6315 (Reactome) | |||
| HA | Arrow | REACT_6309 (Reactome) | ||
| HA | REACT_6177 (Reactome) | |||
| HA | REACT_6309 (Reactome) | |||
| HSP90AA1 | Arrow | REACT_9428 (Reactome) | ||
| HSPA1A(2-641) | TBar | REACT_9407 (Reactome) | ||
| Host Derived Lipid
Bilayer Membrane Rich In Sphingolipids And Cholesterol | REACT_6193 (Reactome) | |||
| IPO5 | Arrow | REACT_9428 (Reactome) | ||
| Influenza A Viral
Envelope Inserted Into The Endocytic Vesicle Membrane | Arrow | REACT_6230 (Reactome) | ||
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | Arrow | REACT_6176 (Reactome) | ||
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | REACT_6315 (Reactome) | |||
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane With An Open Pore | mim-catalysis | REACT_6315 (Reactome) | ||
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane | Arrow | REACT_6180 (Reactome) | ||
| Influenza A Viral
Particle Docked At The Endocytic Vesicle Membrane | REACT_6176 (Reactome) | |||
| Influenza A Viral
Particle With A Fusion Competent HA2 | Arrow | REACT_6219 (Reactome) | ||
| Influenza A Viral
Particle With A Fusion Competent HA2 | REACT_6180 (Reactome) | |||
| Influenza A Viral Particle | Arrow | REACT_6262 (Reactome) | ||
| Influenza A Viral Particle | Arrow | REACT_6348 (Reactome) | ||
| Influenza A Viral Particle | REACT_6219 (Reactome) | |||
| Influenza cRNA (complete) | Arrow | REACT_9438 (Reactome) | ||
| Initiated cRNA-vRNA Complex | Arrow | REACT_9487 (Reactome) | ||
| Initiated cRNA-vRNA Complex | REACT_9438 (Reactome) | |||
| Initiated vRNA
Transcription Complex | Arrow | REACT_6239 (Reactome) | ||
| Initiated vRNA
Transcription Complex | REACT_6210 (Reactome) | |||
| Initiated vRNA-cRNA Complex | Arrow | REACT_9513 (Reactome) | ||
| Initiated vRNA-cRNA Complex | REACT_9404 (Reactome) | |||
| Intracellular assembly complex | Arrow | REACT_10077 (Reactome) | ||
| Intracellular assembly complex | REACT_6193 (Reactome) | |||
| KPNA1 | Arrow | REACT_6164 (Reactome) | ||
| KPNA1 | REACT_6138 (Reactome) | |||
| KPNB1 | Arrow | REACT_6164 (Reactome) | ||
| KPNB1 | REACT_6322 (Reactome) | |||
| Lipid Raft | REACT_6146 (Reactome) | |||
| Lipid Raft | REACT_6271 (Reactome) | |||
| Lipid Raft | REACT_9947 (Reactome) | |||
| M1 mRNA | REACT_9402 (Reactome) | |||
| M1 | Arrow | REACT_6137 (Reactome) | ||
| M1 | Arrow | REACT_6230 (Reactome) | ||
| M1 | REACT_10077 (Reactome) | |||
| M1 | REACT_6137 (Reactome) | |||
| M1 | REACT_9407 (Reactome) | |||
| M2 Tetramer | Arrow | REACT_10123 (Reactome) | ||
| M2 Tetramer | Arrow | REACT_6225 (Reactome) | ||
| M2 Tetramer | Arrow | REACT_6273 (Reactome) | ||
| M2 Tetramer | REACT_10133 (Reactome) | |||
| M2 Tetramer | REACT_6225 (Reactome) | |||
| M2 Tetramer | REACT_6273 (Reactome) | |||
| M2 mRNA | Arrow | REACT_9402 (Reactome) | ||
| M2 mRNA | Arrow | REACT_9528 (Reactome) | ||
| M2 mRNA | REACT_9528 (Reactome) | |||
| M2 | Arrow | REACT_10095 (Reactome) | ||
| M2 | REACT_10095 (Reactome) | |||
| M2 | REACT_10123 (Reactome) | |||
| Mature intronless
transcript derived mRNA with m7G cap removed | Arrow | REACT_6239 (Reactome) | ||
| Mature intronless
transcript derived mRNA | REACT_6142 (Reactome) | |||
| NA | Arrow | REACT_10062 (Reactome) | ||
| NA | REACT_10062 (Reactome) | |||
| NA | REACT_6181 (Reactome) | |||
| NA | mim-catalysis | REACT_6348 (Reactome) | ||
| NEP/NS2 | Arrow | REACT_6230 (Reactome) | ||
| NEP/NS2 | REACT_10077 (Reactome) | |||
| NEP/NS2 | REACT_6303 (Reactome) | |||
| NP:Lipid Raft | Arrow | REACT_10039 (Reactome) | ||
| NP:Lipid Raft | Arrow | REACT_6271 (Reactome) | ||
| NP:Lipid Raft | REACT_10039 (Reactome) | |||
| NP | Arrow | REACT_6142 (Reactome) | ||
| NP | Arrow | REACT_9485 (Reactome) | ||
| NP | Arrow | REACT_9513 (Reactome) | ||
| NP | REACT_10077 (Reactome) | |||
| NP | REACT_6271 (Reactome) | |||
| NP | REACT_9404 (Reactome) | |||
| NP | REACT_9438 (Reactome) | |||
| NP | REACT_9490 (Reactome) | |||
| NS1 mRNA | REACT_9402 (Reactome) | |||
| NS1 | Arrow | REACT_9514 (Reactome) | ||
| NS2 mRNA | Arrow | REACT_9402 (Reactome) | ||
| NS2 mRNA | Arrow | REACT_9528 (Reactome) | ||
| NS2 mRNA | REACT_9528 (Reactome) | |||
| NTP | REACT_6210 (Reactome) | |||
| NTP | REACT_9404 (Reactome) | |||
| NTP | REACT_9438 (Reactome) | |||
| NTP | REACT_9513 (Reactome) | |||
| Nuclear Pore Complex (NPC) | Arrow | REACT_6136 (Reactome) | ||
| Nuclear Pore Complex (NPC) | Arrow | REACT_6289 (Reactome) | ||
| PA | REACT_10077 (Reactome) | |||
| PA | REACT_9428 (Reactome) | |||
| PA | REACT_9485 (Reactome) | |||
| PB1 mRNA | REACT_9524 (Reactome) | |||
| PB1-F2 | Arrow | REACT_9524 (Reactome) | ||
| PB1 | REACT_10077 (Reactome) | |||
| PB1 | REACT_9428 (Reactome) | |||
| PB1 | REACT_9485 (Reactome) | |||
| PB2 | REACT_10077 (Reactome) | |||
| PB2 | REACT_9428 (Reactome) | |||
| PB2 | REACT_9485 (Reactome) | |||
| Pi | Arrow | REACT_6136 (Reactome) | ||
| REACT_10039 (Reactome) | Once processed, the viral proteins are transported from the golgi apparatus to the plasma membrane. | |||
| REACT_10062 (Reactome) | The integral membrane protein NA is synthesized on membrane-bound ribosomes and subsequently transported across the ER where it is folded and glycosylated. Subsequently NA is assembled into a tetramer. | |||
| REACT_10077 (Reactome) | As influenza viruses bud from the plasma membrane of infected cells, complete virions are not seen inside cells. In polarized epithelial cells, assembly and budding of influenza occurs from the apical plasma membrane (Schmitt, 2004). For efficient assembly, all virion components must accumulate at the budding site, and it is believed that the viral glycoprotein accumulation determines the site of virus assembly and budding (Nayak, 2004). M1 is thought to be the bridge between the envelope glycoproteins and the RNPs for assembly (Schmitt, 2004). M2 is also required, because if it is not present RNPs are not packaged into budding virions (McCown, 2005), however it role is not known. | |||
| REACT_10095 (Reactome) | The integral membrane protein M2 is synthesized on membrane-bound ribosomes and subsequently transported across the ER, where it is folded and assembled into a tetramer. | |||
| REACT_10123 (Reactome) | The M2 from influenza A virus is a 97-residue protein with a single transmembrane helix that associates to form a tetramer in the endoplasmic reticulum (Salom et al, 2000). A 15-20-residue segment C-terminal to the membrane-spanning region has been postulated to aid in the stabilization of the tetrameric assembly (Kochendoerfer et al 1999). | |||
| REACT_10133 (Reactome) | Palmitoylation of influenza A M2 occurs in the ER, or cis golgi network, following tetramerisation. The palmitoylation reaction proceeds via a labile thioester type bond at a specific residue of M2 (Sugrue et al., 1990). | |||
| REACT_6136 (Reactome) | Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, are shuttled through the nuclear pore into the cytoplasm (Martin, 1991; O'Neill, 1998; Buolo, 2006). This mechanism may resemble export of HIV-1 ribonucleoprotein, where the HIV-1 Rev export protein interacts with CRM1 (Askjaer, 1998). A number of cofactors are implicated in CRM1-mediated export, including the small GTPase Ran, Ran-binding proteins 1 and 3, and a guanine nucleotide exchange factor (Nilsson, 2001; Nemergut, 2002; Petosa, 2004). Ternary CRM1-cofactor-cargo complexes likely interact transiently with nuclear pore proteins (nucleoporins) as they traverse the pore (reviewed in Suntharalingam, 2003). RanGTP is hydrolyzed to RanGDP in the cytoplasm, an activity that can be stimulated by NEP/NS2 (Akarsu, 2003). Influenza infection activates Raf/MEK/ERK signaling, which is necessary for NEP/NS2-mediated export of viral RNP (Pleschka, 2001; Marjuki, 2006). Influenza vRNP complexes released into the cytoplasm do not re-enter the nucleus, as they are thought to remain bound by M1, preventing re-import (Martin, 1991). It has been suggested that M1 binding of zinc cations could distinguish M1 bound to the vRNP from polymerized, matrix M1 present in nascent virions (Elster, 1994). | |||
| REACT_6137 (Reactome) | There is evidence for the association of M1 with lipid rafts in influenza infected cells, whereas M1 expressed alone remains soluble (Ali et al., 2000; Zhang and Lamb, 1996), suggesting association of M1 with other viral proteins in targetting to the cell membrane. Coexpression of HA and NA together with M1 has been shown to promote raft association of M1. This association requires the TMD and cytoplasmic tails of HA and NA (Ali et al, 2000; Zhang et al, 2000). This is consistent with M1 becoming associated with HA and NA during their passage through the exocytic pathway to raft domains in the apical membrane. alternatively M1 may use the cytoskeleton to reach the virus assembly site, as M1 interacts with cytoskeletal components (Alvalos et al., 1997). The M1 interaction depends on the presence of RNP and is most likely mediated by direct binding of F-actin by NP (Digard et al., 1999). | |||
| REACT_6138 (Reactome) | The eight influenza virus genome segments never exist as naked RNA but are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA, creating the distinctive panhandle structure. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Here karyopherin alpha recognizes the RNP. | |||
| REACT_6141 (Reactome) | Trimerisation of the fully folded and fully oxidised HA monomer is thought to occur in the endoplasmic reticulum and ERGIC compartment, following dissociation of HA from calnexin. Trimerisation is generally thought to be the final step in HA maturation occurring in the endoplasmic reticulum before transport to the Golgi apparatus, although Yewdell et al (1988) provide data suggesing that trimerisation may occur within the Golgi. | |||
| REACT_6142 (Reactome) | The 5' end of the vRNA associates with a binding site on the PB1 subunit of the viral RNA polymerase, distinct from the 3' vRNA binding site, which is subsequenty bound forming a loop. These binding events set off allosteric conformational changes in the trimeric polymerase complex that induce PB2 binding of the methylated cap on a host pre-mRNA (Plotch, 1981; Cianci, 1995; Li, 1998; Brownlee, 2002; Kolpashchikov, 2004). PB2 amino acids 242-282 and 538-577 are involved in cap binding (Honda, 1999). Direct or indirect interaction with active, transcribing host RNA polymerase II is thought to supply host mRNA for the caps (Bouloy, 1978; Engelhardt, 2005). | |||
| REACT_6146 (Reactome) | Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004). | |||
| REACT_6164 (Reactome) | Once the viral RNP and heterodimeric karyopherin complex has been transported into the nucleus the RNP dissasociates from the heterodimeric karyopherins. | |||
| REACT_6176 (Reactome) | The concerted structural change of several hemagglutinin molecules opens a pore through which the viral RNP will be able to pass into the host cell cytosol. | |||
| REACT_6177 (Reactome) | The ectodomain of HA is translocated into the ER lumen, where it undergoes a series of folding events mediated by the formation of disulfide bonds and glycosylation reactions. The formation of a discrete intermediate species of highly folded monomeric protein preceeds trimerisation. The folding process is efficient and rapid, with greater than 90% of the protein trafficked to the golgi apparatus; and mature HA0 subunits appearing in a matter of a few minutes. Calnexin and calreticulin have been identified as cellular lectins which interact transiently with newly synthesized HA by attaching to partially trimmed N-linked oligosaccharides (Herbert et al., 1997), facilitating correct folding of the HA molecule. | |||
| REACT_6180 (Reactome) | The fusion peptide of its HA2 subunit interacts with the endosome membrane. The transmembrane domain of the HA2 is inserted into the viral membrane and the fusion peptide is inserted into the endosomal membrane. In the acidic pH structure of HA the two ends of the HA complex are in juxtaposition. | |||
| REACT_6181 (Reactome) | Glycosylation of NA occurs within the endoplasmic reticulum and is believed to be neccessary for proper tetramerization of the NA dimers. Sugar residues become attached to four of the five potential glycosylation sites in the head of N1 neuraminidase (Hausman et al., 1997). | |||
| REACT_6187 (Reactome) | The hemagglutinin of influenza virus is palmitoylated with long-chain fatty acids. Palmitoylation of HA is believed to occur in the cis golgi network (Veit 1993), shortly after trimerisation of the molecule, and before cleavage of the HA into HA1 and HA2. HA is palmitoylated through thioester linkages at three cysteine residues located in the cytoplasmic domain and at the carboxy-terminal end of the transmembrane region. Lack of acylation has no obvious influence on the biological activities of HA. | |||
| REACT_6193 (Reactome) | The final step in the budding process is the fusion of the lipid membrane surrounding the virion core, producing an extracellular enveloped virus particle. | |||
| REACT_6194 (Reactome) | Virus NEP/NS2 interacts with human CRM1 (hCRM1), possibly dependent on a nuclear export signal (NES) motif in the NEP/NS2 N-terminal region (O'Neill, 1998; Neumann, 2000). The CRM1/exportin-1 pathway is a cellular mechanism for nuclear export, with CRM1 interacting with the Ran small GTPase and a cargo molecule's leucine-rich NES (Fukuda, 1997; Petosa, 2004). Leptomycin B, which specifically inhibits hCRM1, blocks export of viral RNP (Elton, 2001; Ma, 2001; Watanabe, 2001). Thus, NEP/NS2 interaction with cellular nuclear export machinery is essential for nuclear export of vRNP complexes and influenza virus release. A role for NP protein interaction with export machinery has also been proposed (Elton, 2001). | |||
| REACT_6210 (Reactome) | Catalyzed by the RNA polymerase activity of the viral PB1 subunit, an mRNA complementary to the bound vRNA is synthesized (Plotch, 1977). PA and PB2 move down the growing mRNA in complex with PB1, with PB2 possibly dissociating from the cap (Braam, 1983). However, the 5’ end of the vRNA may remain bound during elongation as the template is threaded through in a 3’ to 5’ direction until a polyadenylation signal is encountered (Poon, 1998; Zheng, 1999). | |||
| REACT_6219 (Reactome) | The low pH of the endosome causes the viral HA (hemagglutinin) to undergo a structural change which frees the fusion peptide of its HA2 subunit. | |||
| REACT_6225 (Reactome) | Viral proteins are packaged into a golgi apparatus bound transport vesicle. | |||
| REACT_6230 (Reactome) | The influx of H+ ions into the virion disrupts protein-protein interactions, resulting in the release of the viral RNP from the viral matrix (M1) protein. The uncoating process is complete with the appearance of free RNP complexes in the cytosol. | |||
| REACT_6231 (Reactome) | Tetramerisation of the NA occurs in the ER following an initial dimerisation step. Tetramerisation is believed to be dependant on glycosylation of the NA molecules | |||
| REACT_6232 (Reactome) | Influenza viruses bind via their surface HA (hemagglutinin) to sialic acid in alpha 2,3 or alpha 2,6 linkage with galactose on the host cell surface. Sialic acid in 2,6 linkages is characteristic of human cells while 2,3 linkages are characteristic of avian cells. The specificity of influenza HA for sialic acid in alpha 2,6 or alpha 2,3 linkages is a feature restricting the transfer of influenza viruses between avian species and humans. This species barrier can be overcome, however. Notably, passaged viruses adapt to their host through mutation in the receptor binding site of the viral HA gene. | |||
| REACT_6239 (Reactome) | The host cell mRNA bound to viral RNA polymerase PB2 subunit is cleaved by the viral RNA polymerase PB1 subunit's endonuclease activity, and the capped 5' end plus 10-13 nucleotides of the host mRNA remains bound to the polymerase complex (Plotch, 1981; Krug, 1981; Hagen, 1994; Cianci, 1995, Li, 1998; Li, 2001). Viral mRNA may be protected against cap-snatching by the polymerase complex itself, which tightly binds capped viral mRNA (Shih, 1996). A guanine residue, complementary to a cytosine in the vRNA, is added to the host-derived cap, catalyzed by the RNA polymerase activity of the PB1 viral RNA polymerase subunit (Beaton, 1981; Toyoda, 1986). | |||
| REACT_6262 (Reactome) | Virus particles bound to the cell surface can be internalized by four mechanisms. Most internalization appears to be mediated by clathrin-coated pits. | |||
| REACT_6264 (Reactome) | A poly-uridine sequence motif, consisting in most cases of 5-7 U residues, abuts the "panhandle" duplex structure in the vRNA; this sequence is approximately 16 nucleotides from the 5' end of this RNA duplex structure within the vRNA promoter. Encountering this signal, the viral RNA polymerase stutters, leading to the synthesis of a poly-A tail on the viral mRNA (Robertson, 1981; Luo, 1991; Li,1994; Poon, 1998; Zheng et al. 1999). | |||
| REACT_6271 (Reactome) | There is evidence that NP alone is intrinsically targeted to the apical plasma membrane and associates with lipid rafts in a cholesterol-dependent manner, which suggests that RNPs could reach the assembly site independently of the other viral components. | |||
| REACT_6273 (Reactome) | Once the tranport vesicle arrives at the golgi apparatus, it docks and dumps its contents into the golgi lumen. | |||
| REACT_6289 (Reactome) | These RNPs (10-20nm wide) are too large to passively diffuse into the nucleus and therefore, once released from an incoming particle they must rely on the active import mechanism of the host cell nuclear pore complex (NPC). Once the RNP heterodimeric karyopherin complex docks at the NPC, it is transported into the nucleus. | |||
| REACT_6303 (Reactome) | Structural characterization of NEP/NS2 suggests that acidic residues in the C-terminus of NEP/NS2 bind to M1, with Trp78 critical for interaction (Ward, 1995; Yasuda, 1993; Akarsu, 2003). | |||
| REACT_6309 (Reactome) | The integral membrane protein HA is synthesized on membrane-bound ribosomes and subsequently transported across the endoplasmic reticulum, where it is folded, glycosylated, and assembled into a trimer. | |||
| REACT_6315 (Reactome) | The uncoating of influenza viruses in endosomes is blocked by changes in pH caused by weak bases (e.g. ammonium chloride and chloroquine) or ionophores (e.g. monensin). Effective uncoating is also dependent on the presence of the viral M2 ion channel protein. Early on it was recognized that amantadine and rimantadine inhibit replication immediately following virus infection. Later it was found that the virus-associated M2 protein allows the influx of H+ ions from the endosome into the virion. This disrupts protein-protein interactions, resulting in the release of viral RNP free of the viral matrix (M1) protein. Amantadine and rimantadine have been shown to block the ion channel activity of the M2 protein and thus uncoating. | |||
| REACT_6322 (Reactome) | The eight influenza virus genome segments are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Once the NLS is recognized by karyopherin alpha the karyopherin beta subunit joins the complex. | |||
| REACT_6336 (Reactome) | The random incorporation model as its name suggests proposes that there is no selection at all on which vRNPs are packaged. It is assumed that each vRNP has equal probability of being packaged, and that if enough vRNPS are packaged a particular percentage of budding virions will receive at least one copy of each genome segment. This model is supported by evidence that infectious virions may possess more than eight vRNPs assuring the presence of a full complement of eight vRNPs in a significant percentage of virus particles. Mathematical analysis of packaging suggested that twelve RNA segments would need to be packaged in order to obtain approximately 10% of virus particles that are fully infectious (Enami, 1991), a number that is compatible with experimental data (Donald, 1954). Due to the low amount of RNA per virion (estimated at 1-2% w/w), enumeration of the precise number of RNAs packaged in a virion is difficult. | |||
| REACT_6348 (Reactome) | The release of influenza virus particles after seperation of the virus and infected cell membrane is an active process. During the budding process, HA on the surface of the newly budding virion binds to cell surface molecules containing sialic acid residues as seen during attachment. The NA glycoproteins neuraminidase activity is essential to cleave the link between the HA and sialic acid on the surface of the host cell from which the budding virus is emeging from. Thus the NA mediated cleavage of sialic acid residues terminally linked to glycoproteins and glycolipids is the final step in releasing the virus particle from the host cell. This essential role of NA in release of virus particle has been demonstrated with the use of NA inhibitors (Palese, 1976; Luo, 1999; Garman, 2004), ts NA mutant viruses (Palese, 1974) and with viruses lacking NA activity (Liu, 1995). In all cases, viruses remain bound to the cell surface in clumps in the absence of NA enzymatic activity, resulting in loss of infectivity. Addition of exogenous sialidase results in virus release and recovery of infectivity. The sialidase activity of the NA is also important for removing sialic acid from the HA on virus particles, if this is not removed, virus particles aggregate. | |||
| REACT_9402 (Reactome) | The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Alternately spliced mRNA transcribed from M and NS vRNA segments 7 and 8, producing the spliced mRNA for M2 and NEP/NS2, respectively, are thought to be coupled to the cellular splicing and export mechanisms (Lamb, 1980; Lamb, 1981; Chen, 2000; Li, 2001). As segments 7 and 8 each encode two proteins, splicing must be regulated allowing for alternative mRNAs, with the spliced products in the minority (approximately 10%). M1 splicing may be regulated by the viral polymerase and the cellular SR splicing protein SF2/ASF (Shih, 1995; Shih, 1996); while NS1 splicing appears to be regulated by the viral mRNA intrinsically (Alonso-Caplen, 1991; Valcarel, 1991). | |||
| REACT_9404 (Reactome) | Virion vRNP is capable of synthesizing cRNA immediately following entry into the cell nucleus (Vreede, 2006). The PB1 subunit principally catalyzes extension (Nakagawa, 1996). However, cRNA does not accumulate until later in the infection process, possiby requiring NP and the trimeric polymerase for stabilization (Vreede, 2004). The vRNA template is released. | |||
| REACT_9407 (Reactome) | M1 protein binds to viral RNP through its C-terminal domain (Baudin, 2001). The influenza M1 protein accumulates in the infected cell nucleus through a nuclear localization signal (NLS) RKLKR (residues 101-105) in its N-terminus (Ye, 1999). A host cell protein, HSP70, is thought to inhibit M1 binding at nonpermissive temperatures (Hirayama et al., 2004). | |||
| REACT_9428 (Reactome) | The mature ternary influenza viral polymerase complex consists of PB1, PB2, and PA. The N-terminus of PB1 (residues 1-48) interacts with PB2, and amino acids 506-659 in PB1 interact with the PA subunit (Gonzalez, 1996; Perez, 2001). Although monomeric PB1, PB2 and PA, as well as PB1-PB2 and PB1-PA dimers are likely to exist in infected cells, it is believed that most of the polymerase proteins are assembled into the trimeric PB1-PB2-PA complex (Detjen, 1987). Newly synthesized subunits of the polymerase are imported into the nucleus through nuclear localization signals (NLS), which interact with cellular importin family proteins (Jones, 1986; Buolo, 2006). Importin beta-3 (Ran binding protein 5) facilitates nuclear import of PB1 and a PB1-PA dimer (Deng, 2006); coexpression of PA with PB1 was shown to enhance the import of PB1 (Fodor, 2004). A PB1-PB2 dimer has been found to interact with the molecular chaperone heat shock protein 90 (HSP90) to facilitate import (Naito, 2007). The three subunits assembled in the nucleus form a mature ternary polymerase complex that binds viral vRNA or cRNA (Jones, 1986; Buolo, 2006). | |||
| REACT_9438 (Reactome) | vRNA is synthesized from the complementary cRNA strand by the trimeric polymerase complex, and bound by free NP protein (Honda, 1988; Mikulasova, 2000; Neumann, 2004). The PB1 subunit, with PA, catalyzes extension (Nakagawa, 1996). The cRNA is released. | |||
| REACT_9485 (Reactome) | The nascent vRNP complexes, one for each gene segment, contain the negative-sense viral RNA and polymerase proteins (PB1, PB2, PA, and NP). In a model using negative-sense viral RNP reconstituted from transfected cells, there are multiple NP complexes and one polymerase complex arranged along a closed vRNA loop (Area et al., 2004). The three-dimensional structure of NP has revealed that three NP molecules form a stable trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein (Ye, 2006), with the viral RNA wrapping around the outside of the complex. Viral RNA from purified virions is present in an RNase-sensitive complex with NP and PB1, PB2, and PA, consistent with this structural model (Baudin et al, 1994; Ruigrok et al., 1995; Klumpp et al., 1997). It is not clear what controls the fate of vRNP, whether it is destined to become a template for transcription, for replication, or for export into the cytoplasm for packaging into virions at the plasma membrane, nor how distinct sub-nuclear localization and NP distribution at the nuclear matrix might mark, or polarize, a vRNP for export (Elton, 2005; Takizawa et al., 2006). | |||
| REACT_9487 (Reactome) | Initiation of synthesis of the viral genomic RNA (vRNA) is thought to require hairpin (or panhandle/corkscrew) RNA loop structures formed by both the 5' and 3' ends of the cRNA (Pritlove, 1995; Crow, 2004; Park, 2003; Deng, 2006). The cRNA promoter has a similar structure to the vRNA promoter, but slight sequence differences are believed to result in a stronger cRNA promoter. As with the vRNA promoter, the polymerase is thought to first bind to the 5' end of the cRNA, then to the 3' end, and subsequently initiate RNA synthesis. | |||
| REACT_9490 (Reactome) | Viral genomic RNA (vRNA) and complementary RNA (cRNA) are likely bound by the influenza nucleoprotein (NP) immediately upon synthesis. Although two nuclear localization signals have been mapped in the NP, an unconventional N-terminal NLS and a bipartite NLS within amino acids 198-216 (Wang, 1997; Neumann, 1997; Ozawa, 2007), the crystal structure of the NP suggests that only the unconventional NLS is exposed and can be used as a functional NLS (Ye, 2006). This unconvenetional NLS interacts with importins alpha-1 and -2 (Cros et al., 2005; Wang et al., 1997; Buolo et al., 2006). The three-dimensional structure of NP has revealed that NP molecules associate as a trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein; the viral RNA likely wraps around the outside of the complex (Ye, 2006). | |||
| REACT_9513 (Reactome) | Viral vRNA, complexed with NP protein, is bound by the trimeric viral polymerase complex in a stable secondary structure-dependent manner, referred to as a panhandle, fork or cork-screw (Fodor, 1994; Brownlee, 2002; Park, 2003; Crow, 2004). This RNA structure is made of both the 5’ and 3' ends of the vRNA. The polymerase is thought to first bind the 5' end of the vRNA and then the 3' end. Synthesis of cRNA initiates without a host cell methylated RNA cap as a primer (Beaton, 1986; Galarza, 1996; Deng, 2006; Engehardt, 2006). | |||
| REACT_9514 (Reactome) | Spliced and unspliced viral mRNA exported into the cytoplasm are translated by the host cell ribosomal translation machinery (reviewed in Kash, 2006). At least ten viral proteins are synthesized: HA, NA, PB1, PB2, PA, NP, NS1, NEP/NS2 (from spliced NS mRNA), M1, and M2 (from spliced M mRNA). The abundance of each of these proteins is thought to be controlled by differential mRNA abundances and stability (Tekamp, 1980; Hatada, 1989). As the localization of the nascent polypeptides is different between viral proteins with transmembrane domains (HA, NA and M2, which translocate to the ER and are transported through the Golgi to the plasma membrane) and soluble viral proteins (such as NP, the polymerase subunits, and NS1), mechanisms linking the translation of particular viral mRNA with subsequent protein localization rely on signal sequences recognized by the cell. | |||
| REACT_9524 (Reactome) | For most influenza A strains (such as PR8), the PB1 mRNA segment produces a second protein, PB1-F2, from the +1 open reading frame (Chen, 2001). PB1-F2 is a pro-apoptotic, mitochondria-localized protein (Chen, 2001; Gibbs, 2003) that oligomerizes (Bruns, 2007) and sensitizes cells to death in concert with the mitochondrial ANT3 and VDAC proteins (Zamarin, 2005). | |||
| REACT_9528 (Reactome) | In the cases of spliced, polyadenylated mRNA transcribed from M (segment 7) and NS (segment 8) vRNA templates (producing the spliced mRNA for M2 and NS2/NEP, respectively), export may be coupled to aspects of the cellular splicing and export mechanisms (Chen, 2000; Alonso-Caplan et al, 1992; Amorim, 2006). Simultaneously, the export of cellular mRNA appear to be inhibited by the viral NS1 protein, which binds to the cellular cleavage and polyadenylation specificity factor (CPSF), preventing polyadenylation and completion of pre-mRNA processing (Nemerof et al., 1998; Fortes, 1994; Lu, 1994; Li, 2001). | |||
| REACT_9529 (Reactome) | The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Capped viral mRNAs are selectively exported from the host cell nucleus through a currently unclear mechanism that may rely on components of the host cell mRNA export machinery (Chen, 2000; Engelhardt, 2006). Polyadenylation of viral mRNA appears be required for influenza mRNA export (Poon, 2000). A coupling of viral mRNA export with cellular pre-mRNA processing complexes, recruited by phosphorylation of host RNA polymerase II C-terminal domain which interacts with the viral polymerase (Engelhardt, 2005), has been proposed as controlling the export of a subset (M1, HA, and NS1, but not NP) of viral mRNA from the nucleus (Amorim, 2007). | |||
| REACT_9947 (Reactome) | Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004). | |||
| RNA Polymerase II
(phosphorylated):TFIIF:capped pre-mRNA | Arrow | REACT_6142 (Reactome) | ||
| RNP
Complex:Karyopherin alpha | Arrow | REACT_6138 (Reactome) | ||
| RNP
Complex:Karyopherin alpha | REACT_6322 (Reactome) | |||
| RNP pre-assembly complex | Arrow | REACT_6336 (Reactome) | ||
| RNP pre-assembly complex | REACT_10077 (Reactome) | |||
| RNP:Karyopherin
alpha:Karyopherin beta complex | Arrow | REACT_6289 (Reactome) | ||
| RNP:Karyopherin
alpha:Karyopherin beta complex | Arrow | REACT_6322 (Reactome) | ||
| RNP:Karyopherin
alpha:Karyopherin beta complex | REACT_6164 (Reactome) | |||
| RNP:Karyopherin
alpha:Karyopherin beta complex | REACT_6289 (Reactome) | |||
| Ran GTPase:GTP | REACT_6136 (Reactome) | |||
| Ribonucleoprotein (RNP) Complex | Arrow | REACT_6164 (Reactome) | ||
| Ribonucleoprotein (RNP) Complex | Arrow | REACT_6230 (Reactome) | ||
| Ribonucleoprotein (RNP) Complex | REACT_6138 (Reactome) | |||
| SA | Arrow | REACT_6262 (Reactome) | ||
| SA | REACT_6193 (Reactome) | |||
| SA | REACT_6232 (Reactome) | |||
| Segment 1 RNP | REACT_6336 (Reactome) | |||
| Segment 2 RNP | REACT_6336 (Reactome) | |||
| Segment 3 RNP | REACT_6336 (Reactome) | |||
| Segment 4 RNP | REACT_6336 (Reactome) | |||
| Segment 5 RNP | REACT_6336 (Reactome) | |||
| Segment 6 RNP | REACT_6336 (Reactome) | |||
| Segment 7 RNP | REACT_6336 (Reactome) | |||
| Segment 8 RNP | REACT_6336 (Reactome) | |||
| Sialic Acid Bound
Influenza A Viral Particle | Arrow | REACT_6193 (Reactome) | ||
| Sialic Acid Bound
Influenza A Viral Particle | Arrow | REACT_6232 (Reactome) | ||
| Sialic Acid Bound
Influenza A Viral Particle | REACT_6262 (Reactome) | |||
| Sialic Acid Bound
Influenza A Viral Particle | REACT_6348 (Reactome) | |||
| Viral Polymerase | Arrow | REACT_6264 (Reactome) | ||
| Viral Polymerase | Arrow | REACT_9404 (Reactome) | ||
| Viral Polymerase | Arrow | REACT_9428 (Reactome) | ||
| Viral Polymerase | Arrow | REACT_9438 (Reactome) | ||
| Viral Polymerase | REACT_6142 (Reactome) | |||
| Viral Polymerase | REACT_9487 (Reactome) | |||
| Viral Polymerase | REACT_9513 (Reactome) | |||
| Viral Polymerase | mim-catalysis | REACT_6210 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_6239 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_6264 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_9404 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_9438 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_9487 (Reactome) | ||
| Viral Polymerase | mim-catalysis | REACT_9513 (Reactome) | ||
| Viral Proteins | Arrow | REACT_9514 (Reactome) | ||
| XPO1 | REACT_6194 (Reactome) | |||
| cRNP | Arrow | REACT_9404 (Reactome) | ||
| cRNP | Arrow | REACT_9438 (Reactome) | ||
| cRNP | REACT_9487 (Reactome) | |||
| palmitylated M2 Tetramer | Arrow | REACT_10039 (Reactome) | ||
| palmitylated M2 Tetramer | Arrow | REACT_10133 (Reactome) | ||
| palmitylated M2 Tetramer | REACT_10039 (Reactome) | |||
| palmitylated M2 Tetramer | REACT_10077 (Reactome) | |||
| vRNA (Genomic):NP Complex | Arrow | REACT_6264 (Reactome) | ||
| vRNA (Genomic):NP Complex | Arrow | REACT_9404 (Reactome) | ||
| vRNA (Genomic):NP Complex | Arrow | REACT_9438 (Reactome) | ||
| vRNA (Genomic):NP Complex | Arrow | REACT_9490 (Reactome) | ||
| vRNA (Genomic):NP Complex | REACT_6142 (Reactome) | |||
| vRNA (Genomic):NP Complex | REACT_9513 (Reactome) | |||
| vRNA (genomic) | REACT_9490 (Reactome) | |||
| vRNA Transcription Complex | Arrow | REACT_6142 (Reactome) | ||
| vRNA Transcription Complex | REACT_6239 (Reactome) | |||
| vRNP Export Complex | Arrow | REACT_6194 (Reactome) | ||
| vRNP Export Complex | REACT_6136 (Reactome) | |||
| vRNP destined for Export | Arrow | REACT_9485 (Reactome) | ||
| vRNP destined for Export | REACT_9407 (Reactome) | |||
| vRNP:M1 for Export | Arrow | REACT_9407 (Reactome) | ||
| vRNP:M1 for Export | REACT_6303 (Reactome) | |||
| vRNP:M1:NEP:NP | Arrow | REACT_6136 (Reactome) | ||
| vRNP:M1:NEP | Arrow | REACT_6303 (Reactome) | ||
| vRNP:M1:NEP | REACT_6194 (Reactome) | |||
| vRNP | REACT_9485 (Reactome) | |||
| viral mRNA | Arrow | REACT_6264 (Reactome) | ||
| viral mRNA | Arrow | REACT_9529 (Reactome) | ||
| viral mRNA | REACT_9514 (Reactome) | |||
| viral mRNA | REACT_9529 (Reactome) |
