UniProt UniProt http://www.uniprot.org Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins Multiangle Light Scattering for detection. HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight by comassie molecular weight estimation by coomasie staining weight by comassie Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins In exp involving LEDGF/p75 FLAG-IN was preincubated with increasing concentrations of LEDF/p75 and then TPO3 was added. HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro pull down pull down fingerprinting peptide massfingerprinting fingerprinting Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins IN CTD was incubated with or without TNPO3 and treated with NHS-biotin. To identify IN residues essential for high affinity binding with TNPO3, free IN and the IN–TNPO3 complex are subjected to treatment by small covalent modifiers. Surface residues in free IN and the complex are susceptible to modification, while the interacting amino acids in the complex are shielded from modification. HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins Stable synaptic complexes (SSC; a tetramer of IN associated with a pair of viral DNA ends) have been mixed with purified TNPO3 and passed through a size exclusion spin column; eluate western-blotted. HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J. Biol. Chem. (0021-9258) 2012 imex curation Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Larue R., Gupta K., Wuensch C., Shkriabai N., Kessl J.J., Danhart E., Feng L., Taltynov O., Christ F., Van Duyne G.D., Debyser Z., Foster M.P., Kvaratskhelia M. Virus - Publications including interactions involving viral proteins Stable synaptic complexes (SSC; a tetramer of IN associated with a pair of viral DNA ends) have been mixed with purified TNPO3 and passed through a size exclusion spin column; eluate western-blotted. HIV-1 proteins shave been mapped to the UniProt HIV-1 reference strain. Exp involving recombinant CypA not included as origin of CypA cannot be established from the publication. FLAG-tagged HIV-1 IN according ref 25 (pubmed 22437836) kvaratshkelia.1@osu.edu Accepted 2015-FEB-25 by MGT J. Biol. Chem. (0021-9258) 2012 imex curation p04585-pro_0000042447 Integrase gag-pol Pr160Gag-Pol protein protein hv1h2 Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) HIV-1 FLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED 1148 1435 A39EF048DFDDB104 tnpo3_human Transportin-3 TNPO3 IPO12 Transportin-SR Importin-12 protein protein human Homo sapiens Human MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR CF7CDC14CDBA56AB o75475-1 PC4 and SFRS1-interacting protein p75 PSIP1 PSIP1 DFS70 LEDGF PSIP2 CLL-associated antigen KW-7 Dense fine speckles 70 kDa protein Lens epithelium-derived growth factor Transcriptional coactivator p75/p52 protein protein human Homo sapiens Human MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN Less active than isoform 2 as transcriptional coactivator, but more abundant in cells. 4B653D02B1D0E174 gag_pol-tnpo3-1 4 10 unspecified role unspecified role prey prey n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q9Y5L0:p.[Arg400Glu;Arg402Glu] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain R E Wed May 02 17:40:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg400glu,arg402glu' Tue Jun 30 19:20:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg400Glu;Arg402Glu]' Q9Y5L0:p.Gln761_Arg762delinsGluGlu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain QR EE Thu Jul 07 12:07:07 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was gln761glu_arg762glu Fri Jul 22 11:06:40 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'gln761glu,arg762glu' Wed May 02 19:08:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln_arg761-762glu_glu' Tue Jun 30 17:48:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln761_Arg762delinsGluGlu' ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role bait bait n-terminus flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range direct interaction direct interaction 1D and 8A and C gag_pol-tnpo3-2 6 9 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) physical association physical association 2B gag_pol-psip1-22 4 11 unspecified role unspecified role prey prey n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role bait bait n-terminus flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range true 10 unspecified role unspecified role prey prey n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range true ecoli Escherichia coli (strain K12) association association 2C tnpo3-gag_pol 3 9 unspecified role unspecified role prey prey n-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P04585-PRO_0000042447:p.Lys240Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K E Wed May 02 16:07:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys240glu' Tue Jun 30 17:26:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys240Glu' P04585-PRO_0000042447:p.[Arg262Glu;Arg263Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain R E Wed May 02 15:34:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg262glu,arg263glu' Tue Jun 30 18:03:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg262Glu;Arg263Glu]' P04585-PRO_0000042447:p.Lys264Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K E Wed May 02 15:13:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys264glu' Tue Jun 30 15:52:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys264Glu' P04585-PRO_0000042447:p.[Arg262Glu;Arg263Glu;Lys264Glu] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain K E Wed May 02 14:29:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg262glu,arg263glu,lys264glu' Tue Jun 30 17:58:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg262Glu;Arg263Glu;Lys264Glu]' 10 unspecified role unspecified role bait bait n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range true ecoli Escherichia coli (strain K12) direct interaction direct interaction 3 and 5A Binding with IN C-terminal region is much stronger than with N-terminal region. gag_pol-tnpo3-3 5 9 unspecified role unspecified role unspecified role unspecified role n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag certain certain sequence position certain certain certain sequence position certain 10 unspecified role unspecified role unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction 4 and Table S2 Tryptic peptide 264-269 with K-264 and K-266 biotinylated has a diminished peak upon IN CTD binding to TPNO3. tnpo3-gag_pol-1 8 10 unspecified role unspecified role bait bait n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range true ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role prey prey P04585-PRO_0000042447:p.Arg262_Lys264delinsGluGluGlu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain RRK EEE Wed May 02 20:20:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg_arg_lys262-264glu_glu_glu' Tue Jun 30 18:21:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg262_Lys264delinsGluGluGlu' direct interaction direct interaction 5D psip1-gag_pol 3 11 unspecified role unspecified role bait bait n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role prey prey An IN construct arg262glu_arg263glu_lys264glu also did interact direct interaction direct interaction 5F tnpo3-2 2 10 unspecified role unspecified role neutral component neutral component direct interaction direct interaction 7 tnpo3-2 7 10 unspecified role unspecified role neutral component neutral component n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction 6E and 6D tnpo3-2 1 10 unspecified role unspecified role neutral component neutral component n-terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction 6C