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HSP90

Gene
HSP90
Protein
Endoplasmin homolog
Organism
Catharanthus roseus
Length
817 amino acids
Function
May have a molecular chaperone role in the processing of secreted materials.
Similarity
Belongs to the heat shock protein 90 family.
Mass
93.492 kDa
Sequence
MRKWTVPSVLFLLCPSLSSSCQGRKIHANAEADSDAPVDPPKVEDKIGAVPNGLSTDSDVAKREAESMSMRNLRSDAEKFEFQAEVSRLMDIIINSLYSNKDIFLRELISNASDALDKIRFLALTDKEILGEGDTAKLEIQIKLDKEKKILSIRDRGIGMTKEDLIKNLGTIAKSGTSAFVEKMQTSGDLNLIGQFGVGFYSVYLVPDYVEVISKHNDDKQYIWESKADGAFAISEDVWNEPLGRGTEIRLHLRDEAQEYLDEFKLKELVKRYSEFINFPIYLWASKEVEVEVPAEEDDSSDDEDNKSESSSSEEGEEEETEKEEDEKKPKTKKVKETTYEWELLNDMKAIWLRNPKDVTDDEYTKFYHSLAKDFSEEKPLAWSHFTAEGDVEFKAFTLLPPKAPQDLYESYYNSNKSNLKLYVRRVFISDEFDELLPKYLNFLKGLVDSDTLPLNVSREMLQQHSSLKTIKKKLIRKALDMIRKIADEDPDEANDKDKKEVEESTDNDEKKGQYAKFWNEFGKSIKLGIIEDAANRNRLAKLLRFESTKSEGKLTSLDQYISRMKSGQKDIFYITGTSKEQLEKSPFLERLTKKNYEVILFTDPVDEYLMQYLMDYEDKKFQNVSKEGLKIGKDSKDKELKESFKELTKWWKGALASENVDDVKISNRLANTPCVVVTSKYGWSSNMERIMQSQTLSDASKQAYMRGKRVLEINPRHPIIKELRERVVKDAEDESVKQTARLMYQTALMESGFMLNDPKEFASSIYDSVKSSLKISPDATVEEEDDTEEAEAESGTTESSAAEDAGAETLDLKDEL

Gene
HSP90
Protein
Heat shock protein 90
Organism
Brugia pahangi
Length
717 amino acids
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Similarity
Belongs to the heat shock protein 90 family.
Mass
82.605 kDa
Sequence
MSEEMNGETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYQALTEPAELETGKELYIKITPNKADKTLTIMDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAFLVADKVVVASKHNDDDCYQWESSAGGSFIIRQVNDPELTRGTKITLYIKEDQTDYLEERRIKEIVKKHSQFIGYPIKLTVEKERDKEVSDDEAEEEKKDEDKEKKEGEIEDVGEDEEEDKKDKDKKKKKIKEKYHEDEELNKTKPIWTRNPDDISNEEYAEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPQRAPFDLFENKKTKNAIKLYVRRVFIMENCDELMPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFDEIAEDKDNFKKFYEQFSKNIKLGIHEDSTNRKKLSEFLRFYTSASSEEMTSLKDYVSRMKENQKQIYFITGESREAVASSAFVERVKRRGFEVIYMTDPIDEYCVQQLKEYDGKKLVSVTKEGLELPESEEEKKKFEEDKVKFENLCKVMKDILEKKVEKVAVSNRLVSSPCCIVTSEYGWSANMERIMKAQALRDSSTMGYMAAKKHLEINPDHSVIKALRERVEADKNDKTVKDLVVLLFETALLSSGFSLEDPQLHASRIYRMIKLGLDITEDEEEEAIASVSGEKDECVPNLVGAEEDASRMEEVD

Gene
HSP90
Protein
Heat shock protein 90
Organism
Eimeria tenella
Length
713 amino acids
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Similarity
Belongs to the heat shock protein 90 family.
Mass
82.413 kDa
Sequence
MENKETFAFNADIQQLMSLIINTFYSNKEIFLRELISNASDALDKIRYEAITEPEKLKTKPELFIRLIPDKANNTLTIENSGIGMTKADLVNNLGTIARSGTKAFMEALQAGGDISMIGQFGVGFYSAYLVADSVTVVSKHNDDEQYVWESAAGGSFTVQKDDKYEPLGRGTRIILHLKEDQGEYLEERRLKDLVKKHSEFISFPIELAVEKTHEREVTESEDEEEKKADEKAEEKEGEEKKEGEEKKEGEEEKKEKTGKTKKVQEVTREWEQLNKQKPLWMRKPEEVTEEEYASFYKSLSNDWEEHLAVKHFSVEGQLEFKALLFVPKRAPFDLFETRKKRNNIKLYVRRVFIMDDCEDIIPEWLNFVKGVVDSEDLPLNISRESLQQNKILKVIRKNLVKKCLEMFAEIEEKKENYAKFYEQFSKNLKLGIHEDSANRAKIAELLRFHSSKSGEDMVSFKEYVDRMKEGQKDIYYITGESRQTVANSPFLEKLTKKGYEVLYMTDPIDEYAVQQLKEFDNHKLRCCTKEGLEIDESEEEKKKFEELKAEFEPLLKLIKEVLHDKVDKVVLSNRITDSPCVLVTTEFGWSANMERIMKAQALRDNSMTSYMVSKKTMEVNGHHSIMIEIKNKAAVDKSDKTVKDLIWLLYDTALLTSGFSLEEPTQFAARIHRMIKLGLSIDDDEEAKDDDLPPLEEVEGAADEASKMEEVD

Gene
HSP90
Protein
Heat shock protein 90 homolog
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876)
Length
707 amino acids
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Similarity
Belongs to the heat shock protein 90 family.
Mass
80.823 kDa
Sequence
MADAKVETHEFTAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPSQLESEPELFIRIIPQKDQKVLEIRDSGIGMTKADLVNNLGTIAKSGTKSFMEALSAGADVSMIGQFGVGFYSLFLVADHVQVISKHNDDEQYVWESNAGGKFTVTLDETNERLGRGTMLRLFLKEDQLEYLEEKRIKEVVKKHSEFVAYPIQLVVTKEVEKEVPETEEEDKAAEEDDKKPKLEEVKDEEDEKKEKKTKTVKEEVTETEELNKTKPLWTRNPSDITQDEYNAFYKSISNDWEDPLAVKHFSVEGQLEFRAILFVPKRAPFDAFESKKKKNNIKLYVRRVFITDDAEELIPEWLSFIKGVVDSEDLPLNLSREMLQQNKILKVIRKNIVKKMIETFNEISEDQEQFNQFYTAFSKNIKLGIHEDAQNRQSLAKLLRFYSTKSSEEMTSLSDYVTRMPEHQKNIYYITGESIKAVEKSPFLDALKAKNFEVLFMVDPIDEYAMTQLKEFEDKKLVDITKDFELEESDEEKAAREKEIKEYEPLTKALKDILGDQVEKVVVSYKLVDAPAAIRTGQFGWSANMERIMKAQALRDTTMSSYMSSKKTFEISPSSPIIKELKKKVETDGAEDKTVKDLTTLLFDTALLTSGFTLDEPSNFAHRINRLIALGLNIDDDSEETAVEPEATTTASTDEPAGESAMEEVD

Gene
hsp90
Protein
Heat shock protein 90
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Length
706 amino acids
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
Similarity
Belongs to the heat shock protein 90 family.
Mass
80.64 kDa
Sequence
MSSETFEFQAEISQLLSLIINTVYSNKEIFLRELISNASDALDKIRYQSLSDPTKLDTGKDLRIDIIPDKENKTLTIRDTGIGMTKADLINNLGTIARSGTKQFMEALSAGADISMIGQFGVGFYSAYLVADRVTVVSKNNDDEQYIWESAAGGTFTLTQDTEGEQLGRGTKIILHLKDEQTDYLNESRIKEVVRKHSEFISYPIYLHVLKETEKEVPDEEAEETKEEEDEEKKAKIEEVDDEEEEEKKKKKKTKTVKESKIEEEELNKTKPIWTRNPADITQEEYASFYKSLSNDWEDHLAVKHFSVEGQLEFRAILYVPKRAPFDLFETKKTKNNIKLYVRRVFITDDATDLIPEWLGFIKGVVDSEDLPLNLSRETLQQNKIMKVIKKNIVKKTLELFNEIAEDREQFDKFYSAFSKNIKLGIHEDAQNRQTLAKLLRYQSTKSGDEATSLADYVTRMPEHQKQIYYITGESIKAVAKSPFLDSLKQKNFEVLFLVDPIDEYAFTQLKEFDGKKLVDITKDFELEETEEEKAEREKEEKEYENLAKSLKNILGDKVEKVVVSHKLVGSPCAIRTGQFGWSANMERIMKAQALRDTSMSSYMSSKKTFEISPKSSIIKELKKKVEADGENDRTVKSITQLLFETSLLVSGFTIEEPASFAERIHKLVSLGLNIDEEAETTEEKATEEAAPAEATTGESAMEEVD

Gene
HSP90
Protein
Heat shock protein 90
Organism
Encephalitozoon cuniculi (strain GB-M1)
Length
690 amino acids
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures (By similarity).
Similarity
Belongs to the heat shock protein 90 family.
Mass
79.082 kDa
Sequence
MSSNQEPLVEGKIKDKHSETHGFEVDVNQMMDTMIKSVYSSKELFLRELVSNSSDACDKLKALYFQLREKGCVLDPVTSLGIEIIPNKDNRTLTIKDNGIGMTKPDLMNFIGTIASSGTKKFREEMKEKGNSADASNLIGQFGLGFYSSYLVAERVDLITKHPSDEALVWTSTGRDVYTIEEYDGEPFAHGTSLVLYIKEGEEEFLDPKRISEIVKKYSLFVFYPIYTYVEKEIEEPEEKKDEEKEDEKVEEETAEPRVEEVREKRLKKVTEREQINVEKPLWKRNIKEVPEEELKSFYKTVSGDWDDFLAVDFWHIEGLLSIELLMFIPKRARFDMFNKNKKNNNIKLYCKNVFVTDDFGDAIPEWMSFVSGVVASDDIPMNISREMIQGTNVMKLVKKTLPQKIFEMIGKLALDAEKYKTFYKEFGNCLKMAIGEASEGQQDGYAKCLRYFTTKSGEEAISLDTYVERMAPNQKQIYVITGLSKEQVKSNPALDAFQKYEVIYMHEVMDEVMLRGLKKYKGHTIQRITSEGVELPEDEASNEEVVKSFEEFCKKVKDILSSKVEKVTVNPRLVSVPAVISTTKYSLSGTMENIMKSQPVTEANPFAAMTAVSKKIFEMNPNHQLVKNLKALFDSNEIEKMNRILEVFFETVLIHNGFVLSDPKGFCANVFDFLCSEEVRCEEPVEEVQ