about
Cytochrome P450 family 1 subfamily A member 1Cytochrome P450, family 2, subfamily e, polypeptide 1Stress-induced phosphoprotein 1Microtubule-associated protein tauErb-b2 receptor tyrosine kinase 2TSC complex subunit 1Aryl-hydrocarbon receptorCytochrome P450, family 1, subfamily a, polypeptide 1Nucleoporin 62Nucleoporin 62Neuronal PAS domain protein 2Nitric oxide synthase 3, endothelial cellAryl hydrocarbon receptorTelomere maintenance 2Cysteine and histidine rich domain containing 1Unc-45 myosin chaperone AActivator of HSP90 ATPase activity 1TSC complex subunit 2Aryl hydrocarbon receptor nuclear translocator likeProtein phosphatase with EF-hand domain 2Karyopherin subunit beta 1FKBP prolyl isomerase 6Peptidylprolyl isomerase DProtein phosphatase 5 catalytic subunitEndoplasmic reticulum to nucleus signaling 1Heat shock transcription factor 1STIP1 homology and U-box containing protein 1Cyclin dependent kinase 5Unc-45 myosin chaperone BProstaglandin E synthase 3 likeParkin coregulatedUbiquitin specific peptidase 19Activator of HSP90 ATPase homolog 2, pseudogeneGuanylate binding protein 1Activator of 90 kDa heat shock protein ATPase homolog 1Kinase suppressor of ras 1Ribosomal protein S3Kinase insert domain receptorEukaryotic translation initiation factor 2 alpha kinase 3Cell division cycle 37, HSP90 cochaperone
P680
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteinsThe molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn diseaseCK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stabilityA structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptorA proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinCharacterization of the deubiquitinating activity of USP19 and its role in endoplasmic reticulum-associated degradationCooperation between integrin alphavbeta3 and VEGFR2 in angiogenesisHeat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.An 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 domainRoles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
P921
Q1407929-A4F774D4-0A56-4E11-9228-E3769B3F7547Q14864436-671CA67B-17B0-485F-9841-0326F4DD790EQ14864436-8B072E2C-07BD-40EC-98C9-728D9C289405Q14865012-95D3E34F-D5D9-4E22-8382-3562342AB0BCQ14865012-D7284104-56D0-4AA5-833B-2DDAF965EEB3Q14865311-FF747298-DE1C-4A3F-A223-F704485BE111Q14877504-A010EA5C-773B-4DEA-B241-179D6B11495AQ14908117-EAA56BCE-DD88-416E-844C-3B55A5B01845Q14916326-E79BCBDB-C1A0-417B-A859-39C2C4AF3CBFQ14916463-0D234A5E-D878-4C26-A658-ECBF3FA20AA1Q14916463-B00EA5B6-3A1C-4E34-8F0E-1C33043E9F05Q15316702-80D79C59-BC57-4EC2-AE34-84B58F8CFBFBQ15316762-D0544121-7BE8-4469-B9FA-0B942034A080Q15322565-537F05C1-7274-46E9-98DE-479C2FAC17BFQ15328616-DE7ED78B-5580-489A-B5A6-5C313C0502DBQ155750-BB1F72A7-46F0-4500-A1D9-D83379494BDEQ21106561-B5796784-8A71-433B-921F-FB662E153898Q21106769-2BA1AA0F-A166-4717-A3A3-11B3F9659EDFQ21108013-24C37424-E814-456C-ACC7-9CD6F2B0899AQ21108013-BCBA6A57-844B-4C7D-AC03-36B702D7B0B8Q21108140-F9A20BB9-4CED-4675-8044-E473B360F82DQ21109261-5219799F-AB16-43D0-BA1A-5F6AE4284884Q21109585-F386BDB1-A5E9-4D49-9816-B40F246177EDQ21110528-46A28775-1DC8-4B45-8B15-AD868E171B24Q21110528-F246CC85-B53E-4D2E-897B-A3F6E5524DB5Q21112349-D1B96CAB-8FFB-4FFC-9048-C4257C852BA9Q21112965-F294A2FD-A6C5-4ED9-9296-3029B3AC91C3Q21114583-26FC462D-1C68-45C9-9270-C1B9F9E1C29BQ21114583-4D08EDE3-58FA-4857-9D97-37AB90523757Q21114993-785436F8-9F66-47E7-A161-9E3DB9A17E39Q21115427-5198BD74-82EA-4F5F-BDCE-6E964E283440Q21116003-63EC5701-ABEA-4FB6-A87E-82E978B9ED70Q21116753-81ADB63E-4EC4-45B1-BDF1-24591151E92EQ21116933-00587BC5-569E-4743-834D-C69F8CE8BB39Q21118363-0956D8C8-8C16-4239-9DAD-774B711D2514Q21118363-1A7DEAF4-4289-48AA-B002-A59CF6644AEAQ21123337-36B8CDEE-32B5-4EF9-B21D-61A3D9510E1BQ21123681-2E93F9B5-9DFE-4159-9EB5-62193BFDE01EQ21123681-9D0110DD-8CCC-49E7-AD08-7F96DA9977F9Q21126693-0732A5EC-ACD5-44F3-AF45-372197F21F47
P680
Q24290709-B3476FFE-99D5-41AD-A33F-D4A4B888D116Q24296753-B6AB035F-683D-4727-8CA7-91D37DAFCEA4Q24300796-4A1E1949-56DE-4CA8-B78C-EF9C0D496A82Q24302319-9740E20A-3FDA-4852-9E2F-4A333953F338Q24303612-B6FB516C-4BE3-46CA-9B9F-587A5A6D5254Q24312286-555325CA-CAA1-46CD-9D7A-EC24D149E6F3Q24314783-F7B81FBC-D61E-471D-918C-DF440AC1B25AQ24318607-A6E0F6B4-0029-4CB7-91C4-4BEEED593A8CQ24320638-907D06F9-F4C2-4237-B10B-C05711AB8CE3Q28910360-115CDF48-0ED5-48F8-A843-BDE4ECD380D8Q28910476-27654166-9C54-4918-B61B-3818C679C23DQ35839667-4852DC9D-7AB9-4792-B00B-A61D1628B071
P921
description
Interacting selectively and no ...... proteins around 90kDa in size.
@en
moleculaire functie
@nl
name
Hsp90 protein binding
@en
type
label
Hsp90 protein binding
@en
altLabel
GO:0051879
@en
Hsp90 binding
@en
Hsp90 class protein binding
@en
prefLabel
Hsp90 protein binding
@en
P2888
P686
GO:0051879