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HSP90-beta dimerHSP90-beta dimer [nucleoplasm]Heat shock inducible proteinsHSP90AA1;HSP90AB1SUGT1:HSP90Ficolin-rich granule lumen proteinsFicolin-rich granule lumen proteins [extracellular region]Secretory granule lumen proteinsSecretory granule lumen proteins [extracellular region]AHR:2xHSP90AB1:AIP:PTGES3AHR:2xHSP90AB1:AIP:PTGES3 [nucleoplasm]2xHSP90AB1:AIP:PTGES3DT fragment B transports DT fragment A from target cell endosome membraneSGT1 binds HSP90HSP-90
P527
P688
The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferonsQuantitative analysis of HSP90-client interactions reveals principles of substrate recognitionHsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cellsHsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagyHeat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapyNucleotide sequence and regulation of a human 90-kDa heat shock protein geneBAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesisHistone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradationCrystal structure and activity of human p23, a heat shock protein 90 co-chaperoneInteraction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiationHsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1Distinct roles of molecular chaperones HSP90α and HSP90β in the biogenesis of KCNQ4 channelsSMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formationStat1 mediates an auto-regulation of hsp90beta gene in heat shock responseCurcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERTFunctional requirement of p23 and Hsp90 in telomerase complexesThe activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90Phosphorylation analysis of 90 kDa heat shock protein within the cytosolic arylhydrocarbon receptor complexMechanism of dimer formation of the 90-kDa heat-shock proteinHSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptorsHsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A degradation and cell-cycle attenuation in pancreatic carcinoma cellsExtracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone functionMolecular recognition via coupled folding and binding in a TPR domainN-terminal domain of human Hsp90 triggers binding to the cochaperone p23.Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathiesStructure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
P921
Q50251180-88ACA36C-8612-4555-B040-EC2153C3A371Q50252221-DF58E8BF-563A-41C7-BB65-0D102F7E4D7AQ50252250-A22EC39B-34FB-4B67-B3D0-D34D5DB4F421Q50254020-583BD41E-5972-4E96-8004-E7971ADA148AQ50261468-A0B054C8-10F0-42F7-AC96-0DFA79B0901FQ50262418-16876008-BF6F-4F01-B1CE-43DC8F3D2992Q50262422-ADA99845-6491-4230-8693-C4B7E4981424Q50262429-267F946D-2AAE-4A3A-AE16-1F29EE6BCC72Q50262432-767A08FE-8703-465B-9174-C6A6BB57DC3AQ50267016-4B4EA4F7-FE5D-4A3B-9730-00D46099256AQ50267021-A04BB886-DD49-4E33-8335-BCA8E63C1040Q50267023-E67FE22B-B70C-48A1-B863-5F38AF0D07B0Q50289642-68C43A6E-C00F-4BA9-B610-B3EAAC2D157FQ50291966-F389F87A-4106-44EE-8A19-D7D2FC2D6A87Q55192543-384016FE-735F-4BD9-B164-D0572FB988A3
P527
Q24294462-40DC3E65-1471-41F4-A25C-FDB4789845E5Q24297748-A4CF246F-8549-4847-AB95-90206AD12CDAQ24323386-821FC2A6-D805-4569-9FB6-C4D153A35527Q24323790-408F5550-56A9-49E4-A513-7035B71A764DQ24337770-40EA2537-5AD6-4B68-BD5C-05EC8ACED94CQ24339558-6843BC56-993F-4292-8715-2BA13B306E69Q24534836-BA4362ED-3EF3-427D-A8FE-ACAE1C0BEEB8Q24669732-44A8195C-B33A-4706-B7C8-A6B159A3FD13Q24671304-64DE1EAB-7414-4B0C-8207-4E9508EEAE01Q27622547-7A665A53-C8FD-4CB8-9C84-AEBF6A176860Q28114973-730F485B-D57E-4AED-A13F-E03BC702A59FQ28115152-B855AA50-5053-486B-B9FB-FD947D9D8009Q28115218-6E1AC498-9194-45C1-8A3D-A323AF1598C8Q28115389-DF87C809-EF22-4400-BEA0-EA8583071FAFQ28115478-C3E2078B-6DC4-40AA-94E1-AB2B961E0727Q28115618-B87B3ED5-51B7-471F-A370-B528F566D944Q28115669-5EE9F810-C9A4-453E-B414-BF3CE241D71FQ28115788-43E4DDBF-B891-400A-805E-D0D755C75212Q28117011-FEC57B7B-026C-4A38-852F-7B91EACCB7FAQ28119047-83350AFD-37C8-4531-B644-56895254AB62Q28215191-A573E003-43D1-47D9-B0CD-78B642616E0FQ28854586-EB969372-97D8-4603-A525-7550E2BFB2EDQ28854589-6B2E1577-6D78-4CE8-A8EF-5D60C123CCFCQ28910360-721AB962-292D-482E-8FC7-669291789CE0Q28910476-3D51896B-4324-4361-AEC9-56906546B6AFQ34490414-4DAAFD7F-7F49-43AA-8D54-188C9763A652Q35839667-E522D6D5-6122-413E-81E0-8147019A8D73Q58090204-CEED56DF-3E18-4B32-8AA3-E36B493657D2
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
proteinë
@sq
proteïne in Heat shock protein 90 alpha family class B member 1
@nl
protèin
@ace
بروتين في الإنسان العاقل
@ar
name
Heat shock protein 90 alpha family class B member 1
@en
type
label
Heat shock protein 90 alpha family class B member 1
@en
altLabel
HSP 84
@en
HSP84
@en
HSP90-beta
@en
HSP90AB1
@en
heat shock 84 kDa
@en
heat shock 90kD protein 1, beta
@en
heat shock protein 90 kDa
@en
heat shock protein 90kDa alpha (cytosolic), class B member 1
@en
heat shock protein 90kDa alpha family class B member 1
@en
heat shock protein HSP 90-beta
@en
prefLabel
Heat shock protein 90 alpha family class B member 1
@en
P361
P527
P637
P638
P680
P681
P682
P705
P352
P31
P352
P361
P527
P637
NP_001258898
NP_001258899
NP_001258900
NP_001258901
NP_001358167
P638
P680
P681
P682
P702
P703
P705
ENSP00000325875
ENSP00000360609
ENSP00000360709
ENSP00000481908