DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252163X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252155X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252157X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252159X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252160X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252162X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252156X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252158X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252164X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure (London, England : 1993) 2013 imex curation Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Liu X., Shepherd TR., Murray AM., Xu Z., Fuentes EJ. DIP original experiment: DIP-252161X Structure (London, England : 1993) 2013 IMEx The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. 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_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 q9c0a0-1 Contactin-associated protein-like 4 CNTNAP4 CASPR4 KIAA1763 Cell recognition molecule Caspr4 protein protein human Homo sapiens Human MGSVTGAVLKTLLLLSTQNWNRVEAGNSYDCDDPLVSALPQASFSSSSELSSSHGPGFARLNRRDGAGGWSPLVSNKYQWLQIDLGERMEVTAVATQGGYGSSNWVTSYLLMFSDSGWNWKQYRQEDSIWGFSGNANADSVVYYRLQPSIKARFLRFIPLEWNPKGRIGMRIEVFGCAYRSEVVDLDGKSSLLYRFDQKSLSPIKDIISLKFKTMQSDGILLHREGPNGDHITLQLRRARLFLLINSGEAKLPSTSTLVNLTLGSLLDDQHWHSVLIQRLGKQVNFTVDEHRHHFHARGEFNLMNLDYEISFGGIPAPGKSVSFPHRNFHGCLENLYYNGVDIIDLAKQQKPQIIAMGNVSFSCSQPQSMPVTFLSSRSYLALPDFSGEEEVSATFQFRTWNKAGLLLFSELQLISGGILLFLSDGKLKSNLYQPGKLPSDITAGVELNDGQWHSVSLSAKKNHLSVAVDGQMASAAPLLGPEQIYSGGTYYFGGCPDKSFGSKCKSPLGGFQGCMRLISISGKVVDLISVQQGSLGNFSDLQIDSCGISDRCLPNYCEHGGECSQSWSTFHCNCTNTGYRGATCHNSIYEQSCEAYKHRGNTSGFYYIDSDGSGPLEPFLLYCNMTETAWTIIQHNGSDLTRVRNTNPENPYAGFFEYVASMEQLQATINRAEHCEQEFTYYCKKSRLVNKQDGTPLSWWVGRTNETQTYWGGSSPDLQKCTCGLEGNCIDSQYYCNCDADRNEWTNDTGLLAYKEHLPVTKIVITDTGRLHSEAAYKLGPLLCQGDRSFWNSASFDTEASYLHFPTFHGELSADVSFFFKTTASSGVFLENLGIADFIRIELRSPTVVTFSFDVGNGPFEISVQSPTHFNDNQWHHVRVERNMKEASLQVDQLTPKTQPAPADGHVLLQLNSQLFVGGTATRQRGFLGCIRSLQLNGMTLDLEERAQVTPEVQPGCRGHCSSYGKLCRNGGKCRERPIGFFCDCTFSAYTGPFCSNEISAYFGSGSSVIYNFQENYLLSKNSSSHAASFHGDMKLSREMIKFSFRTTRTPSLLLFVSSFYKEYLSVIIAKNGSLQIRYKLNKYQEPDVVNFDFKNMADGQLHHIMINREEGVVFIEIDDNRRRQVHLSSGTEFSAVKSLVLGRILEHSDVDQDTALAGAQGFTGCLSAVQLSHVAPLKAALHPSHPDPVTVTGHVTESSCMAQPGTDATSRERTHSFADHSGTIDDREPLANAIKSDSAVIGGLIAVVIFILLCITAIAVRIYQQKRLYKRSEAKRSENVDSAEAVLKSELNIQNAVNENQKEYFF DIP protein Q9C0A0-1 original sequence version: 109 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 tiam1_human Rho guanine nucleotide exchange factor TIAM1 TIAM1 T-lymphoma invasion and metastasis-inducing protein 1 protein protein human Homo sapiens Human MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI DIP protein Q13009 original sequence version: 132 DIP protein Q13009 original sequence version: 130 DIP protein Q13009 original sequence version: 119 0DAFBEE9A84B3452 cntnap4-tiam1-1 3 13 unspecified role unspecified role unspecified role unspecified role Region 1301-1308 Region 1301-1308 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc1-tiam1-1 1 11 unspecified role unspecified role unspecified role unspecified role Region 303-310 Region 303-310 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Dansyl-label Dansyl-label dansyl label dansyl label 5-dimethylaminonaphthalene-1-sulfonyl tag dansyl tag 5-dimethylaminonaphthalene-1-sulfonyl tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P18827:p.Glu306Lys E306K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E306K'. Wed May 02 14:38:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu306lys' Tue Jun 30 15:58:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu306Lys' in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc1-tiam1-2 2 11 unspecified role unspecified role unspecified role unspecified role Region 303-310 Region 303-310 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc3-tiam1-1 10 14 unspecified role unspecified role unspecified role unspecified role Region 435-442 Region 435-442 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Dansyl-label Dansyl-label dansyl label dansyl label 5-dimethylaminonaphthalene-1-sulfonyl tag dansyl tag 5-dimethylaminonaphthalene-1-sulfonyl tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 cntnap4-tiam1-2 4 13 unspecified role unspecified role unspecified role unspecified role Region 1301-1308 Region 1301-1308 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc1-tiam1-3 8 11 unspecified role unspecified role unspecified role unspecified role Region 303-310 Region 303-310 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc4-tiam1-1 6 15 unspecified role unspecified role unspecified role unspecified role Region 191-198 Region 191-198 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Dansyl-label Dansyl-label dansyl label dansyl label 5-dimethylaminonaphthalene-1-sulfonyl tag dansyl tag 5-dimethylaminonaphthalene-1-sulfonyl tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc1-tiam1-4 7 11 unspecified role unspecified role unspecified role unspecified role Region 303-310 Region 303-310 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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 sdc1-tiam1-5 9 11 unspecified role unspecified role unspecified role unspecified role Region 303-310 Region 303-310 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Dansyl-label Dansyl-label dansyl label dansyl label 5-dimethylaminonaphthalene-1-sulfonyl tag dansyl tag 5-dimethylaminonaphthalene-1-sulfonyl tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q13009:p.Lys912Glu K912E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K912E'. Wed May 02 17:46:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys912glu' Tue Jun 30 18:26:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys912Glu' Q13009:p.Lys879Glu K879E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K879E'. Wed May 02 19:53:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys879glu' Tue Jun 30 18:14:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys879Glu' ecolx Escherichia coli direct interaction direct interaction sdc2-tiam1-1 5 12 unspecified role unspecified role unspecified role unspecified role Region 194-201 Region 194-201 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Dansyl-label Dansyl-label dansyl label dansyl label 5-dimethylaminonaphthalene-1-sulfonyl tag dansyl tag 5-dimethylaminonaphthalene-1-sulfonyl tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 16 unspecified role unspecified role unspecified role unspecified role PDZ domain Region 841-930 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