DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil. Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil. Structure (London, England : 1993) 2006 imex curation Yamaguchi H., Kasa M., Amano M., Kaibuchi K., Hakoshima T. Only protein-protein interactions spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Yamaguchi H., Kasa M., Amano M., Kaibuchi K., Hakoshima T. DIP original experiment: DIP-66150X Structure (London, England : 1993) 2006 IMEx Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil. rock2_bovin Rho-associated protein kinase 2 Rho-associated, coiled-coil-containing protein kinase II ROCK2 Rho-associated, coiled-coil-containing protein kinase 2 p164 ROCK-2 protein protein bovin Bos taurus (Bovine) Bovine MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNPLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQSRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEITLRKNVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDVKNGKILLAKVELEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEETEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLSEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLLEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKEAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDTEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS DIP protein Q28021 original sequence version: 56 CA83CE7D3860465D rock2-1 1 2 unspecified role unspecified role unspecified role unspecified role Region 18-417 Region 18-417 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction