DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. Only protein-protein interactions in vitro In vitro polymerization polymerization predetermined predetermined participant predetermined Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250065X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250064X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250068X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. Only protein-protein interactions in vitro In vitro polymerization polymerization predetermined predetermined participant predetermined Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250067X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250066X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. 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 Nag S., Ma Q., Wang H., Chumnarnsilpa S., Lee WL., Larsson M., Kannan B., Hernandez-Valladares M., Burtnick LD., Robinson RC. DIP original experiment: DIP-250063X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin. acts_rabit Actin, alpha skeletal muscle ACTA1 ACTA Alpha-actin-1 protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF DIP protein P68135 original sequence version: 41 DIP protein P68135 original sequence version: 27 DIP protein P68135 original sequence version: 28 DIP protein P68135 original sequence version: 96 DIP protein P68135 original sequence version: 29 DIP protein P68135 original sequence version: 89 DIP protein P68135 original sequence version: 39 DIP protein P68135 original sequence version: 42 DIP protein P68135 original sequence version: 59 DIP protein P68135 original sequence version: 55 DIP protein P68135 original sequence version: 60 DIP protein P68135 original sequence version: 65 DIP protein P68135 original sequence version: 67 DIP protein P68135 original sequence version: 63 DIP protein P68135 original sequence version: 68 DIP protein P68135 original sequence version: 79 DIP protein P68135 original sequence version: 88 DIP protein P68135 original sequence version: 84 DIP protein P68135 original sequence version: 101 DIP protein P68135 original sequence version: 94 DIP protein P68135 original sequence version: 95 DIP protein P68135 original sequence version: 97 DIP protein P68135 original sequence version: 100 DIP protein P68135 original sequence version: 102 DIP protein P68135 original sequence version: 83 DF2A3A046346A179 gels_human Gelsolin GSN Actin-depolymerizing factor Brevin AGEL protein protein human Homo sapiens Human MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA DIP protein P06396 original sequence version: 89 DIP protein P06396 original sequence version: 176 DIP protein P06396-1 original sequence version: 115 DIP protein P06396 original sequence version: 138 DIP protein P06396-1 original sequence version: 138 DIP protein P06396 original sequence version: 184 DIP protein P06396 original sequence version: 137 8CEBC52257A160F7 acta1-6 3 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-gsn-4 6 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role G1-3 domain Region 52-399 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-gsn-5 5 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role Region 52-728 Region 52-728 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-gsn-6 2 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role G1-3 domain Region 52-399 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-gsn-7 1 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role G2-3 domain Region 159-399 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain G4-6 domain Region 431-729 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 direct interaction direct interaction acta1-7 4 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction