5.2.1.8: peptidylprolyl isomerase
This is an abbreviated version!
For detailed information about peptidylprolyl isomerase, go to the full flat file.
Word Map on EC 5.2.1.8
-
5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
-
calcineurin
-
isomerases
-
necrosis
-
cardiac
-
lymphocyte
-
immunodeficiency
-
capsid
-
ryanodine
-
t-cells
-
steroid
-
glucocorticoid
-
alzheimer
-
tetratricopeptide
-
tacrolimus
-
refolding
-
hsp70
-
mtor
-
interactor
-
virion
-
imperfecta
-
gapdh
-
co-chaperone
-
genorm
-
dnak
-
anti-hcv
-
ptp
-
groel
-
legionella
-
osteogenesis
-
sarcoplasmic
-
translocase
-
heterocomplexes
-
pneumophila
-
voltage-dependent
-
phosphorylation-dependent
-
ns5a
-
analysis
-
ca2+-induced
-
direct-acting
-
sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
-
medicine
-
ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
-
agriculture
-
pharmacology
- 5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
- calcineurin
- isomerases
- necrosis
- cardiac
- lymphocyte
- immunodeficiency
- capsid
-
ryanodine
- t-cells
- steroid
- glucocorticoid
- alzheimer
-
tetratricopeptide
- tacrolimus
-
refolding
- hsp70
- mtor
- interactor
- virion
- imperfecta
- gapdh
-
co-chaperone
-
genorm
- dnak
-
anti-hcv
- ptp
- groel
- legionella
-
osteogenesis
-
sarcoplasmic
- translocase
-
heterocomplexes
- pneumophila
-
voltage-dependent
-
phosphorylation-dependent
- ns5a
- analysis
-
ca2+-induced
-
direct-acting
- sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
- medicine
- ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
- agriculture
- pharmacology
Reaction
peptidylproline (omega = 180)
Synonyms
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, At3g56070, CeCYP-16, CGI-124, Cgl0830, Chl-Mip, Cj0596, CPH, CTHT_0005290, Cwc27, Cyclophilin, Cyclophilin 18, cyclophilin 3, 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-A, cyclophilin-D, Cyclophilin-like protein Cyp-60, Cyclophilin-related protein, Cyclosporin A-binding protein, Cyp, CYP-3, CYP-40, CYP-5, CYP-6, cyp-A, CYP-S1, Cyp1, Cyp18, Cyp19-3, Cyp2, CYP20-2, CYP20-3, Cyp3, Cyp3 PPIase, Cyp40, CyPA, CypA-1, CyPB, CyPJ, DDB_G0268618, Dod, EF0685, EF1534, EF2898, Estrogen receptor binding cyclophilin, FF1 antigen, FK506 binding protein 12, FK506 binding protein 35, FK506-binding protein, 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, FkbP10, FKBP12, FKBP13, FKBP17, FKBP1B, FKBP22, FKBP25, FKBP3, FKBP33, FKBP35, FKBP38, FKBP51, FKBP52, FKBP52 protein, FKBP54, FKBP59, FKBP65, FKBP65RS, FKBP77, FklB, FkpA, h Par14, HBI, HcCYP, 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, L.p.Cyp18, Macrolide binding protein, Macrophage infectivity potentiator, mimicyp, MIP, mip-like peptidyl-prolyl cis-trans isomerase, More, MtFK, MtFKBP17, mzFKBP-66, Ng-MIP, NIMA-1, Nucleolar proline isomerase, OvCYP-16, p17.7, P31, P54, p59 protein, Par10, Par14, Par27, Par45, Parvulin, Parvulin 14, parvulin-like protein, parvulin-type peptidyl-prolyl isomerase, parvulin1 4, pCYP B, Peptide bond isomerase, peptidyl prolyl cis-trans 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 cis-trans isomerase, peptidylprolyl cis/trans isomerase, peptidylprolyl isomerase, PfCyP, Pin1, PIN1-type parvulin 1, PIN1At, PinA, Planta-induced rust protein 28, Plp, PP2A phosphatase activator, PpiA, PPIase, PPIase Pin1, PPIase Pin4, PpiB, PPIC, PpiD, PPIE, PPIF, PPIG, PPIH, PPIL1, PPWD1, Proline rotamase, prolyl cis-trans isomerase, prolyl-peptidyl isomerase, protein phosphatase 2A phosphatase activator, Proteins, cyclophilins, Proteins, specific or class, cyclophilins, PrsA, Ptf1/Ess1, PtpA, PvFKBP35, Rapamycin-binding protein, Rapamycin-selective 25 kDa immunophilin, ROF2, Rotamase, Rotamase Pin1, Rotamase Pin4, Rotamase plp, S-cyclophilin, S1205-06, SAUSA300_0857, SCYLP, SDCCAG-10, sFkpA, SlrA, SLyD, SmCYP A, SmCYP B, Smp17.7, SP18, spliceosome-associated protein CWC27 homolog, SurA, TcFKBP18, TF, TLP20, trigger factor, TTHA0346, WHP, Ypa
ECTree
5.2.1.8 peptidylprolyl isomeraseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 5.2.1.8 - peptidylprolyl isomerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(cis)-Pro in microtubule associated protein tau
(trans)-Pro in microtubule associated protein tau
-
-
-
?
(cis)-Pro residue in HIF-1alpha
(trans)-Pro residue in HIF-1alpha
-
-
-
r
(cis)-Pro residue in phosphorylated protein PERIOD
(trans)-Pro residue in phosphorylated protein PERIOD
phosphorylated isoforms of PERIOD serve as Dod substrates, leading to Dod-mediated conformational changes of PERIOD
-
-
r
(cis)-Pro residue in protein FOXO3
(trans)-Pro residue in protein FOXO3
-
-
-
r
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
6-(dimethylamino)-2-naphthoyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
acetyl-Ala-Ala-(cis)-Pro-Ala-Lys-NH2
acetyl-Ala-Ala-(trans)-Pro-Ala-Lys-NH2
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
barstar C40A/C82A/P27A
?
-
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
-
?
cis-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
trans-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
-
-
-
?
GFPRALPAWARPDYNPPLVE
?
-
a synthetic peptide, named PepD2, corresponding to residues 304-323 of NS5A
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Pro-(cis)-Phe 4-nitroanilide
Glutaryl-Ala-Pro-(trans)-Phe 4-nitroanilide
-
-
-
?
interleukin-2 tyrosine kinase
?
-
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
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
100% activity, Par45 shows a strong preference for a substrate with the basic Arg residue preceding Pro
-
-
?
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
7.6% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
reduced carboxymethylated bovine alpha-lactalbumin
reduced carboxymethylated bovine alpha-lactalbumin
-
-
-
?
RNase A S-protein
RNase A S-protein
partially folded
action of enzyme greatly reduces the population of aggregated oligomeric species
-
?
Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Ala-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
suc-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
suc-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
Suc-Ala-Leu-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Leu-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
succinyl-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Arg-p-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Arg-p-nitroanilide
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
50% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Gln-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gln-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Gln-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gln-(trans)-Pro-Phe-4-nitroanilide
65% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Gln-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Gln-(trans)-Pro-Phe-p-nitroanilide
-
27% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
-
13% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-7-amido-4-methylcoumarin
succinyl-Ala-Glu-(cis)-Pro-Phe-7-amido-4-methylcoumarin
-
-
-
r
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Gly-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Gly-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-p-nitroanilide
-
37% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
succinyl-Ala-Leu-Pro(omega180)-Phe-4-nitroanilide
succinyl-Ala-Leu-Pro(omega0)-Phe-4-nitroanilide
the substrate binds to PvFKBD35 in a cis conformation involving residues D55, H67, V73, and I74
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Lys-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Lys-(trans)-Pro-Phe-4-nitroanilide
83% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Nle-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Nle-(trans)-Pro-Phe-4-nitroanilide
194% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ser-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ser-(trans)-Pro-Phe-4-nitroanilide
23% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
Succinyl-Ala-Val-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Val-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Val-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Val-(trans)-Pro-Phe-4-nitroanilide
18% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Val-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Val-(trans)-Pro-Phe-p-nitroanilide
-
76% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Arg-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Arg-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Leu-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Leu-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Phe-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Phe-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ser-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ser-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide
Trp-Phe-Tyr-Ser(PO3H2)-(trans)-Pro-Arg-4-nitroanilide
-
-
-
-
?
VYKS-(cis)-PVVSGDTS-(cis)-PRHL
VYKS-(trans)-PVVSGDTS-(trans)-PRHL
interconversion occurs at both P5 and P13
-
-
?
(cis)-Pro residue in nuclease Nuc
(trans)-Pro residue in nuclease Nuc
-
-
-
r
(cis)-Pro residue in nuclease Nuc
(trans)-Pro residue in nuclease Nuc
-
-
-
r
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
-
-
-
-
?
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
-
-
-
-
?
AGL24 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
hepatitis C virus NS5A protein
?
-
nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain. Mutations in this domain are linked to cyclosporin A resistance
-
-
?
hepatitis C virus NS5A protein
?
-
substrate is the domain 2 of the nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain, recombinantly expressed His-tagged substrate. Determination of direct molecular interaction between NS5A-D2 and both cyclophilins by NMR spectrometry, overview
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
r
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
6.9% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
ratio kcat to Km value is 15400 per M and s
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Ala-Phe-(cis)-Pro-4-nitroanilide
N-succinyl-Ala-Ala-Phe-(trans)-Pro-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
ratio kcat to Km value is 397000 per M and s
-
?
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
r
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
26.7% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
r
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
4.3% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
preferred substrate
-
-
?
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
preferred substrate
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
computational study on protein dynamics, network of protein vibrations, comparison with structures from different species
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
-
solvent-assisted mechanism, H43 and Q52 are active sites
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
-
Pin1 prevents activation of Bax, prevents Bax cleavage by calpain, and prevents Bax translocation to mitochondria
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
-
-
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
-
-
-
-
?
RNA polymerase II
?
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
RNA polymerase II
?
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
RNAse T1
?
-
reduced and carboxymethylated form of the S54G/P55N variant of RNAse T1. In the native state the Rnase T1 contains a single prolyl bond Tyr38-Pro39. Of all reduced and carboxymethylated RNAse T1 molecules, 85% fold in a monophasic and reversible reaction, which is limited in rate by the slow trans to cis isomerization at Pro39
-
?
RNAse T1
?
-
reduced and carboxymethylated RNAse T1, refolding by trans to cis isomerization of peptidyl-prolyl bonds at Pro39 and Pro55
-
?
RNAse T1
?
-
rate-limiting isomerization of -(trans)-Pro to -(cis)-Pro. Disulfide-reduced and S-carboxymethylated form of a variant of Rnase T1 with Ser54Gly and Pro55Asn. The trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
serine/threonine protein kinase B
?
-
i.e. Akt, reduced activity with Akt mutants T92A/T450A and T92D/T450D. Akt-Pin1 interaction analysis using HA-tagged Akt and GST-tagged Pin1, overview
-
-
?
SOC1 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
-
-
?
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Lys-4-methylcoumarin-7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
trans
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
38% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
70fold decrease in activity compared with succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
-
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
11% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
-
67% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
mimicyp lacks peptidyl-prolyl isomerase activity
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
33% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
-
35% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
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-
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?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
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-
r
additional information
?
-
not essential for protein import into chloroplast
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?
additional information
?
-
not essential for protein import into chloroplast
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?
additional information
?
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-
not essential for protein import into chloroplast
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?
additional information
?
-
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24
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?
additional information
?
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
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?
additional information
?
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AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
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?
additional information
?
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-
only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity
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?
additional information
?
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-
only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity. The prolyl isomerases become essential for growth under starvation conditions
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?
additional information
?
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isoform Par27 displays both prolyl-peptidyl isomerase and chaperone activities in vitro
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?
additional information
?
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isoform Par27 displays both prolyl-peptidyl isomerase and chaperone activities in vitro
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?
additional information
?
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Par27 exhibits both chaperone and PPIase activities in vitro. Full-length and isolated PPIase domain show PPIase activity using either reduced carboxymethylated RNAse T1 or a 16-mer peptide as substrates, product analysis by NMR, overview. Functional analysis of enzyme domains and structure modeling, overview
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?
additional information
?
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-
the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
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-
?
additional information
?
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
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?
additional information
?
-
-
class3 cyclophilins are involved in cellular responses to stress caused by changes in redox environment or by upregulation of cellular activity
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?
additional information
?
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-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
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?
additional information
?
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-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
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-
?
additional information
?
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-
the kinesin-related protein, KRMP1 is a mitotic target regulated by Pin1 and vice versa
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?
additional information
?
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-
increases the refolding of type IV procollagen
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-
?
additional information
?
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catalyzes the refolding of thermally denatured type III collagen
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-
?
additional information
?
-
the enzyme has peptidylprolyl isomerase activity and chaperone activity
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?
additional information
?
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the enzyme has peptidylprolyl isomerase activity and chaperone activity
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?
additional information
?
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the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
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?
additional information
?
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-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
additional information
?
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-
PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS, and derived model peptides. Substrate specificity of PpiD is less specific than that for isoform SurA. The substrate specificity of PpiD is determined more by the hydrophobicity of residues in the model peptides than the presence of aromatic residues
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-
?
additional information
?
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peptidyl-prolyl cis-trans isomerase FKBP22 binds FK506 and rapamycin, that are both immunosuppressive drugs
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-
?
additional information
?
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Escherichia coli B / ATCC 11303
-
increases the refolding of type IV procollagen
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-
?
additional information
?
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purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
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-
?
additional information
?
-
-
purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
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-
?
additional information
?
-
purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity
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?
additional information
?
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-
cyclophilin B complexed to cyclosporin A inhibits phosphatase activity of recombinant human calcineurin
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?
additional information
?
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-
no catalysis is observed with the substrates Ala-(cis)-Pro, Ala-Ala-(cis)-Pro, Ala-(cis)-Pro-Ala, Ser-(cis)-Pro and Ser(PO3H2)-(cis)-Pro
-
?
additional information
?
-
the mechanism determining the substrate specificity seems to be different between hPAR14 and hPin1
-
?
additional information
?
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-
the mechanism determining the substrate specificity seems to be different between hPAR14 and hPin1
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?
additional information
?
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-
the presence of cyclophilin A in the human immunodeficiency virus type 1, HIV-1, is required for HIV-1 to infect and replicate
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-
?
additional information
?
-
-
the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
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-
?
additional information
?
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cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
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-
?
additional information
?
-
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cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
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-
?
additional information
?
-
-
enzyme is required for cell cycle progression
-
?
additional information
?
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-
folding helper enzyme that plays a role in cell-cycle and chromatin remodeling
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?
additional information
?
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peptidylprolyl isomerase Pin1 interacts with Cdk9-phosphorylated hSpt5. Cdk9 dependent phosphorylation of Rpb1 and hSpt5 followed by Pin1 interaction might contribute to the regulation of transcription, pre-mRNA maturation and the dynamics of proteins in interphase and mitosis
-
?
additional information
?
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substrates are proteins involved in regulation of cell cycle, transcription, Alzheimers disease, and cancer pathogenesis
-
?
additional information
?
-
-
the peptidylprolyl isomerase Cyp40, FKBP51 and FKBP52 are components of the Hsp90 chaperone complex. The peptidylprolyl isomerase monomers bind to a Hsp90 dimer. The three isomerase differ both in their affinity for Hsp90 and their chaperone activity suggesting that they play distinct roles in the Hsp90 chaperone complex
-
?
additional information
?
-
-
selective for substrate SRC-3, phosphorylated steroid receptor coactivator 3. Enzyme and SRC-3 synergistically activate nuclear-receptor-regulated transcription
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-
?
additional information
?
-
enzyme isoform Pin1 interacts with Bruton tyrosine kinase in a cell-cycle dependent manner, regulating the Bruton tyrosine kinase expression level. Interaction requires a functionally intact tyrosine kinase and occurs via S21 and S115 residues of the kinase
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?
additional information
?
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-
enzyme isoform Pin1 interacts with Bruton tyrosine kinase in a cell-cycle dependent manner, regulating the Bruton tyrosine kinase expression level. Interaction requires a functionally intact tyrosine kinase and occurs via S21 and S115 residues of the kinase
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-
?
additional information
?
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isoform Pin1 modulates oxidative stress-induced neurofilament NF-H phosphorylation. In vitro, the addition of Pin1 substantially increases phosphorylation of NF-H KSP repeats by proline-directed kinases, Erk1/2, Cdk5/p35, and JNK3 in a concentration-dependent manner. In vivo, dominant-negative Pin1 and Pin1 small interfering RNA inhibit epidermal growth factor-induced NF-H phosphorylation
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-
?
additional information
?
-
-
incorporation of the HCV polymerase into the replication complex depends on its interaction with a cellular chaperone protein, cyclosporine inhibits HCV replication by blocking this critical interaction and the PPIase activity of CyPA, modeling of the pathway, overview. CyPA is associated with CRC-incorporated HCV replicase in a cyclosporine-sensitive manner
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?
additional information
?
-
-
Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
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-
?
additional information
?
-
-
Pin1 enhances Plk1-mediated phosphorylation of the centrosome protein Cep55, overview
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-
?
additional information
?
-
-
Pin1 interacts with human T-cell leukemia virus type 1 Tax, phosphorylated at Ser258, and modulates its activation of NF-kappaB. Pin1 contributes to Tax signaling through NF-kappaB, and it cooperates with Tax to enhance cellular proliferation
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-
?
additional information
?
-
-
Pin1 interacts with NF-kappaB via its WW domain
-
-
?
additional information
?
-
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins from cis to trans, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, that produce the phosphorylated substrates of the isomerase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, regulation, overview
-
-
?
additional information
?
-
-
prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways
-
-
?
additional information
?
-
-
promyelocytic leukemia protein, PML, and silencing mediator for retinoic acid and thyroid hormone receptor, SMRT, are Pin1 substrates
-
-
?
additional information
?
-
-
Pin1 can stimulate proteins phosphorylation, e.g. of the RNA polymerase II CTD domain, but it can also inhibit protein dephosphorylation, e.g. of NFAT transcription factor or calcineurin. Pin1 interacts with neuronal cytoskeleton proteins such as tau, amyloid-beta protein precursor, alpha-synuclein, and with neurofilaments
-
-
?
additional information
?
-
-
Pin1 inhibits the dephosphorylation of NF by PP2A in vitro
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
-
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
?
additional information
?
-
-
Pin1 specifically recognizes the phosphorylated serine/threonine residue followed by proline. Pin1 binds preferentially to the phosphorylated Ser16-Pro17 motif of the capsid core of the human immunodeficiency virus type 1
-
-
?
additional information
?
-
Pin1 is a peptidyl-prolyl isomerase (PPIase), that catalyzes the cis-trans isomerization of pSer/pThr-Pro substrates in vivo and in vitro
-
-
?
additional information
?
-
-
the enzyme is not essential for Legionella pneumophila although the Cyp18-negative mutant strain is less infective for Acanthamoeba castellanii
-
-
?
additional information
?
-
-
the IF domain is a novel-folding motif and exposes a hydrophobic surface, which is considered to play an important role in the chaperone-like activity
-
?
additional information
?
-
-
the enzyme is involved in cell cycle progression
-
?
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
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-
?
additional information
?
-
-
Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
-
-
?
additional information
?
-
-
neither the active domain nor the intact protein can catalyze the cis/trans isomerization of the tripeptide Ala-Pro-Phe, less than 5% of the activity with succinyl-Ala-Ala-Pro-Phe-p-nitroanilide is observed with: succinyl-Ala-Gly-Pro-Phe-p-nitroanilide, succinyl-Ala-Lys-Pro-Phe-p-nitroanilide, succinyl-Ala-Glu-Pro-Phe-p-nitroanilide. The organism is devoid of all known peptidyl-prolyl cis/trans isomerases except the trigger factor. The trigger factor shows dual function as chaperone and prolyl isomerase
-
?
additional information
?
-
-
the trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
additional information
?
-
-
protein is not involved in binding to macrophages and does not impair the ability of macrophages to phagocytose the gonococci
-
-
?
additional information
?
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Val-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
no activity with Ala-Ala-(cis)-Pro-Phe, Ala-Gly-(cis)-Pro-Phe, Ala-Val-(cis)-Pro-Phe, Ala-Phe-(cis)-Pro-Phe, Ala-Trp-(cis)-Pro-Phe, Ala-His-(cis)-Pro-Phe and Ala-Lys-(cis)-Pro-Phe
-
?
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
-
-
?
additional information
?
-
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
?
additional information
?
-
-
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
?
additional information
?
-
-
enzyme inhibits the phosphatase activity of calcineurin independently of FK506 binding. Enzyme also inhibits thermal aggregation of two model substrates indicating chaperone proterties
-
-
?
additional information
?
-
PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview
-
-
?
additional information
?
-
-
PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview
-
-
?
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
additional information
?
-
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins from cis to trans, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, that produce the phosphorylated substrates of the isomerase, and with protein phosphatases, such as protein phosphatase 1A and 2B, in a wide range of cellular processes including cell division, DNA damage response, and gene transcription, and in susceptibilty to cancer and neurogenerative diseases, regulation, overview
-
-
?
additional information
?
-
-
prolyl isomerase Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. Pin1 can directly modulate the NF dephosphorylation mediated by PP2A, independent of JNK, extracellular signal-regulated kinase, and Cdk5 pathways
-
-
?
additional information
?
-
-
Pin1 can stimulate proteins phosphorylation, e.g. of the RNA polymerase II CTD domain, but it can also inhibit protein dephosphorylation, e.g. of NFAT transcription factor or calcineurin. Pin1 interacts with neuronal cytoskeleton proteins such as tau, amyloid-beta protein precursor, alpha-synuclein, and with neurofilaments
-
-
?
additional information
?
-
-
Pin1 inhibits the dephosphorylation of NF by PP2A in vitro
-
-
?
additional information
?
-
-
cyclophilin A and Ess1 function in parallel pathways and act on common targets by a mechanism that requires prolyl isomerization. One of these targets is the Sin3-Rdp3 histone deacetylase complex. Cyclophilin A increases and Ess1 decreases disruption of gene silencing by this complex. Ess1 and cyclophilin A modulate the activity of the Sin3-Rdp3 complex, and excess histone deacetylation causes mitotic arrest in ess1 mutants
-
?
additional information
?
-
-
the peptidylprolyl isomerase activity of cyclophilin A promotes proper subcellular localization of Zpr1p. Zpr1p is an essential zinc-finger-containing protein that translocates to the nucleus in response to groth stimuli
-
?
additional information
?
-
-
Fpr4 mediates cis-trans conversion of proline residues within histone tails, Pro16 and Pro30 of histone H3 are the major proline targets of Fpr4, with little activity against Pro38, mechanistic importance of substrate residues C-terminal to the peptidylprolyl bond
-
-
?
additional information
?
-
-
proline isomerization of histone peptides by Fpr4(280-392)
-
-
?
additional information
?
-
-
enzyme enhances the refolding of urea-denatured ribonuclease A
-
-
?
additional information
?
-
-
enzyme increases refolding of denatured type III collagen
-
-
?
additional information
?
-
-
catalyzes slow steps in the refolding of a number of proteins. The efficiency of catalysis depends on the accessibility for the isomerase of the particular proline peptide bonds in the refolding protein chain
-
-
?
additional information
?
-
-
increases refolding of cytochrome c and RNAase T1
-
-
?
additional information
?
-
-
isomerase activity of peptidylprolyl isomerase is independent of the chaperone activity. The proper molar ratio is important for the chaperone activity. The cysteine residues of peptidylprolyl isomerase may be a peptide binding site, and may be an essential group for the chaperone function
-
?
additional information
?
-
-
the enzyme is essential for protein folding during protein synthesis and may be involved in events, such as those occuring early in T-cell activation
-
-
?
additional information
?
-
-
the enzyme shows chaperone-like protein refolding activity in addition to peptidylprolyl isomerase
-
?
additional information
?
-
-
cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins.The enzyme might be important at growth temperatures lower than the optimum in Thermococcus sp. KS-1
-
?
additional information
?
-
-
the enzyme shows chaperone-like protein refolding activity in addition to peptidylprolyl isomerase
-
?
additional information
?
-
-
cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins.The enzyme might be important at growth temperatures lower than the optimum in Thermococcus sp. KS-1
-
?
additional information
?
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
peptide substrates derived from ribosomal proteins S2 and S3 display a dual binding mode with both a high- and a low-affinity binding site. Peptide TRYWNPKMKPFIFGA from protein S2 binds to both the insert-in-flap and FK506-binding domains
-
-
?
additional information
?
-
Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds
-
-
?
additional information
?
-
-
Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
-
?
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
