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Information on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
hsp90, heat shock protein, grp78, hsp60, groel, molecular chaperone, heat shock protein 70, hsc70, heat shock protein 90, hsp40, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chaperone Hsp90alpha
-
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chaperone Hsp90beta
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hATPase
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heat shock protein 70
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heat shock protein 90
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heat shock protein 90-alpha
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heat shock protein-90
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-
heat-shock protein 90
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Hsp90 molecular chaperone
P07900; P08238
-
Hsp90alpha
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HSPA1L
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HspA8
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HtpG
P07900; P08238
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human alphabeta crystallin
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human Hsp70 molecular chaperone
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human stress70c
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mitochondrial chaperone
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mitochondrial hsp70
molecular chaperone Hsc70 ATPase
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-
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mortalin/mtHsp70
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mtHSP70
p97-valosin-containing protein
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p97-VCP
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-polymerizing)
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
-
NEF binding stabilizes the ATPase domain in an open form and thereby facilitates the nucleotide exchange step of the chaperone cycle
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
approx. 15% of activity with Mg2+ at 20 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1aR,2Z,4E,6Z,14R)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylacetyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-6-([[(dimethylamino)acetyl]oxy]imino)-9,11-dihydroxy-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-(methylimino)-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylcarbonyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-6-(hydroxyimino)-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
KF25706
(1aS,2Z,15R,16aR)-9-chloro-10,12-dihydroxy-15-methyl-1a,15,16,16a-tetrahydro-1H-7,4-(metheno)cyclopropa[h][12,2,3,4]benzoxatriazacyclopentadecin-13(8H)-one
-
-
(1R)-2-(5-chloro-2,4-dihydroxybenzoyl)-N-ethyl-2,3-dihydro-1H-isoindole-1-carboxamide
-
-
(3R,5E,9E,11Z)-13-chloro-7,14,16-trihydroxy-3-methyl-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(3S)-14,16-dihydroxy-3-methyl-3,4,5,6,9,10,11,12-octahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-amino-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
IPI-493
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[benzyl(ethyl)amino]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-20-chloro-13,19-dihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-9-(carbamoyloxy)-13,20,22-trihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-N-(prop-2-en-1-yl)-2-azabicyclo[16.3.1]docosa-1(22),4,6,10,18,20-hexaen-19-aminium chloride
-
IPI-504
(4E,6Z,8S,9S,10E,12S,13R,14S,16S,17R)-22-hydroxy-8,13,14,17-tetramethoxy-4,10,12,16,20-pentamethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,8S,9S,10E,12S,13R,14S,16R)-13,20-dihydroxy-8,14-dimethoxy-10,12,16-trimethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(22),4,10,18,20-pentaen-9-yl carbamate
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KOSN1559
(5-[4-amino-6-[(2-methoxyphenyl)sulfanyl]-1,3,5-triazin-2-yl]-2,4-dichlorophenoxy)acetonitrile
-
-
(5E)-5-[(1-benzyl-1H-indol-3-yl)methylidene]-1-(2-fluorocyclohexyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5E,9E,11Z)-13-chloro-14,16-dihydroxy-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(5Z)-7-[4-fluoro-2-(pyridin-3-yl)phenyl]-5-(hydroxyimino)-4-methyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-2-amine
-
-
(7R)-2-amino-7-[5-(6-methoxypyrazin-2-yl)-1,3-thiazol-4-yl]-4-methyl-7,8-dihydropyrido[4,3-d]pyrimidin-5(6H)-one
-
-
1,3-dihydro-2H-isoindol-2-yl[2,4-dihydroxy-5-(propan-2-yl)phenyl]methanone
-
-
1,3-dihydro-2H-isoindol-2-yl[6-hydroxy-3-(3-methylbenzyl)-1H-indazol-5-yl]methanone
-
-
1-(3H-imidazo[4,5-c]pyridin-2-yl)-2,3-dihydro-5H-pyrrolo[2,1-a]isoindol-5-one
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-
1-(4-aminoquinazolin-6-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indol-4-one
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-
1-(5-ethyl-2,4-dihydroxyphenyl)-5-(trifluoromethyl)-1,3-dihydro-2H-benzimidazol-2-one
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-
1-(6-amino-9H-purin-8-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indazol-4-one
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-
1-[4-(2-[6-amino-8-[(7-bromo-2,3-dihydro-1,4-benzodioxin-6-yl)sulfanyl]-3H-purin-3-yl]ethyl)piperidin-1-yl]-2-hydroxy-2-methylpropan-1-one
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-
17-(2-dimethylaminoethyl)amino-17-demethoxygeldanamycin
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-
17-(allylamino)-17-demethoxygeldanamycin
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-
17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride
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17-dimethylaminoethylamino-17-demethoxygeldanamycin hydrochloride
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-
2'-methoxy-5-[4-(2-methoxyethyl)-4H-1,2,4-triazol-3-yl]-5'-(propan-2-yl)biphenyl-2,4-diol
-
-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-pentylbenzamide
-
-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-[2-(3-methylphenyl)ethyl]benzamide
-
-
2,4-dihydroxy-N-methyl-N-(3-methylbenzyl)-5-[1-(2-methylphenyl)-1H-pyrazol-5-yl]benzamide
-
-
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
-
-
2-(5-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-hydroxy-4H-1,2,4-triazol-4-yl]-1H-indol-1-yl)ethyl dihydrogen phosphate
-
-
2-([3-[2-(dimethylamino)ethoxy]-4-methoxyphenyl]amino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)benzamide
-
-
2-amino-4-chloro-8-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-5-propyl-7,8-dihydropteridin-6(5H)-one
-
-
2-amino-4-methyl-7-[2-(phenylamino)phenyl]-7,8-dihydroquinazolin-5(6H)-one
-
-
2-amino-4-[2,4-dichloro-5-[3-(pyrrolidin-1-yl)propoxy]phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide
-
NVP-BEP800/VER-82576
2-amino-6-benzyl-4-(2,4-dichlorophenyl)-5,6-dihydro-7H-pyrrolo[3,4-d]pyrimidin-7-one
-
-
2-amino-6-chloro-9-[(4-iodo-3,5-dimethylpyridin-2-yl)methyl]-7-[2-(1H-pyrrol-1-yl)ethyl]-7,9-dihydro-8H-purin-8-one
-
-
2-amino-N-ethyl-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
SNX-7081, weak inhibitor
2-bromo-4-(5-oxo-5,6,7,8-tetrahydronaphthalen-1-yl)benzonitrile
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2-chloro-6-(2,4-dichlorophenyl)-9H-purine
-
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2-chloro-N-[3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazol-4-yl]benzamide
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2-fluoro-6-(tetrahydro-2H-pyran-4-ylamino)-4-(2,3,6,6-tetramethyl-4-oxo-4,5,6,7-tetrahydro-1H-indol-1-yl)benzamide
-
-
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide
-
-
2-[(6-bromo-1,3-benzodioxol-5-yl)methyl]-1-methyl-5-(propanoylamino)-1H-imidazole-4-carboxamide
-
-
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxycyclohexyl)quinazolin-4(3H)-one
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-
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxyphenyl)quinazolin-4(3H)-one
-
micromolar inhibitor
2-[2-[(4-methoxy-3,5-dimethyl-3,4-dihydropyridin-2-yl)methyl]-7,8-dihydro-2H-6-thia-1,2,3,5-tetraazaacenaphthylen-7-yl]-N-(5-methyl-1,3-thiazol-2-yl)acetamide
-
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2-[4-(1-methyl-1H-indol-5-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)pyridine-3,5-diol
-
-
2-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9H-purin-9-yl]ethyl sulfamate
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-
2-[6-amino-8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-N-hydroxyacetamide
-
-
2-[[4-(2-chloro-5-hydroxy-4-methoxyphenyl)-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-2-yl]sulfanyl]-N,N-dimethylacetamide
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-
2-[[5-(1,3-benzodioxol-5-yl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1-phenylethanone
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-
2-[[6-(dimethylamino)-1,3-benzodioxol-5-yl]sulfanyl]-1-[2-[(2,2-dimethylpropyl)amino]ethyl]-1H-imidazo[4,5-c]pyridin-4-amine
-
CUDC-305
3,6-diamino-5-cyano-4-(4-methoxy-3-[[3-(trifluoromethyl)benzoyl]amino]phenyl)thieno[2,3-b]pyridine-2-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-fluorophenyl)-4H-pyrazole-4-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-methoxyphenyl)-4H-pyrazole-4-carboxamide
-
-
3-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1H-pyrazole-5-carboxamide
-
VER-49009
3-(5-chloro-2,4-dihydroxyphenyl)-N-[3-(trifluoromethyl)phenyl]-4H-pyrazole-4-carboxamide
-
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3-(cyclopentylmethyl)-6-hydroxy-N-methyl-N-[4-(morpholin-4-yl)phenyl]-1H-indazole-5-carboxamide
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-
3-benzyl-4-fluoro-1H-indazol-6-ol
-
-
3-[(4-hydroxycyclohexyl)amino]-2',3'-dimethoxybiphenyl-4-carbonitrile
-
-
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
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-
4-(1,3-benzodioxol-5-yl)-3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazole-5-carboxylic acid
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G3129
4-(1-phenyl-1H-1,2,3-triazol-4-yl)-6-(propan-2-yl)benzene-1,3-diol
-
-
4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
4-(2,4-dichloro-5-methoxyphenyl)-2-[2-(diethylamino)ethoxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
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-
4-(2,4-dichlorophenyl)-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
-
4-(4-[4-methoxy-3-[methyl(2-methylpropyl)amino]phenyl]-5-sulfanyl-4H-1,2,4-triazol-3-yl)-6-(propan-2-yl)benzene-1,3-diol
-
-
4-(but-2-yn-1-yl)-6-[4-(4-methoxyphenyl)-5-methyl-1,2-oxazol-3-yl]benzene-1,3-diol
-
-
4-([2-carbamoyl-5-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]phenyl]amino)cyclohexyl glycinate
-
SNX-5422
4-([2-[3,5-bis(trifluoromethyl)phenyl]-4,5-bis(4-methoxyphenyl)-1H-imidazol-1-yl]methyl)benzoic acid
-
inhibits the ATPase activity of Hsc70 by binding to its ATPase domain
4-amino-11,18,20-trimethyl-7-thia-3,5,11,15-tetraazatricyclo[15.3.1.12,6]docosa-1(21),2(22),3,5,17,19-hexaene-10,16-dione
-
-
4-chloro-6-(2,4-dichlorophenyl)pyrimidin-2-amine
-
-
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-(5-[[2-(morpholin-4-yl)ethyl]amino]-1,2-benzoxazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-phenylpyrimidin-2-amine
-
-
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
-
CCT072440
4-chloro-6-[5-(4-ethoxyphenyl)-1,2,3-thiadiazol-4-yl]benzene-1,3-diol
-
-
4-ethyl-6-[4-(1H-imidazol-4-yl)-1H-pyrazol-3-yl]benzene-1,3-diol
-
G3130
4-ethyl-6-[4-(4-methoxynaphthalen-1-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]benzene-1,3-diol
-
-
4-ethyl-6-[5-hydroxy-4-(naphthalen-1-yl)-1H-pyrazol-3-yl]benzene-1,3-diol
-
-
4-[2-amino-4-chloro-7-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidin-5-yl]but-3-yn-1-ol
-
-
4-[4-(1,3-benzodioxol-5-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
-
-
4-[4-(1-methyl-1H-indol-5-yl)-5-[(pyridin-3-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
-
CCT08159/RBT0028535
4-[4-(2-fluorophenyl)-5-hydroxy-4H-1,2,4-triazol-3-yl]-6-(2-phenylethyl)benzene-1,3-diol
-
-
4-[4-(2-methyl-1,3-thiazol-4-yl)-5-(trifluoromethyl)-1,2-oxazol-3-yl]benzene-1,3-diol
-
micromolar inhibitor
4-[4-(4-benzylpiperazin-1-yl)-1H-pyrazol-3-yl]-6-chlorobenzene-1,3-diol
-
-
4-[4-(6-fluoro-1H-benzimidazol-2-yl)-9H-carbazol-9-yl]-2-[(trans-4-hydroxycyclohexyl)amino]benzamide
-
-
4-[4-(diethylamino)phenyl]-5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-1,2-oxazole-3-carboxamide
-
-
4-[5-hydroxy-4-(1-methyl-1H-indol-5-yl)-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[5-hydroxy-4-[4-(morpholin-4-yl)phenyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
-
-
4-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]-2-[(4-hydroxycyclohexyl)amino]benzamide
-
SNX-2112
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
5-(5-ethyl-2,4-dihydroxyphenyl)-1-(naphthalen-1-yl)-1,3-dihydro-2H-imidazol-2-one
-
-
5-amino-1-(5-aminopentyl)-2-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-1H-imidazole-4-carboxamide
-
-
5-amino-1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-1H-imidazole-4-carboxamide
-
-
5-hydroxy-4-[5-hydroxy-4-[6-(morpholin-4-yl)pyridin-3-yl]-4H-1,2,4-triazol-3-yl]-2-(propan-2-yl)phenyl dihydrogen phosphate
-
-
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
6-(4-benzylpiperazin-1-yl)-2-chloro-9H-purine
-
-
6-bromo-N-[4-(quinolin-3-yl)-9H-fluoren-9-yl]-1,8a-dihydropyrido[2,3-d]pyrimidine-5-carboxamide
-
-
6-chloro-9-[(3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
-
-
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
-
-
6-[(2R)-2-[(5-fluoro-2-methoxyphenoxy)methyl]pyrrolidin-1-yl]-9H-purine
-
-
7-[2,4-dichloro-6-[2-(1H-pyrazol-1-yl)ethoxy]phenyl][1,3]thiazolo[5,4-d]pyrimidin-5-amine
-
-
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
PU24FCl
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
-
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
potent Hsp90 binder
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
PU-H71
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
-
-
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
-
-
8-[[5-(diethylamino)pentyl]amino]quinolin-6-ol
-
-
9-butyl-8-(3,4,5-trimethoxybenzyl)-9H-purin-6-amine
-
PU3
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
-
-
9-[2-(tert-butylamino)ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[2-[(2,2-dimethylpropyl)amino]ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
alvespimycin
-
-
Apg2
-
at high concentration (0.002 mM), Agp2 inhibits the ATPase activity of the enzyme
-
apoptozole
-
inhibits Hsc70 activity by binding to its ATPase domain
ATI3387
P07900; P08238
competitive inhibitor
cisplatin
-
-
CNF1010
-
-
cyclohexyl 5-[6-amino-8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-L-norvalinate
-
-
cycloproparadicicol
-
-
deguelin
-
inhibits HSP90 by interacting with its ATP-binding pocket
desmethoxy-geldanamycin
-
-
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
ethyl (4-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-sulfanyl-4H-1,2,4-triazol-4-yl]benzyl)carbamate
-
-
ethyl 2-amino-4-(4-bromo-2-chloro-5-methoxyphenyl)-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidine-6-carboxylate
-
-
ethyl 4-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-6-methyl-2-oxo-1,2-dihydropyrimidine-5-carboxylate
-
-
geldanamycin
KW-2478
-
-
MDC-3100
P07900; P08238
competitive inhibitor
methyl (2E)-3-[2-amino-4-(1,3-dihydro-2H-isoindol-2-ylcarbonyl)quinazolin-6-yl]prop-2-enoate
-
-
Mg2+
-
above 20 mM, approx. 50% inhibition at 100 mM
MPC-3100
-
-
mycograb
-
-
-
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-4H-pyrazole-4-carboxamide
-
-
N-benzyl-6-(3-[[(2,6-dichloro-9H-purin-9-yl)acetyl]amino]-8-azabicyclo[3.2.1]oct-8-yl)pyridine-3-carboxamide
-
-
N-butyl-2,4-dihydroxy-5-[(5-hydroxy-1,3-dihydro-2H-isoindol-2-yl)carbonyl]benzamide
-
-
N-ethylmaleimide
-
5 mM, approx. 85% inhibition
N-[2-(dimethylamino)ethyl]-6-[3-[(4-methoxy-2-methylbenzoyl)amino]-8-azabicyclo[3.2.1]oct-8-yl]pyridine-3-carboxamide
-
-
N-[4-(3H-imidazo[4,5-c]pyridin-2-yl)-9H-fluoren-9-yl]quinoline-5-carboxamide
-
-
N-[4-(aminosulfonothioyl)benzyl]-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]thiophene-2-sulfonamide
-
-
NaCl
-
approx. 50% inhibition at 100 mM, approx. 90% inhibition at 600 mM
novobiocin
-
analogs
NVP-AUY922
P07900; P08238
competitive inhibitor
NVPHSP990
-
-
p23 protein
-
cochaperone, interacts with Hsp90 in both the absence and presence of nucleotide, with a higher affinity in presence of the ATP analogue 5'-adenylyl-beta,gamma-imidodiphosphate. Mixed inhibition, one p23 binds to each subunit of the Hsp90 dimer. Complex formation between Hsp90 and p23 increases the apparent affinity of Hsp90 for 5'-adenylyl-beta,gamma-imidodiphosphate and completely inhibits the ATPase activity
-
pochonin A
-
good inhibitor of Hsp90
pochonin D
radamide
-
-
radester
-
-
radicicol
retaspimycin
-
IP-504
retaspimycin hydrochloride
P07900; P08238
competitive inhibitor
STA-1474
-
-
STA-9090
-
-
tanespimycin
-
-
XL888
-
-
[(2R)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
-
-
[1-(3-bromo-4-cyanophenyl)-2-oxo-2,4,5,6,7,7a-hexahydro-1H-indol-3-yl]acetic acid
-
-
[2,4-dihydroxy-5-(propan-2-yl)phenyl](5-[[methyl(piperidin-1-yl)amino]methyl]-1,3-dihydro-2H-isoindol-2-yl)methanone
-
AT-13387
[4-[(2S)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl]phenyl](3,3-difluoropyrrolidin-1-yl)methanone
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Aha1
P07900; P08238
potent activator of the ATPase subunit of the enzyme
-
Apg2
-
at low concentration (0.0004 mM), Agp2 stimulates the ATPase activity of the enzyme
-
Hsc20
-
the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU
-
ISCU
-
the iron-sulfur cluster scaffold protein, the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU, detailed interaction analysis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 0.33
ATP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
ATP
recombinant enzyme, pH 7.5, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00009
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.001 - 0.002
9-butyl-8-(3,4,5-trimethoxybenzyl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00018
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00086
purified recombinant enzyme, pH 7.5, 37°C
0.00167
-
purified recombinant enzyme, pH 7.5, 25°C, in absence of activators
0.00283
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.006 mM HSC20
0.0075
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.015 mM ISCU
0.025
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.004 mM HSC20 and 0.015 mM ISCU
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
50 - 55
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 70
-
approx. 64% of maximal activity at 40°C, approx. 50% of maximal activity at 65°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
overexpression of mortalin/mtHsp70 extends the in vitro lifespan of normal human fibroblasts
Manually annotated by BRENDA team
-
Helicobacter pylori (cagA+, vacA+) and Hp (cagA-, vacA-) inhibit expression of HSP70 in gastric carcinoma MKN7 cells independently of the presence or absence of cagA genes
Manually annotated by BRENDA team
-
knock-down of mortalin/mtHsp70 causes their growth arrest
Manually annotated by BRENDA team
additional information
-
Hsp90s are overexpressed in cancer cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
accumulation during heat shock
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
a highly conserved molecular chaperone of the Hsp70 family that is primarily found in the mitochondria
malfunction
in vivo deregulation of mortalin expression and/or function is correlated with agerelated diseases and certain cancers due to its interaction with the p53 protein
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HS90A_HUMAN
732
0
84660
Swiss-Prot
other Location (Reliability: 1)
SPA5L_HUMAN
753
0
80710
Swiss-Prot
other Location (Reliability: 2)
HSP7C_HUMAN
646
0
70898
Swiss-Prot
other Location (Reliability: 2)
BIP_HUMAN
654
0
72333
Swiss-Prot
Secretory Pathway (Reliability: 1)
SPAT5_HUMAN
893
0
97904
Swiss-Prot
Mitochondrion (Reliability: 3)
GRP75_HUMAN
679
0
73680
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
P07900; P08238
gel filtration
44000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
1 * 36000-66000, recombinant enzyme, monomeric and monodisperse mortalin, analytical ultracentrifugation and crystal structure analysis, mortalin has an elongated shape in solution, modeling, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
41.9-kDa human Hsp70 ATPase domain
-
atomic resolution analysis of the Hsp90 N-terminal domain binding energy landscape by simulating protein dynamics with binding partners such as ATP, ADP, shepherdin. The activity of the molecular chaperone may be linked to local folding-unfolding transitions and conformational switching of the active site lid upon binding and differences in the underlying protein dynamics as a function of the binding partner
-
Bag2-BNB-Hsc70-nucleotide-binding domain complex
-
cDNa sequence encoding alphabeta crystallin inserted into pET16b, expressed in Escherichia coli Bl21
-
crystal structures of four human Hsp70 isoforms are presented: nucleotide binding domains NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. All four proteins crystallize in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB is observed for the HSPA5-ADP complex. The structures presented support the view that the nucleotide binding domains of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the substrate binding domains and by accessory proteins
-
molecular docking studies with Hsc70 and apoptozole. The 3,5-bis(trifluoromethyl)phenyl group of apoptozole interacts with the binding site of a triphosphate moiety of ATP through polar interactions, and the two 4-methoxy phenyl moieties of apoptozole are located at the adenosine binding site of Hsc70. The CONH2 group of apoptozole can interact with the Glu376 side chain of Hsc70 via a hydrogen-bonding interaction
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis, small angle X-ray scattering, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A116N
-
reduced affinity to co-chaperone Hop in the presence of ATP analogue AMPPNP
K71E
-
no ATPase activity
T110I
-
wild-type affinity to co-chaperone Hop
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration
recombinant His-tagged SUMO fusion enzyme mtHSP70 from Escherichia coli by nickel affinity chromatography, His-tag and SUMO cleavage and again nickel affinity exchange chromatography for tag removal, followed by gel filtration
-
recombinant p97-VCP
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression of GFP-Hsp70 fusion protein in HeLa cells
-
Hsc 70, Hsc70 nucleotide binding domain (residue 1-381)
-
Hsp90beta, Hsp90beta-delta, Hsp90 C-terminal domain (residue 546-724), Hsp90beta-MC (residue 546-724)
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), production of folded and soluble recombinant mortalin when co-expressed with the human Hsp70-escort protein 1, but Hsp70 is still likely prone to self-association
recombinant expression of His-tagged enzyme mtHSP70 as N-terminal SUMO fusion protein, lacking the gene sequence coding for N-terminal mitochondrial targeting peptide, in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miernyk, J.A.; Hayman, G.T.
ATPase activity and molecular chaperone function of the stress70 proteins
Plant Physiol.
110
419-424
1996
Escherichia coli, Homo sapiens, Solanum lycopersicum, Zea mays
Manually annotated by BRENDA team
Sriram, M.; Osipiuk, J.; Freeman, B.C.; Morimoto, R.I.; Joachimiak, A.
Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
Structure
5
403-414
1997
Bos taurus, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Muchowski, P.J.; Clark, J.I.
ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
Proc. Natl. Acad. Sci. USA
95
1004-1009
1998
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Song, C.; Wang, Q.; Li, C.C.
ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
J. Biol. Chem.
278
3648-3655
2003
Homo sapiens
Manually annotated by BRENDA team
Tupling, A.R.; Gramolini, A.O.; Duhamel, T.A.; Kondo, H.; Asahi, M.; Tsuchiya, S.C.; Borrelli, M.J.; Lepock, J.R.; Otsu, K.; Hori, M.; MacLennan, D.H.; Green, H.J.
HSP70 binds to the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1a) and prevents thermal inactivation
J. Biol. Chem.
279
52382-52389
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Zeng, X.C.; Bhasin, S.; Wu, X.; Lee, J.G.; Maffi, S.; Nichols, C.J.; Lee, K.J.; Taylor, J.P.; Greene, L.E.; Eisenberg, E.
Hsp70 dynamics in vivo: effect of heat shock and protein aggregation
J. Cell Sci.
117
4991-5000
2004
Homo sapiens
Manually annotated by BRENDA team
McLaughlin, S.H.; Ventouras, L.A.; Lobbezoo, B.; Jackson, S.E.
Independent ATPase activity of hsp90 subunits creates a flexible assembly platform
J. Mol. Biol.
344
813-826
2004
Homo sapiens
Manually annotated by BRENDA team
Sharp, S.; Workman, P.
Inhibitors of the HSP90 molecular chaperone: current status
Adv. Cancer Res.
95
323-348
2006
Homo sapiens
Manually annotated by BRENDA team
Wadhwa, R.; Takano, S.; Kaur, K.; Aida, S.; Yaguchi, T.; Kaul, Z.; Hirano, T.; Taira, K.; Kaul, S.C.
Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60
Biochem. J.
391
185-190
2005
Homo sapiens
Manually annotated by BRENDA team
Brough, P.A.; Barril, X.; Beswick, M.; Dymock, B.W.; Drysdale, M.J.; Wright, L.; Grant, K.; Massey, A.; Surgenor, A.; Workman, P.
3-(5-Chloro-2,4-dihydroxyphenyl)-pyrazole-4-carboxamides as inhibitors of the Hsp90 molecular chaperone
Bioorg. Med. Chem. Lett.
15
5197-5201
2005
Homo sapiens
Manually annotated by BRENDA team
Wegele, H.; Wandinger, S.K.; Schmid, A.B.; Reinstein, J.; Buchner, J.
Substrate transfer from the chaperone Hsp70 to Hsp90
J. Mol. Biol.
356
802-811
2006
Homo sapiens
Manually annotated by BRENDA team
Targosz, A.; Pierzchalski, P.; Krawiec, A.; Szczyrk, U.; Brzozowski, T.; Konturek, S.J.; Pawlik, W.W.
Helicobacter pylori inhibits expression of heat shock protein 70 (HSP70) in human epithelial cell line. Importance of Cag A protein
J. Physiol. Pharmacol.
57
265-278
2006
Homo sapiens
Manually annotated by BRENDA team
McLaughlin, S.H.; Sobott, F.; Yao, Z.P.; Zhang, W.; Nielsen, P.R.; Grossmann, J.G.; Laue, E.D.; Robinson, C.V.; Jackson, S.E.
The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins
J. Mol. Biol.
356
746-758
2006
Homo sapiens
Manually annotated by BRENDA team
Colombo, G.; Morra, G.; Meli, M.; Verkhivker, G.
Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution
Proc. Natl. Acad. Sci. USA
105
7976-7981
2008
Homo sapiens
Manually annotated by BRENDA team
Onuoha, S.C.; Coulstock, E.T.; Grossmann, J.G.; Jackson, S.E.
Structural studies on the co-chaperone Hop and its complexes with Hsp90
J. Mol. Biol.
379
732-744
2008
Homo sapiens
Manually annotated by BRENDA team
Southworth, D.R.; Agard, D.A.
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
Mol. Cell
32
631-640
2008
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Xu, Z.; Page, R.C.; Gomes, M.M.; Kohli, E.; Nix, J.C.; Herr, A.B.; Patterson, C.; Misra, S.
Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2
Nat. Struct. Mol. Biol.
15
1309-1317
2008
Homo sapiens
Manually annotated by BRENDA team
Neckers, L.; Mollapour, M.; Tsutsumi, S.
The complex dance of the molecular chaperone Hsp90
Trends Biochem. Sci.
34
223-226
2009
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Wisniewska, M.; Karlberg, T.; Lehtioe, L.; Johansson, I.; Kotenyova, T.; Moche, M.; Schueler, H.
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B, and HSPA5/BiP/GRP78
PLoS ONE
5
e8625
2010
Homo sapiens
Manually annotated by BRENDA team
Taldone, T.; Sun, W.; Chiosis, G.
Discovery and development of heat shock protein 90 inhibitors
Bioorg. Med. Chem.
17
2225-2235
2009
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Janin, Y.L.
ATPase inhibitors of heat-shock protein 90, second season
Drug Discov. Today
15
342-353
2010
Homo sapiens
Manually annotated by BRENDA team
Cho, H.J.; Gee, H.Y.; Baek, K.H.; Ko, S.K.; Park, J.M.; Lee, H.; Kim, N.D.; Lee, M.G.; Shin, I.
A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator
J. Am. Chem. Soc.
133
20267-20276
2011
Homo sapiens
Manually annotated by BRENDA team
Gao, X.C.; Zhou, C.J.; Zhou, Z.R.; Wu, M.; Cao, C.Y.; Hu, H.Y.
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation
J. Biol. Chem.
287
6044-6052
2012
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Gierasch, L.; Bahar, I.
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs
PLoS Comput. Biol.
6
e1000931
2010
Homo sapiens
-
Manually annotated by BRENDA team
Araujo, T.L.; Borges, J.C.; Ramos, C.H.; Meyer-Fernandes, J.R.; Oliveira Junior, R.S.; Pascutti, P.G.; Foguel, D.; Palhano, F.L.
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
Biochemistry
53
2884-2889
2014
Homo sapiens
Manually annotated by BRENDA team
Cai, K.; Frederick, R.O.; Kim, J.H.; Reinen, N.M.; Tonelli, M.; Markley, J.L.
Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
J. Biol. Chem.
288
28755-28770
2013
Homo sapiens
Manually annotated by BRENDA team
Bartolini, M.; Wainer, I.W.; Bertucci, C.; Andrisano, V.
The rapid and direct determination of ATPase activity by ion exchange chromatography and the application to the activity of heat shock protein-90
J. Pharm. Biomed. Anal.
73
77-81
2013
Homo sapiens
Manually annotated by BRENDA team
Dores-Silva, P.R.; Barbosa, L.R.; Ramos, C.H.; Borges, J.C.
Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization
PLoS ONE
10
e0117170
2015
Homo sapiens (P38646), Homo sapiens
Manually annotated by BRENDA team
Pearl, L.
Review The HSP90 molecular chaperone - an enigmatic ATPase
Biopolymers
105
594-607
2016
Homo sapiens (P07900 and P08238)
Manually annotated by BRENDA team
Cabrera, Y.; Dublang, L.; Fernandez-Higuero, J.; Albesa-Jove, D.; Lucas, M.; Viguera, A.; Guerin, M.; Vilar, J.; Muga, A.; Moro, F.
Regulation of human Hsc70 ATPase and chaperone activities by Apg2 role of the acidic subdomain
J. Mol. Biol.
431
444-461
2019
Homo sapiens
Manually annotated by BRENDA team