Information on EC 5.2.1.8 - Peptidylprolyl isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
5.2.1.8
-
RECOMMENDED NAME
GeneOntology No.
Peptidylprolyl isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
the refolding mechanism is similar in the presence and absence of the enzyme
-
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
mechanism that involves distortion of bound substrate with a twisted, 90 , peptidyl-propyl amide bond
-
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
covalent mechanism which involves an approximately tetravalent carbon of the prolyl imidic bond for the transition state of reaction
-
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
simple twisted amide transition state catalytic mechanism, modeling, overview. The serine carbonyl does not rehybridize from sp2 to sp3 in the rate-determining step, ruling out a nucleophilic addition mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cis-trans-isomerization
-
-
cis-trans-isomerization
-
-
cis-trans-isomerization
-
-
cis-trans-isomerization
B8XP93
-
cis-trans-isomerization
Escherichia coli AB2847
-
-
-
rotation
-
-
single bond
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
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
-
-
-
-
CeCYP-16
Q7KFC0
-
CGI-124
-
-
-
-
Chl-Mip
-
-
-
-
Cj0596
Campylobacter jejuni 81-176
-
-
-
CPH
-
-
-
-
Cyclophilin
-
-
-
-
Cyclophilin
-
-
Cyclophilin
-
-
Cyclophilin
O43447, P23284, P30405, P45877, P62937, Q08752, Q13427, Q6UX04, Q9UNP9
-
Cyclophilin 18
-
-
-
-
cyclophilin 3
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
-
-
-
-
Cyclophilin A
-
-
Cyclophilin A
-
-
Cyclophilin A
-
-
Cyclophilin B
-
-
-
-
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-40
-
-
-
-
CYP-S1
-
-
-
-
Cyp1
Q40672
-
Cyp18
-
-
Cyp2
Q40673
-
CYP20-2
Q9SCY2
i.e. cyclophilin 20-2
CYP20-3
Q9SCY2
i.e. cyclophilin 20-3
Cyp3 PPIase
-
-
-
-
Cyp40
-
-
CyPA
-
-
-
-
CyPB
-
-
-
-
CyPJ
-
-
EF0685
Q837Y9
gene name
EF1534
Q834U8
gene name
EF2898
Q82ZZ9
gene name
Estrogen receptor binding cyclophilin
-
-
-
-
FF1 antigen
-
-
-
-
FK506 binding protein 12
-
-
FK506 binding protein 35
A5K8X6
-
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
-
-
-
-
FKBP13
Q9SCY2
i.e. FK506-binding protein 13
FKBP1B
-
-
FKBP22
-
-
-
-
FKBP22
Q9NWM8
-
FKBP33
Halobacterium salinarum DSM 669
Q9P9H4
-
-
FKBP38
-
-
FKBP51
-
-
FKBP52
-
-
FKBP52 protein
-
-
-
-
FKBP54
-
-
-
-
FKBP59
-
-
-
-
FKBP65
-
-
-
-
FKBP65RS
-
-
-
-
FkpA
Escherichia coli AB2847
-
-
-
h Par14
-
-
HBI
-
-
-
-
HcCYP
Q4G338
-
hCyP33
-
-
Histidine rich protein
-
-
-
-
hPar14
-
-
-
-
hPar14
-
-
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
-
-
-
-
MtFK
Methanothermococcus thermolithotrophicus DSM2095
O52980
-
-
mzFKBP-66
-
-
NIMA-1
Q13526
-
Nucleolar proline isomerase
-
-
-
-
OvCYP-16
Q8IA80
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par10
P0A9L5
-
Par14
-
-
-
-
Par27
P40415
-
Par45
B8XP93
-
Parvulin
-
-
-
-
Parvulin
-
-
Parvulin 14
-
-
-
-
parvulin-like protein
Q9ZCX6
-
parvulin-type peptidyl-prolyl isomerase
Q4KNC9
-
parvulin-type peptidyl-prolyl isomerase
Gossypium hirsutum ZM3
Q4KNC9
-
-
parvulin1 4
-
-
pCYP B
-
-
Peptide bond isomerase
-
-
-
-
peptidyl prolyl cis-trans isomerase
-
-
peptidyl prolyl cis-trans isomerase
Campylobacter jejuni 81-176
-
-
-
peptidyl prolyl isomerase-like protein 1
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
-
-
Peptidyl-prolyl cis-trans isomerase
Q9FJL3
-
Peptidyl-prolyl cis-trans isomerase
-
-
Peptidyl-prolyl cis-trans isomerase
Bacillus subtilis IH8478
-
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
Peptidyl-prolyl cis-trans isomerase
Q9NWM8
-
Peptidyl-prolyl cis-trans isomerase
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
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
Q4KNC9
-
peptidyl-prolyl cis/trans isomerase
Gossypium hirsutum ZM3
Q4KNC9
-
-
peptidyl-prolyl cis/trans isomerase
-
-
peptidyl-prolyl cis/trans isomerase
B8XP93
-
Peptidyl-prolyl cis/trans isomerase EPVH
-
-
-
-
peptidyl-prolyl cis/trans isomerase NIMA-interacting 1
-
-
peptidyl-prolyl isomerase
Q9SCY2
-
peptidyl-prolyl isomerase
-
-
peptidyl-prolyl isomerase
-
-
peptidyl-prolyl isomerase
Escherichia coli B/E1
-
-
-
peptidyl-prolyl isomerase
O43447, P23284, P30405, P45877, P62937, Q08752, Q13427, Q6UX04, Q9UNP9
-
peptidyl-prolyl isomerase
-
-
peptidyl-prolyl isomerase
-
-
peptidyl-prolyl isomerase
O42123
-
peptidyl-prolyl isomerase
-
-
peptidyl-prolyl isomerase
O42123
-
peptidyl-prolyl isomerase 1
-
-
peptidylproline cis-trans-isomerase
-
-
peptidylprolyl cis,trans-isomerase
-
-
Peptidylprolyl cis-trans isomerase
-
-
-
-
Peptidylprolyl cis-trans isomerase
A5K8X6
-
peptidylprolyl cis/trans isomerase
Q82ZZ9, Q834U8, Q837Y9
-
peptidylprolyl isomerase
B2LU30
-
peptidylprolyl isomerase
-
-
PfCyP
-
-
-
-
Pin1
-
i.e. protein interacting with NIMA
Pin1
Q13526
-
Pin1
-
i.e. protein interacting with NIMA
PIN1-type parvulin 1
-
-
Planta-induced rust protein 28
-
-
-
-
PP2A phosphatase activator
-
-
PpiA
P62937
peptidyl-prolyl isomerase domain
PPIase
-
-
-
-
PPIase
Q9SCY2
-
PPIase
Bacillus subtilis IH8478
-
-
-
PPIase
B2LU30
-
PPIase
Q82ZZ9, Q834U8, Q837Y9
-
PPIase
Escherichia coli AB2847
-
-
-
PPIase
Q4KNC9
-
PPIase
Gossypium hirsutum ZM3
Q4KNC9
-
-
PPIase
Halobacterium salinarum DSM 669
Q9P9H4
-
-
PPIase
O43447, P23284, P30405, P45877, P62937, Q08752, Q13427, Q6UX04, Q9UNP9
-
PPIase
-
-
PPIase
O42123
-
PPIase
B8XP93
-
PPIase
O42123
-
PPIase Pin1
-
-
-
-
PPIase Pin4
-
-
-
-
PpiB
B2LU30
-
PpiB
P23284
peptidyl-prolyl isomerase domain
PPIC
P45877
peptidyl-prolyl isomerase domain
PpiD
Q08752
peptidyl-prolyl isomerase domain
PPIE
Q9UNP9
peptidyl-prolyl isomerase domain
PPIF
P30405
peptidyl-prolyl isomerase domain
PPIG
Q13427
peptidyl-prolyl isomerase domain
PPIH
O43447
peptidyl-prolyl isomerase domain
PPIL1
-
-
PPWD1
-
-
Proline rotamase
-
-
-
-
prolyl cis-trans isomerase
-
-
prolyl cis-trans isomerase
Escherichia coli AB2847
-
-
-
prolyl-peptidyl isomerase
-
-
protein phosphatase 2A phosphatase activator
-
-
Proteins, cyclophilins
-
-
-
-
Proteins, specific or class, cyclophilins
-
-
-
-
PrsA
Bacillus subtilis IH8478
-
-
-
PvFKBP35
A5K8X6
-
Rapamycin-binding protein
-
-
-
-
Rapamycin-selective 25 kDa immunophilin
-
-
-
-
ROF2
Q9FJL3
gene name
Rotamase
-
-
-
-
Rotamase
P34790
-
Rotamase
-
-
Rotamase Pin1
-
-
-
-
Rotamase Pin4
-
-
-
-
Rotamase plp
-
-
-
-
S-cyclophilin
-
-
-
-
S1205-06
-
-
-
-
SCYLP
-
-
-
-
SDCCAG-10
P30405
peptidyl-prolyl isomerase domain
SDCCAG-10
Q6UX04
-
SLyD
Escherichia coli B/E1
-
-
-
SmCYP A
-
-
-
-
SmCYP B
-
-
-
-
Smp17.7
-
-
-
-
SP18
-
-
-
-
TcFKBP18
-
-
trigger factor
-
-
trigger factor
-
-
trigger factor
-
-
WHP
-
-
-
-
mip-like peptidyl-prolyl cis-trans isomerase
-
-
additional information
B2LU30
PPIB contains conserved and unique cyclophilin domain and belongs to cyclophilin superfamily
additional information
-
the enzyme belongs to the CyP family of proteins
additional information
-
the enzyme belongs to the parvulin family of PPIases
additional information
O42123
the enzyme is a member of the FKBP family
CAS REGISTRY NUMBER
COMMENTARY
95076-93-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cyclophilin CYP20-3
SwissProt
Manually annotated by BRENDA team
gene ROF2
UniProt
Manually annotated by BRENDA team
ROC1, cytosolic enzyme; two genes encoding CypP: ROC1 and ROC4
Swissprot
Manually annotated by BRENDA team
ROC4, chloroplastic enzyme; two genes encoding CypP: ROC1 and ROC4
SwissProt
Manually annotated by BRENDA team
Bacillus subtilis IH8478
-
-
-
Manually annotated by BRENDA team
gene PPIB
UniProt
Manually annotated by BRENDA team
Par27 belongs to parvulin family
UniProt
Manually annotated by BRENDA team
the organism expressed 18 cyclophilin isoforms, eight of which are conserved single domain forms, comprising two closely related secreted or type B forms, CYP-5 and CYP-6
Uniprot
Manually annotated by BRENDA team
strain 81-176, gene cj0596
-
-
Manually annotated by BRENDA team
Campylobacter jejuni 81-176
strain 81-176, gene cj0596
-
-
Manually annotated by BRENDA team
cyclophilin A
UniProt
Manually annotated by BRENDA team
gene ef0685
UniProt
Manually annotated by BRENDA team
gene ef1534
UniProt
Manually annotated by BRENDA team
gene ef2898
UniProt
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
-
-
Manually annotated by BRENDA team
2 distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments
-
-
Manually annotated by BRENDA team
isoform Par10
Swissprot
Manually annotated by BRENDA team
isoform PpiD
-
-
Manually annotated by BRENDA team
isoform SlyD
-
-
Manually annotated by BRENDA team
isoforms FkpA, PpiA, PpiD, SurA
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
Escherichia coli AB2847
-
-
-
Manually annotated by BRENDA team
Escherichia coli B/E1
-
-
-
Manually annotated by BRENDA team
Gossypium hirsutum ZM3
-
UniProt
Manually annotated by BRENDA team
isoform cyclophilin A
UniProt
Manually annotated by BRENDA team
isoform cyclophilin B
UniProt
Manually annotated by BRENDA team
Halobacterium salinarum DSM 669
-
UniProt
Manually annotated by BRENDA team
; isoform cyclophilin J
Swissprot
Manually annotated by BRENDA team
cyclophilin A
UniProt
Manually annotated by BRENDA team
cyclophilin B, is critical for the efficient replication of the hepatitis C virus genome
-
-
Manually annotated by BRENDA team
gene FKBP14 encodes enzyme FKBP22
SwissProt
Manually annotated by BRENDA team
isoform cyclophilin A
-
-
Manually annotated by BRENDA team
isoform cyclophilin B
-
-
Manually annotated by BRENDA team
isoform cyclophilin Cyp-18
-
-
Manually annotated by BRENDA team
isoform cyclophorin A
-
-
Manually annotated by BRENDA team
isoform CypA is necessary for the prolactin-induced activation of Janus-activated kinase 2 and the progression of human breast cancer
-
-
Manually annotated by BRENDA team
isoform FKBP
-
-
Manually annotated by BRENDA team
isoform FKBP12
Uniprot
Manually annotated by BRENDA team
isoform FKBP12, recombinant protein
-
-
Manually annotated by BRENDA team
isoform FKBP38
Uniprot
Manually annotated by BRENDA team
isoform Pin1
-
-
Manually annotated by BRENDA team
isoform Pin1, recombinant enzyme
-
-
Manually annotated by BRENDA team
isoform PPIL1
-
-
Manually annotated by BRENDA team
isoform PPIL1
Uniprot
Manually annotated by BRENDA team
peptidylprolyl isomerase containing WD40 repeat
Uniprot
Manually annotated by BRENDA team
recombinant protein, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q
-
-
Manually annotated by BRENDA team
isoform Mip, FK506-binding protein
-
-
Manually annotated by BRENDA team
Methanothermococcus thermolithotrophicus DSM2095
DSM2095
SwissProt
Manually annotated by BRENDA team
immature female mice, isoform Pin1
SwissProt
Manually annotated by BRENDA team
male C57BJ/6J mice
-
-
Manually annotated by BRENDA team
wild type and and isoform Pin1-/- mice
-
-
Manually annotated by BRENDA team
soluble expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
soluble expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
isoform cyclophilin A
Uniprot
Manually annotated by BRENDA team
recombinant wild-type enzyme and a His-tagged version
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mRNA
SwissProt
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
isoform RcCyp1
UniProt
Manually annotated by BRENDA team
GenBank
SwissProt
Manually annotated by BRENDA team
3 molecular forms: PPI-I, PPI-II, and PPI-III
-
-
Manually annotated by BRENDA team
isoforms Ypa1, Ypa2; isoform Ypa1
-
-
Manually annotated by BRENDA team
strains C5 and SL1344, genes surA and fkpA. SurA can functionally compensate for the absence of FkpA, but when SurA is missing, or especially when both SurA and FkpA are missing, the ability of cells to survive or recover from prolonged periods of C-starvation is significantly impaired
-
-
Manually annotated by BRENDA team
cyclophilin A
SwissProt
Manually annotated by BRENDA team
enzyme form SmCYP A and SmCYP B. SmCYP B is the major schistosomal enzyme form
-
-
Manually annotated by BRENDA team
study on enzyme activity in drought tolerant and drought susceptible cultivars. In drought tolerant cultivars, significant water stress increases leaf enzyme activity, whereas in drought-susceptible cultivar enzyme activity decreases in response to drought
-
-
Manually annotated by BRENDA team
isoform PIN1, parvulin-type, present in both dividing and non-dividing forms
SwissProt
Manually annotated by BRENDA team
FKBP12
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Q9FJL3
ROF2 encodes a peptidyl-prolyl cis-trans isomerase of the FK506-binding protein class
evolution
-
the enzyme belongs to the FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases, PPIases, which share a canonical domain fold consisting of a beta-sheet composed of four large and two small -strands, opposed by a single main alpha-helix
evolution
Q9NWM8
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
evolution
Q4KNC9
the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
evolution
Gossypium hirsutum ZM3
-
the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases
-
malfunction
-
Pin1 blockade leads to Bax cleavage, mitochondrial translocation and caspase 9 and 3 activation, irrespective of the presence of cytokines, and Pin1 blockade accelerates eosinophil apoptosis
malfunction
-
Pin1 is deregulated in many tumors
malfunction
-
Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
malfunction
-
Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
malfunction
-
knockdown of FKBP1B induces eye formation malfunction
malfunction
-
knockdown of Pin1 does not prevent CK2alpha phosphorylation
malfunction
-
Pin1 depletion is linked to a dysfunction of uncoating of human immunodeficiency virus type 1
malfunction
-
Pin1 knock-out mice exhibit impaired insulin signaling with glucose intolerance. Pin1 knock-out mice are resistant to diet-induced obesity
malfunction
-
silencing of Pin1 expression results in decrease of hepatitis C virus replication in both hepatitis C virus replicon cells and cell culture grown hepatitis C virus-infected cells
malfunction
-
a DELTAef0685/DELTAef1534 mutant is more resistant to oxidative stress, is able to grow under a high manganese concentration, and shows altered resistance to ampicillin and quinolone antibiotics
malfunction
Q9FJL3
loss of function of ROF2, and especially double mutation of ROF2 and the closely related gene ROF1, results in acid sensitivity, stress and development phenotypes of ROF mutants, overview
physiological function
-
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. The Ser/Thr-Pro motifs are important for Pin1At function in promoting flowering through AGL24 and SOC1. Phosphorylation-dependent prolyl cis/trans isomerization of key transcription factors is an important flowering regulatory mechanism, overview
physiological function
-
Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
physiological function
-
cyclophilin A is an essential cofactor for hepatitis C virus infection and the intracellular target of cyclosporines anti-HCV effect, mechanism by which CyPA facilitates HCV replication, overview
physiological function
O42123
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
-
peptidyl-prolyl isomerase, Pin1, is a critical regulator of NF-kappaB activation facilitating NF-kappaB binding in hepatocytes and protects against hepatic ischemia/reperfusion injury. Pin1 is required for full production of MIP-2, but not for production of TNFalpha
physiological function
B2LU30
peptidylprolyl isomerases play essential roles in protein folding and are implicated in immune response and cell cycle control. Bombyx mori PPIases may be involved in anti-Bombyx mori nucleopolyhedrovirus response, mechanism, overview
physiological function
-
Pin1 is a key mediator of pro-survival signaling and a regulator of the pro-apoptotic Bcl-2-associated X protein, Bax, function. Pin1 likely functions as a downstream effector of GM-CSF and IL-5 signaling, and regulates cell death through the intrinsic, mitochondria- and caspase 9-dependent, apoptotic pathway, overview
physiological function
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, 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 susceptibility to cancer and neurogenerative diseases, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 mediates the neural-specific apoptosis machinery. Pin1 is involved in regulation of SMRT levels. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
-
Pin1 is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-serine/threonine-proline motifs of its target proteins, it functions in concert with proline directed kinases, such as cyclin-dependent protein kinases, extracellular signal-regulated kinases, and c-Jun N-terminal kinase, 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, detailed overview. Pin1 modulates excitotoxic and oxidative stress induced by perkaryal phosphorylation of NF-H. Pin1 is involved in regulation of SMRT levels. Pin1 mediates the neural-specific apoptosis machinery. Pin1 plays a post-phosphorylation role in regulating protein function, mechanisms, overview
physiological function
-
Pin1 is critical for the regulation of serine/threonine protein kinase B, PKB/Akt, stability and activation phosphorylation at S473 through the phosphorylated Thr-Pro motifs of Akt. Roles of Akt and Pin1 in oncogenesis, overview
physiological function
-
Pin1 markedly enhances transformation in primary lymphocytes by the c-Rel protein and by viral Rel/NF-kappaB oncoprotein v-Rel, it enhances the nuclear translocation of the Rel proteins, overview
physiological function
-
Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylation-dependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
-
Pin1 recognizes and induces cis-trans isomerization of pSer/Thr-Pro bonds, conferring phosphorylationdependent conformational changes relevant for protein function. In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis, signaling role of PP2A by Pin1, overview
physiological function
-
Pin1 regulates the function and/or stability of phosphoproteins by altering the conformation of specific pSer/pThr-Pro peptide bonds
physiological function
-
SurA may function to repair, or prevent damage to, the outer membrane upon exposure to PmB and may consequently limit damage to the inner-membrane
physiological function
-
the Pin1 is located in the midbody ring in HeLa cells and regulates cell cycle progression and cytokinesis through centrosome protein Cep55, which is an essential component of the midbody ring
physiological function
-
colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
physiological function
B8XP93
Par45 is a phosphorylation-independent parvulin required for normal cell proliferation in a unicellular eukaryotic cell
physiological function
-
peptidyl-prolyl isomerase Pin1 is required for CK2alpha mitotic spindle localization. Pin1 protects CK2alpha from dephosphorylation in vivo
physiological function
-
peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
physiological function
-
Pin1 is a host factor for hepatitis C virus propagation and may contribute to hepatitis C virus-induced liver pathogenesis. Both binding and isomerase activities of Pin1 are essential for hepatitis C virus replication
physiological function
-
Pin1 plays a critical role in adipose differentiation. Pin1 binds to IRS-1 and thereby markedly enhances insulin action, essential for adipogenesis
physiological function
-
Pin1 prolyl isomerase activity is required for the disassembly of the human immunodeficiency virus type 1 core
physiological function
-
PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
physiological function
-
Xenopus peptidyl-prolyl cis-trans isomerase FKBP1B induces ectopic secondary axis and is involved in eye formation during Xenopus embryogenesis
physiological function
-
Fpr4 has been described as a histone chaperone, and is implicated in epigenetic function in part due to its mediation of cis-trans conversion of proline residues within histone tails
physiological function
Q9FJL3
peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis. As ROF2 induction and intracellular acidification are common consequences of many stresses, this mechanism of pH homeostasis may be of general importance for stress tolerance. Chaperone ROF2 not only helps to refold proteins but also activates H+ extrusion to restore intracellular pH
physiological function
-
peptidyl-prolyl isomerase activity of FKBP12 is essential for prevention of aggregation of tau, an Alzheimer's disease-related protein. Tau aggregates into neurofibrillary tangles when it is hyperphosphorylated, only the cis-isomer can aggregate. FKBP12 catalyzes isomerization of the tau R3 peptide peptide in both the monomeric and aggregative states, once the cis-isomer is converted into the trans-isomer in the aggregative state, the trans-isomer is quickly released from the aggregation because the trans-isomer cannot aggregate, inhibitory mechanism of R3 peptide aggregation by simple binding of FKBP12, overview. IC50 of FKBP12 is 0.003 mM. The aggregation inhibitory activity of FKBP12 is independent of the affinity between FKBP12 and the R3 peptide. Therefore, the aggregation inhibitory activity of FKBP12 depends only on the PPIase activity of FKBP12
physiological function
-
peptidylprolyl cis/trans isomerases are enzymes involved in protein folding. The parvulin family rotamase EF0685 and the cyclophilin family member EF1534 are important for virulence and resistance to NaCl, while EF2898 is not important for the Enterococcus faecalis stress response or virulence
physiological function
Bacillus subtilis IH8478
-
PrsA catalyses the post-translocational folding of exported proteins and is essential for normal growth of Bacillus subtilis. PrsA is involved in the biosynthesis of the cylindrical lateral wall. PrsA is required for the folding of penicillin-binding protein 2a
-
physiological function
Escherichia coli B/E1
-
peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
-
physiological function
Campylobacter jejuni 81-176
-
Cj0596 plays a role in interaction with host cells. Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization
-
physiological function
Escherichia coli AB2847
-
colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
-
malfunction
Bacillus subtilis IH8478
-
Bacillus subtilis cells depleted of the PrsA protein are able to grow in the presence of a high concentration of magnesium (20 mM). PrsA depletion destabilizes penicillin-binding proteins
-
additional information
-
SurA and FkpA are not involved in the starvation-stress response, SSR. Genes surA and fkpA appear to be dispensable for the cross-resistance of carbon-starved cells to oxidative stress
additional information
-
active site Cys113
additional information
-
EF0685, EF1534, and EF2898 protein sequence comparisons, overview
additional information
-
length of helix alpha3 contributes significantly to the preservation of the structure, function, and stability of Escherichia coli FKBP22. Homology modeling of the three-dimensional enzyme structure, overview
additional information
Q9FJL3
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
-
the canonical FKBP catalytic domain actively increases the rate of isomerization of three decapeptides derived from the N-terminus of yeast histone H3, whereas maintaining intrinsic cis and trans populations. A notable feature of the FKBP catalytic domain is a prominent hydrophobic pocket that is thought to bind the proline. Specifically, Trp345 lies at the bottom of the hydrophobic pocket, with the additional residues Tyr313, Phe323, Phe332, Phe334, Val341, Ile342, Tyr368, and Phe384 forming the sides of the proline-binding cavity. The final residue, Asp324, provides a contrast to the largely hydrophic nature of the cavity. Asp324 along with the less-conserved Glu340 together comprise a small acidic region at the side of the hydrophobic pocket in Fpr4 that is otherwise surrounded by a large surface region enriched in positively charged amino acids
additional information
Q4KNC9
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
A5K8X6
Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview
additional information
Gossypium hirsutum ZM3
-
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
show the reaction diagram
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
show the reaction diagram
Escherichia coli, Escherichia coli AB2847
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
show the reaction diagram
Escherichia coli, Escherichia coli AB2847
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
show the reaction diagram
Escherichia coli, Escherichia coli AB2847
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
AGL24 protein
?
show the reaction diagram
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
Ala-Ala-(cis)-Pro-Ala
Ala-Ala-(trans)-Pro-Ala
show the reaction diagram
-
-
-
?
Ala-Ala-(trans)-Pro-Phe
Ala-Ala-(cis)-Pro-Phe
show the reaction diagram
-
-
-
r
Ala-Ala-Ala-(trans)-Pro-Phe
Ala-Ala-Ala-(cis)-Pro-Phe
show the reaction diagram
-
-
-
r
Ala-Gln-(cis)-Pro-Phe
Ala-Gln-(trans)-Pro-Phe
show the reaction diagram
Q8IA80
-
-
?
Ala-Gln-(cis)-Pro-Phe
Ala-Gln-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
Ala-Glu-(cis)-Pro-Phe
Ala-Glu-(trans)-Pro-Phe
show the reaction diagram
Q8IA80
-
-
?
Ala-Glu-(cis)-Pro-Phe
Ala-Glu-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Ala-Ile-(cis)-Pro-Phe
Ala-Ile-(trans)-Pro-Phe
show the reaction diagram
Q8IA80
-
-
?
Ala-Ile-(cis)-Pro-Phe
Ala-Ile-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
Ala-Leu-(cis)-Pro-Phe
Ala-Leu-(trans)-Pro-Phe
show the reaction diagram
Q8IA80
-
-
?
Ala-Leu-(cis)-Pro-Phe
Ala-Leu-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
Ala-Nle-(cis)-Pro-Phe
Ala-Nle-(trans)-Pro-Phe
show the reaction diagram
Q8IA80
-
-
?
Ala-Nle-(cis)-Pro-Phe
Ala-Nle-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
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
-
-
-
?
Ala-Val-(cis)-Pro-Phe
Ala-Val-(trans)-Pro-Phe
show the reaction diagram
Q7KFC0
-
-
?
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
-
?
cis-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
trans-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
show the reaction diagram
P62942
-
-
-
?
colicin M
?
show the reaction diagram
Escherichia coli, Escherichia coli AB2847
-
-
-
-
?
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
-
-
?
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Glutaryl-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Glutaryl-Ala-Ala-Ala-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Glutaryl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Glutaryl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Glutaryl-Ala-Pro-(cis)-Phe 4-nitroanilide
Glutaryl-Ala-Pro-(trans)-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
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, 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
show the reaction diagram
B8XP93
6.9% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
P9WHW3
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
Q9P9H4
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
P9WHW3
-
-
-
?
N-succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
Halobacterium salinarum DSM 669
Q9P9H4
-
-
-
?
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-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q96BP3
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
P82536
-
-
?
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-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-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
P52014
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
O52980
-
-
r
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
O49886
-
-
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q2I5R9
-
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
show the reaction diagram
Methanothermococcus thermolithotrophicus DSM2095
O52980
-
-
r
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
?
show the reaction diagram
Gossypium hirsutum, Gossypium hirsutum ZM3
Q4KNC9
-
-
-
?
N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
B8XP93
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
show the reaction diagram
B8XP93
7.6% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-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
Q2I5R9
-
ratio kcat to Km value is 397000 per M and s
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
B8XP93
26.7% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
N-succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
Halobacterium salinarum, Halobacterium salinarum DSM 669
Q9P9H4
-
-
-
?
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
Methanothermococcus thermolithotrophicus, Methanothermococcus thermolithotrophicus DSM2095
O52980
-
-
r
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
B8XP93
4.3% activity compared to N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
-
-
?
N-succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
-
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
P62937
computational study on protein dynamics, network of protein vibrations, comparison with structures from different species
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
-
solvent-assisted mechanism, H43 and Q52 are active sites
-
-
?
Phe-Phe-L-pSer-Pro-Arg-pNA
?
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, i.e. Bax
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
show the reaction diagram
-
-
-
-
?
protein tau
?
show the reaction diagram
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
reduced carboxymethylated bovine alpha-lactalbumin
reduced carboxymethylated bovine alpha-lactalbumin
show the reaction diagram
-
-
-
-
?
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
-
-
?
RNase A S-protein
RNase A S-protein
show the reaction diagram
-
partially folded
action of enzyme greatly reduces the population of aggregated oligomeric species
-
?
RNAse T1
?
show the reaction diagram
P40415
-
-
-
?
RNAse T1
?
show the reaction diagram
-
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
-
?
RNAse T1
?
show the reaction diagram
-
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
?
show the reaction diagram
-
reduced and carboxymethylated RNAse T1, refolding by trans to cis isomerization of peptidyl-prolyl bonds at Pro39 and Pro55
-
?
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
-
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
?
show the reaction diagram
-
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
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-Ala-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Ala-trans-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9SCY2
cis/trans-isomerization
-
-
?
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
-
-
-
-
?
Suc-Ala-Leu-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Leu-trans-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9SCY2
cis/trans-isomerization
-
-
?
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-Lys 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Lys 4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
?
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
Succinyl-Ala-Ala-(trans)-Pro-Phe 4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
Succinyl-Ala-Ala-(trans)-Pro-Phe 4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
Succinyl-Ala-Ala-(trans)-Pro-Phe 4-methylcoumarin 7-amide
show the reaction diagram
-
-
-
-
?
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
Succinyl-Ala-Ala-(trans)-Pro-Phe 4-methylcoumarin 7-amide
show the reaction diagram
-
-
trans
-
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q26548
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q8VX73
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
B2ZWT4, B2ZWT5
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
38% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
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-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
70fold decrease in activity compared with succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Arg-p-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Arg-p-nitroanilide
show the reaction diagram
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
r
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
O52980
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Arg-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
-
-
-
-
succinyl-Ala-Gln-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gln-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
-
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
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-(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
Q9ZCX6
11% of activity compared to succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
-
-
?
succinyl-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-7-amido-4-methylcoumarin
succinyl-Ala-Glu-(cis)-Pro-Phe-7-amido-4-methylcoumarin
show the reaction diagram
-
-
-
r
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-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
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
-
-
-
?
succinyl-Ala-Gly-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-His-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-His-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
r
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(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-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(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
O52980
-
-
-
-
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
Q4G338
-
-
-
?
succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Leu-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
67% of the activity with succinyl-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
-
-
?
succinyl-Ala-Leu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
r
succinyl-Ala-Leu-Pro(omega180)-Phe-4-nitroanilide
succinyl-Ala-Leu-Pro(omega0)-Phe-4-nitroanilide
show the reaction diagram
A5K8X6
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
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-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(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-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Lys-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
Q9ZCX6
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
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-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
Q5UP71
mimicyp lacks peptidyl-prolyl isomerase activity
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Phe-(cis)-Pro-Phe-p-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
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
show the reaction diagram
-
-
-
r
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Phe-Pro-Phe-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ser-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ser-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
-
-
-
-
succinyl-Ala-Val-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Val-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
Q9ZCX6
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
show the reaction diagram
-
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
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
-
-
-
-
?
VYKS-(cis)-PVVSGDTS-(cis)-PRHL
VYKS-(trans)-PVVSGDTS-(trans)-PRHL
show the reaction diagram
P40415
interconversion occurs at both P5 and P13
-
-
?
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
-
?
additional information
?
-
-
-
-
-
-
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 the refolding of type IV procollagen
-
-
-
additional information
?
-
-
catalyzes the refolding of type III collagen
-
-
-
additional information
?
-
-
increases refolding of cytochrome c and RNAase T1
-
-
-
additional information
?
-
-
catalyzes refolding of RNAase T1
-
-
-
additional information
?
-
-
catalyzes the refolding of thermally denatured type III collagen
-
-
-
additional information
?
-
-
substrate specificity of the 3 isoforms
-
-
-
additional information
?
-
-
cyclophilin B complexed to cyclosporin A inhibits phosphatase activity of recombinant human calcineurin
-
?
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
?
-
-
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
?
-
Q7KFC0
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
?
-
Q8IA80
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 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
?
-
-
only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity
-
?
additional information
?
-
P45523
the enzyme has peptidylprolyl isomerase activity and chaperone activity
-
?
additional information
?
-
-
the enzyme shows chaperone-like protein refolding activity in addition to peptidylprolyl isomerase
-
?
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 mechanism determining the substrate specificity seems to be different between hPAR14 and hPin1
-
?
additional information
?
-
-
the presence of cyclophilin A in the human immunodeficiency virus type 1, HIV-1, is required for HIV-1 to infect and replicate
-
-
-
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 functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
-
-
-
additional information
?
-
-
the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
-
-
-
additional information
?
-
-
the enzyme is not essential for Legionella pneumophila although the Cyp18-negative mutant strain is less infective for Acanthamoeba castellanii
-
-
-
additional information
?
-
P62937
cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
-
-
-
additional information
?
-
-
class3 cyclophilins are involved in cellular responses to stress caused by changes in redox environment or by upregulation of cellular activity
-
?
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
?
-
-
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
?
-
-
enzyme is required for cell cycle progression
-
?
additional information
?
-
-
expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
-
?
additional information
?
-
-
folding helper enzyme that plays a role in cell-cycle and chromatin remodeling
-
?
additional information
?
-
-
heat-stress-induced protein
-
?
additional information
?
-
P34790, P34791
not essential for protein import into chloroplast
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
?
-
Q13526
substrates are proteins involved in regulation of cell cycle, transcription, Alzheimers disease, and cancer pathogenesis
-
?
additional information
?
-
-
the enzyme is involved in cell cycle progression
-
?
additional information
?
-
-
the kinesin-related protein, KRMP1 is a mitotic target regulated by Pin1 and vice versa
-
?
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
?
-
-
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
?
-
-
the trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
additional information
?
-
-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
additional information
?
-
-
enzyme inibits the phosphatase activity of calcineurin independently of FK506 binding. Enzyme also inhibits thermal aggregation of two model substrates indicating chaperone proterties
-
-
-
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
-
-
-
additional information
?
-
-
protein is not involved in binding to macrophages and does not impair the ability of macrophages to phagocytose the gonococci
-
-
-
additional information
?
-
-
selective for substrate SRC-3, phosphorylated steroid receptor coactivator 3. Enzyme and SRC-3 synergistically activate nuclear-receptor-regulated transcription
-
-
-
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
-
-
-
additional information
?
-
Q9TTC6
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
-
additional information
?
-
P40415
isoform Par27 displays both prolyl-peptidyl isomerase and chaperone activities in vitro
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
Q9SCY2
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
-
additional information
?
-
O42123
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
?
-
-
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
-
-
-
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
?
-
-
Pin1 enhances Plk1-mediated phosphorylation of the centrosome protein Cep55, overview
-
-
-
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
-
-
-
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 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
?
-
-
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
?
-
-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
-
-
additional information
?
-
-
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
-
-
-
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
?
-
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
-
additional information
?
-
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporine
-
-
-
additional information
?
-
O43447, P23284, P30405, P45877, Q08752, Q13427, Q6UX04, Q9UNP9
cyclophilins catalyze the cis-trans-isomerization of pralines, cyclophilin activity against short peptides is correlated with an ability to ligate cyclosporin
-
-
-
additional information
?
-
B8XP93
Par45 does not accelerate the cis/trans interconversion of acidic substrates containing Glu-Pro bonds
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
peptidyl-prolyl cis-trans isomerase FKBP22 binds FK506 and rapamycin, that are both immunosuppressive drugs
-
-
-
additional information
?
-
A5K8X6
PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview
-
-
-
additional information
?
-
-
proline isomerization of histone peptides by Fpr4(280-392)
-
-
-
additional information
?
-
Gossypium hirsutum, Gossypium hirsutum ZM3
Q4KNC9
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
-
-
-
additional information
?
-
Campylobacter jejuni 81-176
-
Cj0596 has PPIase activity, cleavage of N-Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AGL24 protein
?
show the reaction diagram
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
amyloidbeta precursor protein
?
show the reaction diagram
-
interaction with Thr688
-
-
?
colicin M
?
show the reaction diagram
Escherichia coli, Escherichia coli AB2847
-
-
-
-
?
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
-
-
?
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
-
-
?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
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
-
-
?
serine/threonine protein kinase B
?
show the reaction diagram
-
-
-
-
?
SOC1 protein
?
show the reaction diagram
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
-
-
?
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
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the presence of cyclophilin A in the human immunodeficiency virus type 1, HIV-1, is required for HIV-1 to infect and replicate
-
-
-
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 functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
-
-
-
additional information
?
-
-
the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
-
-
-
additional information
?
-
-
the enzyme is not essential for Legionella pneumophila although the Cyp18-negative mutant strain is less infective for Acanthamoeba castellanii
-
-
-
additional information
?
-
P62937
cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
-
-
-
additional information
?
-
-
class3 cyclophilins are involved in cellular responses to stress caused by changes in redox environment or by upregulation of cellular activity
-
?
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
?
-
-
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
?
-
-
enzyme is required for cell cycle progression
-
?
additional information
?
-
-
expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
-
?
additional information
?
-
-
folding helper enzyme that plays a role in cell-cycle and chromatin remodeling
-
?
additional information
?
-
-
heat-stress-induced protein
-
?
additional information
?
-
P34790, P34791
not essential for protein import into chloroplast
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
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
?
-
Q13526
substrates are proteins involved in regulation of cell cycle, transcription, Alzheimers disease, and cancer pathogenesis
-
?
additional information
?
-
-
the enzyme is involved in cell cycle progression
-
?
additional information
?
-
-
the kinesin-related protein, KRMP1 is a mitotic target regulated by Pin1 and vice versa
-
?
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
?
-
-
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
?
-
-
the trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
-
?
additional information
?
-
-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
additional information
?
-
-
enzyme inibits the phosphatase activity of calcineurin independently of FK506 binding. Enzyme also inhibits thermal aggregation of two model substrates indicating chaperone proterties
-
-
-
additional information
?
-
-
general function of enzyme in binding of cargo for retrograde movement along microtubules
-
-
-
additional information
?
-
-
protein is not involved in binding to macrophages and does not impair the ability of macrophages to phagocytose the gonococci
-
-
-
additional information
?
-
-
selective for substrate SRC-3, phosphorylated steroid receptor coactivator 3. Enzyme and SRC-3 synergistically activate nuclear-receptor-regulated transcription
-
-
-
additional information
?
-
Q9TTC6
cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
-
-
-
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
-
-
-
additional information
?
-
Q9SCY2
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
-
additional information
?
-
O42123
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
?
-
-
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
-
-
-
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
?
-
-
Pin1 enhances Plk1-mediated phosphorylation of the centrosome protein Cep55, overview
-
-
-
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
-
-
-
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 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
?
-
-
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
?
-
-
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
?
-
-
Pin1 is a peptidyl-prolyl isomerase (PPIase), that catalyzes the cis-trans isomerization of pSer/pThr-Pro substrates in vivo and in vitro
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
stimulation
Mg2+
-
at least 3fold stimulation
Mg2+
-
at least 3fold stimulation; stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
-
(6,8aR)-6-N,N-monophenylimino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: above 0.2 mM
(6R,8a,R)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.017 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-acetyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.0015 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.047 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-indolizidine methyl ester
-
dissociation constant: 0.077 mM
(6R,8aR)-6-benzyl-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.14 mM
(6R,8aR)-6-benzyl-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.124 mM
(6R,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: 0.2 mM
(6S,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: above 0.2 mM
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
-
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
-
-
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
P62942
-
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
2,7-dimethylbenzo[lmn][3,8]phenanthroline-1,3,6,8(2H,7H)-tetrone
-
IC50: 0.002 mM
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
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
P62942
-
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
P62942
-
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 inhibition of wild-type and mutant C69A within 30 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-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
-
-
Ala-Pro
-
IC50: 30 mM
alpha-Lactalbumin
-
unfolded
-
ATP
-
at least 3fold stimulation, excess of ATP over Mg2+ is inhibitory
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
-
-
Cu2+
-
-
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
-
-
cyclolinopeptide A
-
interaction with several synthetic analogues cyclolinopeptide A
cyclosporin A
-
-
cyclosporin A
-
-
cyclosporin A
-
the combination of cyclosporin A or its analogues with other drugs, such as nucleotide analogues, e.g. 3'-azido-3'-deoxy-thymidine, or 2',3'-dideoxycytidine, HIV-1-protease inhibitors, and antibiotics, might provide long-term benefit to HIV-1-infected individuals
cyclosporin A
-
-
cyclosporin A
O52980
no inhibition by cyclosporins
cyclosporin A
-
-
cyclosporin A
-
the sequence MeLeu9-trans-MeLeu10-MeVal is responsible for the efficient binding in the active site of cyclophilin. The cis-conformer is inactive as inhibitor
cyclosporin A
-
and analogs
cyclosporin A
-
-
cyclosporin A
-
-
cyclosporin A
-
inhibits cytosolic and microsomal enzyme form
cyclosporin A
-
-
cyclosporin A
-
no inhibition
cyclosporin A
-
and analogs
cyclosporin A
P82536
-
cyclosporin A
-
-
cyclosporin A
-
inhibits the activity largely localized to the mitochondrial matrix
cyclosporin A
-
IC50: 16 nM
cyclosporin A
P52014
IC50: 50 nM
cyclosporin A
-
-
cyclosporin A
-
-
cyclosporin A
Q4G338
-
cyclosporin A
Q26548
-
cyclosporin A
-
-
cyclosporin A
Q9TTC6
and cyclosporin derivative with modifications in the D-Ser side chain. Inhibition leads to failure of polymerization of the extracellular multi-domain protein hensin, plus the loss of the apical cytoskeleton, apical microvilli, and the columnar epithelial shape of clone C cells
cyclosporin A
Q8VX73
almost complete inhibition
cyclosporin A
B2ZWT4, B2ZWT5
;
cyclosporin A
-
forms an inhibitory complex with cyclophilin. CyPA is a major intracellular target of cyclosporines
cyclosporin A
Q9SCY2
-
D-Ser(PO3H2)-Pro
-
1 mM, 20% inhibition
diethyl 1,3,8,10-tetrahydro-1,3,8,10-tetraoxoanthra[2,1,9-def:6,5,10-d'e'f']diisoquinoline-2,9-diacetate
-
IC50: 0.0015 mM
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
-
-
diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo[lmn][3,8]phenanthroline 2,7-diacetate
-
IC50: 0.0015 mM, inhibitor with the least non-specific toxicity
dipentamethylene thiuram monosulfide
-
-
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
-
only one of the 4 domains can be inhibited by the immunosuppressive drug
FK506
O52980
; IC50: 250 nM
FK506
-
IC50: 110 nM
FK506
-
50% inhibition at 0.00032 mM
FK506
A5K8X6
an immunosuppressive drug
FK506
-
binds at the catalytic domain
FK506
Q9FJL3
-
FK506
-
-
Hg2+
-
-
juglone
B0BNL2
pharmacological inhibitor of isoform Pin1, application of juglone partially prevents dephosphorylation of phosphoptotein Tau at Thr231
juglone
-
Pin1 inhibition leads to relocalization of endogenous c-Rel to the cytoplasm coincident with lymphoma cell death and/or growth inhibition
juglone
-
i.e. 5-hydroxy-1,4-naphthalenedione, from leaves, roots, and bark of plants of family Juglandaceae. The compound causes a partial unfolding of the PPIase active site
juglone
-
i.e. 5-hydroxy-1,4-naphthoquinone, selective and irreversible inhibition. Juglone reduces PPIase activity but does not alter Pin1 expression
juglone
-
i.e. 5-hydroxy-1,4-naphthoquinone, natural inhibitor of Pin1
lactalbumin
-
reduced and carboxymethylated, strong inhibition by the permanently unfolded protein
-
linear CRYPEVEIC
-
-
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
-
-
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
-
-
NEM
-
cytosolic enzyme form
non-folding vartiant of ribonuclease T1
-
that lacks Pro39
-
PCMB
-
-
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
Phenylglyoxal
-
cytosolic enzyme form
QAEGPK
Q96BP3
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
Rapamycin
-
inhibits the activity associated with the mitochondrial membranes
Rapamycin
-
50% inhibition at 0.00048 mM
Rapamycin
-
50% inhibition at 5 nM
Rapamycin
A5K8X6
an immunosuppressive drug
Rapamycin
-
binds at the catalytic domain
RNase T1
-
reduced and carboxymethylated form of the P39A variant, strong inhibition by the permanently unfolded protein
-
SDS
-
-
Ser(PO3H2)-Pro
-
; IC50: 2.0 mM
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
-
-
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
-
-
additional information
-
no inhibition: chlorotosylamidophenylbutane, diisopropylphosphorofluoridate
-
additional information
O52980
no inhibition by cyclosporine, even at 0.01 mM
-
additional information
-
Pin1 inhibitors may be used as a novel type of anticancer drug that acts by blocking cell cycle progression
-
additional information
P82536
no inhibition by FK506
-
additional information
Q7KFC0
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
Q8IA80
no inhibition by cyclosporin A even at 0.005 mM
-
additional information
-
cyclosporin A is not inhibitory up to 0.005 mM
-
additional information
Q4G338
not inhibitory: FK506
-
additional information
Q8VX73
not inhibitory: FK506
-
additional information
-
the OBOC peptide library screening for and selection of selected inhibitors containing a consensus motif of D-pThr-L-piperidine-2-carboxylic acid-L-2-naphthylalanine using inactive enzyme mutant S16A/Y23A, interaction analysis by Isothermal titration calorimetry, overview. A second generation of cell permeable Pin1 inhibitors, that have have antiproliferative activity against the cancer cells, is designed by replacing the noncritical residues within the cyclic peptide ring with arginine residues. Effects of inhibitor peptides in vivo on cancer cells, e.g. HeLa cells, overview
-
additional information
-
inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis
-
additional information
-
no inhibition by 3-[(2,5-dimethyl-1-benzofuran-3-yl)carbonyl]-4-hydroxybenzonitrile
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
stimulation
ATP
-
at least 3fold stimulation, excess of ATP over Mg2+ is inhibitory
ATP
-
at least 3fold stimulation, excess of ATP over Mg2+ is inhibitory; stimulation
equine chorionic gonadotropin
Q9QUR7
significant increase in expression of isoform Pin1 mRNA, application of human chorionic gonadotropin attenuates this increase. mRNA expression of E2F transcription factor, which controls the expression of Pin1, is decreased in the ovaries after treatment with equine chorionic gonadotropin. Protein level of Pin1 shows the same tendencies as the expression of RNA
-
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
LITERATURE
IMAGE
0.17
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant R68A/R69A, 0C, pH 7.5
0.31
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
wild-type, 0C, pH 7.5
0.37
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant C113D, 0C, pH 7.5
0.41
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant C113S, 0C, pH 7.5
0.00045
RNase T1
-
trigger factor
-
0.451
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
1.247
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.12
succinyl-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
-
-
0.585
succinyl-Ala-Lys-Pro-Phe 4-nitroanilide
-
-
0.788
succinyl-Ala-Lys-Pro-Phe 4-nitroanilide
-
-
0.53
Ala-Gly-PSI[CS-N]-Pro-Phe 4-nitroanilide
-
-
additional information
additional information
O49886
ratio of kcat/Km is 4600000 per s and M at 15C, pH 7.8
-
additional information
additional information
-
kinetic analysis of Pin1, overview
-
0.7
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant K63A, 0C, pH 7.5
additional information
RNase T1
P40415
ratio kcat/Km value of 43 per mM and s, pH 6.6
-
0.00065
RNase T1
-
disulfide-reduced and S-carboxymethylated form of a variant of Rnase T1 with Ser54Gly and Pro55Asn
-
additional information
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
Q8VX73
specificity constant kcat/Km for (His)6-RcCYP1 is 9.48 per microM and s
additional information
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
B2ZWT4, B2ZWT5
kcat/Km ratio is 14.1 per mM and s; kcat/Km ratio is 21 per mM and s
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.7
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant C113S, 0C, pH 7.5
11
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant K63A, 0C, pH 7.5
18
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant R68A/R69A, 0C, pH 7.5
29
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
mutant C113D, 0C, pH 7.5
140
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
-
wild-type, 0C, pH 7.5
0.45
RNase T1
-
disulfide-reduced and S-carboxymethylated form of a variant of Rnase T1 with Ser54Gly and Pro55Asn
-
0.006
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, mutant DELTA208-213
0.008
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, mutant DELTA208-213, presence of 1 mM MgATP
0.011
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, mutant D205G of Ypa1
0.016
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, mutant D205G of Ypa1, presence of 1 mM MgATP
0.03
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type
0.03
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type Ypa2
0.05
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type Ypa2, presence of 1 mM MgATP
0.1
succinyl-Ala-Ala-(cis)-Pro-Lys 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type, presence of 1 mM MgATP
0.02
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type Ypa1
0.03
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type
0.07
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type Ypa1, presence of 1 mM MgATP
0.19
Succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
-
20C, pH 7.4, wild-type, presence of 1 mM MgATP
1480
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
1820
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
14600
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
1060
succinyl-Ala-Lys-Pro-Phe 4-nitroanilide
-
-
additional information
additional information
-
-
-
additional information
additional information
P9WHW3
ratio of kcat/Km-value is 2,000,000 per M and s
-
additional information
additional information
-
ratio of kcat/Km-value is 410000 per M and s
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.11
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
mutant enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10C
166190
115
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10C
166190
96.9
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10C
166191
3.45
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
mutant enzyme G148D, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10C
166189
1380
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10C
166189
6.7
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
B8XP93
at 10 C in 35 mM sodium HEPES buffer, pH 7.8
55665
97.1
N-succinyl-Ala-Arg-(cis)-Pro-Phe-4-nitroanilide
B8XP93
at 10 C in 35 mM sodium HEPES buffer, pH 7.8
166188
7.4
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
B8XP93
at 10 C in 35 mM sodium HEPES buffer, pH 7.8
67173
25.9
N-succinyl-Ala-Leu-(cis)-Pro-Phe-4-nitroanilide
B8XP93
at 10 C in 35 mM sodium HEPES buffer, pH 7.8
55664
0.78
N-succinyl-Ala-Leu-(cis)-Pro-Phe-p-nitroanilide
Q9P9H4
pH 7.8, 15C
0
4.2
N-succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
B8XP93
at 10 C in 35 mM sodium HEPES buffer, pH 7.8
55666
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
0C, 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
-
-
0.0083
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
P62942
pH 8.0
0.03
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
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
P62942
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
P62942
pH 8.0
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
-
-
0.0000559
5-hydroxy-1,4-naphthoquinone
-
mutant enzyme C69A
0.258
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
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, 10C
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, 10C
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, 10C
0.0183
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.547
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
19
Ala-Pro
-
-
0.00005
alpha-Lactalbumin
-
unfolded alpha-lactalbumin
-
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
cyclic CRYPEVEIC
-
using Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22C
0.00052
cyclic 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 22C
0.0034
cycloheximide
-
-
0.0000039
cyclosporin A
-
-
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 22C
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
LITERATURE
IMAGE
0.0485
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
-
-
0.0092
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.01
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
-
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
-
pH and temperature not specified in the publication
0.0275
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.0079
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.002
2,7-dimethylbenzo[lmn][3,8]phenanthroline-1,3,6,8(2H,7H)-tetrone
-
IC50: 0.002 mM
0.0216
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
-
-
0.00088
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
-
-
0.00062
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
0.00069
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
0.00087
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
-
-
0.0009 - 4
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
-
-
0.0036
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
-
-
0.0223
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
-
-
0.0044
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
-
-
0.1
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
-
-
0.077
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
-
-
0.065
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
-
-
0.215
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
10C
1
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
8
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
-
pH 7.8, 10C
15
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
15
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, 10C
7
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.001
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.001 mM
0.085
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.085 mM
7
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
-
IC50: 7 mM
0.77
acetyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.77 mM
30
Ala-Pro
-
IC50: 30 mM
0.0011
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
-
-
0.3
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
-
above
0.063
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
-
-
0.000043
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
-
-
0.0011
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
-
-
0.00031
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
-
-
0.000032
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
-
-
0.0025
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
0.00022
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
-
-
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
above
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
-
above
0.00000265
cyclosporin A
-
-
0.000014
cyclosporin A
Q26548
10C, pH 7.9
0.000016
cyclosporin A
-
IC50: 16 nM
0.00005
cyclosporin A
P52014
IC50: 50 nM
0.0015
diethyl 1,3,8,10-tetrahydro-1,3,8,10-tetraoxoanthra[2,1,9-def:6,5,10-d'e'f']diisoquinoline-2,9-diacetate
-
IC50: 0.0015 mM
0.0015
diethyl-1,3,6,8-tetrahydro-1,3,6,8-tetraoxobenzo[lmn][3,8]phenanthroline 2,7-diacetate
-
IC50: 0.0015 mM, inhibitor with the least non-specific toxicity
0.00011
FK506
-
IC50: 110 nM
0.00025
FK506
O52980
IC50: 250 nM
0.0086
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
-
-
0.00059
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
-
-
0.00093
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
-
-
0.004
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.004 mM
0.097
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.097 mM
2
Ser(PO3H2)-Pro
-
IC50: 2.0 mM
0.54
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
10C
0.015
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
10C
14
succinyl-Ala-Ala-Pro-NH2
-
IC50: 14 mM
4.4
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
-
IC50: 4.4 mM
0.54
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.54 mM
5.8
succinyl-Ala-Pro-Phe-4-aminoanilide
-
IC50: 5.8 mM
0.7
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
-
IC50: 0.7 mM
0.17
succinyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.17 mM
1.09
succinyl-Pro-Phe-4-nitroanilide
-
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
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
additional information
-
-
additional information
-
-
additional information
O52980
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
WW module of enzyme can act as a negative regulator of enzymatic activity when multiple phosphorylation is present in substrates
additional information
P34791
the isomerization and disulfide-reduction activities are two independent functions of the enzyme that both are regulated by the redox state of the active centre. Dithiol-disulfide transitions have a regulatory role in protein function
additional information
Q26548
ratio kcat/Km is 11000000 per M and s
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6
-
assay at
7.8
-
assay at
7.8
Q9P9H4
assay at
8
Q4KNC9
assay at
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6.0: about 50% of maximal activity, pH 9.0: about 45% of maximal activity, no activity below pH 5.0 and above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
Q9P9H4
assay at
25
-
assay at
37
Q4KNC9
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.05
B2LU30
sequence calculation
8.1
P40415
calculated
8.3
B2ZWT4, B2ZWT5
calculated
8.7
Q6USC1
-
8.9
Q8VX73
calculated
9.1
B2ZWT4, B2ZWT5
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
neuronal cell line
Manually annotated by BRENDA team
-
foetal brain
Manually annotated by BRENDA team
-
comparative analysis of enzyme activities and mRNA level of Pin1 and other prolyl cis/trans isomerases
Manually annotated by BRENDA team
-
strong correlation between the expression levels of an oncogenic peptidyl-prolyl cis/trans isomerase Pin1 and levels of Akt phosphorylation at S473 and the Thr92-Pro and Thr450-Pro motifs in multiple cancer types, overview
Manually annotated by BRENDA team
-
the enzyme is upregulated in cancer cells
Manually annotated by BRENDA team
-
primary cortical culture
Manually annotated by BRENDA team
Q2I5R9
neither cell growth kinetics nor cell morphology are affected by the overexpression of Pin1
Manually annotated by BRENDA team
-
foetal brain
Manually annotated by BRENDA team
-
embryonic fibroblast,comparative analysis of enzyme activities and mRNA level of Pin1 and other prolyl cis/trans isomerases
Manually annotated by BRENDA team
P34790, P34791
ROC1 and ROC4
Manually annotated by BRENDA team
Q6USC1
highest expression level of mRNA, expression is inducible
Manually annotated by BRENDA team
Q6USC1
constitutive expression
Manually annotated by BRENDA team
-
a Hodkin's lymphoma cell line
Manually annotated by BRENDA team
-
a fibroblast cell line
Manually annotated by BRENDA team
Q40672, Q40673
expressed as a 1000 nt transcript in leaf and root
Manually annotated by BRENDA team
-
mRNA level is high,expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
Manually annotated by BRENDA team
P34790, P34791
ROC1 and ROC4
Manually annotated by BRENDA team
Q40672, Q40673
the enzyme is expressed as 800 nt and 900 nt transcripts. Whereas the 900 nt transcript is present in both root and leaf mRNA, the 800 nt transcript is only detectable in root mRNA
Manually annotated by BRENDA team
-
comparative analysis of enzyme activities and mRNA level of Pin1 and other prolyl cis/trans isomerases
Manually annotated by BRENDA team
-
comparative analysis of enzyme activities and mRNA level of Pin1 and other prolyl cis/trans isomerases
Manually annotated by BRENDA team
-
CD4+ lymphocyte. 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
-
breast cancer cell
Manually annotated by BRENDA team
B0BNL2
primary cortical neuron, enzyme isoform Pin1 partly colocalizes with phosphoprotein Tau,which is involved in Alzheimers disease
Manually annotated by BRENDA team
-
primary cortical, Pin1 is present in both axons and cell bodies
Manually annotated by BRENDA team
Q9QUR7
of mice treated with equine or human chorionic gonadotropin, eCG or hCG, resp.
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
Q8VX73
phloem translocation stream
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
Q40672, Q40673
expressed as a 1000 nt transcript in leaf and root
Manually annotated by BRENDA team
-
from germinated seeds
Manually annotated by BRENDA team
P34790, P34791
ROC1, no ROC4 mRNA detected
Manually annotated by BRENDA team
Q40672, Q40673
the enzyme is expressed as 800 nt and 900 nt transcripts. Whereas the 900 nt transcript is present in both root and leaf mRNA, the 800 nt transcript is only detectable in root mRNA
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
-
etiolated
Manually annotated by BRENDA team
-
comparative analysis of enzyme activities and mRNA level of Pin1 and other prolyl cis/trans isomerases
Manually annotated by BRENDA team
additional information
-
mRNA level for pCyP B is not detectable in root
Manually annotated by BRENDA team
additional information
P34790, P34791
no activity detected in root. ROC4 is expressed only in photosynthetic organs
Manually annotated by BRENDA team
additional information
P34790, P34791
ROC1 is expressed in all tested plant organs
Manually annotated by BRENDA team
additional information
Q8VX73
abundant protein in the companion cell sieve element complex
Manually annotated by BRENDA team
additional information
-
mRNA expression level is homogeneous in different tissues
Manually annotated by BRENDA team
additional information
Q6USC1
mRNA transcripts are detected in all tissues examined
Manually annotated by BRENDA team
additional information
B2LU30
broad tissue PPIase expression pattern
Manually annotated by BRENDA team
additional information
-
expression of cj0596 is slightly higher at 37C than at 42C
Manually annotated by BRENDA team
additional information
Campylobacter jejuni 81-176
-
expression of cj0596 is slightly higher at 37C than at 42C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cyclosporin A-sensitive activity in the chloroplast is mostly localized to the thylakoids, activity associated with the chloroplast stroma and the thylakoids is not inhibited by rapamycin
Manually annotated by BRENDA team
P34790, P34791
in stroma of chloroplasts, not in thylakoid membrane and thylakoid lumen the ROC4 protein is imported into chloroplasts where it is processed to the predicted mature size
Manually annotated by BRENDA team
-
lumen of thylakoid, enzyme isoforms AtCYP20-2 and AtFKBP13. In thiol-reducing conditions, enzyme activity of AtFKBP13 is suppressed severalfold
Manually annotated by BRENDA team
Q9SCY2
stroma and lumen
Manually annotated by BRENDA team
-
anionic enzyme form. Antibodies against the periplasmic enzyme form do not recognize the cytoplasmic enzyme, indicating significant differences in epitopes between the two forms
Manually annotated by BRENDA team
-
Pin1 and the inhibitor of apoptosis protein, Survivin partially co-localize in interphase and mitotic cells
Manually annotated by BRENDA team
-
isoform CyP1
Manually annotated by BRENDA team
-
enzyme is present in 17C supernatants of type II and type IV secretion mutants, although it lacks a signal sequence
-
Manually annotated by BRENDA team
-
and/or organelles, isoforms CyP2 and CyP3
Manually annotated by BRENDA team
Bacillus subtilis IH8478
-
-
-
Manually annotated by BRENDA team
-
mitochondrial form not detected
Manually annotated by BRENDA team
-
bound to double-stranded DNA. The subcellular localization is regulated by posttranslational modification of its N-terminal domain
Manually annotated by BRENDA team
-
Pin1 and the inhibitor of apoptosis protein, Survivin partially co-localize in interphase and mitotic cells
Manually annotated by BRENDA team
-
endogenous Par14 is present in nuclear Pre-40 S and Pre-60 S ribosomal fractions
Manually annotated by BRENDA team
B8XP93
Par45 is mainly concentrated in the nucleus
Manually annotated by BRENDA team
Gossypium hirsutum ZM3
-
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
-
-
Manually annotated by BRENDA team
-
cationic enzyme form
-
Manually annotated by BRENDA team
Campylobacter jejuni 81-176, Escherichia coli AB2847
-
-
-
-
Manually annotated by BRENDA team
Q8VX73
purified recombinant enzyme interacts with plasmodesmata to both induce an increase in size exclusion limit and mediate its own cell-to-cell trafficking
Manually annotated by BRENDA team
-
cyclophilin H is a component of the human U4/U5 small nuclear ribonucleoprotein particle, interacting with homologous sequences in the proteins U4/U6-60K and hPr18 during Pre-mRNA splicing
-
Manually annotated by BRENDA team
Q9SCY2
lumen, CYP20-2 and FKBP13
Manually annotated by BRENDA team
Q5UP71
surface of the mature virion
Manually annotated by BRENDA team
-
cyclosporin A-sensitive activity is largely localized to the mitochondrial matrix. Rapamycin-sensitive activity is associated with the mitochondrial membranes
Manually annotated by BRENDA team
additional information
-
presence of distinct classes of peptidyl cis,trans-isomerases in the mitochondria and the chloroplast of plants
-
Manually annotated by BRENDA team
additional information
-
co-localizing with the nucleolar-specific protein B23 in quiescent cells, Par14 localizes to the nucleolus of those cells during interphase, and Par14 co-localized almost completely with B23 in the spindle apparatus during mitosis
-
Manually annotated by BRENDA team
additional information
-
in mitotic cells, Pin1 is located in the midbody ring
-
Manually annotated by BRENDA team
additional information
-
Pin1 associates with neurofilaments
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Cenarchaeum symbiosum (strain A)
Cenarchaeum symbiosum (strain A)
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Cryptosporidium parvum (strain Iowa II)
Cryptosporidium parvum (strain Iowa II)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Encephalitozoon cuniculi (strain GB-M1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
Helicobacter pylori (strain ATCC 700392 / 26695)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Leishmania donovani (strain BPK282A1)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Plasmodium vivax (strain Salvador I)
Plasmodium vivax (strain Salvador I)
Plasmodium vivax (strain Salvador I)
Plasmodium vivax (strain Salvador I)
Pseudomonas syringae pv. tomato (strain DC3000)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9000
-
gel filtration
2527
11000 - 16000
-
cytosolic enzyme form, gel filtration on various matrices
2535
12440
-
peptidylprolyl isomerase domain, N-terminal sequence analysis
651071
17600
-
cyclophilin
649837
20000
P82536
-
651323
42000
O52980
gel filtration
2525
47300
-
trigger factor
649837
48910
-
recombinant mutant rFKBP22D30, gel filtration
727002
52330
-
trigger factor, N-terminal sequence analysis
651071
60780
-
recombinant wild-type enzyme, gel filtration
727002
65000
-
the cross-linking of cells expressing either wild-type PrsA or PrsA-Myc revealed, in addition to the 33 kDa PrsA or PrsA-Myc monomers, two other PrsA-containing bands of higher molecular weights, one migrating (in SDS-PAGE) at approximately 65 kDa and the other one slightly above it (about 68 kDa)
716254
65710
-
recombinant mutant rFKBP22D5, gel filtration
727002
68000
-
the cross-linking of cells expressing either wild-type PrsA or PrsA-Myc revealed, in addition to the 33 kDa PrsA or PrsA-Myc monomers, two other PrsA-containing bands of higher molecular weights, one migrating (in SDS-PAGE) at approximately 65 kDa and the other one slightly above it (about 68 kDa)
716254
71180
-
recombinant mutant rFKBP22I3, gel filtration
727002
80950
-
recombinant mutant rFKBP22I6, gel filtration
727002
200000
Q9P9H4
gel filtration
727584
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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O52980
x * 16000, SDS-PAGE
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x * 18181, calculation from amino acid sequence
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x * 19000, SDS-PAGE
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x * 20600, SDS-PAGE
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x * 20000, mitochondrial form, SDS-PAGE
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x * 18000, SDS-PAGE
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x * 18000, SDS-PAGE
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x * 18137, cationic enzyme form, calculation from amino acid sequence
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x * 22000, microsomal isoform
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x * 18600, major mitochondrial enzyme form, SDS-PAGE
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x * 16500, enzyme form PPI-II, SDS-PAGE
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x * 17968, calculation from nucleotide sequence
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x * 17000, SDS-PAGE, x * 17737, calculation from amino acid sequence
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x * 17200, enzyme form PPI-III, SDS-PAGE
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x * 18000, cytosolic isoforms, SDS-PAGE
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x * 17000, cytosolic enzyme form, SDS-PAGE
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x * 77000, SDS-PAGE
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Q2I5R9
x * 13000, SDS-PAGE
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P9WHW3
x * 19200, calculated
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x * 28908, calculated
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Q9ZCX6
x * 29500, SDS-PAGE, enzyme heated in sample buffer to 100C migrates electrophoretically slower than untreated enzyme, x * 30819, electrospray mass spectrometry
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Q4G338
x * 32500, SDS-PAGE and predicted
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x * 34800, calculated
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Q6USC1
x * 17700, calculated
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O49886
x * 18000, SDS-PAGE of recombinant enzyme
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Q8VX73
x * 18154, calculated, x * 22000, SDS-PAGE
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B2ZWT4, B2ZWT5
x * 20100, calculated, x * 24000, SDS-PAGE
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B2ZWT4, B2ZWT5
x * 23500, calculated for mature protein, x * 23500, SDS-PAGE
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x * 14000, about, SDS-PAGE
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x * 18000, about
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B2LU30
x * 21474, sequence calculation
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B8XP93
x * 45400, calculated from amino acid sequence
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x * 19200, calculated
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Methanothermococcus thermolithotrophicus DSM2095
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x * 16000, SDS-PAGE
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dimer
Q9NWM8
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dimer
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245-residue subunit is divided into two domains, the overall form of the dimer is V-shaped, and the two C-terminal domains are located at the extremities of the V
dimer
P40415
2 * 27000, SDS-PAGE, 2 * 27034, calculated
dimer
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Par27 is the first identified parvulin protein that forms dimers in solution. Par27 is a tripartite protein with a central PPIase domain surrounded by N- and C-terminal sub-domains, NTD and CTD. Par27 structure analysis by X-ray crystallography, small-angle X-ray scattering and template-based modeling, rigid-body modeling, overview
dimer
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2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
hexamer
Q9P9H4
6 * 33345, calculated from sequence, 6 * 43000, recombinant enzyme, SDS-PAGE
hexamer
Halobacterium salinarum DSM 669
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6 * 33345, calculated from sequence, 6 * 43000, recombinant enzyme, SDS-PAGE
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monomer
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1 * 17700, microsomal enzyme form, SDS-PAGE, 1 * 17500, cytosolic enzyme form, SDS-PAGE
oligomer
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x * 33000, SDS-PAGE
oligomer
Bacillus subtilis IH8478
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x * 33000, SDS-PAGE
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trimer
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gel filtration and analytical ultracentrifugation
trimer
Escherichia coli B/E1
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gel filtration and analytical ultracentrifugation
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monomer
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x * 68000, SDS-PAGE under reducing conditions and under nonreducing conditions
additional information
Q9ZCX6
N-terminal sequence
additional information
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PPIase domain and WW domain show weak interaction at their interface in solution, The flexible linker, connecting both domains, potomes binding
additional information
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solution structure determined by three-dimensional nuclear magnetic resonance spectroscopy
additional information
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tertiary structure of hPAR14 is determined by nuclear magnetic resonance spectroscopy
additional information
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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
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three-dimensional solution structure. 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
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consists of two RNA binding domains at the N-terminus and a peptidylprolyl isomerase domain at the C-terminus
additional information
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isoform Cyp-A exists in native heterocomplexes containing cytoplasmic dynein. Enzyme activity is not required for formation of dynein complexes. Binding to dynamitin is dependent on peptidylprolyl isomerase domain. Heterocomplexes containing tubulin and dynein can be formed in cytosol under microtubule-stabilizing conditions
additional information
Q4G338
protein consists of a N-terminal RNA recognition motif and a C-terminal cyclophilin domain
additional information
P0A9L5
structure analysis by multidimensional solution-state NMR spectroscopy, model of substrate binding pocket, comparison with human and plant proteins
additional information
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enzyme interacts with SNW1/SKI-binding protein and with stathmin
additional information
Q14318
isoform FKBP38 interacts with prolyl-4-hydroxylase domain-containing enzyme PHD2 by association of their N-terminal regions. FKBP38 does not interact with PHD1 or PHD3. Depletion of FKBP38 by RNAi results in increased PHD2 hydroxylation activity and decreased protein levels of PHD2 substrate HIF. downregulation of FKBP38 does not affect PHD2 mRNA levels, but prolongs PHD2 protein stability
additional information
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isoform Pin1 forms a complex with inhibitor of apoptosis protein, Survivin
additional information
Q9Y3C6
isoform PPIL1 stably associates with SKIP, an essential component of 45S activated spliceosome. Dissociation constant is 1.25e -7 M for the N-terminal peptide of SKIP with PPIL1
additional information
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CypB interacts with the endoplasmic reticulum stress-related chaperones, Bip and Grp94
additional information
P40415
isoform Par27 binds to an unfolded filamentous hemagglutinin fragment
additional information
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isoform Pin1 interacts with brain-specifc protein BNIP-H after nerve growth factor stimulation. Both proteins co-localize in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Expression of Pin1 disrupts the BNIP-H/glutaminase complex formation in PC-12 cells under nerve growth factor-stimulation
additional information
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isoform Pin1 is a critical regulator of p27kip1 through inhibition of Forkhead box O, FOXO4. Oxidative stress induces binding of Pin1 to FOXO4 thereby attenuating its monoubiquitination. Pin1 prevents nuclear FOXO4 accumulation and acts on FOXO through stimulation of the activity of the deubiquitinating enzyme HAUSP/USP7
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
additional information
O49886
recombinant enzyme is able to interact with nucleic acids, both single and double stranded DNA fragments as well as RNA
additional information
B2LU30
peptide mass fingerprinting and mass spectrometric analysis, homology-modeling
additional information