5.2.1.8: peptidylprolyl isomerase
This is an abbreviated version!
For detailed information about peptidylprolyl isomerase, go to the full flat file.
Word Map on EC 5.2.1.8
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5.2.1.8
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cyclosporine
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immunophilins
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isomerization
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calcineurin
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isomerases
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necrosis
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cardiac
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lymphocyte
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immunodeficiency
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capsid
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ryanodine
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t-cells
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steroid
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glucocorticoid
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alzheimer
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tetratricopeptide
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tacrolimus
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refolding
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hsp70
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mtor
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interactor
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virion
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imperfecta
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gapdh
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co-chaperone
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genorm
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dnak
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anti-hcv
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ptp
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groel
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legionella
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osteogenesis
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sarcoplasmic
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translocase
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heterocomplexes
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pneumophila
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voltage-dependent
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phosphorylation-dependent
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ns5a
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analysis
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ca2+-induced
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direct-acting
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sirolimus
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csa-induced
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proline-directed
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bestkeeper
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excitation-contraction
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medicine
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ribavirin
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emmprin
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normfinder
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ribosome-associated
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agriculture
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pharmacology
- 5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
- calcineurin
- isomerases
- necrosis
- cardiac
- lymphocyte
- immunodeficiency
- capsid
-
ryanodine
- t-cells
- steroid
- glucocorticoid
- alzheimer
-
tetratricopeptide
- tacrolimus
-
refolding
- hsp70
- mtor
- interactor
- virion
- imperfecta
- gapdh
-
co-chaperone
-
genorm
- dnak
-
anti-hcv
- ptp
- groel
- legionella
-
osteogenesis
-
sarcoplasmic
- translocase
-
heterocomplexes
- pneumophila
-
voltage-dependent
-
phosphorylation-dependent
- ns5a
- analysis
-
ca2+-induced
-
direct-acting
- sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
- medicine
- ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
- agriculture
- pharmacology
Reaction
peptidylproline (omega = 180)
Synonyms
12 kDa FKBP, 12.6 kDa FKBP, 13 kDa FKBP, 15 kDa FKBP, 19 kDa FK506-binding protein, 22 kDa FK506-binding protein, 25 kDa FKBP, 27 kDa membrane protein, 36 kDa FK506 binding protein, 40 kDa thylakoid lumen PPIase, 40 kDa thylakoid lumen rotamase, 51 kDa FK506-binding protein, 52 kDa FK506 binding protein, 54 kDa progesterone receptor-associated immunophilin, 65 kDa FK506-binding protein, At3g56070, CeCYP-16, CGI-124, Cgl0830, Chl-Mip, Cj0596, CPH, CTHT_0005290, Cwc27, Cyclophilin, Cyclophilin 18, cyclophilin 3, Cyclophilin 33, Cyclophilin A, Cyclophilin B, Cyclophilin C, Cyclophilin cyp2, cyclophilin H, cyclophilin hCyp-18, Cyclophilin homolog, cyclophilin J, Cyclophilin ScCypA, Cyclophilin ScCypB, Cyclophilin-10, Cyclophilin-11, Cyclophilin-40, Cyclophilin-60, cyclophilin-A, cyclophilin-D, Cyclophilin-like protein Cyp-60, Cyclophilin-related protein, Cyclosporin A-binding protein, Cyp, CYP-3, CYP-40, CYP-5, CYP-6, cyp-A, CYP-S1, Cyp1, Cyp18, Cyp19-3, Cyp2, CYP20-2, CYP20-3, Cyp3, Cyp3 PPIase, Cyp40, CyPA, CypA-1, CyPB, CyPJ, DDB_G0268618, Dod, EF0685, EF1534, EF2898, Estrogen receptor binding cyclophilin, FF1 antigen, FK506 binding protein 12, FK506 binding protein 35, FK506-binding protein, FKBP, FKBP 12, FKBP-12, FKBP-12.6, FKBP-13, FKBP-15, FKBP-19, FKBP-21, FKBP-22, FKBP-23, FKBP-25, FKBP-36, FKBP-51, FKBP-70, FkbP10, FKBP12, FKBP13, FKBP17, FKBP1B, FKBP22, FKBP25, FKBP3, FKBP33, FKBP35, FKBP38, FKBP51, FKBP52, FKBP52 protein, FKBP54, FKBP59, FKBP65, FKBP65RS, FKBP77, FklB, FkpA, h Par14, HBI, HcCYP, hCyP33, Histidine rich protein, hPar14, hPin1, HSP binding immunophilin, HSP90-binding immunophilin, Immunophilin FKBP12, Immunophilin FKBP12.6, Immunophilin FKBP36, Immunophilin FKBP65, Isomerase, peptidylprolyl cis-trans, L.p.Cyp18, Macrolide binding protein, Macrophage infectivity potentiator, mimicyp, MIP, mip-like peptidyl-prolyl cis-trans isomerase, More, MtFK, MtFKBP17, mzFKBP-66, Ng-MIP, NIMA-1, Nucleolar proline isomerase, OvCYP-16, p17.7, P31, P54, p59 protein, Par10, Par14, Par27, Par45, Parvulin, Parvulin 14, parvulin-like protein, parvulin-type peptidyl-prolyl isomerase, parvulin1 4, pCYP B, Peptide bond isomerase, peptidyl prolyl cis-trans isomerase, peptidyl prolyl isomerase-like protein 1, Peptidyl-prolyl cis-trans isomerase, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Peptidyl-prolyl cis-trans isomerase plp, Peptidyl-prolyl cis-trans isomerase surA, peptidyl-prolyl cis/trans isomerase, Peptidyl-prolyl cis/trans isomerase EPVH, peptidyl-prolyl cis/trans isomerase NIMA-interacting 1, peptidyl-prolyl isomerase, peptidyl-prolyl isomerase 1, peptidylproline cis-trans-isomerase, peptidylprolyl cis,trans-isomerase, Peptidylprolyl cis-trans isomerase, peptidylprolyl cis/trans isomerase, peptidylprolyl isomerase, PfCyP, Pin1, PIN1-type parvulin 1, PIN1At, PinA, Planta-induced rust protein 28, Plp, PP2A phosphatase activator, PpiA, PPIase, PPIase Pin1, PPIase Pin4, PpiB, PPIC, PpiD, PPIE, PPIF, PPIG, PPIH, PPIL1, PPWD1, Proline rotamase, prolyl cis-trans isomerase, prolyl-peptidyl isomerase, protein phosphatase 2A phosphatase activator, Proteins, cyclophilins, Proteins, specific or class, cyclophilins, PrsA, Ptf1/Ess1, PtpA, PvFKBP35, Rapamycin-binding protein, Rapamycin-selective 25 kDa immunophilin, ROF2, Rotamase, Rotamase Pin1, Rotamase Pin4, Rotamase plp, S-cyclophilin, S1205-06, SAUSA300_0857, SCYLP, SDCCAG-10, sFkpA, SlrA, SLyD, SmCYP A, SmCYP B, Smp17.7, SP18, spliceosome-associated protein CWC27 homolog, SurA, TcFKBP18, TF, TLP20, trigger factor, TTHA0346, WHP, Ypa
ECTree
5.2.1.8 peptidylprolyl isomeraseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 5.2.1.8 - peptidylprolyl isomerase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AGL24 protein
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cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
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hepatitis C virus NS5A protein
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nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain. Mutations in this domain are linked to cyclosporin A resistance
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interleukin-2 tyrosine kinase
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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
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?
phosphorylated pro-apoptotic Bcl-2-associated X protein
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Pin1 prevents activation of Bax, prevents Bax cleavage by calpain, and prevents Bax translocation to mitochondria
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?
SOC1 protein
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cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
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?
PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
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PP2A phosphatase with cis-P190
PP2A phosphatase with trans-P190
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?
RNA polymerase II
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Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
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?
RNA polymerase II
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Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
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?
additional information
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not essential for protein import into chloroplast
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?
additional information
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not essential for protein import into chloroplast
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?
additional information
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not essential for protein import into chloroplast
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?
additional information
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Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24
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?
additional information
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AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
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additional information
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AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
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additional information
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only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity. The prolyl isomerases become essential for growth under starvation conditions
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?
additional information
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the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
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additional information
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class3 cyclophilins are involved in cellular responses to stress caused by changes in redox environment or by upregulation of cellular activity
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?
additional information
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the kinesin-related protein, KRMP1 is a mitotic target regulated by Pin1 and vice versa
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?
additional information
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the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
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?
additional information
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trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
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?
additional information
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the presence of cyclophilin A in the human immunodeficiency virus type 1, HIV-1, is required for HIV-1 to infect and replicate
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additional information
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the functional role may involve signal transduction of specific genes essential for T-lymphocyte activation and proliferation
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additional information
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cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
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additional information
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cyclophilin A performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection
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additional information
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enzyme is required for cell cycle progression
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?
additional information
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folding helper enzyme that plays a role in cell-cycle and chromatin remodeling
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?
additional information
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peptidylprolyl isomerase Pin1 interacts with Cdk9-phosphorylated hSpt5. Cdk9 dependent phosphorylation of Rpb1 and hSpt5 followed by Pin1 interaction might contribute to the regulation of transcription, pre-mRNA maturation and the dynamics of proteins in interphase and mitosis
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?
additional information
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substrates are proteins involved in regulation of cell cycle, transcription, Alzheimers disease, and cancer pathogenesis
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?
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
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?
additional information
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selective for substrate SRC-3, phosphorylated steroid receptor coactivator 3. Enzyme and SRC-3 synergistically activate nuclear-receptor-regulated transcription
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additional information
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incorporation of the HCV polymerase into the replication complex depends on its interaction with a cellular chaperone protein, cyclosporine inhibits HCV replication by blocking this critical interaction and the PPIase activity of CyPA, modeling of the pathway, overview. CyPA is associated with CRC-incorporated HCV replicase in a cyclosporine-sensitive manner
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additional information
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Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
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additional information
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Pin1 enhances Plk1-mediated phosphorylation of the centrosome protein Cep55, overview
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additional information
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Pin1 interacts with human T-cell leukemia virus type 1 Tax, phosphorylated at Ser258, and modulates its activation of NF-kappaB. Pin1 contributes to Tax signaling through NF-kappaB, and it cooperates with Tax to enhance cellular proliferation
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additional information
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Pin1 interacts with NF-kappaB via its WW domain
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additional information
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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
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additional information
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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
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?
additional information
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promyelocytic leukemia protein, PML, and silencing mediator for retinoic acid and thyroid hormone receptor, SMRT, are Pin1 substrates
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additional information
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Pin1 is a peptidyl-prolyl isomerase (PPIase), that catalyzes the cis-trans isomerization of pSer/pThr-Pro substrates in vivo and in vitro
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?
additional information
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the enzyme is not essential for Legionella pneumophila although the Cyp18-negative mutant strain is less infective for Acanthamoeba castellanii
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?
additional information
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the enzyme is involved in cell cycle progression
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?
additional information
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general function of enzyme in binding of cargo for retrograde movement along microtubules
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additional information
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Par14 behaves as a component of the preribosomal ribonucleoprotein, pre-rRNP, complexes in vivo interacting via its residues 36-41, proteomics analysis of the Par14-associated pre-rRNP complexes, overview
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?
additional information
?
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the trigger factor accepts only unfolded protein substrates, no action on protein chains that have partially folded already
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?
additional information
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protein is not involved in binding to macrophages and does not impair the ability of macrophages to phagocytose the gonococci
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?
additional information
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general function of enzyme in binding of cargo for retrograde movement along microtubules
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?
additional information
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cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
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additional information
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cyclophilin A mediates the polymerization and matrix assembly of hensin, a multifunctional, multi-domain protein implicated in the regulation of epithelial differentiation
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additional information
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enzyme inhibits the phosphatase activity of calcineurin independently of FK506 binding. Enzyme also inhibits thermal aggregation of two model substrates indicating chaperone proterties
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
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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
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?
additional information
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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
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?
additional information
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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
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additional information
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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
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?
additional information
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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
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?
additional information
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expression of the transcript in the leaf tissue is regulated by light and induced by heat shock
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?
additional information
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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
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