DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253648X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253650X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253647X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253649X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253651X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Ghai R., Mobli M., Norwood SJ., Bugarcic A., Teasdale RD., King GF., Collins BM. DIP original experiment: DIP-253646X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. q6p8y7-2 Sorting nexin-31 Snx31 protein protein mouse Mus musculus Mouse MKMHFCIPVSQQRPDALGGRYVLYSVYLDGFLFCKVRYSQLHRWDEQLRRVFGNCLPPFPPKYYLAMTTAMAEERRDQLERYLQNVTADPRVTRSDVFTEFLTLVQLHTLNITIQNVELAVFLPDGRSIKVEGLTSDTAERVLEVMAHKLGLQPDLVGYFGLFLIQCFPEGKLSVVKKLADFELPYTSLQSSEMENCKIGLRKWYLDPALDSMLMDCRAAGDLLYMQAVQDIEKEWMKPTQAQREELKALQKKENQTKFLELSQEVRHYGYVQLDPCTCNHPEPGCGAQLSIGNNEISCCITLPNGQIQDIAFQMSRVKCWQVTFLGTLLDTDGPQRTLNQNLELRFQYSEDSCQQWFVIYTKQAFFLSSCLKKMISERMTKLTEQSPEMQIEVPEQGRSKKHPSQPSQKVYFNFLRKGKMKRSEGDYVWDTLMEEGL No experimental confirmation available. app Amyloid precursor peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) CKQNGYENPTYKFFE rash_human GTPase HRas HRAS HRAS1 Transforming protein p21 p21ras H-Ras-1 c-H-ras Ha-Ras protein protein human Homo sapiens Human MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS DIP protein P01112 original sequence version: 91 DIP protein P01112 original sequence version: 106 DIP protein P01112 original sequence version: 144 DIP protein P01112 original sequence version: 118 DIP protein P01112 original sequence version: 143 DIP protein P01112 original sequence version: 152 DIP protein P01112-1 original sequence version: 159 DIP protein P01112 original sequence version: 170 DIP protein P01112-1 original sequence version: 185 DIP protein P01112 original sequence version: 192 DIP protein P01112-1 original sequence version: 196 DIP protein P01112-1 original sequence version: 202 EE6DC2D933E2856A q3uhd6-2 Sorting nexin-27 Snx27 Kiaa0488 SNX27b protein protein mouse Mus musculus Mouse MADEDGEGIHPSAPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVINHSFVRKLAPNEFPHKLYVQNYTSAVPGTCLTIRKWLFTTEEEVLLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLHEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKEEY DIP protein Q3UHD6-2 original sequence version: 61 snx17_human Sorting nexin-17 SNX17 KIAA0064 protein protein human Homo sapiens Human MHFSIPETESRSGDSGGSAYVAYNIHVNGVLHCRVRYSQLLGLHEQLRKEYGANVLPAFPPKKLFSLTPAEVEQRREQLEKYMQAVRQDPLLGSSETFNSFLRRAQQETQQVPTEEVSLEVLLSNGQKVLVNVLTSDQTEDVLEAVAAKLDLPDDLIGYFSLFLVREKEDGAFSFVRKLQEFELPYVSVTSLRSQEYKIVLRKSYWDSAYDDDVMENRVGLNLLYAQTVSDIERGWILVTKEQHRQLKSLQEKVSKKEFLRLAQTLRHYGYLRFDACVADFPEKDCPVVVSAGNSELSLQLRLPGQQLREGSFRVTRMRCWRVTSSVPLPSGSTSSPGRGRGEVRLELAFEYLMSKDRLQWVTITSPQAIMMSICLQSMVDELMVKKSGGSIRKMLRRRVGGTLRRSDSQQAVKSPPLLESPDATRESMVKLSSKLSAVSLRGIGSPSTDASASDVHGNFAFEGIGDEDL DIP protein Q15036 original sequence version: 123 B1C8650CB8AFB5EE app-snx17-1 6 8 unspecified role unspecified role unspecified role unspecified role app:p.Tyr11Ala Y11A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y11A'. Wed May 02 19:50:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr11ala' Tue Jun 30 18:42:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr11Ala' in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction snx17-hras-1 5 11 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range FERM domain Region 109-388 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role prey prey Region 1-166 Region 1-166 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction snx27-hras-1 4 9 unspecified role unspecified role prey prey Region 1-166 Region 1-166 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 10 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 156-526 Region 156-526 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction app-snx27-1 3 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role app:p.Tyr11Ala Y11A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y11A'. Wed May 02 17:50:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr11ala' Tue Jun 30 19:02:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr11Ala' in vitro In vitro direct interaction direct interaction snx31-hras-1 2 7 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 9 unspecified role unspecified role prey prey Region 1-166 Region 1-166 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction app-snx27-2 1 10 unspecified role unspecified role unspecified role unspecified role FERM domain Region 271-526 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role in vitro In vitro direct interaction direct interaction