DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight by comassie molecular weight estimation by coomasie staining weight by comassie Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261908X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261912X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261904X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions ecolx Escherichia coli crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261910X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261916X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261915X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions ecolx Escherichia coli crosslink cross-linking study crosslink predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261909X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261919X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261913X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261903X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261918X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261914X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261911X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261917X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261905X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261906X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure (London, England : 1993) 2014 imex curation Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. 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 Pal M., Morgan M., Phelps SE., Roe SM., Parry-Morris S., Downs JA., Polier S., Pearl LH., Prodromou C. DIP original experiment: DIP-261907X Structure (London, England : 1993) 2014 IMEx Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. hs90a_human Heat shock protein HSP 90-alpha HSP90AA1 HSP90A HSPC1 Heat shock 86 kDa Renal carcinoma antigen NY-REN-38 HSPCA Lipopolysaccharide-associated protein 2 protein protein human Homo sapiens Human MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD DIP protein P07900 original sequence version: 197 DIP protein P07900 original sequence version: 116 DIP protein P07900 original sequence version: 150 DIP protein P07900-1 original sequence version: 158 DIP protein P07900 original sequence version: 207 DIP protein P07900 original sequence version: 192 DIP protein P07900 original sequence version: 156 969F65FCC0BC86FD telo2_mouse Telomere length regulation protein TEL2 homolog Kiaa0683 Telo2 protein protein mouse Mus musculus Mouse MDPALSAVRLTVQEAIHILSSSEDAGHILSTLGTLKRYLGGTEDPVLPEEKEEFATVHFSAVLRCLVSKLSPGWLELSPGGQLERLWESFFLDGPPDQAFLVLMEAIESTAGPSFRLMKMAQLLDTFLSTGRVAALMEEQCRPQTKPSFPLFQETLLSKVVGLPDLLGNCLQRDNLTQFFPQNYFPLLGQEVVQALKAVVNFLQDGLDCSVSFVSRVLGKVCIQGRKREILSVLVPQLTVLTQDSCLWQRVCWRLVEQVPDRAVEAVLTGLVEAAPRPEVLSRLLGNLVVKNKKARFVVTRKLLLLQYQHTTPMVQSLLGYLALDSQRRPLLIQVLKELLETWGCSSAVRHTPLEQQCYISKAILVCLAHLGEPELQDIRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVISSRIHPEGPLLKFQYEDDEMSRELLALATPEPAGDCSSVSRGPSPAPVDTESPVEMPEKAVESDVPPTQPQGSDSELDSDDEFIPYDMSGDRELKSSKEPLYIRDCVEALTTSEDMERWEASLKGLEGLVYRSPTATREVSVELAKVLLHLEEKTCVAEFEQLRQSALVAVTVTDPEQVAKYLTSQFYGLNYSLRQRMDILDVLVLAAQALSRPKSLQRRSQHGPPVPGTMCSPALAVSQTGNVAAPDWQVVVEERIRSKTRRFSKGCPQRELSGVPNEFSSVAGYFFFPLLQHFDRPLVTFDLLGDDQLVLGRLTHTLASLMYLAVNTTVAVPMGKALLEFVWALRFHVDIYVRRGLLSAVSSVLLSVPTERLLGDLPDELLEARSWLADVAEKDVDEDCRELAVRALLLLERLKDKLLSSSSPQP DIP protein Q9DC40 original sequence version: 74 C3ADB9DCE1724EAC tah1_yeast TPR repeat-containing protein associated with Hsp90 YCR60W YCR060W TAH1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSQFEKQKEQGNSLFKQGLYREAVHCYDQLITAQPQNPVGYSNKAMALIKLGEYTQAIQMCQQGLRYTSTAEHVAIRSKLQYRLELAQGAVGSVQIPVVEVDELPEGYDRS 3738DE6F227F803A 3738DE6F227F803A pihd1_mouse PIH1 domain-containing protein 1 Pih1d1 Nop17 Nucleolar protein 17 homolog protein protein mouse Mus musculus Mouse MADSTFLAPELSDTESMGEETVRFQELLLKASKELQQAQTARPDSTQIQPKPGFCVKTNSSEGKVFINICHSPSIPPPADVTEDELLQMLEEDQAGFRIPMSLGEPHAELDAKGQGCTAYDVAVNSNFYLRMQNSDFLRELVVTIAREGLEDKYGLQLNPEWRMLKYRSFLGSISQQNIRSQQRPRIQELGTLDASGSLGTCHGPERPHLNLWLEAPDLLLAEVDLPKLDGAQGLALEIGENRLVIGGPQQLYHLDATVPLRINSEASRAAFHRRRKQLMVSMPLLTASS DIP protein Q9CQJ2 original sequence version: 82 8624B7EF592E3F59 rpap3_human RNA polymerase II-associated protein 3 RPAP3 protein protein human Homo sapiens Human MTSANKAIELQLQVKQNAEELQDFMRDLENWEKDIKQKDMELRRQNGVPEENLPPIRNGNFRKKKKGKAKESSKKTREENTKNRIKSYDYEAWAKLDVDRILDELDKDDSTHESLSQESESEEDGIHVDSQKALVLKEKGNKYFKQGKYDEAIDCYTKGMDADPYNPVLPTNRASAYFRLKKFAVAESDCNLAVALNRSYTKAYSRRGAARFALQKLEEAKKDYERVLELEPNNFEATNELRKISQALASKENSYPKEADIVIKSTEGERKQIEAQQNKQQAISEKDRGNGFFKEGKYERAIECYTRGIAADGANALLPANRAMAYLKIQKYEEAEKDCTQAILLDGSYSKAFARRGTARTFLGKLNEAKQDFETVLLLEPGNKQAVTELSKIKKELIEKGHWDDVFLDSTQRQNVVKPIDNPPHPGSTKPLKKVIIEETGNLIQTIDVPDSTTAAAPENNPINLANVIAATGTTSKKNSSQDDLFPTSDTPRAKVLKIEEVSDTSSLQPQASLKQDVCQSYSEKMPIEIEQKPAQFATTVLPPIPANSFQLESDFRQLKSSPDMLYQYLKQIEPSLYPKLFQKNLDPDVFNQIVKILHDFYIEKEKPLLIFEILQRLSELKRFDMAVMFMSETEKKIARALFNHIDKSGLKDSSVEELKKRYGG DIP protein Q9H6T3 original sequence version: 97 70D5A965E4F1EE35 mre11_human Double-strand break repair protein MRE11 MRE11 Double-strand break repair protein MRE11A HNGS1 MRE11A Meiotic recombination 11 homolog 1 Meiotic recombination 11 homolog A protein protein human Homo sapiens Human MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR DIP protein P49959 original sequence version: 152 DIP protein P49959 original sequence version: 146 DIP protein P49959 original sequence version: 114 DIP protein P49959 original sequence version: 161 DIP protein P49959 original sequence version: 168 DIP protein P49959 original sequence version: 173 DIP protein P49959 original sequence version: 154 DIP protein P49959-1 original sequence version: 127 DIP protein P49959 original sequence version: 96 DIP protein P49959 original sequence version: 115 D94ABFBDDF6106AD pih1_yeast Protein interacting with Hsp90 1 PIH1 NOP17 Nucleolar protein 17 YHR034C protein protein yeast Saccharomyces cerevisiae Baker's yeast MADFLLRPIKQRHRNEDKYVSVDAADGSVSKIEPIADFVIKTKLLSANGPEKLQDGRKVFINVCHSPLVPKPEVDFNARIVFPLIIQNEWEIPIITSCYRMDHDKKGQECYVWDCCINSDCSRWICDDIQLREILVEWCLESCEIRDSVVLCRDRIAFPKMKKKGAELPALEVLNDELHQDYKAKMHKIIEEEAGDPMSILRGRNDDGDDNNDPDDGTLPPLFPIENKISGAKIEEIDKNEIAHRNLKQAPAPAPAPHEQQEDVPEYEVKMKRFKGAAYKLRILIENKAPNSKPDRFSPSYNFAENILYINGKLSIPLPRDIVVNAADIKIFHIRKERTLYIYI 02C06D0A113B1B3B 02C06D0A113B1B3B hsp82_yeast ATP-dependent molecular chaperone HSP82 HSP90 YPL240C HSP82 Heat shock protein Hsp90 heat-inducible isoform 82 kDa heat shock protein protein protein yeast Saccharomyces cerevisiae Baker's yeast MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD D7C35676D668FB63 D7C35676D668FB63 hs90b_human Heat shock protein HSP 90-beta HSP90AB1 HSP90B HSPC2 HSPCB Heat shock 84 kDa protein protein human Homo sapiens Human MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD DIP protein P08238 original sequence version: 91 DIP protein P08238 original sequence version: 149 DIP protein P08238 original sequence version: 165 DIP protein P08238 original sequence version: 167 DIP protein P08238 original sequence version: 210 DIP protein P08238 original sequence version: 187 A93118C214D03810 yhsp90-1 17 25 unspecified role unspecified role unspecified role unspecified role Region 600-709 Region 600-709 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ypih1-ytah1-1 10 24 unspecified role unspecified role unspecified role unspecified role Region 187-344 Region 187-344 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hsp90aa1-rpap3-1 2 18 unspecified role unspecified role unspecified role unspecified role Region 726-732 Region 726-732 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 22 unspecified role unspecified role unspecified role unspecified role Region 265-380 Region 265-380 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pih1d1-telo2-9 5 19 unspecified role unspecified role unspecified role unspecified role Region 489-496 Region 489-496 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pS492 pS492 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain in vitro In vitro 21 unspecified role unspecified role unspecified role unspecified role Region 1-200 Region 1-200 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ytah1-yhsp90-1 1 25 unspecified role unspecified role prey prey Region 600-709 Region 600-709 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction hsp90aa1-ypih1-1 3 18 unspecified role unspecified role unspecified role unspecified role Region 726-732 Region 726-732 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 24 unspecified role unspecified role unspecified role unspecified role Region 187-344 Region 187-344 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association pih1d1-telo2-10 14 19 unspecified role unspecified role unspecified role unspecified role Region 488-496 Region 488-496 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pS492 pS492 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain in vitro In vitro 21 unspecified role unspecified role unspecified role unspecified role Region 47-179 Region 47-179 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hsp90aa1-rpap3-2 9 18 unspecified role unspecified role unspecified role unspecified role Region 723-732 Region 723-732 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 22 unspecified role unspecified role unspecified role unspecified role Region 120-395 Region 120-395 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9H6T3:p.[Asn172Glu;Asn321Glu] N172E/N321E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain N E certain certain sequence position certain certain certain sequence position certain N E This feature has been corrected as a result of our quality control procedures. The original label was 'N172E/N321E'. Wed May 02 17:58:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn172glu,asn321glu' Tue Jun 30 17:07:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asn172Glu;Asn321Glu]' Q9H6T3:p.Asn172Glu N172E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain N E This feature has been corrected as a result of our quality control procedures. The original label was 'N172E'. Wed May 02 16:03:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn172glu' Tue Jun 30 17:52:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn172Glu' ecolx Escherichia coli direct interaction direct interaction mre11-pih1d1-1 8 23 unspecified role unspecified role unspecified role unspecified role pS558 pS558 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain in vitro In vitro 21 unspecified role unspecified role unspecified role unspecified role Region 1-200 Region 1-200 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction yhsp90-2 7 25 unspecified role unspecified role unspecified role unspecified role Region 600-709 Region 600-709 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pih1d1-telo2-11 11 19 unspecified role unspecified role unspecified role unspecified role Region 484-496 Region 484-496 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pS492 pS492 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm pS492/488 pS492/488 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm pS488 pS488 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm pS486/488 pS486/488 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm pS486 pS486 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm in vitro In vitro 21 unspecified role unspecified role unspecified role unspecified role Region 1-200 Region 1-200 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9CQJ2:p.Lys57Glu K57E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K57E'. Wed May 02 18:04:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys57glu' Tue Jun 30 17:56:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys57Glu' Q9CQJ2:p.Lys64Glu K64E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K64E'. Wed May 02 19:50:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys64glu' Tue Jun 30 20:18:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys64Glu' ecolx Escherichia coli direct interaction direct interaction yhsp90-ytah1-1 15 25 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ytah1-1 4 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rpap3-yhsp90-1 12 25 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 22 unspecified role unspecified role unspecified role unspecified role Region 120-395 Region 120-395 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction yhsp90-ypih1-1 16 24 unspecified role unspecified role unspecified role unspecified role Region 187-344 Region 187-344 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 25 unspecified role unspecified role unspecified role unspecified role Region 600-709 Region 600-709 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association hsp90aa1-rpap3-3 13 18 unspecified role unspecified role unspecified role unspecified role Region 726-732 Region 726-732 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 22 unspecified role unspecified role unspecified role unspecified role Region 120-255 Region 120-255 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hsp90ab1-rpap3-1 6 26 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 22 unspecified role unspecified role prey prey Region 120-395 Region 120-395 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9H6T3:p.Asn172Glu N172E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain N E This feature has been corrected as a result of our quality control procedures. The original label was 'N172E'. Wed May 02 19:34:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn172glu' Tue Jun 30 17:40:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn172Glu' Q9H6T3:p.[Asn172Glu;Asn321Glu] N172E/N321E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain N E certain certain sequence position certain certain certain sequence position certain N E This feature has been corrected as a result of our quality control procedures. The original label was 'N172E/N321E'. Wed May 02 14:28:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn172glu,asn321glu' Tue Jun 30 17:51:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asn172Glu;Asn321Glu]' ecolx Escherichia coli direct interaction direct interaction