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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Homo sapiens and UniProt Accession P62942

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EC Tree
IUBMB Comments
The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
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This record set is specific for:
Homo sapiens
UNIPROT: P62942
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclophilin, cyclophilin a, fkbp12, ppiase, fkbp51, trigger factor, fkbp52, fk506-binding protein, peptidyl-prolyl isomerase, cyclophilin b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12 kDa FKBP
-
-
-
-
12.6 kDa FKBP
-
-
-
-
13 kDa FKBP
-
-
-
-
15 kDa FKBP
-
-
-
-
19 kDa FK506-binding protein
-
-
-
-
22 kDa FK506-binding protein
-
-
-
-
25 kDa FKBP
-
-
-
-
27 kDa membrane protein
-
-
-
-
36 kDa FK506 binding protein
-
-
-
-
40 kDa thylakoid lumen PPIase
-
-
-
-
40 kDa thylakoid lumen rotamase
-
-
-
-
51 kDa FK506-binding protein
-
-
-
-
52 kDa FK506 binding protein
-
-
-
-
54 kDa progesterone receptor-associated immunophilin
-
-
-
-
65 kDa FK506-binding protein
-
-
-
-
CGI-124
-
-
-
-
Chl-Mip
-
-
-
-
CPH
-
-
-
-
Cyclophilin
Cyclophilin 18
-
-
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
Cyclophilin B
Cyclophilin C
-
-
-
-
Cyclophilin cyp2
-
-
-
-
cyclophilin H
-
-
cyclophilin hCyp-18
-
-
Cyclophilin homolog
-
-
-
-
cyclophilin J
-
-
Cyclophilin ScCypA
-
-
-
-
Cyclophilin ScCypB
-
-
-
-
Cyclophilin-10
-
-
-
-
Cyclophilin-11
-
-
-
-
Cyclophilin-40
-
-
-
-
Cyclophilin-60
-
-
-
-
Cyclophilin-like protein Cyp-60
-
-
-
-
Cyclophilin-related protein
-
-
-
-
Cyclosporin A-binding protein
-
-
-
-
CYP-40
-
-
-
-
CYP-S1
-
-
-
-
Cyp18
-
-
Cyp3 PPIase
-
-
-
-
Cyp40
-
-
Estrogen receptor binding cyclophilin
-
-
-
-
FF1 antigen
-
-
-
-
FK506 binding protein 12
-
-
FKBP
-
-
-
-
FKBP 12
-
-
FKBP-12
-
-
-
-
FKBP-12.6
-
-
-
-
FKBP-13
-
-
-
-
FKBP-15
-
-
-
-
FKBP-19
-
-
-
-
FKBP-21
-
-
-
-
FKBP-22
-
-
-
-
FKBP-23
-
-
-
-
FKBP-25
-
-
-
-
FKBP-36
-
-
-
-
FKBP-51
-
-
-
-
FKBP-70
-
-
-
-
FKBP22
FKBP51
-
-
FKBP52
-
-
FKBP52 protein
-
-
-
-
FKBP54
-
-
-
-
FKBP59
-
-
-
-
FKBP65
-
-
-
-
FKBP65RS
-
-
-
-
h Par14
-
-
HBI
-
-
-
-
hCyP33
-
-
Histidine rich protein
-
-
-
-
hPar14
hPin1
HSP binding immunophilin
-
-
-
-
HSP90-binding immunophilin
-
-
-
-
Immunophilin FKBP12
-
-
-
-
Immunophilin FKBP12.6
-
-
-
-
Immunophilin FKBP36
-
-
-
-
Immunophilin FKBP65
-
-
-
-
Isomerase, peptidylprolyl cis-trans
-
-
-
-
Macrolide binding protein
-
-
-
-
Macrophage infectivity potentiator
-
-
-
-
MtFK
-
-
-
-
Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
Parvulin
Parvulin 14
-
-
-
-
parvulin1 4
-
-
Peptide bond isomerase
-
-
-
-
peptidyl prolyl isomerase-like protein 1
-
Peptidyl-prolyl cis-trans isomerase
peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
-
-
Peptidyl-prolyl cis-trans isomerase plp
-
-
-
-
Peptidyl-prolyl cis-trans isomerase surA
-
-
-
-
peptidyl-prolyl cis/trans isomerase
-
-
Peptidyl-prolyl cis/trans isomerase EPVH
-
-
-
-
peptidyl-prolyl cis/trans isomerase NIMA-interacting 1
-
-
peptidyl-prolyl isomerase
peptidyl-prolyl isomerase 1
-
-
peptidylproline cis-trans-isomerase
-
-
Peptidylprolyl cis-trans isomerase
-
-
-
-
peptidylprolyl isomerase
-
-
PfCyP
-
-
-
-
Planta-induced rust protein 28
-
-
-
-
PpiA
peptidyl-prolyl isomerase domain
PPIase
PPIase Pin1
-
-
-
-
PPIase Pin4
-
-
-
-
PpiB
peptidyl-prolyl isomerase domain
PPIC
peptidyl-prolyl isomerase domain
PpiD
peptidyl-prolyl isomerase domain
PPIE
peptidyl-prolyl isomerase domain
PPIF
peptidyl-prolyl isomerase domain
PPIG
peptidyl-prolyl isomerase domain
PPIH
peptidyl-prolyl isomerase domain
PPIL1
-
-
Proline rotamase
-
-
-
-
prolyl-peptidyl isomerase
-
-
protein phosphatase 2A phosphatase activator
-
-
Proteins, cyclophilins
-
-
-
-
Proteins, specific or class, cyclophilins
-
-
-
-
PtpA
-
-
Rapamycin-binding protein
-
-
-
-
Rapamycin-selective 25 kDa immunophilin
-
-
-
-
Rotamase
-
-
-
-
Rotamase Pin1
-
-
-
-
Rotamase Pin4
-
-
-
-
Rotamase plp
-
-
-
-
S-cyclophilin
-
-
-
-
S1205-06
-
-
-
-
SCYLP
-
-
-
-
SDCCAG-10
SmCYP A
-
-
-
-
SmCYP B
-
-
-
-
Smp17.7
-
-
-
-
SP18
-
-
-
-
spliceosome-associated protein CWC27 homolog
-
WHP
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-trans-isomerization
-
-
SYSTEMATIC NAME
IUBMB Comments
Peptidylproline cis-trans-isomerase
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
CAS REGISTRY NUMBER
COMMENTARY hide
95076-93-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cis-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
trans-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
?
(cis)-Pro residue in HIF-1alpha
(trans)-Pro residue in HIF-1alpha
show the reaction diagram
-
-
-
r
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
show the reaction diagram
-
-
-
-
?
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
acetyl-Ala-Ala-(cis)-Pro-Ala-Lys-NH2
acetyl-Ala-Ala-(trans)-Pro-Ala-Lys-NH2
show the reaction diagram
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
Ala-Ala-(cis)-Pro-Ala
Ala-Ala-(trans)-Pro-Ala
show the reaction diagram
-
-
-
?
Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Ala-Gly-PSI[CS-N]-Pro-Phe-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Ala-Ser(PO3H2)-(cis)-Pro
Ala-Ser(PO3H2)-(trans)-Pro
show the reaction diagram
-
-
-
?
Ala-Ser(PO3H2)-(cis)-Pro-Arg
Ala-Ser(PO3H2)-(trans)-Pro-Arg
show the reaction diagram
-
-
-
?
amyloidbeta precursor protein
?
show the reaction diagram
-
interaction with Thr688
-
-
?
barstar C40A/C82A/P27A
?
show the reaction diagram
-
the mutant of barstar lacks complications arising from oxidation of Cys in wild-type or isomerization affecting the peptidyl-Pro27 bond. Refolding is comprised by several kinetically detectable folding phases. The slowest phase in refolding, the trans to cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
?
GFPRALPAWARPDYNPPLVE
?
show the reaction diagram
-
a synthetic peptide, named PepD2, corresponding to residues 304-323 of NS5A
-
-
?
hepatitis C virus NS5A protein
?
show the reaction diagram
interleukin-2 tyrosine kinase
?
show the reaction diagram
-
catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
N-succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
Phe-Phe-L-pSer-Pro-Arg-pNA
?
show the reaction diagram
-
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
show the reaction diagram
protein tau
?
show the reaction diagram
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
Ser(PO3H2)-(cis)-Pro-Arg
Ser(PO3H2)-(trans)-Pro-Arg
show the reaction diagram
-
-
-
?
Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
serine/threonine protein kinase B
?
show the reaction diagram
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
suc-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
suc-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Arg-p-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Arg-p-nitroanilide
show the reaction diagram
-
-
-
r
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Gly-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Lys-Pro-Phe-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Val-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Val-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Arg-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Arg-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Leu-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Leu-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Phe-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Phe-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ser-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ser-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
?
Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide
Trp-Phe-Tyr-Ser(PO3H2)-(trans)-Pro-Arg-4-nitroanilide
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
amyloidbeta precursor protein
?
show the reaction diagram
-
interaction with Thr688
-
-
?
hepatitis C virus NS5A protein
?
show the reaction diagram
-
nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain. Mutations in this domain are linked to cyclosporin A resistance
-
-
?
interleukin-2 tyrosine kinase
?
show the reaction diagram
-
catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
-
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
show the reaction diagram
-
Pin1 prevents activation of Bax, prevents Bax cleavage by calpain, and prevents Bax translocation to mitochondria
-
-
?
protein tau
?
show the reaction diagram
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
serine/threonine protein kinase B
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
-
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
-
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
-
(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
-
-
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
-
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
-
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
-
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
-
(E)-6-phenylhexyl 3-(3,4-dihydroxyphenyl)acrylate
20 micorM, 15% residual activity
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
-
-
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
-
-
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
-
-
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells. Compound is able to significantly speed nerve regeneration in a rat sciatic nerve neurotomy model
5-hydroxy-1,4-naphthoquinone
-
i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
-
-
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
-
-
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
-
-
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.127 mM
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.001 mM
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.085 mM
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
-
IC50: 7 mM
acetyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.77 mM
Ala-Pro
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
cyclic CRYPEVEIC
-
the cyclic peptide is specific for the active site of the PPIase domain
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
-
-
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
-
-
cycloheximide
-
-
cyclosporin A
D-Ser(PO3H2)-Pro
-
1 mM, 20% inhibition
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
-
-
diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
-
-
dipentamethylene thiuram monosulfide
-
-
epigallocatechin-3-gallate
10 microM, 55% residual activity
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
FK506
-
-
juglone
linear CRYPEVEIC
-
-
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
-
-
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
-
-
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
-
-
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.004 mM
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.097 mM
QAEGPK
peptide corresponding to peptide QAEGP487KR at the N-terminus of the enzyme's isomerase domain. Peptide binds to the active site, but the enzyme does not catalyze its isomerization
Ser(PO3H2)-Pro
Ser-Pro
-
-
Ser-PSI[CS-N]-Pro
-
-
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.138 mM
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.02 mM. Selectively inhibits Cyp-18, but not enzyme isoform FKBP12
succinyl-Ala-Ala-Pro-NH2
-
IC50: 14 mM
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
-
IC50: 4.4 mM
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.54 mM
succinyl-Ala-Pro-Phe-4-aminoanilide
-
IC50: 5.8 mM
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
-
IC50: 0.7 mM
succinyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.17 mM
succinyl-Pro-Phe-4-nitroanilide
-
IC50: 1.09 mM
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
[3-[(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)carbonyl]-2-methyl-1-benzofuran-5-yl]acetonitrile
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
stimulation
additional information
-
GM-CSF-induced activation of Erk1/2, which phosphorylated Thr167 of the pro-apoptotic Bcl-2-associated X protein, Bax, facilitates de novo interaction of Bax with the prolyl isomerase Pin1
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
Ala-Gly-PSI[CS-N]-Pro-Phe-4-nitroanilide
-
-
0.814
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
pH 8.0, 8.5°C
0.17 - 0.7
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
1.247
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.585
succinyl-Ala-Lys-Pro-Phe-4-nitroanilide
-
-
additional information
additional information
kinetic analysis of Pin1, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34.2
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
pH 8.0, 8.5°C
3.7 - 140
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
1480 - 14600
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
pH 8.0, 8.5°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
pH 8.0
0.0012
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.0081
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.00222
(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.00001
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
0.01
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.007
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.004 - 0.01
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000005
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.002 - 0.006
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.01
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.02
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.000005
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00016
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.000007
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0002
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
0.001
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
pH and temperature not specified in the publication
0.0074
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
pH and temperature not specified in the publication
0.0041
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
pH and temperature not specified in the publication
0.0072
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
pH and temperature not specified in the publication
0.00366
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.0001
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
0.000001
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
0.0021
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0037
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
pH and temperature not specified in the publication
0.0018
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0006
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0029
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0026
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0086
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
0°C, pH 8.0
0.00005
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0167
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
0.0092
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.0079
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.000084
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.055
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000059
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.03
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
0.000012
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.012
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00023
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.00006
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.0023
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
0.00009
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.000019
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.258
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0012
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.183
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0048
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.0183
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
0.547
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10°C
19
Ala-Pro
-
-
0.000068
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0000028
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.000081
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0002 - 0.00052
cyclic CRYPEVEIC
0.0034
cycloheximide
-
-
0.00066
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0043
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.008
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
0.004
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.044
linear CRYPEVEIC
-
using succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C
1
Ser(PO3H2)-Pro
-
-
27
Ser-Pro
-
-
0.009
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.026
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.016
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.015
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.044
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
0.032
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0485
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0092
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.01
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
Homo sapiens
-
above, pH and temperature not specified in the publication
0.00167
(2,5-dimethyl-1-benzofuran-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
Homo sapiens
-
pH and temperature not specified in the publication
0.0275
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0079
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0216
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
Homo sapiens
-
-
0.00088
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
Homo sapiens
-
-
0.00062
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
Homo sapiens
-
-
0.00069
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
Homo sapiens
-
-
0.00087
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
Homo sapiens
-
-
0.0009 - 4
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
Homo sapiens
-
-
0.0036
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
Homo sapiens
-
-
0.0223
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
Homo sapiens
-
-
0.0044
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
Homo sapiens
-
-
0.1
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
Homo sapiens
-
-
0.077
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
Homo sapiens
-
-
0.065
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
Homo sapiens
-
-
0.215
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
Homo sapiens
-
10°C
1
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10°C
8
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
Homo sapiens
-
pH 7.8, 10°C
15
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10°C
15
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10°C
7
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10°C
0.001
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.001 mM
0.085
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.085 mM
7
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
Homo sapiens
-
IC50: 7 mM
0.77
acetyl-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.77 mM
30
Ala-Pro
Homo sapiens
-
IC50: 30 mM
0.0011
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
Homo sapiens
-
-
0.3
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
Homo sapiens
-
above
0.063
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
Homo sapiens
-
-
0.000043
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
Homo sapiens
-
-
0.0011
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
Homo sapiens
-
-
0.00031
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
Homo sapiens
-
-
0.000032
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
Homo sapiens
-
-
0.0025
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
Homo sapiens
-
-
0.00022
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
Homo sapiens
-
-
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
Homo sapiens
-
above
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
Homo sapiens
-
above
0.00000265 - 0.012
cyclosporin A
0.0086
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
Homo sapiens
-
-
0.00059
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
Homo sapiens
-
-
0.00093
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
Homo sapiens
-
-
0.004
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.004 mM
0.097
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.097 mM
2
Ser(PO3H2)-Pro
Homo sapiens
-
IC50: 2.0 mM
0.54
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
10°C
0.015
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
Homo sapiens
-
10°C
14
succinyl-Ala-Ala-Pro-NH2
Homo sapiens
-
IC50: 14 mM
4.4
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
Homo sapiens
-
IC50: 4.4 mM
0.54
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.54 mM
5.8
succinyl-Ala-Pro-Phe-4-aminoanilide
Homo sapiens
-
IC50: 5.8 mM
0.7
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
Homo sapiens
-
IC50: 0.7 mM
0.17
succinyl-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.17 mM
1.09
succinyl-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 1.09 mM
0.0045
[3-[(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)carbonyl]-2-methyl-1-benzofuran-5-yl]acetonitrile
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FKBP12
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
primary cortical culture
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
-
foetal brain
Manually annotated by BRENDA team
-
a Hodkin's lymphoma cell line
Manually annotated by BRENDA team
enzyme isoform Pin1 is necessary for activation-dependent mRNA stabilization, accumulation, and protein secretion of cytokine GM-CSF. Pin1 mediates the association of the AU-rich element-binding protein, AUF1, with GM-CSF mRNA
Manually annotated by BRENDA team
-
co-localization of cyclophilin B and channel protein TRPV6 in the syncytiotropoblast layer, with small amounts of both in microvilli apical membrane
Manually annotated by BRENDA team
neuroblastoma cell, overexpression of isoform Pin1 decreases levels of the inhibitor of apoptosis protein, Survivin. Pin1 and Survivin partially co-localize in interphase and mitotic cells and form a complex. Pin1 silencing leads to an increase in Survivin levels
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
and/or organelles, isoforms CyP2 and CyP3
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the FK506-binding protein (FKBP) family whose members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum. Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. All FKBP-EFs contain an endoplasmic reticulum retention signal at the C-terminus
malfunction
physiological function
additional information
active site Cys113
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FKB1A_HUMAN
108
0
11951
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
x * 14000, about, SDS-PAGE
17000
-
x * 17000, SDS-PAGE
17737
-
x * 17737, calculation from amino acid sequence
18000
-
x * 18000, about
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphorylated at Ser19 in vivo and in vitro. In human HeLa cells the protein is most likely modified by casein kinase 2
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor 1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
1.65 A resolution. The N-terminus of one isomerase domain is bound in the active site of a neighbouring isomerase molecule in a manner analogous to the substrate. This sequence binds to the active site of the enzyme, but cannot be turned over
2.0 A resolution, space group P3121
crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide, hanging drop vapour diffusion method
-
crystal structure of cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
crystal structure of cyclophilin A complexed with a binding site peptide from HIV-1 capsid protein
-
crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]4,4-dimethylthreonine cyclosporin A
-
crystallization of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes
-
hanging drop vapor diffusion method, using 25% (w/v) PEG MME 550, 0.1 M zinc acetate, 0.1 M MES at pH 6.5
in complex with inhibitor 4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate. Fluorine atoms of inhibitor participate in discrete interactions with the Phe36 phenyl ring and the Tyr26 hydroxyl group of enzyme, with the latter resembling a moderate-to-weak hydrogen bond
-
in complex with inhibitors (1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate, (1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate, (24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21H)-tetrone
-
mutant K125A/E126A is crystallized by the hanging drop vapor diffusion method, using 2 M NH4SO4, 0.2 M NaCl, 0.1 M HEPES, pH 7.5
mutant P9Q/R13F/K17V/R18F in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
purified recombinant detagged wild-type and selenomethionine-labeled FKBP22, hanging drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 1 mM Tris/HCl, pH 7.2, and 0.05 mM CaCl2, with 0.001 ml of reservoir solution containing 0.1 M MES, 25% 1,2-propanediol, and 11-12% PEG 20000, pH 7.0-7.2, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.9 A and 2.46 A resolution, respectively
recombinant enzyme
recombinant enzyme expressed in Escherichia coli
-
recombinant protein, overall structure and analysis of cyclosporin A binding site
-
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M NaI
sitting drop vapor diffusion method, using 34% (w/v) PEG 8K, 0.2 M NH4SO4, and 0.1 M bis-Tris, pH 6.0
solution structure of protein determined by NMR spectroscopy
structure of a relatively protease-resistant N-terminal fragment containing the PPIase domain, t 2.0 A resolution. Residues Arg56, Phe61, Ile62, Gln64, Ala102, Asn103, Phe114, Glu122, Leu123 and His127 in beta-strands 3, 4 and 6, as well as in the extended loop connecting beta-strands 6 and 7, form the proline-binding pocket
structure of CYPJ at 2.0 A and in complex with cyclosporin A. Residues His43, Arg44 and Gln52 are conserved active-site residues located in the shallow pocket, and Arg44 displayes flexible conformation
-
structure of human cyclophilin and its binding site for cyclophilin A determined by X-ray crystallography and NMR spectroscopy
-
X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
-
X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A16S
-
site-directed mutagenesis, dominant-negative Pin1 point mutation
C113A
C113D
mutation does not compromise isoform Pin1 function in vivo nor does it abolish catalytic activity. C113 may not be the catalytic nucleophile
C113S
C115A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C161A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C52A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C62A
-
Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
D155R
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
D158R
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
DELTA208-213
-
dramatic reduction of peptidylprolyl isomerase activity and 400fold reduction of protein phosphatase 2A activation
F133A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
F60A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
G77H
-
mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
H126Q
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H157A
-
mutant supports viability in yeast complementation assay
H157F
-
mutant supports viability in yeast complementation assay
H157L
-
mutant supports viability in yeast complementation assay
H157N
-
mutant supports viability in yeast complementation assay
H157S
-
mutant supports viability in yeast complementation assay
H47Q
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H59A
-
mutant supports viability in yeast complementation assay
H59F
-
mutant supports viability in yeast complementation assay but displays significantly reduced growth in yeast compared to wild-type Pin1
H59L
-
mutant is not viable
H59L/H157A
-
about 50% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157F
-
about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, 3% activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157L
-
mutant supports viability in yeast complementation assay, mutation H157L rescues mutant H59L
H59L/H157S
-
about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59N
-
mutant supports viability in yeast complementation assay
H59S
-
mutant supports viability in yeast complementation assay
K120A
-
87% of wild-type activity
P16S
-
10fold decrease in ratio kcat/Km at 10°C. Mutant is extremely sensitive to guanidinium-HCl and shows increased susceptibility to urea. Folding time of the mutant is extended
P9Q/R13F/K17V/R18F
-
mutant designed for crytallizability, crystal structure in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
Q111A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
R44A
-
57% of wild-type activity
R44A/F49A
-
32% of wild-type activity
R55A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
R68/69A
-
catalytically inactive
R68A/R69A
decrease in both kcat and Km value
S16A/Y23A
-
the mutations of Pin1 protein do not affect the structure of Pin1 but abolishes the ability of the WW domain to bind pSer/pThr-Pro ligands
S16E
-
mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
S19A
-
mutation abolishes phosphorylation and alters the subcellular localization from predominantly nuclear to significantly cytoplasmic
S19E
-
mutant enzyme is localized around the nuclear envelope, but does not penetrate into the nucleoplasm, in vitro DNA-binding affinity is strongly reduced
V55R
-
site-directed mutagenesis, the mutation increases the PPIase activity by a factor of 11
W121A
-
mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
W34A/K63A
-
catalytically inactive
Y82K
-
site-directed mutagenesis, the mutation decreases the PPIase activity by a factor of 7
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
melting temperature, peptidyl-prolyl cis-trans isomerase domain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 isoforms: CyP1, CyP2, CyP3
-
glutathione-Sepharose 4B column chromatography
-
glutathione-Sepharose column chromatography and S-Sepharose column chromatography
-
Ni-NTA resin column chromatography and Superdex 200 gel filtration
recombinant enzyme and mutant P16S
-
recombinant GST-tagged enzyme from Escherichia coli
-
recombinant His6-tagged wild-type and selenomethionine-labeled FKBP22 from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography, tag cleavage by enterokinase, anion exchanchromatography, and dialysis
recombinant MBP-Pin1 fusion protein from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 isoforms expressed in Escherichia coli
-
co-expression with TRPV6 channel protein in Xenopus laevis oocytes
-
expressed in COS-1 cells
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21 Gold DE3 cells
expressed in Escherichia coli JM105 cells
-
expression in 293-T cells
-
expression in Escherichia coli
expression in T47D cell, MCF-7 cell, MDA-231 cell
-
expression of GST-tagged Pin1
-
expression of MBP-Pin1 fusion protein in Escherichia coli strain BL21(DE3)
-
gene FKBP14, expression of His6-tagged wild-type and selenomethionine-labeled FKBP22 in Escherichia coli strains BL21(DE3) and B834(DE3), respectively
neutral isoelectric form
-
Par14, sequence comparisons, expression of GST-tagged enzyme in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes
-
wild-type and mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q, expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYPJ expression is upregulated in over 60% hepatocellular carcinoma tissues
-
Pin1 expression is enhanced in transformed T-cell lines C8166-45, MT4, and JPX9 expressing oncoprotein Tax from human T-cell leukemia virus type 1
-
Pin1 expression is increased by NS5B protein
-
the enzyme is upregulated in cancer cells
-
the overexpression of Pin1 in Hep-G2 cells markedly enhances insulin-induced IRS-1 phosphorylation and its downstream events: phosphatidylinositol 3-kinase binding with IRS-1andAkt phosphorylation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harding, M.W.; Handschumacher, R.E.; Speicher, D.W.
Isolation and amino acid sequence of cyclophilin
J. Biol. Chem.
261
8547-8555
1986
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Schutkowski, M.; Wllner, S.; Fischer, G.
Inhibition of peptidyl-prolyl cis/trans isomerase activity by substrate analog structures: thioxo tetrapeptide-4-nitroanilides
Biochemistry
34
13016-13026
1995
Homo sapiens
Manually annotated by BRENDA team
Levy, M.A.; Brandt, M.; Livi, G.P.; Bergsma, D.J.
Purification and characterization of human T-cell cyclophilin expressed in Escherichia coli
Transplant. Proc.
23
319-322
1991
Homo sapiens
Manually annotated by BRENDA team
Huss, R.
Inhibition of cyclophilin function in HIV-I infection by cyclosporin A
Trends Immunol.
17
259-260
1996
Homo sapiens
Manually annotated by BRENDA team
Schmidt, B.; Tradler, T.; Rahfeld, J.U.; Ludwig, B.; Jain, B.; Mann, K.; Rucknagel, K.P.; Janowski, B.; Schierhorn, A.; Kullertz, G.; Hacker, J.M.; Fischer, G.
A cyclophilin-like peptidyl-prolyl cis/trans isomerase from Legionella pneumophila - characterization, molecular cloning and overexpression
Mol. Microbiol.
21
1147-1160
1996
Homo sapiens, Legionella pneumophila
Manually annotated by BRENDA team
Kofron, J.L.; Kuzmic, P.; Kishore, V.; Gemmecker, G.; Fesik, S.W.; Rich, D.H.
Lithium chloride pertubation of cis-trans peptide bond equilibria: effect on conformational equilibria in cyclosporin A and on time-dependent inhibition of cyclophilin
J. Am. Chem. Soc.
114
2670-2675
1992
Homo sapiens
-
Manually annotated by BRENDA team
Holzman, T.F.; Egan, D.A.; Edalji, R.; Simmer, R.L.; Helfrich, R.; Taylor, A.; Burres, N.S.
Preliminary characterization of a cloned neutral isoelectric form of the human peptidyl prolyl isomerase cyclophilin
J. Biol. Chem.
266
2474-2479
1991
Homo sapiens
Manually annotated by BRENDA team
Bergsma, D.J.; Eder, C.; Gross, M.; Kersten, H.; Sylvester, D.; Appelbaum, E.; Cusimano, D.; Livi, G.P.; McLaughlin, M.M.; Kasyan, K.; Porter, T.G.; Silverman, C.; Dunnington, D.; Hand, A.; Prichett, W.P.; Bossard, M.J.; Brandt, M.; Levy, M.A.
The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms
J. Biol. Chem.
266
23204-23214
1991
Homo sapiens
Manually annotated by BRENDA team
Liu, J.; Albers, M.W.; Chen, C.M.; Schreiber, S.L.; Walsh, C.T.
Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis
Proc. Natl. Acad. Sci. USA
87
2304-2308
1990
Homo sapiens
Manually annotated by BRENDA team
Vajdos, F.F.; Yoo, S.; Houseweart, M.; Sundquist, W.I.; Hill, C.P.
Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein
Protein Sci.
6
2297-2307
1997
Homo sapiens
Manually annotated by BRENDA team
Gamble, T.R.; Vajdos, F.F.; Yoo, S.; Worthylake, D.K.; Houseweart, M.; Sundquist, W.I.; Hill, C.P.
Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
Cell
87
1285-1294
1996
Homo sapiens (P62937), Homo sapiens
Manually annotated by BRENDA team
Ke, H.; Mayrose, D.; Belshaw, P.J.; Alberg, D.G.; Schreiber, S.L.; Chang, Z.Y.; Etzkorn, F.A.; Ho, S.; Walsh, C.T.
Crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]-4,4-dimethylthreonine cyclosporin A
Structure
2
33-44
1994
Homo sapiens
Manually annotated by BRENDA team
Mikol, V.; Kallen, J.; Pfugl, G.; Walkinshaw, M.D.
X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution
J. Mol. Biol.
234
1119-1130
1993
Homo sapiens
Manually annotated by BRENDA team
Pflugl, G.; Kallen, J.; Schirmer, T.; Jansonius, J.N.; Zurini, M.G.; Walkinshaw, M.D.
X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
Nature
361
91-94
1993
Homo sapiens
Manually annotated by BRENDA team
Ke, H.M.; Zydowski, L.D.; Liu, J.; Walsh, C.T.
Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution
Proc. Natl. Acad. Sci. USA
88
9483-9487
1991
Homo sapiens
Manually annotated by BRENDA team
Kallen, J.; Spitzfaden, C.; Zurini, M.G.; Wider, G.; Widmer, H.; Wuthrich, K.; Walkinshaw, M.D.
Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
Nature
353
276-279
1991
Homo sapiens
Manually annotated by BRENDA team
Zurini, M.; Kallen, J.; Mikol, V.; Pfluegel, G.; Jansonius, J.N.; Walkinshaw, M.D.
Crystallisation and preliminary X-ray diffraction studies of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes
FEBS Lett.
276
63-66
1990
Homo sapiens
Manually annotated by BRENDA team
Zydowsky, L.D.; Etzkorn, F.A.; Chang, H.Y.; Ferguson, S.B.; Stolz, L.A.; Ho, S.I.; Walsh, C.T.
Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
Protein Sci.
1
1092-1099
1992
Homo sapiens
Manually annotated by BRENDA team
Hennig, L.; Christner, C.; Kipping, M.; Schelbert, B.; Rucknagel, K.P.; Grabley, S.; Kullertz, G.; Fischer, G.
Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone
Biochemistry
37
5953-5960
1998
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Fuessel, S.; Reimer, U.; Schutkowski, M.; Fischer, G.
Substrate-based design of reversible Pin1 inhibitors
Biochemistry
41
11868-11877
2002
Homo sapiens
Manually annotated by BRENDA team
Demange, L.; Moutiez, M.; Vaudry, K.; Dugave, C.
Interaction of human cyclophilin hCyp-18 with short peptides suggests the existence of two functionally independent subsites
FEBS Lett.
505
191-195
2001
Homo sapiens
Manually annotated by BRENDA team
Bayer, E.; Goettsch, S.; Mueller, J.W.; Griewel, B.; Guiberman, E.; Mayr, L.M.; Bayer, P.
Structural analysis of the mitotic regulator hPin1 in solution. insights into domain architecture and substrate binding
J. Biol. Chem.
278
26183-26193
2003
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Terada, T.; Shirouzu, M.; Fukumori, Y.; Fujimori, F.; Ito, Y.; Kigawa, T.; Yokoyama, S.; Uchida, T.
Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14
J. Mol. Biol.
305
917-926
2001
Homo sapiens (Q13526), Homo sapiens
Manually annotated by BRENDA team
Pirkl, F.; Buchner, J.
Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
J. Mol. Biol.
308
795-806
2001
Homo sapiens
Manually annotated by BRENDA team
Lavoie, S.B.; Albert, A.L.; Handa, H.; Vincent, M.; Bensaude, O.
The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9
J. Mol. Biol.
312
675-685
2001
Homo sapiens
Manually annotated by BRENDA team
Reimer, T.; Weiwad, M.; Schierhorn, A.; Ruecknagel, P.K.; Rahfeld, J.U.; Bayer, P.; Fischer, G.
Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14
J. Mol. Biol.
330
955-966
2003
Homo sapiens
Manually annotated by BRENDA team
Reidt, U.; Wahl, M.C.; Fasshauer, D.; Horowitz, D.S.; Luhrmann, R.; Ficner, R.
Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide
J. Mol. Biol.
331
45-56
2003
Homo sapiens
Manually annotated by BRENDA team
Brazin, K.N.; Mallis, R.J.; Fulton, D.B.; Andreotti, A.H.
Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A
Proc. Natl. Acad. Sci. USA
99
1899-1904
2002
Homo sapiens
Manually annotated by BRENDA team
Golbik, R.; Fischer, G.; Fersht, A.R.
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)
Protein Sci.
8
1505-1514
1999
Homo sapiens
Manually annotated by BRENDA team
Carpentier, M.; Allain, F.; Haendler, B.; Slomianny, M.C.; Spik, G.
Delineation of the calcineurin-interacting region of cyclophilin B
Protein Sci.
9
2386-2393
2000
Homo sapiens
Manually annotated by BRENDA team
Huang, L.L.; Zhao, X.M.; Huang, C.Q.; Yu, L.; Xia, Z.X.
Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family
Acta Crystallogr. Sect. D
D61
316-321
2005
Homo sapiens
Manually annotated by BRENDA team
Hu, H.; Huang, C.Q.; Liu, H.L.; Han, Y.; Yu, L.; Bi, R.C.
Crystallization and preliminary x-ray crystallographic studies of human cyclophilin J
Acta Crystallogr. Sect. F
F61
216-218
2005
Homo sapiens (Q9H2H8), Homo sapiens
Manually annotated by BRENDA team
Wang, T.; Yun, C.H.; Gu, S.Y.; Chang, W.R.; Liang, D.C.
1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase
Biochem. Biophys. Res. Commun.
333
845-849
2005
Homo sapiens
Manually annotated by BRENDA team
Agarwal, P.K.; Geist, A.; Gorin, A.
Protein dynamics and enzymatic catalysis: investigating the peptidyl-prolyl cis-trans isomerization activity of cyclophilin A
Biochemistry
43
10605-10618
2004
Homo sapiens (P62937), Homo sapiens
Manually annotated by BRENDA team
Smet, C.; Wieruszeski, J.M.; Buee, L.; Landrieu, I.; Lippens, G.
Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein
FEBS Lett.
579
4159-4164
2005
Homo sapiens
Manually annotated by BRENDA team
Jordens, J.; Janssens, V.; Longin, S.; Stevens, I.; Martens, E.; Bultynck, G.; Engelborghs, Y.; Lescrinier, E.; Waelkens, E.; Goris, J.; Van Hoof, C.
The PP2A phosphatase activator (PTPA) is a novel peptidyl-prolyl cis/trans isomerase
J. Biol. Chem.
281
6349-6357
2005
Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Watashi, K.; Ishii, N.; Hijikata, M.; Inoue, D.; Murata, T.; Miyanari, Y.; Shimotohno, K.
Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase
Mol. Cell
19
111-122
2005
Homo sapiens
Manually annotated by BRENDA team
Yi, P.; Wu, R.C.; Sandquist, J.; Wong, J.; Tsai, S.Y.; Tsai, M.J.; Means, A.R.; O'Malley, B.W.
Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1)
Mol. Cell. Biol.
25
9687-9699
2005
Homo sapiens
Manually annotated by BRENDA team
Dourlen, P.; Ando, K.; Hamdane, M.; Begard, S.; Buee, L.; Galas, M.C.
The peptidyl prolyl cis/trans isomerase Pin1 downregulates the inhibitor of apoptosis protein Survivin
Biochim. Biophys. Acta
1773
1428-1437
2007
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Dubowchik, G.M.; Ditta, J.L.; Herbst, J.J.; Bollini, S.; Vitnitsky, A.
Fluoresceinated FKBP12 ligands for a high-throughput fluorescence polarization assay
Bioorg. Med. Chem. Lett.
10
559-562
2000
Homo sapiens
Manually annotated by BRENDA team
Halt, D.A.; Konialian-Beck, A.L.; Oh, H.J.; Yen, H.K.; Rozamus, L.W.; Krog, A.J.; Erhard, K.F.; Ortiz, E.; Levy, M.A.; Brandt, M.; Bossard, M.; Luengo, J.I.
Structure-activity studies of synthetic FKBP ligands as peptidyl-prolyl isomerase inhibitors
Bioorg. Med. Chem. Lett.
4
315-322
1994
Homo sapiens
-
Manually annotated by BRENDA team
Luengo, J.I.; Konialian-Beck, A.; Levy, M.A.; Brandt, M.; Eggleston, D.S.; Holt, D.A.
Synthesis and structure-activity relationship of macrocyclic FKBP ligands
Bioorg. Med. Chem. Lett.
4
321-324
1994
Homo sapiens
-
Manually annotated by BRENDA team
Yamashita, D.S.; Oh, H.J.; Yen, H.K.; Bossard, M.J.; Brandt, M.; Levy, M.A.; Newman-Tarr,T.; Badger,A.; Luengo J.I.; Halt, D.A.
Design, synthesis and evaluation of dual domain FKBP ligands
Bioorg. Med. Chem. Lett.
4
325-328
1994
Homo sapiens
-
Manually annotated by BRENDA team
Babine, R.E.; Bleckman, T.M.; Kissinger, C.R.; Showalter, R.; Pelletier, L.A.; Lewis, C.; Tucker, K.; Moomaw, E.; Parge H.E.; Villafranca, J.E.
Design, synthesis and X-ray crystallographic studies of novel FKBP-12 ligands
Bioorg. Med. Chem. Lett.
5
1719-1724
1995
Homo sapiens
-
Manually annotated by BRENDA team
Tatlock, J.H.; Kalish, V.j.; Parge, H.E.; Knighton, D.R.; Showalter, R.E.; Lewis, C.T.; French, J.V.; Villafranca, J.E.
High-affinity FKBP-12 ligands derived from (R)-(-)-carvone. Synthesis and evaluation of FK506 pyranose ring replacements
Bioorg. Med. Chem. Lett.
5
2489-2492
1995
Homo sapiens
-
Manually annotated by BRENDA team
Babine, R.E.; Bleckman, T.M.; Littlefield, E.S.; Parge, H.E.; Pelletier, L.A.K.; Lewis, C.T.; French, J.V.; Imbacuan, M.; Katoh, S.; Tatlock, J.H.; Showalter, R.E.; Villafranca, J.E.
Design, synthesis and X-ray crystallographic studies of [7.3.1] and [8.3.1] macrocyclic FKBP-12 ligands
Bioorg. Med. Chem. Lett.
6
385-390
1996
Homo sapiens (P62942)
-
Manually annotated by BRENDA team
Wang, X.J.; Etzkorn, F.A.
Peptidyl-prolyl isomerase inhibitors
Biopolymers
84
125-146
2006
Homo sapiens
Manually annotated by BRENDA team
Obama, K.; Kato, T.; Hasegawa, S.; Satoh, S.; Nakamura, Y.; Furukawa, Y.
Overexpression of peptidyl-prolyl isomerase-like 1 is associated with the growth of colon cancer cells
Clin. Cancer Res.
12
70-76
2006
Homo sapiens
Manually annotated by BRENDA team
Siegrist, R.; Zurcher, M.; Baumgartner, C.; Seiler, P.; Diederich, F.; Daum, S.; Fischer, G.; Klein, C.; Dangl, M.; Schwaiger, M.
A novel synthesis of highly substituted perhydropyrrolizines, perhydroindolizines, and pyrrolidines: inhibition of the peptidyl-prolyl cis/trans isomerase (PPIase) Pin1
Helv. Chim. Acta
90
217-259
2007
Homo sapiens (Q13526)
-
Manually annotated by BRENDA team
Holt, D.A.; Luengo, J.I.; Yamashita, D.S.; Oh, H.J.; Konialian, A.L.; Yen, H.K.; Rozamus, L.W.; Brandt, M.; Bossard, M.J.; Levy, m.A.; Eggleston, D.S.; g Liang, J.; Schultz, L.W.; Stout, t.J.; Clardyt, J.
Design, synthesis and kinetic evaluation of high-affinity FKBP ligands and the X-ray Crystal structures of their complexes with FKBP12
J. Am. Chem. Soc.
115
9925-9938
1993
Homo sapiens
-
Manually annotated by BRENDA team
Xu, C.; Zhang, J.; Huang, X.; Sun, J.; Xu, Y.; Tang, Y.; Wu, J.; Shi, Y.; Huang, Q.; Zhang, Q.
Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP
J. Biol. Chem.
281
15900-15908
2006
Homo sapiens (Q9Y3C6), Homo sapiens
Manually annotated by BRENDA team
Yu, L.; Mohamed, A.J.; Vargas, L.; Bergloef, A.; Finn, G.; Lu, K.P.; Smith, C.I.
Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1
J. Biol. Chem.
281
18201-18207
2006
Homo sapiens (Q13526), Homo sapiens
Manually annotated by BRENDA team
Esnault, S.; Shen, Z.J.; Whitesel, E.; Malter, J.S.
The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes
J. Immunol.
177
6999-7006
2006
Homo sapiens (Q13526), Homo sapiens
Manually annotated by BRENDA team
Christner, C.; Wyrwa, R.; Marsch, S.; Kullertz, G.; Thiericke, R.; Grabley, S.; Schumann, D.; Fischer, G.
Synthesis and cytotoxic evaluation of cycloheximide derivatives as potential inhibitors of FKBP12 with neurogenerative properties
J. Med. Chem.
42
3615-3622
1999
Homo sapiens
Manually annotated by BRENDA team
Demange, L.; Moutiez, M.; Dugave, C.
Synthesis and evaluation of Glypsi(PO2R-N)Pro-containing pseudopeptides as novel inhibitors of the human cyclophilin hCyp-18
J. Med. Chem.
45
3928-3933
2002
Homo sapiens
Manually annotated by BRENDA team
Wu, Y-Q.; Belyakov, S.; choi, c.; Limburg, D.; thomas, b.E.; Vaal, m.; Wei, L.; Wilkinson, D.E.; Holmes, A.; Fuller, M.; McCormick, J.; Conolly, M.; Moeller, T.; Steiner, J.; Hamilton, G.S.
Synthesis and biological evaluation of non-peptidic cyclophilin ligands
J. Med. Chem.
46
1112-1115
2003
Homo sapiens
Manually annotated by BRENDA team
Wildemann, D.; Erdmann, F.; Alvarez, B.H.; Stoller, G.; Zhou, X.Z.; Fanghaenel, J.; Schutkowski, M.; Lu, K.P.; Fischer, G.
Nanomolar inhibitors of the peptidyl prolyl cis/trans isomerase Pin1 from combinatorial peptide libraries
J. Med. Chem.
49
2147-2150
2006
Homo sapiens
Manually annotated by BRENDA team
Behrsin, C.D.; Bailey, M.L.; Bateman, K.S.; Hamilton, K.S.; Wahl, L.M.; Brandl, C.J.; Shilton, B.H.; Litchfield, D.W.
Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution
J. Mol. Biol.
365
1143-1162
2007
Homo sapiens (Q13526), Homo sapiens
Manually annotated by BRENDA team
Andres, C.J.; Macdonald, T.L.
Conformationally defined analogs of prolylamides. trans-Prolyl peptidomimetics
J. Org. Chem.
58
6609-6613
1993
Homo sapiens
-
Manually annotated by BRENDA team
Barth, S.; Nesper, J.; Hasgall, P.A.; Wirthner, R.; Nytko, K.J.; Edlich, F.; Katschinski, D.M.; Stiehl, D.P.; Wenger, R.H.; Camenisch, G.
The peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability
Mol. Cell. Biol.
27
3758-3768
2007
Homo sapiens (Q14318)
Manually annotated by BRENDA team
Dubowchik, G.M.; Vrudhula, V.M.; Dasgupta, B.; Ditta, J.; Chen, T.; Sheriff, S.; Sipman, K.; Witmer, M.; Tredup, J.; Vyas, d.M.; Verdoorn, T.A.; Bollini, S.; Vinitsky, A.
2-aryl-2,2-difluoroacetamide FKBP12 ligands: synthesis and X-ray structural studies
Org. Lett.
3
3987-3990
2001
Homo sapiens
Manually annotated by BRENDA team
Kim, M.R.; Choi, H.S.; Heo, T.H.; Hwang, S.W.; Kang, K.W.
Induction of vascular endothelial growth factor by peptidyl-prolyl isomerase Pin1 in breast cancer cells
Biochem. Biophys. Res. Commun.
369
547-553
2008
Homo sapiens
Manually annotated by BRENDA team
Bailey, M.L.; Shilton, B.H.; Brandl, C.J.; Litchfield, D.W.
The dual histidine motif in the active site of Pin1 has a structural rather than catalytic role
Biochemistry
47
11481-11489
2008
Homo sapiens
Manually annotated by BRENDA team
Xu, L.R.; Yan, X.; Luo, M.; Guan, Y.X.; Yao, S.J.
Preparation, characterization and refolding in vitro of a recombinant human cyclophilin A mutant: effect of a single Pro/Ser substitution on cyclophilin A structure and properties
Biotechnol. Prog.
24
302-310
2008
Homo sapiens
Manually annotated by BRENDA team
Brenkman, A.B.; de Keizer, P.L.; van den Broek, N.J.; van der Groep, P.; van Diest, P.J.; van der Horst, A.; Smits, A.M.; Burgering, B.M.
The peptidyl-isomerase Pin1 regulates p27kip1 expression through inhibition of Forkhead box O tumor suppressors
Cancer Res.
68
7597-7605
2008
Homo sapiens
Manually annotated by BRENDA team
Zheng, J.; Koblinski, J.E.; Dutson, L.V.; Feeney, Y.B.; Clevenger, C.V.
Prolyl isomerase cyclophilin A regulation of Janus-activated kinase 2 and the progression of human breast cancer
Cancer Res.
68
7769-7778
2008
Homo sapiens
Manually annotated by BRENDA team
Davis, T.L.; Walker, J.R.; Ouyang, H.; MacKenzie, F.; Butler-Cole, C.; Newman, E.M.; Eisenmesser, E.Z.; Dhe-Paganon, S.
The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1)
FEBS J.
275
2283-2295
2008
Homo sapiens (Q96BP3), Homo sapiens
Manually annotated by BRENDA team
Stumpf, T.; Zhang, Q.; Hirnet, D.; Lewandrowski, U.; Sickmann, A.; Wissenbach, U.; Doerr, J.; Lohr, C.; Deitmer, J.W.; Fecher-Trost, C.
The human TRPV6 channel protein is associated with cyclophilin B in human placenta
J. Biol. Chem.
283
18086-18098
2008
Homo sapiens
Manually annotated by BRENDA team
Rudrabhatla, P.; Zheng, Y.L.; Amin, N.D.; Kesavapany, S.; Albers, W.; Pant, H.C.
Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein
J. Biol. Chem.
283
26737-26747
2008
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Braun, M.; Hessamian-Alinejad, A.; de Lacroix, B.F.; Alvarez, B.H.; Fischer, G.
Novel spiroannulated 3-benzofuranones. Synthesis and inhibition of the human peptidyl prolyl cis/trans isomerase Pin1
Molecules
13
995-1003
2008
Homo sapiens
Manually annotated by BRENDA team
Buschdorf, J.P.; Chew, L.L.; Soh, U.J.; Liou, Y.C.; Low, B.C.
Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons
PLoS ONE
3
e2686
2008
Homo sapiens
Manually annotated by BRENDA team
Fan, G.; Fan, Y.; Gupta, N.; Matsuura, I.; Liu, F.; Zhou, X.Z.; Lu, K.P.; Gelinas, C.
Peptidyl-prolyl isomerase Pin1 markedly enhances the oncogenic activity of the rel proteins in the nuclear factor-kappaB family
Cancer Res.
69
4589-4597
2009
Homo sapiens
Manually annotated by BRENDA team
van der Horst, A.; Khanna, K.K.
The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55
Cancer Res.
69
6651-6659
2009
Homo sapiens
Manually annotated by BRENDA team
Rudrabhatla, P.; Pant, H.C.
Phosphorylation-specific peptidyl-prolyl isomerization of neuronal cytoskeletal proteins by Pin1: implications for therapeutics in neurodegeneration
J. Alzheimers Dis.
19
389-403
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hanoulle, X.; Badillo, A.; Wieruszeski, J.M.; Verdegem, D.; Landrieu, I.; Bartenschlager, R.; Penin, F.; Lippens, G.
Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B
J. Biol. Chem.
284
13589-13601
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, T.; Liu, Y.; Kao, H.Y.; Pei, D.
Membrane permeable cyclic peptidyl inhibitors against human peptidylprolyl isomerase Pin1
J. Med. Chem.
53
2494-2501
2010
Homo sapiens
Manually annotated by BRENDA team
Rudrabhatla, P.; Albers, W.; Pant, H.C.
Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins
J. Neurosci.
29
14869-14880
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Peloponese, J.M.; Yasunaga, J.; Kinjo, T.; Watashi, K.; Jeang, K.T.
Peptidylproline cis-trans-isomerase Pin1 interacts with human T-cell leukemia virus type 1 tax and modulates its activation of NF-kappaB
J. Virol.
83
3238-3248
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, Z.; Yang, F.; Robotham, J.M.; Tang, H.
Critical role of cyclophilin A and its prolyl-peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex
J. Virol.
83
6554-6565
2009
Homo sapiens
Manually annotated by BRENDA team
Fujiyama-Nakamura, S.; Yoshikawa, H.; Homma, K.; Hayano, T.; Tsujimura-Takahashi, T.; Izumikawa, K.; Ishikawa, H.; Miyazawa, N.; Yanagida, M.; Miura, Y.; Shinkawa, T.; Yamauchi, Y.; Isobe, T.; Takahashi, N.
Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage
Mol. Cell. Proteomics
8
1552-1565
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Shen, Z.J.; Esnault, S.; Schinzel, A.; Borner, C.; Malter, J.S.
The peptidyl-prolyl isomerase Pin1 facilitates cytokine-induced survival of eosinophils by suppressing Bax activation
Nat. Immunol.
10
257-265
2009
Homo sapiens
Manually annotated by BRENDA team
Liao, Y.; Wei, Y.; Zhou, X.; Yang, J.Y.; Dai, C.; Chen, Y.J.; Agarwal, N.K.; Sarbassov, D.; Shi, D.; Yu, D.; Hung, M.C.
Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation
Oncogene
28
2436-2445
2009
Homo sapiens
Manually annotated by BRENDA team
Misumi, S.; Inoue, M.; Dochi, T.; Kishimoto, N.; Hasegawa, N.; Takamune, N.; Shoji, S.
Uncoating of human immunodeficiency virus type 1 requires prolyl isomerase Pin1
J. Biol. Chem.
285
25185-25195
2010
Homo sapiens
Manually annotated by BRENDA team
Nakatsu, Y.; Sakoda, H.; Kushiyama, A.; Zhang, J.; Ono, H.; Fujishiro, M.; Kikuchi, T.; Fukushima, T.; Yoneda, M.; Ohno, H.; Horike, N.; Kanna, M.; Tsuchiya, Y.; Kamata, H.; Nishimura, F.; Isobe, T.; Ogihara, T.; Katagiri, H.; Oka, Y.; Takahashi, S.; Kurihara, H.; Uchida, T.; Asano, T.
Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 associates with insulin receptor substrate-1 and enhances insulin actions and adipogenesis
J. Biol. Chem.
286
20812-20822
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
St-Denis, N.A.; Bailey, M.L.; Parker, E.L.; Vilk, G.; Litchfield, D.W.
Localization of phosphorylated CK2alpha to the mitotic spindle requires the peptidyl-prolyl isomerase Pin1
J. Cell Sci.
124
2341-2348
2011
Homo sapiens
Manually annotated by BRENDA team
Duncan, K.E.; Dempsey, B.R.; Killip, L.E.; Adams, J.; Bailey, M.L.; Lajoie, G.A.; Litchfield, D.W.; Brandl, C.J.; Shaw, G.S.; Shilton, B.H.
Discovery and characterization of a nonphosphorylated cyclic peptide inhibitor of the peptidylprolyl isomerase, Pin1
J. Med. Chem.
54
3854-3865
2011
Homo sapiens
Manually annotated by BRENDA team
Lim, Y.S.; Tran, H.T.; Park, S.J.; Yim, S.A.; Hwang, S.B.
Peptidyl-prolyl isomerase Pin1 is a cellular factor required for hepatitis C virus propagation
J. Virol.
85
8777-8888
2011
Homo sapiens
Manually annotated by BRENDA team
Davis, T.L.; Walker, J.R.; Campagna-Slater, V.; Finerty, P.J.; Paramanathan, R.; Bernstein, G.; MacKenzie, F.; Tempel, W.; Ouyang, H.; Lee, W.H.; Eisenmesser, E.Z.; Dhe-Paganon, S.
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases
PLoS Biol.
8
e1000439
2010
Homo sapiens (O43447), Homo sapiens (P23284), Homo sapiens (P30405), Homo sapiens (P45877), Homo sapiens (P62937), Homo sapiens (Q08752), Homo sapiens (Q13427), Homo sapiens (Q6UX04), Homo sapiens (Q9UNP9), Homo sapiens
Manually annotated by BRENDA team
Mercedes-Camacho, A.Y.; Mullins, A.B.; Mason, M.D.; Xu, G.G.; Mahoney, B.J.; Wang, X.; Peng, J.W.; Etzkorn, F.A.
Kinetic isotope effects support the twisted amide mechanism of Pin1 peptidyl-prolyl isomerase
Biochemistry
52
7707-7713
2013
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Hediger, T.; Frank, W.; Schumann, M.; Fischer, G.; Braun, M.
Aryl hetaryl ketones and thioketones as efficient inhibitors of peptidyl-prolyl cis-trans isomerases
Chem. Biodivers.
9
2618-2634
2012
Homo sapiens
Manually annotated by BRENDA team
Ikura, T.; Ito, N.
Peptidyl-prolyl isomerase activity of FK506 binding protein 12 prevents tau peptide from aggregating
Protein Eng. Des. Sel.
26
539-546
2013
Homo sapiens
Manually annotated by BRENDA team
Boudko, S.P.; Ishikawa, Y.; Nix, J.; Chapman, M.S.; Baechinger, H.P.
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs
Protein Sci.
23
67-75
2014
Homo sapiens (Q9NWM8), Homo sapiens
Manually annotated by BRENDA team
Ulrich, A.; Wahl, M.C.
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27
Acta Crystallogr. Sect. D
70
3110-3123
2014
Homo sapiens (Q6UX04), Homo sapiens, Thermochaetoides thermophila (G0RY38), Thermochaetoides thermophila DSM 1495 (G0RY38)
Manually annotated by BRENDA team
Hidaka, M.; Kosaka, K.; Tsushima, S.; Uchida, C.; Takahashi, K.; Takahashi, N.; Tsubuki, M.; Hara, Y.; Uchida, T.
Food polyphenols targeting peptidyl prolyl cis/trans isomerase Pin1
Biochem. Biophys. Res. Commun.
499
681-687
2018
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Ettelaie, C.; Collier, M.E.W.; Featherby, S.; Greenman, J.; Maraveyas, A.
Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles
Biochim. Biophys. Acta
1865
12-24
2018
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Jalouli, M.; Dery, M.A.; Lafleur, V.N.; Lamalice, L.; Zhou, X.Z.; Lu, K.P.; Richard, D.E.
The prolyl isomerase Pin1 regulates hypoxia-inducible transcription factor (HIF) activity
Cell. Signal.
26
1649-1656
2014
Homo sapiens (Q13526)
Manually annotated by BRENDA team
Jiang, Q.; Li, X.R.; Wang, C.K.; Cheng, J.; Tan, C.; Cui, T.T.; Lu, N.N.; James, T.D.; Han, F.; Li, X.
A fluorescent peptidyl substrate for visualizing peptidyl-prolyl cis/trans isomerase activity in live cells
Chem. Commun. (Camb.)
54
1857-1860
2018
Homo sapiens (Q00688)
Manually annotated by BRENDA team
Chen, J.; Chen, S.; Wang, J.; Zhang, M.; Gong, Z.; Wei, Y.; Li, L.; Zhang, Y.; Zhao, X.; Jiang, S.; Yu, L.
Cyclophilin J is a novel peptidyl-prolyl isomerase and target for repressing the growth of hepatocellular carcinoma
PLoS ONE
10
e0127668
2015
Homo sapiens
Manually annotated by BRENDA team
Han, H.J.; Kwon, N.; Choi, M.A.; Jung, K.O.; Piao, J.Y.; Ngo, H.K.; Kim, S.J.; Kim, D.H.; Chung, J.K.; Cha, Y.N.; Youn, H.; Choi, B.Y.; Min, S.H.; Surh, Y.J.
Peptidyl prolyl isomerase PIN1 directly binds to and stabilizes hypoxia-inducible factor-1alpha
PLoS ONE
11
e0147038
2016
Homo sapiens (Q13526), Mus musculus (Q9QUR7)
Manually annotated by BRENDA team