HPIDb Host Pathogen Interaction database http://www.agbase.msstate.edu/hpi/main.html Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell host & microbe 2008 imex curation Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu Accepted 2016-JAN-27 AT 10:04 GMT AT 10:04 GMT by ORCHARD Cell host & microbe 2008 imex curation Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell host & microbe 2008 imex curation Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu Accepted 2016-JAN-27 AT 10:04 GMT AT 10:04 GMT by ORCHARD Cell host & microbe 2008 imex curation Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell host & microbe 2008 imex curation Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 confocal microscopy confocal microscopy tag fluorescence tag visualisation by fluorescence tag fluorescence Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu Accepted 2016-JAN-27 AT 10:04 GMT AT 10:04 GMT by ORCHARD Cell host & microbe 2008 imex curation Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation. Cell host & microbe 2008 imex curation Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Ohlson MB., Huang Z., Alto NM., Blanc MP., Dixon JE., Chai J., Miller SI. interactions with GST-RhoA are not added since the species is not specified millersi@u.washington.edu Accepted 2016-JAN-27 AT 10:04 GMT AT 10:04 GMT by ORCHARD Cell host & microbe 2008 imex curation sifa_salty Secreted effector protein SifA STM1224 sifA protein protein salty Salmonella typhimurium MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFAERAPTRERLTEIFFELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKSHPQMTAMIKRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYTELRKGHLDGWKAQEKATYLAAKIQSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDPSTSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL 83C6185148A774B9 83C6185148A774B9 a0a0f6b063_salt1 sifA STM14_1400 protein protein salt1 Salmonella typhimurium (strain 14028s / SGSC 2262) MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFAERAPTRERLTEIFFELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKSHPQMTAMIKRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYTELRKGHLDGWKAQEKATYLAAKIQSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDPSTSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL 83C6185148A774B9 a0a0f6b1q8_salt1 STM14_1974 sseJ protein protein salt1 Salmonella typhimurium (strain 14028s / SGSC 2262) MPLSVGQGYFTSSISSEKFNAIKESARLPELSLWEKIKAYFFTTHHAEALECIFNLYHHQELNLTPVQVRGAYIKLRALASQGCKEQFIIESQEHADKLIIKDDNGENILSIEVECHPEAFGLAKEINKSHPKPKNISLGDITRLVFFGDSLSDSLGRMFEKTHHILPSYGQYFGGRFTNGFTWTEFLSSPHFLGKEMLNFAEGGSTSASYSCFNCIGDFVSNTDRQVASYTPSHQDLAIFLLGANDYMTLHKDNVIMVVEQQIDDIEKIISGGVNNVLVMGIPDLSLTPYGKHSDEKRKLKDESIAHNALLKTNVEELKEKYPQHKICYYETADAFKVIMEAASNIGYDTENPYTHHGYVHVPGAKDPQLDICPQYVFNDLVHPTQEVHHCFAIMLESFIAHHYSTE 8917A5A5590566F4 pkhm2_human Pleckstrin homology domain-containing family M member 2 KIAA0842 SKIP Salmonella-induced filaments A and kinesin-interacting protein PLEKHM2 protein protein human Homo sapiens Human MEPGEVKDRILENISLSVKKLQSYFAACEDEIPAIRNHDKVLQRLCEHLDHALLYGLQDLSSGYWVLVVHFTRREAIKQIEVLQHVATNLGRSRAWLYLALNENSLESYLRLFQENLGLLHKYYVKNALVCSHDHLTLFLTLVSGLEFIRFELDLDAPYLDLAPYMPDYYKPQYLLDFEDRLPSSVHGSDSLSLNSFNSVTSTNLEWDDSAIAPSSEDYDFGDVFPAVPSVPSTDWEDGDLTDTVSGPRSTASDLTSSKASTRSPTQRQNPFNEEPAETVSSSDTTPVHTTSQEKEEAQALDPPDACTELEVIRVTKKKKIGKKKKSRSDEEASPLHPACSQKKCAKQGDGDSRNGSPSLGRDSPDTMLASPQEEGEGPSSTTESSERSEPGLLIPEMKDTSMERLGQPLSKVIDQLNGQLDPSTWCSRAEPPDQSFRTGSPGDAPERPPLCDFSEGLSAPMDFYRFTVESPSTVTSGGGHHDPAGLGQPLHVPSSPEAAGQEEEGGGGEGQTPRPLEDTTREAQELEAQLSLVREGPVSEPEPGTQEVLCQLKRDQPSPCLSSAEDSGVDEGQGSPSEMVHSSEFRVDNNHLLLLMIHVFRENEEQLFKMIRMSTGHMEGNLQLLYVLLTDCYVYLLRKGATEKPYLVEEAVSYNELDYVSVGLDQQTVKLVCTNRRKQFLLDTADVALAEFFLASLKSAMIKGCREPPYPSILTDATMEKLALAKFVAQESKCEASAVTVRFYGLVHWEDPTDESLGPTPCHCSPPEGTITKEGMLHYKAGTSYLGKEHWKTCFVVLSNGILYQYPDRTDVIPLLSVNMGGEQCGGCRRANTTDRPHAFQVILSDRPCLELSAESEAEMAEWMQHLCQAVSKGVIPQGVAPSPCIPCCLVLTDDRLFTCHEDCQTSFFRSLGTAKLGDISAVSTEPGKEYCVLEFSQDSQQLLPPWVIYLSCTSELDRLLSALNSGWKTIYQVDLPHTAIQEASNKKKFEDALSLIHSAWQRSDSLCRGRASRDPWC DIP protein Q8IWE5 original sequence version: 33 DIP protein Q8IWE5 original sequence version: 97 FFD857F4C11BC0DB a0a0f6b1m5_salt1 sifB STM14_1940 protein protein salt1 Salmonella typhimurium (strain 14028s / SGSC 2262) MPITIGRGFLKSEMFSQSAISQRSFFTLLWEKIKDFFCDTQRSTADQYIKELCDVASPPDAQRLFDLFCKLYELSSPSCRGNFHFQHYKDAECQYTNLCIKDGEDIPLCIMIRQDHYYYEIMNRTVLCVDTQSAHLKRYSDINIKASTYVCEPLCCLFPERLQLSLSGGITFSVDLKNIEETLIAMAEKGNLCDWKEQERKAAISSRINLGIAQAGVTAIDDAIKNKIAAKVIENTNLKNAAFEPNYAQSSVTQIVYSCLFKNEILMNMLEESSSHGLLCLNELTEYVALQVHNSLFSEDLSSLVETTKNEAHHQS 12F8F63130A41EA3 ssej-sifa-1 3 6 unspecified role unspecified role neutral component neutral component n teminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 7 unspecified role unspecified role neutral component neutral component n terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range colocalization colocalization 1 sifb-ssej-1 3 9 unspecified role unspecified role neutral component neutral component n teminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 7 unspecified role unspecified role neutral component neutral component n terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range colocalization colocalization 1 sifa-ssej-skip-1 3 8 unspecified role unspecified role neutral component neutral component n terminal myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 6 unspecified role unspecified role neutral component neutral component n teminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 7 unspecified role unspecified role neutral component neutral component n terminus ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range colocalization colocalization 2 sifa-skip-2 2 6 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction 5B skip-sifa-2 4 5 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction 5C, 6A and table S1 2.6A R working 0.258 R free 0.288 sifa-plekhm2-1 1 6 unspecified role unspecified role bait bait purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined A0A0F6B063:p.Leu130Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L D Wed May 02 16:34:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu130asp' Tue Jun 30 18:17:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu130Asp' undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:19:10 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'met131asp' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q8IWE5:p.Arg831Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R D Wed May 02 14:44:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg831asp' Tue Jun 30 17:58:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg831Asp' Q8IWE5:p.Cys869Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain C D Wed May 02 19:47:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys869asp' Tue Jun 30 18:46:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys869Asp' Q8IWE5:p.Gly828Asp 829 mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain G D Wed May 02 19:59:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly828asp' Tue Jun 30 17:31:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly828Asp' Q8IWE5:p.Arg831Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R A Wed May 02 19:35:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg831ala' Tue Jun 30 17:53:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg831Ala' ecoli Escherichia coli (strain K12) Skip mutation corresponding to UniProt id Q8IWE5 seq are different from what is stated in the publication 42 44 direct interaction direct interaction 5A and E