DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133478X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133480X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133481X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133479X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. 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 Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133475X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133473X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133483X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight identificat confirmation by molecular weight weight identificat Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133477X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133482X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight identificat confirmation by molecular weight weight identificat Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133474X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. 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 Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133476X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Kudryashov DS., Durer ZA., Ytterberg AJ., Sawaya MR., Pashkov I., Prochazkova K., Yeates TO., Loo RR., Loo JA., Satchell KJ., Reisler E. DIP original experiment: DIP-133472X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. 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 martx_vibch Multifunctional-autoprocessing repeats-in-toxin rtxA rtx VC_1451 protein protein vibch Vibrio cholerae MVFYLIPKRRVWLMGKPFWRSVEYFFTGNYSADDGNNNIVAIGFGGQIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLKVEDSTGHLIVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNHGDVSYGGAAAYNGITRKGLSGNVTFAGAGGYNALWHETNQGNLSFTGAGAGNKLDRTWSNRYQGSHGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTHQAEDVYTQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTIIRKGSGNDFAKEGMTNAKADEIVLTKAVMSGSWIGQDHHVTAVKSASEPNTYLFAFADSTYTKINKVQLRNDPQTGELKYYSTAWYKEVNHLSNLANQDISDNGGFTAVNINGAYTLSDLKVEHQQSVTVHAVEKSLTEYEWVTYANGAVIDAKEVSLSDAKMGGHAIYADGTKVDVKAVKSNRQPNTYIYAKVLGPYTKIVVVELANDPETGALKYQARSWYKEGDHTANIANQDISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTDQTLFKPANDSGESSGDVRFNGAGGGNVIKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTVLGVGGSQAINYLVQGDEASSSGTHKGRGAIATPEITKLDGFQMDAIKEVSSDLGDSLTGSVTKVDTPDLNKMQHALNVDDSSVQAPNLIVNGDFELGEHGWQSTHGVEASYAGSVYGVEGEGHGARVTELDTYTNTSLYQDLANLAQGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDESAWQQKNLKLTAQAGSNRIEFKGTGHNDGLGYILDNVVATSESSQQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALENNGQAQRDAVKEESEAVTAELAKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGDRPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQINAGIRAKNSVSSMTSMFSETNSKSIVVPTKVSPEPERQEVTRRDVRISGVNLESLSAVQGSQPTGQLASKSVPGFKSHFASTSIGIENELSGLVVVLPKNSAQTFGYVHDSQGNPLFMLTKDMNQGGYSNPVGINDIQGVNNWQTHTIELVTYPSEISDTAAVESRKEAMLWLAKEFTDHINQSNHQSLPHLVSDDGRFTLVISNSKHLIAAGNGTSIDAQGKTIGMTPSGQQATMAISAKEFGTSSSPEVRLLESAPWYQAGLRDEFLANAKNTTLDDPATAQNVYAYLTSVYSKTADLAKEYGIYINDWDPASEGFSPNAQGLTDPKVKNAWSILPRTKPVRMLELLSAEDSRYVRQQIAEKLKGTYSESLAKNVFEYFQYGGEVAGHGINNATTGSVQQPEPAILFEFRSVPSALSDFVPKTASTVKVDVKALDHFDSASRKAIITEVNALVSGSEDFDAWYQEYRASKGQPPVKNPKSSASANHKAEWLMTQHAEQWAKITAPYTDNHETLTSTKLASNDKEELHALGETSNLENNKQQENVASIINTMLNDMLPFYALRTERNLLVQEGDEGFEVRAWPGTEDKSKTIILEDPEDAAQHKAIERFILANFDNFEQMPDELFLVDNKVISHHEGRTHVLAQKVDGAWQYNATVELMSVTELLDAANVTGKIRGESYQQVIDALTDYHASITEHADYEPESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQVNTRLDEVSLLSVAEQTIQAQNSFSRLYDQLEAANLKESKHLYLDQNGDFVTKGKGNLANIDLLGSREAVLEKVKLTVSNEYGQTVADTIFAGLSAKDLAKDGKGVDIAGLNKVHQAIEQHLSPVSATLYIWKPSDHSALGHAALQIGQGRTQLEGQAAADFNQQNYVSWWPLGSKSSNISNILNVATKDQPDLKLRWSDFSQPAHQNDTLEHDVASEENDGFGLHDGDIKLKRFIEKLNAAKGIDASFKEASEGYASVLLGNPDMLETTSIPAHVFQPFVEQWNDTSYDMMDVAHRFAQELRLQAQRSDDPELLEKRIGNVIRQFAERALEEIETFKASQADQGRVFRINLEGLDVAAMQAEWHRLSNDPDARYQLLTKNCSSTVAKVLKAGGADKLIGHTWLPKFGVWTPTELFNFGQALQEAQLEIAAKKQSHQVTDVLDALSGNEKPKENVAIENDGTPPRDKESLSPLTRFLNNELYGDKEARRKIGEITQTLLDHAVEKGESQKITLQGEAGRLTGYYHQGTAPSEGETSSPSGKVVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVSGLLLDRPMPSMTKAITAHEVANPAGIVGAIAKAVNGQFSVEKNLEGLPKETSILLLTDNEGLGNEGEKLRTKLTASGYNVTGEQTFYGHEASNRLMSQYADQIVSGLSSSASVDEDLDQQGLDTTSTKDQGISNKNDHLQVVDSKEALADGKILHNQNVNSWGPITVTPTTDGGETRFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDHSETNNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHTKDANGDWVQKAENNKVSLSWDAQGEVVAKDERIRNGIAEGDIDLSRIGVNNVDEPARGAIGDNNDVFDAPEKRKPETEVIANSSSSNQFSYSGNIQVNVGEGEFTAVNWGTSNVGIKVGTGGFKSLAFGDNNVMVHIGDGESKHSVDIGGYQALEGAQMFLGNRNVSFNFGHSNDLILMMDKSIPTPPLVNPFDGAARISGVLQGIATSGEGEDWLAAQEQQWTLSGAKKFVKDMSGLDQSSSVDYTTLVELDSQNERDSRGLKHDAEATLNKQYNQWLSGNGNSGTSQLSRADKLRQANEKLAFNFAVGGQGADIQVTTGNWNFMFGDNIQSILDTNLGSLFGLMTQQFTATGQAKTTFTYTPQDLPRQLKNKLLGQLAGVGAETTLADIFGVDYTASGQIVSRNGQAVDGVAILKEMLEVIGEFSGDQLQAFVDPAKLLDSLKAGIDMGADGIKSFAETHGLKEKAPEEEKDNSSVSVNGANVNSAQGATVADGNTETAETQDRAFGFNSLNLPNLFATIFSQDKQKEMKSLVENLKQNLTADLLNMKEKTFDFLRNSGHLQGDGDINISLGNYNFNWGGDGKDLGAYLGDNNNFWGGRGDDVFYATGKSNIFTGGEGNDMGVLMGRENMMFGGDGNDTAVVAGRINHVFLGAGDDQSFVFGEGGEIDTGSGRDYVVTSGNFNRVDTGDDQDYSVTIGNNNQVELGAGNDFANIFGNYNRINAGAGNDVVKLMGYHAVLNGGDGDDHLIATAISKFSQFNGGEGRDLMVLGGYQNTFKGGTDVDSFVVSGDVIDNLVEDIRSEDNIVFNGIDWQKLWFERSGYDLKLSILRDPSNDSDQSKFEHIGSVTFSDYFNGNRAQVVIGMSEKDLSGEREYTMLSDSAIDALVQAMSGFEPQAGDNGFIDSLESKSQAAISMAWSDVVHKKGLMV 800DD5D1D119AE19 act_yeast Actin ACT1 ABY1 END7 YFL039C protein protein yeast Saccharomyces cerevisiae Baker's yeast MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF 87AC19B0B0BC9E71 87AC19B0B0BC9E71 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 dnas1_bovin Deoxyribonuclease-1 DNASE1 DNL1 Deoxyribonuclease I protein protein bovin Bos taurus (Bovine) Bovine MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT DIP protein P00639 original sequence version: 78 DIP protein P00639 original sequence version: 132 DIP protein P00639 original sequence version: 109 mint Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization 43904EF0D5F2E0E2 acta1-24 10 13 unspecified role unspecified role unspecified role unspecified role Region 48-68 Region 48-68 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Region 227-375 Region 227-375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain rabit Oryctolagus cuniculus (Rabbit) Rabbit covalent binding covalent binding acta1-25 2 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acd-acta1-1 12 14 enzyme enzyme unspecified role unspecified role Region 1963-2375 Region 1963-2375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 enzyme target enzyme target substrate substrate unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit enzymatic reaction enzymatic reaction Biochemical reaction Biochemical reaction acd-acta1-2 7 14 unspecified role unspecified role unspecified role unspecified role Region 1963-2375 Region 1963-2375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acd-acta1-3 3 14 unspecified role unspecified role unspecified role unspecified role Region 1963-2375 Region 1963-2375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-dnase1-3 5 17 unspecified role unspecified role unspecified role unspecified role bovin Bos taurus (Bovine) Bovine 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit physical association physical association scactin-1 8 15 unspecified role unspecified role unspecified role unspecified role P60010:p.[Lys50Cys;Cys374Ala] K50C/C374A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K C certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'K50C/C374A'. Wed May 02 19:16:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys50cys,cys374ala' Tue Jun 30 17:40:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys50Cys;Cys374Ala]' P60010:p.[Glu270Cys;Cys374Ala] E270C/C374A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C A certain certain sequence position certain certain certain sequence position certain E C This feature has been corrected as a result of our quality control procedures. The original label was 'E270C/C374A'. Wed May 02 17:22:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu270cys,cys374ala' Tue Jun 30 17:08:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu270Cys;Cys374Ala]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast covalent binding covalent binding acd-scactin-1 6 14 enzyme enzyme unspecified role unspecified role Region 1963-2375 Region 1963-2375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 enzyme target enzyme target substrate substrate unspecified role unspecified role P60010:p.[Lys50Cys;Cys374Ala] K50C/C374A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K C certain certain sequence position certain certain certain sequence position certain C A This feature has been corrected as a result of our quality control procedures. The original label was 'K50C/C374A'. Wed May 02 19:53:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys50cys,cys374ala' Tue Jun 30 17:49:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys50Cys;Cys374Ala]' P60010:p.[Glu270Cys;Cys374Ala] E270C/C374A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C A certain certain sequence position certain certain certain sequence position certain E C This feature has been corrected as a result of our quality control procedures. The original label was 'E270C/C374A'. Wed May 02 16:11:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu270cys,cys374ala' Tue Jun 30 17:46:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu270Cys;Cys374Ala]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast enzymatic reaction enzymatic reaction Biochemical reaction Biochemical reaction acta1-26 1 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-27 4 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acd-acta1-4 9 14 unspecified role unspecified role unspecified role unspecified role Region 1963-2375 Region 1963-2375 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-gsn-8 11 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction