#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q08IG9	uniprotkb:P03459	intact:EBI-9118544	intact:EBI-9118555|uniprotkb:Q67087	psi-mi:m2_i80a6(display_long)|uniprotkb:M(gene name)|psi-mi:M(display_short)|uniprotkb:Proton channel protein M2(gene name synonym)	psi-mi:hema_i34a0(display_long)|uniprotkb:HA(gene name)|psi-mi:HA(display_short)	psi-mi:"MI:0055"(fluorescent resonance energy transfer)	Thaa et al. (2014)	imex:IM-22259|pubmed:24561202	taxid:387207(i80a6)|taxid:387207("Influenza A virus (strain A/Duck/Hokkaido/8/1980 H3N8)")	taxid:392810(i34a0)|taxid:392810("Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1)")	psi-mi:"MI:2364"(proximity)	psi-mi:"MI:0471"(MINT)	intact:EBI-9118538|imex:IM-22259-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0584"(fluorescence acceptor)	psi-mi:"MI:0583"(fluorescence donor)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	interpro:IPR002089(Influenza virus matrix protein 2)|go:"GO:0005216"(ion channel activity)|go:"GO:0015078"(proton transmembrane transporter activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039521"(suppression by virus of host autophagy)|go:"GO:0039707"(pore formation by virus in membrane of host cell)|go:"GO:0044385"(integral to membrane of host cell)|go:"GO:0051259"(protein complex oligomerization)|go:"GO:0055036"(virion membrane)	interpro:IPR008980(Viral capsid/haemagglutinin protein)|interpro:IPR013828(Haemagglutinin, HA1 chain, alpha/beta region)|interpro:IPR000149(Haemagglutinin, influenza A/B virus type, HA1 chain)|interpro:IPR001364(Haemagglutinin, influenza A/B virus type, HA1/HA2 chain)|go:"GO:0016021"(integral component of membrane)|go:"GO:0019031"(viral envelope)|go:"GO:0019062"(virion attachment to host cell)|go:"GO:0019064"(fusion of virus membrane with host plasma membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039654"(fusion of virus membrane with host endosome membrane)|go:"GO:0046761"(viral budding from plasma membrane)|go:"GO:0046789"(host cell surface receptor binding)|go:"GO:0055036"(virion membrane)|go:"GO:0075512"(clathrin-dependent endocytosis of virus by host cell)	go:"GO:0045121"(membrane raft)	-	-	figure legend:f2 f3a|comment:"When HA–Cer-C3S (lacking all three acylation sites) was employed for FLIM-FRET a relative KD value of 0.72 was determined (Fig. 3A), clearly higher than in the experiments with  HA–Cer-wt (KD = 0.13, Fig. 2C). Also, the fitting curve appears quasi-linear rather than distinctly  leveling off as in the case of clustering. The FLIM-FRET measurement with HA–Cer-VIL3A and  M2–YFP-wt yielded a relative KD of 0.29 (Fig. 3B). Thus, removing the raft-targeting features of  HA clearly reduced clustering with M2, more pronounced with non-acylated HA. Acylation of HA  may thus be more important for budozone organization than the VIL motif. Accordingly, lack of  HA’s VIL motif in recombinant viruses is less dramatic than mutating individual HA acylation  sites (viruses with non-acylated HA cannot be rescued; virus titers of virus with HA-VIL3A are  reduced by 2–4 logs [14])."|comment:"The evaluation of clustering between HA–Cer-wt and M2–YFP-wt yielded a relative KD value of  0.13 (Fig. 2C). This is very similar to the result obtained previously [25] for the same FRET pair  (relative KD = 0.09). Thus, we corroborated that HA–Cer and M2–YFP cluster in the plasma  membrane of live cells."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:10029(crigr-cho)|taxid:10029(chinese hamster ovary cell line)	-	2014/02/06	2014/10/16	rogid:gshRwJgIwlRAxI6BrjsGRb8OFLk387207	rogid:CEU9e/T2OGX4MLE0quKM2OowSSI392810	intact-crc:28A85F862714E3B8|rigid:LUka0anB/xQOvrTzp4qxuqELn1U	false	yellow fluorescent protein tag:?-?	fluorescent protein tag:?-?|mutation decreasing interaction:551-551,559-559,562-562	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P03459	uniprotkb:Q08IG9	intact:EBI-9118555|uniprotkb:Q67087	intact:EBI-9118544	psi-mi:hema_i34a0(display_long)|uniprotkb:HA(gene name)|psi-mi:HA(display_short)	psi-mi:m2_i80a6(display_long)|uniprotkb:M(gene name)|psi-mi:M(display_short)|uniprotkb:Proton channel protein M2(gene name synonym)	psi-mi:"MI:0055"(fluorescent resonance energy transfer)	Thaa et al. (2014)	imex:IM-22259|pubmed:24561202	taxid:392810(i34a0)|taxid:392810("Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1)")	taxid:387207(i80a6)|taxid:387207("Influenza A virus (strain A/Duck/Hokkaido/8/1980 H3N8)")	psi-mi:"MI:2364"(proximity)	psi-mi:"MI:0471"(MINT)	intact:EBI-9118662|imex:IM-22259-2	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0583"(fluorescence donor)	psi-mi:"MI:0584"(fluorescence acceptor)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	interpro:IPR008980(Viral capsid/haemagglutinin protein)|interpro:IPR013828(Haemagglutinin, HA1 chain, alpha/beta region)|interpro:IPR000149(Haemagglutinin, influenza A/B virus type, HA1 chain)|interpro:IPR001364(Haemagglutinin, influenza A/B virus type, HA1/HA2 chain)|go:"GO:0016021"(integral component of membrane)|go:"GO:0019031"(viral envelope)|go:"GO:0019062"(virion attachment to host cell)|go:"GO:0019064"(fusion of virus membrane with host plasma membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039654"(fusion of virus membrane with host endosome membrane)|go:"GO:0046761"(viral budding from plasma membrane)|go:"GO:0046789"(host cell surface receptor binding)|go:"GO:0055036"(virion membrane)|go:"GO:0075512"(clathrin-dependent endocytosis of virus by host cell)	interpro:IPR002089(Influenza virus matrix protein 2)|go:"GO:0005216"(ion channel activity)|go:"GO:0015078"(proton transmembrane transporter activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039521"(suppression by virus of host autophagy)|go:"GO:0039707"(pore formation by virus in membrane of host cell)|go:"GO:0044385"(integral to membrane of host cell)|go:"GO:0051259"(protein complex oligomerization)|go:"GO:0055036"(virion membrane)	go:"GO:0045121"(membrane raft)	-	-	figure legend:f2 f3b|comment:"When HA–Cer-C3S (lacking all three acylation sites) was employed for FLIM-FRET a relative KD value of 0.72 was determined (Fig. 3A), clearly higher than in the experiments with  HA–Cer-wt (KD = 0.13, Fig. 2C). Also, the fitting curve appears quasi-linear rather than distinctly  leveling off as in the case of clustering. The FLIM-FRET measurement with HA–Cer-VIL3A and  M2–YFP-wt yielded a relative KD of 0.29 (Fig. 3B). Thus, removing the raft-targeting features of  HA clearly reduced clustering with M2, more pronounced with non-acylated HA. Acylation of HA  may thus be more important for budozone organization than the VIL motif. Accordingly, lack of  HA’s VIL motif in recombinant viruses is less dramatic than mutating individual HA acylation  sites (viruses with non-acylated HA cannot be rescued; virus titers of virus with HA-VIL3A are  reduced by 2–4 logs [14])."|comment:"The evaluation of clustering between HA–Cer-wt and M2–YFP-wt yielded a relative KD value of  0.13 (Fig. 2C). This is very similar to the result obtained previously [25] for the same FRET pair  (relative KD = 0.09). Thus, we corroborated that HA–Cer and M2–YFP cluster in the plasma  membrane of live cells."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:10029(crigr-cho)|taxid:10029(chinese hamster ovary cell line)	-	2014/02/06	2014/10/16	rogid:CEU9e/T2OGX4MLE0quKM2OowSSI392810	rogid:gshRwJgIwlRAxI6BrjsGRb8OFLk387207	intact-crc:6412E03CCFC2B344|rigid:LUka0anB/xQOvrTzp4qxuqELn1U	false	fluorescent protein tag:?-?|mutation decreasing interaction:527-529	yellow fluorescent protein tag:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:P03459	uniprotkb:Q08IG9	intact:EBI-9118555|uniprotkb:Q67087	intact:EBI-9118544	psi-mi:hema_i34a0(display_long)|uniprotkb:HA(gene name)|psi-mi:HA(display_short)	psi-mi:m2_i80a6(display_long)|uniprotkb:M(gene name)|psi-mi:M(display_short)|uniprotkb:Proton channel protein M2(gene name synonym)	psi-mi:"MI:0055"(fluorescent resonance energy transfer)	Thaa et al. (2014)	imex:IM-22259|pubmed:24561202	taxid:392810(i34a0)|taxid:392810("Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1)")	taxid:387207(i80a6)|taxid:387207("Influenza A virus (strain A/Duck/Hokkaido/8/1980 H3N8)")	psi-mi:"MI:2364"(proximity)	psi-mi:"MI:0471"(MINT)	intact:EBI-9118680|imex:IM-22259-3	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0583"(fluorescence donor)	psi-mi:"MI:0584"(fluorescence acceptor)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	interpro:IPR008980(Viral capsid/haemagglutinin protein)|interpro:IPR013828(Haemagglutinin, HA1 chain, alpha/beta region)|interpro:IPR000149(Haemagglutinin, influenza A/B virus type, HA1 chain)|interpro:IPR001364(Haemagglutinin, influenza A/B virus type, HA1/HA2 chain)|go:"GO:0016021"(integral component of membrane)|go:"GO:0019031"(viral envelope)|go:"GO:0019062"(virion attachment to host cell)|go:"GO:0019064"(fusion of virus membrane with host plasma membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039654"(fusion of virus membrane with host endosome membrane)|go:"GO:0046761"(viral budding from plasma membrane)|go:"GO:0046789"(host cell surface receptor binding)|go:"GO:0055036"(virion membrane)|go:"GO:0075512"(clathrin-dependent endocytosis of virus by host cell)	interpro:IPR002089(Influenza virus matrix protein 2)|go:"GO:0005216"(ion channel activity)|go:"GO:0015078"(proton transmembrane transporter activity)|go:"GO:0016021"(integral component of membrane)|go:"GO:0020002"(host cell plasma membrane)|go:"GO:0039521"(suppression by virus of host autophagy)|go:"GO:0039707"(pore formation by virus in membrane of host cell)|go:"GO:0044385"(integral to membrane of host cell)|go:"GO:0051259"(protein complex oligomerization)|go:"GO:0055036"(virion membrane)	go:"GO:0045121"(membrane raft)	-	-	figure legend:f2 f4|comment:"Finally, we assessed whether the raft-association features of M2 play a role for the intrinsic  clustering with HA. We performed FLIM-FRET experiments with HA–Cer-wt and mutants of M2–  YFP. The results (Fig. 4) show that HA–M2 clustering was evident irrespective of the M2 version,  relative KD values in the same range as for HA–Cer-wt and M2–YFP-wt were obtained: 0.04 for  HA–Cer-wt and M2–YFP-C50S (lacking acylation; Fig. 4A), 0.11 with M2–YFP-Y52S, Y57S  (cholesterol-interaction motifs disrupted; Fig. 4B), and 0.10 with the M2 mutant lacking both  raft-targeting features (Fig. 4C).  Surprisingly, M2–HA clustering was not even diminished in the absence of cholesterol-binding  sites and/or acylation."|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:10029(crigr-cho)|taxid:10029(chinese hamster ovary cell line)	-	2014/02/06	2014/10/16	rogid:CEU9e/T2OGX4MLE0quKM2OowSSI392810	rogid:gshRwJgIwlRAxI6BrjsGRb8OFLk387207	intact-crc:A94A469345D10EFA|rigid:LUka0anB/xQOvrTzp4qxuqELn1U	false	fluorescent protein tag:?-?	yellow fluorescent protein tag:?-?	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)