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AlbuminTransformation related protein 53Fibronectin 1ThyroglobulinVon Willebrand factorParkin RBR E3 ubiquitin protein ligaseCeruloplasminCystic fibrosis transmembrane conductance regulatorHeat shock protein 1 (chaperonin)Heat shock protein 1 (chaperonin 10)Stress-induced phosphoprotein 1AlbuminMicrotubule-associated protein tauPrion proteinHeat shock protein 8Cathepsin CBCL2-associated X proteinTSC complex subunit 1Lamin B receptorAryl-hydrocarbon receptorTelomerase reverse transcriptaseSuperoxide dismutase 1, solubleSuperoxide dismutase 1PodoplaninMajor prion proteinATPase Na+/K+ transporting subunit alpha 1ATPase Na+/K+ transporting subunit alpha 3ATPase Na+/K+ transporting subunit alpha 2BAG cochaperone 5Ubiquitin like 4ADNL-type zinc fingerST13 Hsp70 interacting proteinDnaJ heat shock protein family (Hsp40) member B5Endoplasmic reticulum protein 29Scavenger receptor class B member 2BAG cochaperone 3HscB mitochondrial iron-sulfur cluster cochaperoneDnaJ heat shock protein family (Hsp40) member A2Activator of HSP90 ATPase activity 1FIC domain protein adenylyltransferase
P680
Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cellsCharacterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartinA novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretionCharacterization of a brain-enriched chaperone, MRJ, that inhibits Huntingtin aggregation and toxicity independentlyIdentification of a novel HSP70-binding cochaperone critical to HSP90-mediated activation of small serine/threonine kinaseSGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradationThe copper chaperone CCS directly interacts with copper/zinc superoxide dismutasePathway leading to correctly folded beta-tubulinMajor histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusActivation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiationThe FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug bindingThe clathrin-binding and J-domains of GAK support the uncoating and chaperoning of clathrin by Hsc70 in the brainHsp90 regulates the activity of wild type p53 under physiological and elevated temperaturesHsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A degradation and cell-cycle attenuation in pancreatic carcinoma cellsCytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidisIdentification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosisBifidobacterial enolase, a cell surface receptor for human plasminogen involved in the interaction with the hostExtracellular heat shock protein A9 is a novel interaction partner of podoplanin in oral squamous cell carcinoma cells.Progranulin Recruits HSP70 to β-Glucocerebrosidase and Is Therapeutic Against Gaucher Disease.Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90
P921
Q11721976-14C3C989-9174-4791-9B79-BBD19B1D7F60Q14818136-8A245863-9770-4FA7-A56F-AD7472536CB5Q14818136-B953A09B-4FFA-470A-B6BC-11B705CBF4A9Q14819493-DF6D2419-7050-469E-84F3-47AD0C777CA8Q14860782-78D539D9-7A95-46E2-BCB2-42A87B2AD6D1Q14863680-751AEACA-5CF7-4111-A912-F294D1EEDE64Q14864264-177E74CC-162A-42A3-A6C9-F5DB7C203B99Q14864378-53DF5039-27B4-4AB5-A17C-F8E483A853A4Q14864378-68C9318E-D48C-49AA-8D6C-1D1C03226A66Q14864718-D4F1E2DC-7E03-4204-A4EF-6E6D09E9D4C5Q14865001-26459D15-DFFB-4B88-BB8D-CDCC9867F364Q14865001-DF3D3FC9-57AD-48EE-A9AA-C0460D68AD13Q14865009-EE976BBE-BF79-4754-BFD7-35187809F296Q14865012-66B9A249-7E2A-48C1-98B8-89E32A9665E3Q14865034-9B470717-133C-4489-9E35-94F2804662F7Q14865311-032B24F3-6872-49C7-9513-886E459C5B75Q14881308-1DB3AEAE-A197-4C02-94DE-AF9DD54D7F7FQ14881308-538B3D4F-50D1-411E-9FAE-7D58D213253BQ14888957-23F8F286-7D46-446D-9562-1273029B2F30Q14888957-29677419-14F9-48EA-AC8D-C868AE0A67C1Q14902086-E3276756-D759-43B1-A9BC-0B91EE5A33FFQ14905404-4F467639-9613-4737-90A3-3989E8761D7DQ14905404-78DE416F-EE57-4BE5-81B2-8046D7A4BD01Q14908117-DC7EAD52-1DE6-454F-BED1-6A95AE218D0FQ14911838-A6676C22-07BC-457C-AED9-0B75BCB5C78FQ14916326-B6A450D8-2AF4-4AA8-9033-339D5EDB89D8Q15315162-C106D2F3-9D78-4198-BB1D-D3F30FE5413FQ15328173-E35349A8-9C5D-4B29-B7D7-620F987B421AQ2041084-3C196C44-D0F6-4EF4-8C13-70B3162A9245Q2100344-21358F04-E29F-4166-837C-CAEEB2F32435Q21096129-3E612787-DAF4-4125-B071-EA295FBACB4FQ21096129-C86BD2EC-9F5F-43C9-8026-26383AB60C9BQ21097491-6423149E-E898-4E7B-8585-799D448B11F9Q21097506-7C7F1CB0-CF5E-4099-AD1B-02927A5E4CD9Q21097513-098A7331-6634-4757-9E9A-D2461692CAB3Q21100428-944971EE-0EFA-4058-9FC8-F96B94EFF8B4Q21100588-9E541ABB-336B-4A8C-A4C9-DFFC43B1706EQ21101110-42F08E58-FCCD-4725-AD37-5579C92EA092Q21101878-2138C2F7-7D10-48F8-8A67-96AB1900B175Q21102125-90E1FEC5-F16D-4E2D-B7CD-3D5A0713646E
P680
Q22009395-D3455920-72D3-4D63-8E1F-6B3CEBAAB15DQ22010879-2E1B7B22-1B3D-41EE-B334-2FA02603CE6AQ22010879-53905AD1-B5EC-4889-A925-D95E6B864398Q22254572-4A541F72-B6FB-401B-A77F-AD60BE0E7838Q24292471-81520017-8339-403A-9E96-4DF202E8FE0BQ24299263-4F9A047E-0496-4ABE-A3EE-FC959EB61C9FQ24306367-BE9A4619-2572-473E-8AD1-6FF469F62CECQ24310363-B54D2E59-92ED-4C6E-8D6C-EAC25AF180E7Q24312761-6EC36261-A98B-4CAC-969F-E1F366979F9BQ24322887-EB542CBD-195D-4FF7-9782-E9EC90C75A9AQ24337678-3FED35EF-912A-459F-A66B-4CC5123459E1Q28114973-20817330-1584-4E1A-9F90-966D022FACA0Q28115175-C98E4799-0A40-4A3F-B177-A51B196209C7Q28115999-1C275F99-61C3-45B2-9454-B8C447656C63Q28854583-41383E1E-261C-44E8-8739-00BA27BF374DQ28854586-FD557BA9-BCEC-45F6-86D0-15DF0436A928Q28903782-C2EC61D0-54C2-47BB-9D74-1911CA019940Q28909146-3292F21D-7487-456E-B64F-2F3FEA910640Q28910467-B58DECA9-4262-4E96-9C3F-57959A83CA29Q30032657-11D0C753-A959-4FAA-BBCE-37675C45E03BQ37604580-25AF67EA-89EA-4754-A3BF-A9F9C67EB45AQ61806867-72206FC5-0820-4324-A925-E24EFFD4D675
P921
description
Interacting selectively and no ...... correct folding or transport.
@en
biologisch proces
@nl
name
chaperonbinding
@nn
chaperone binding
@en
type
label
chaperonbinding
@nn
chaperone binding
@en
altLabel
GO:0051087
@en
GO:0051087
@nn
chaperon-proteinbinding
@nn
chaperone protein binding
@en
prefLabel
chaperonbinding
@nn
chaperone binding
@en
P279
P2888
P686
GO:0051087