DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68722X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68718X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68715X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Please compare description of experiment (E5 - E13) from the text with fig.3 and Table1 - ''SNSyn2, SNSyn3, and SNSyn4 interact with to give complexes'' - I cannot see interaction of SNSyn4 with syn1pep on Fig.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68723X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68721X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli comigration in gel comigration in gel electrophoresis comigration in gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Dews IC., Mackenzie KR. DIP original experiment: DIP-68725X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli toxcat tox-r dimerization assay toxcat predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68711X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli comigration in gel comigration in gel electrophoresis comigration in gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Dews IC., Mackenzie KR. DIP original experiment: DIP-68724X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli comigration in gel comigration in gel electrophoresis comigration in gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Dews IC., Mackenzie KR. DIP original experiment: DIP-68727X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli toxcat tox-r dimerization assay toxcat predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68713X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli toxcat tox-r dimerization assay toxcat predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68714X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68717X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli toxcat tox-r dimerization assay toxcat predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68712X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68728X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68730X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68716X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Dews IC., Mackenzie KR. DIP original experiment: DIP-68729X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68719X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions in vitro In vitro comigration in gel comigration in gel electrophoresis comigration in gel predetermined predetermined participant predetermined Dews IC., Mackenzie KR. DIP original experiment: DIP-68720X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx f.3 Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. Proceedings of the National Academy of Sciences of the United States of America 2007 imex curation Dews IC., Mackenzie KR. Only protein-protein interactions ecolx Escherichia coli comigration in gel comigration in gel electrophoresis comigration in gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Dews IC., Mackenzie KR. DIP original experiment: DIP-68726X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions. sdc3_human Syndecan-3 SDC3 KIAA0468 protein protein human Homo sapiens Human MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELPEEETTQPDTANEVVAVGGAAAKASSPPGTLPKGARPGPGLLDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA DIP protein O75056 original sequence version: 64 DIP protein O75056 original sequence version: 107 D4C284CBC36A92E2 sdc4_human Syndecan-4 SDC4 Amphiglycan Ryudocan core protein protein protein human Homo sapiens Human MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA DIP protein P31431 original sequence version: 87 DIP protein P31431-1 original sequence version: 134 8229AA2733F77A10 sdc2_human Syndecan-2 SDC2 HSPG1 Fibroglycan Heparan sulfate proteoglycan core protein protein protein human Homo sapiens Human MRRAWILLTLGLVACVSAESRAELTSDKDMYLDNSSIEEASGVYPIDDDDYASASGSGADEDVESPELTTSRPLPKILLTSAAPKVETTTLNIQNKIPAQTKSPEETDKEKVHLSDSERKMDPAEEDTNVYTEKHSDSLFKRTEVLAAVIAGGVIGFLFAIFLILLLVYRMRKKDEGSYDLGERKPSSAAYQKAPTKEFYA DIP protein P34741 original sequence version: 74 DIP protein P34741 original sequence version: 119 DIP protein P34741 original sequence version: 102 7DA4159D54741054 sdc1_human Syndecan-1 SDC1 SDC protein protein human Homo sapiens Human MRRAALWLWLCALALSLQPALPQIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA DIP protein P18827 original sequence version: 77 DIP protein P18827 original sequence version: 127 8E9EF4A57F5FDBD0 sdc2-1 6 23 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc1-sdc2-3 12 24 unspecified role unspecified role unspecified role unspecified role 241-287 binding site 241-287 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role P34741:p.Gly152Leu G152L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G152L'. Wed May 02 16:15:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly152leu' Tue Jun 30 19:32:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly152Leu' P34741:p.Gly156Leu G156L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G156L'. Wed May 02 18:12:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly156leu' Tue Jun 30 19:31:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly156Leu' ecolx Escherichia coli direct interaction direct interaction sdc1-1 7 24 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc3-sdc4-2 5 22 unspecified role unspecified role unspecified role unspecified role 135-176 binding site 135-176 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role G392L G392L sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain O75056:p.Gly396Leu G396L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G396L'. Wed May 02 19:27:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly396leu' Tue Jun 30 18:20:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly396Leu' ecolx Escherichia coli direct interaction direct interaction sdc1-2 8 24 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc2-2 13 23 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc4-1 9 22 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc3-1 10 21 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc3-2 20 21 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc4-sdc4-3 15 22 unspecified role unspecified role unspecified role unspecified role 135-176 binding site 135-176 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 22 unspecified role unspecified role unspecified role unspecified role P31431:p.Gly153Leu G153L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G153L'. Wed May 02 15:12:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly153leu' Tue Jun 30 17:02:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly153Leu' P31431:p.Gly157Leu G157L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G157L'. Wed May 02 15:09:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly157leu' Tue Jun 30 18:00:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly157Leu' ecolx Escherichia coli direct interaction direct interaction sdc4-2 11 22 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction sdc2-sdc3-2 2 21 unspecified role unspecified role unspecified role unspecified role 375-418 binding site 375-418 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role P34741:p.Gly152Leu G152L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G152L'. Wed May 02 19:09:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly152leu' Tue Jun 30 15:38:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly152Leu' P34741:p.Gly156Leu G156L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G156L'. Wed May 02 19:01:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly156leu' Tue Jun 30 19:14:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly156Leu' ecolx Escherichia coli direct interaction direct interaction sdc1-sdc2-4 3 23 unspecified role unspecified role unspecified role unspecified role 134-175 binding site 134-175 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role P18827:p.Gly259Leu G259L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G259L'. Wed May 02 15:38:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly259leu' Tue Jun 30 17:13:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly259Leu' P18827:p.Gly263Leu G263L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G263L'. Wed May 02 15:16:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly263leu' Tue Jun 30 17:40:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly263Leu' ecolx Escherichia coli direct interaction direct interaction sdc2-sdc4-5 1 23 unspecified role unspecified role unspecified role unspecified role 134-175 binding site 134-175 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 22 unspecified role unspecified role unspecified role unspecified role P31431:p.Gly153Leu G153L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G153L'. Wed May 02 15:16:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly153leu' Tue Jun 30 18:06:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly153Leu' P31431:p.Gly157Leu G157L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G157L'. Wed May 02 17:59:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly157leu' Tue Jun 30 17:30:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly157Leu' ecolx Escherichia coli direct interaction direct interaction sdc2-sdc2-3 14 23 unspecified role unspecified role unspecified role unspecified role 134-175 binding site 134-175 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role P34741:p.Gly152Leu G152L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G152L'. Wed May 02 18:08:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly152leu' Tue Jun 30 16:24:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly152Leu' P34741:p.Gly156Leu G156L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G156L'. Wed May 02 20:01:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly156leu' Tue Jun 30 16:28:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly156Leu' ecolx Escherichia coli direct interaction direct interaction sdc2-sdc4-6 18 22 unspecified role unspecified role unspecified role unspecified role 135-176 binding site 135-176 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role P34741:p.Gly152Leu G152L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G152L'. Wed May 02 15:30:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly152leu' Tue Jun 30 18:47:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly152Leu' P34741:p.Gly156Leu G156L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G156L'. Wed May 02 19:20:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly156leu' Tue Jun 30 16:19:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly156Leu' ecolx Escherichia coli direct interaction direct interaction sdc1-sdc3-1 16 21 unspecified role unspecified role unspecified role unspecified role binding site 375-418 binding site 375-418 sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role P18827:p.Gly259Leu G259L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G259L'. Wed May 02 18:32:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly259leu' Tue Jun 30 16:48:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly259Leu' P18827:p.Gly263Leu G263L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G263L'. Wed May 02 16:55:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly263leu' Tue Jun 30 16:01:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly263Leu' ecolx Escherichia coli direct interaction direct interaction sdc3-sdc4-3 4 21 unspecified role unspecified role unspecified role unspecified role 375-418 binding site 375-418 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 22 unspecified role unspecified role unspecified role unspecified role P31431:p.Gly153Leu G153L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G153L'. Wed May 02 16:27:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly153leu' Tue Jun 30 16:47:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly153Leu' P31431:p.Gly157Leu G157L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G157L'. Wed May 02 18:32:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly157leu' Tue Jun 30 15:55:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly157Leu' ecolx Escherichia coli direct interaction direct interaction sdc3-sdc3-1 17 21 unspecified role unspecified role unspecified role unspecified role binding site 375-418 binding site 375-418 sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role O75056:p.Gly392Leu G392L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G392L'. Wed May 02 14:44:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly392leu' Tue Jun 30 18:47:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly392Leu' O75056:p.Gly396Leu G396L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G396L'. Wed May 02 15:44:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly396leu' Tue Jun 30 16:54:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly396Leu' ecolx Escherichia coli direct interaction direct interaction sdc2-sdc3-3 19 23 unspecified role unspecified role unspecified role unspecified role binding site 134-175 binding site 134-175 sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role O75056:p.Gly392Leu G392L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G392L'. Wed May 02 20:08:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly392leu' Tue Jun 30 19:37:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly392Leu' O75056:p.Gly396Leu G396L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain G L This feature has been corrected as a result of our quality control procedures. The original label was 'G396L'. Wed May 02 14:28:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly396leu' Tue Jun 30 18:37:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly396Leu' ecolx Escherichia coli direct interaction direct interaction