#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:P69277	uniprotkb:P27986	intact:EBI-7168926|intact:MINT-4509639|uniprotkb:Q02599	intact:EBI-79464|intact:EBI-28974553|ensembl:ENSP00000428056|ensembl:ENSP00000429277|uniprotkb:Q15747|uniprotkb:Q4VBZ7|uniprotkb:Q53EM6|uniprotkb:Q8IXA2|uniprotkb:Q8N1C5|uniprotkb:D3DWA0|uniprotkb:B3KT19|uniprotkb:E7EX19	psi-mi:ns1_i68a0(display_long)|uniprotkb:NS(gene name)|psi-mi:NS(display_short)|uniprotkb:NS1A(gene name synonym)	psi-mi:p85a_human(display_long)|uniprotkb:PIK3R1(gene name)|psi-mi:PIK3R1(display_short)|uniprotkb:GRB1(gene name synonym)|uniprotkb:Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha(gene name synonym)	psi-mi:"MI:0096"(pull down)	Shin et al. (2007)	pubmed:17170431|mint:MINT-5219446	taxid:387139(i68a0)|taxid:387139("Influenza A virus (strain A/Aichi/2/1968 H3N2)")	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0915"(physical association)	psi-mi:"MI:0471"(MINT)	intact:EBI-7168958|mint:MINT-4509661	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0498"(prey)	psi-mi:"MI:0496"(bait)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	interpro:IPR004208("Influenza B non-structural protein (NS1)")|mint:P69277|go:"GO:0003723"(RNA binding)|go:"GO:0030430"(host cell cytoplasm)|go:"GO:0039502"(suppression by virus of host type I interferon-mediated signaling pathway)|go:"GO:0039524"(suppression by virus of host mRNA processing)|go:"GO:0039540"(suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity)|go:"GO:0039580"(suppression by virus of host PKR signaling)|go:"GO:0042025"(host cell nucleus)|interpro:IPR038064|interpro:IPR000256("Influenza non-structural protein (NS1)")|interpro:IPR009068(S15/NS1, RNA-binding)|mint:MINT-4509662(identity)	refseq:NP_001229395.1|refseq:NP_852556.2|refseq:NP_852664.1|refseq:NP_852665.1|ensembl:ENSG00000145675(gene)|ensembl:ENST00000521381(transcript)|ensembl:ENST00000521657(transcript)|go:"GO:0001678"(cellular glucose homeostasis)|go:"GO:0001784"(phosphotyrosine residue binding)|go:"GO:0001953"(negative regulation of cell-matrix adhesion)|go:"GO:0005068"(transmembrane receptor protein tyrosine kinase adaptor activity)|go:"GO:0005158"(insulin receptor binding)|go:"GO:0005159"(insulin-like growth factor receptor binding)|go:"GO:0005168"(neurotrophin TRKA receptor binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005801"(cis-Golgi network)|go:"GO:0005829"(cytosol)|go:"GO:0005886"(plasma membrane)|go:"GO:0005911"(cell-cell junction)|go:"GO:0005942"(phosphatidylinositol 3-kinase complex)|go:"GO:0005943"(phosphatidylinositol 3-kinase complex, class IA)|go:"GO:0006468"(protein phosphorylation)|go:"GO:0006606"(protein import into nucleus)|go:"GO:0008134"(transcription factor binding)|go:"GO:0008286"(insulin receptor signaling pathway)|ensembl:ENST00000320694|ensembl:ENSP00000323512|ensembl:ENST00000336483|ensembl:ENSP00000338554|ensembl:ENSP00000428056|ensembl:ENSP00000429277|ensembl:ENST00000523872|ensembl:ENSP00000430098|rcsb pdb:5SXA|rcsb pdb:5SXB|rcsb pdb:5SXC|rcsb pdb:5SXD|rcsb pdb:5SXE|rcsb pdb:5SXF|rcsb pdb:5SXI|rcsb pdb:5SXJ|rcsb pdb:5SXK|rcsb pdb:5UBT|rcsb pdb:5UK8|rcsb pdb:5UKJ|rcsb pdb:5SX9|rcsb pdb:5UL1|rcsb pdb:5VLR|rcsb pdb:5XGH|rcsb pdb:5XGI|rcsb pdb:5XGJ|rcsb pdb:6NCT|rcsb pdb:6PYR|rcsb pdb:6PYU|reactome:R-HSA-1660499|rcsb pdb:7CIO|rcsb pdb:7LM2|reactome:R-HSA-180292|reactome:R-HSA-109704|reactome:R-HSA-1839117|reactome:R-HSA-112399|reactome:R-HSA-114604|reactome:R-HSA-1236382|reactome:R-HSA-186763|reactome:R-HSA-1963642|reactome:R-HSA-1250342|reactome:R-HSA-1257604|reactome:R-HSA-1266695|reactome:R-HSA-198203|reactome:R-HSA-202424|reactome:R-HSA-2029485|reactome:R-HSA-1433557|reactome:R-HSA-210993|reactome:R-HSA-2219530|reactome:R-HSA-2424491|reactome:R-HSA-2730905|reactome:R-HSA-373753|reactome:R-HSA-388841|reactome:R-HSA-389357|reactome:R-HSA-416476|reactome:R-HSA-430116|reactome:R-HSA-4420097|reactome:R-HSA-512988|reactome:R-HSA-5637810|reactome:R-HSA-5654689|reactome:R-HSA-5654695|reactome:R-HSA-5654710|reactome:R-HSA-5654720|reactome:R-HSA-9035034|reactome:R-HSA-912526|reactome:R-HSA-912631|reactome:R-HSA-9603381|reactome:R-HSA-9607240|reactome:R-HSA-9664565|reactome:R-HSA-9665348|reactome:R-HSA-9670439|reactome:R-HSA-9673767|reactome:R-HSA-9673770|reactome:R-HSA-9696264|reactome:R-HSA-9696270|reactome:R-HSA-9696273|reactome:R-HSA-9703465|reactome:R-HSA-9703648|reactome:R-HSA-983695|reactome:R-HSA-5655253|reactome:R-HSA-5655302|reactome:R-HSA-5673001|reactome:R-HSA-6785807|reactome:R-HSA-6811558|reactome:R-HSA-8851907|reactome:R-HSA-8853334|reactome:R-HSA-8853338|reactome:R-HSA-8853659|reactome:R-HSA-8980692|reactome:R-HSA-9009391|reactome:R-HSA-9013026|reactome:R-HSA-9013106|reactome:R-HSA-9013148|reactome:R-HSA-9013149|reactome:R-HSA-9013404|reactome:R-HSA-9013405|reactome:R-HSA-9013408|reactome:R-HSA-9013409|reactome:R-HSA-9013420|reactome:R-HSA-5655291|reactome:R-HSA-9013423|reactome:R-HSA-9013424|reactome:R-HSA-9027276|reactome:R-HSA-9028335|go:"GO:0008630"(intrinsic apoptotic signaling pathway in response to DNA damage)|go:"GO:0010592"(positive regulation of lamellipodium assembly)|go:"GO:0014065"(phosphatidylinositol 3-kinase signaling)|go:"GO:0016020"(membrane)|go:"GO:0019903"(protein phosphatase binding)|go:"GO:0030183"(B cell differentiation)|go:"GO:0030335"(positive regulation of cell migration)|go:"GO:0032760"(positive regulation of tumor necrosis factor production)|go:"GO:0032869"(cellular response to insulin stimulus)|go:"GO:0033120"(positive regulation of RNA splicing)|go:"GO:0034446"(substrate adhesion-dependent cell spreading)|go:"GO:0008625"(extrinsic apoptotic signaling pathway via death domain receptors)|go:"GO:0034644"(cellular response to UV)|go:"GO:0034976"(response to endoplasmic reticulum stress)|go:"GO:0035014"(phosphatidylinositol 3-kinase regulator activity)|go:"GO:0036312"(phosphatidylinositol 3-kinase regulatory subunit binding)|go:"GO:0045944"(positive regulation of transcription by RNA polymerase II)|go:"GO:0042307"(positive regulation of protein import into nucleus)|go:"GO:0046326"(positive regulation of glucose import)|go:"GO:0046626"(regulation of insulin receptor signaling pathway)|go:"GO:0046854"(phosphatidylinositol phosphate biosynthetic process)|go:"GO:0043066"(negative regulation of apoptotic process)|go:"GO:0043125"(ErbB-3 class receptor binding)|go:"GO:0043548"(phosphatidylinositol 3-kinase binding)|go:"GO:0046935"(1-phosphatidylinositol-3-kinase regulator activity)|go:"GO:0046982"(protein heterodimerization activity)|go:"GO:0043551"(regulation of phosphatidylinositol 3-kinase activity)|go:"GO:0043559"(insulin binding)|go:"GO:0048009"(insulin-like growth factor receptor signaling pathway)|go:"GO:0048471"(perinuclear region of cytoplasm)|go:"GO:0050821"(protein stabilization)|go:"GO:0051491"(positive regulation of filopodium assembly)|go:"GO:0043560"(insulin receptor substrate binding)|go:"GO:0051497"(negative regulation of stress fiber assembly)|go:"GO:0045671"(negative regulation of osteoclast differentiation)|go:"GO:0060396"(growth hormone receptor signaling pathway)|go:"GO:0120183"(positive regulation of focal adhesion disassembly)|go:"GO:1900103"(positive regulation of endoplasmic reticulum unfolded protein response)|go:"GO:1990578"(perinuclear endoplasmic reticulum membrane)|interpro:IPR000198(RhoGAP)|interpro:IPR000980(SH2 motif)|interpro:IPR001452(Src homology-3)|interpro:IPR008936(Rho GTPase activation protein)|interpro:IPR032498|interpro:IPR035020|interpro:IPR035022|interpro:IPR035591|interpro:IPR036028|interpro:IPR036860|interpro:IPR044124|mint:P27986|rcsb pdb:1A0N|rcsb pdb:1AZG|rcsb pdb:1H9O|rcsb pdb:1PBW|rcsb pdb:1PHT|rcsb pdb:1PIC|rcsb pdb:1PKS|rcsb pdb:1PKT|rcsb pdb:2IUG|go:"GO:1903078"(positive regulation of protein localization to plasma membrane)|rcsb pdb:2IUH|rcsb pdb:2IUI|rcsb pdb:2RD0|rcsb pdb:3HHM|rcsb pdb:3HIZ|rcsb pdb:3I5R|rcsb pdb:3I5S|rcsb pdb:4A55|rcsb pdb:4JPS|rcsb pdb:4L1B|rcsb pdb:4L23|rcsb pdb:4L2Y|rcsb pdb:4OVU|rcsb pdb:4OVV|rcsb pdb:4WAF|rcsb pdb:4YKN|rcsb pdb:4ZOP|rcsb pdb:5AUL|rcsb pdb:5FI4|rcsb pdb:5GJI|rcsb pdb:5ITD|rcsb pdb:5M6U|rcsb pdb:5SW8|rcsb pdb:5SWG|rcsb pdb:5SWO|rcsb pdb:2V1Y|rcsb pdb:5SWP|rcsb pdb:5SWR|rcsb pdb:5SWT|rcsb pdb:5SX8|refseq:XP_016865074.1|refseq:XP_005248599.1|dip:DIP-119N|mint:MINT-4509663(identity)	-	function:"Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells"|comment:mint|function:"Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor (CPSF4) and the poly(A)-binding protein 2 (PABPN1). This results in the accumulation of unprocessed 3' end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off very early after virus infection. This protein synthesis shut off is presumably necessary for the virus to escape interferon synthesis after activation of the IRF3 pathway, and therefore prevents establishment of cellular antiviral state. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase, through a stuttering mechanism"	-	figure legend:F1A|comment:homomint|comment:mint|dataset:Virus - Publications including interactions involving viral proteins|partial coverage:partial coverage	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2007/04/18	2014/10/16	rogid:HcFiQ1f7zt+hhBx95f5ZFP1mrhc387139	rogid:pANLtVCSWVr64OXaS6bCjGBwfig9606	intact-crc:18748D531C8DD296|rigid:iusVYKhuHWKJmDTRBFaeGQBHoB4	false	-	binding-associated region:3-79(MINT-4509671)|glutathione s tranferase tag:?-?(MINT-4509667)	-	-	psi-mi:"MI:0113"(western blot)	psi-mi:"MI:0078"(nucleotide sequence identification)