mbinfo MBInfo http://www.mechanobio.info/ Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J. Cell Biol. (0021-9525) 1990 imex curation Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J., Hartwig J.H. host organism: chlae cos cells. Cross-linking agent DMA - dimethyl adipimidate, a membrane-permeable crosslinker Within the gelsolin-filamin A fusion protein, the source of gelsolin traced from references and the source of filamin A (ABP) specified by the author. No contact-email given in the publication. 15-Nov-2012: Contacted by pporras. Only protein-protein interactions chlae Chlorocebus aethiops Cercopithecus aethiops Grivet Green monkey crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot Gorlin J.B., Yamin R., Egan S., Stewart M., Stossel T.P., Kwiatkowski D.J., Hartwig J.H. host organism: chlae cos cells. Cross-linking agent DMA - dimethyl adipimidate, a membrane-permeable crosslinker Within the gelsolin-filamin A fusion protein, the source of gelsolin traced from references and the source of filamin A (ABP) specified by the author. No contact-email given in the publication. Accepted 2012-NOV-06 by ORCHARD 15-Nov-2012: Contacted by pporras. J. Cell Biol. (0021-9525) 1990 Only protein-protein interactions imex curation flna_human Filamin-A FLNA FLN FLN1 Alpha-filamin Filamin-1 Endothelial actin-binding protein Actin-binding protein 280 Non-muscle filamin protein protein human Homo sapiens Human MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP DIP protein P21333 original sequence version: 185 DIP protein P21333-1 original sequence version: 187 DIP protein P21333 original sequence version: 115 DIP protein P21333 original sequence version: 144 DIP protein P21333-1 original sequence version: 156 DIP protein P21333 original sequence version: 201 DIP protein P21333 original sequence version: 197 DIP protein P21333 original sequence version: 170 6C1A07041DF50142 flna-flna-1 1 2 unspecified role unspecified role unspecified role unspecified role c-terminal region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain The C-terminal region [2282-2647] includes repeats 21-24 of filamin A. region uncategorized protein modification uncategorized protein modification undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined The C-terminal Filamin A constructs are fused to 12 amino acids corresponding to the plasma extension region of gelsolin. 2 unspecified role unspecified role unspecified role unspecified role c-terminal region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain The C-terminal region [2282-2647] includes repeats 21-24 of filamin A. region uncategorized protein modification uncategorized protein modification undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined The C-terminal Filamin A constructs are fused to 12 amino acids corresponding to the plasma extension region of gelsolin. 8 5 physical association physical association Fig 11B. The C-terminal region including repeat 24 of filamin A [2282-2647] is required for the dimerization of filamin A, since a filamin A c-terminal mutant [2282-2582] did not homodimerize [Fig 11B].