DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111193X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight silver stain molecular weight estimation by silver staining weight silver stain Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111200X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111194X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm dls dynamic light scattering dls predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111195X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm dls dynamic light scattering dls predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111196X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111197X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight silver stain molecular weight estimation by silver staining weight silver stain Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111192X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111198X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Wenta N., Strauss H., Meyer S., Vinkemeier U. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Wenta N., Strauss H., Meyer S., Vinkemeier U. DIP original experiment: DIP-111199X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations. p42224-1 Signal transducer and activator of transcription 1-alpha/beta STAT1 Transcription factor ISGF-3 components p91/p84 p91 protein protein human Homo sapiens Human MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV DIP protein P42224-1 original sequence version: 108 DIP protein P42224 original sequence version: 188 DIP protein P42224 original sequence version: 181 DIP protein P42224-1 original sequence version: 181 stat4_human Signal transducer and activator of transcription 4 STAT4 protein protein human Homo sapiens Human MSQWNQVQQLEIKFLEQVDQFYDDNFPMEIRHLLAQWIENQDWEAASNNETMATILLQNLLIQLDEQLGRVSKEKNLLLIHNLKRIRKVLQGKFHGNPMHVAVVISNCLREERRILAAANMPVQGPLEKSLQSSSVSERQRNVEHKVAAIKNSVQMTEQDTKYLEDLQDEFDYRYKTIQTMDQSDKNSAMVNQEVLTLQEMLNSLDFKRKEALSKMTQIIHETDLLMNTMLIEELQDWKRRQQIACIGGPLHNGLDQLQNCFTLLAESLFQLRRQLEKLEEQSTKMTYEGDPIPMQRTHMLERVTFLIYNLFKNSFVVERQPCMPTHPQRPLVLKTLIQFTVKLRLLIKLPELNYQVKVKASIDKNVSTLSNRRFVLCGTNVKAMSIEESSNGSLSVEFRHLQPKEMKSSAGGKGNEGCHMVTEELHSITFETQICLYGLTIDLETSSLPVVMISNVSQLPNAWASIIWYNVSTNDSQNLVFFNNPPPATLSQLLEVMSWQFSSYVGRGLNSDQLHMLAEKLTVQSSYSDGHLTWAKFCKEHLPGKSFTFWTWLEAILDLIKKHILPLWIDGYVMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDHSESGEVRFHSVEPYNKGRLSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPCEVSRPTERGDKGYVPSVFIPISTIRSDSTEPHSPSDLLPMSPSVYAVLRENLSPTTIETAMKSPYSAE DIP protein Q14765 original sequence version: 81 11E43803A9AF4FFA p42224-2 Signal transducer and activator of transcription 1-alpha/beta STAT1 Transcription factor ISGF-3 components p91/p84 p84 protein protein human Homo sapiens Human MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEV DIP protein P42224-2 original sequence version: 108 stat1-1 7 10 unspecified role unspecified role unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat4-1 9 11 unspecified role unspecified role unspecified role unspecified role Region 2-124 Region 2-124 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction stat1-4 5 12 unspecified role unspecified role unspecified role unspecified role Region 132-712 Region 132-712 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat1-5 6 12 unspecified role unspecified role unspecified role unspecified role Region 132-712 Region 132-712 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat1-6 3 12 unspecified role unspecified role unspecified role unspecified role Region 132-712 Region 132-712 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat1-7 2 12 unspecified role unspecified role unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat1-8 8 10 unspecified role unspecified role unspecified role unspecified role Region 132-712 Region 132-712 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Region 1-130 Region 1-130 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat1-9 4 10 unspecified role unspecified role unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction stat4-3 1 11 unspecified role unspecified role unspecified role unspecified role Region 2-124 Region 2-124 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction