5.2.1.8: peptidylprolyl isomerase
This is an abbreviated version!
For detailed information about peptidylprolyl isomerase, go to the full flat file.
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
Subunits
Subunits on EC 5.2.1.8 - peptidylprolyl isomerase
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x * 23000, SDS-PAGE, 18920, calculated from sequence, His-tagged recombinant protein
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x * 21474, sequence calculation
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x * 18181, calculation from amino acid sequence
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x * 18137, cationic enzyme form, calculation from amino acid sequence
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x * 20100, calculated, x * 24000, SDS-PAGE
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x * 23500, calculated for mature protein, x * 23500, SDS-PAGE
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x * 32500, SDS-PAGE and predicted
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x * 17737, calculation from amino acid sequence
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x * 14000, about, SDS-PAGE
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x * 53800, calculated for full-length protein, x * 17000, N-terminal fragment
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x * 17968, calculation from nucleotide sequence
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x * 18000, SDS-PAGE of recombinant enzyme
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x * 16000, SDS-PAGE
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x * 14000, about, SDS-PAGE
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x * 19200, calculated
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x * 28908, calculated
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x * 18000, SDS-PAGE, His-tagged recombinant protein
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x * 20000, mitochondrial form, SDS-PAGE
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x * 34800, calculated
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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 * 18000, cytosolic isoforms, SDS-PAGE
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x * 17000, cytosolic enzyme form, SDS-PAGE
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x * 18154, calculated, x * 22000, SDS-PAGE
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x * 29500, SDS-PAGE, enzyme heated in sample buffer to 100°C migrates electrophoretically slower than untreated enzyme, x * 30819, electrospray mass spectrometry
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x * 16500, enzyme form PPI-II, SDS-PAGE
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x * 17200, enzyme form PPI-III, SDS-PAGE
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x * 12000, calculated from sequence
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x * 45400, calculated from amino acid sequence
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x * 17000, SDS-PAGE, recombinant protein including His-tag
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x * 22000, calculated from sequence
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x * 22000, calculated from sequence
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x * 17000, SDS-PAGE, recombinant protein including His-tag
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dimer
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
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
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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
dimer
2 * 23000, calculated from sequence
hexamer
6 * 33345, calculated from sequence
hexamer
6 * 43000, recombinant enzyme, SDS-PAGE
hexamer
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6 * 33345, calculated from sequence
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hexamer
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6 * 43000, recombinant enzyme, SDS-PAGE
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monomer
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x * 68000, SDS-PAGE under reducing conditions and under nonreducing conditions
monomer
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1 * 17700, microsomal enzyme form, SDS-PAGE
monomer
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1 * 17500, cytosolic enzyme form, SDS-PAGE
oligomer
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x * 33000, SDS-PAGE
oligomer
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x * 33000, SDS-PAGE
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trimer
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gel filtration and analytical ultracentrifugation
trimer
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gel filtration and analytical ultracentrifugation
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additional information
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solution structure determined by three-dimensional nuclear magnetic resonance spectroscopy
additional information
peptide mass fingerprinting and mass spectrometric analysis, homology-modeling
additional information
isoform Par27 binds to an unfolded filamentous hemagglutinin fragment
additional information
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isoform Par27 binds to an unfolded filamentous hemagglutinin fragment
additional information
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the variability in the orientation of the PPIase domains relative to the NTD/CTD core platform, inter-domain flexibility can be important for the biological activity of this protein. Small angle X-ray and neutron scattering, molecular dynamics simulation, and homology modeling, overview
additional information
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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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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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
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homology modeling of the three-dimensional enzyme structure, structures of the helix alpha3 mutants, overview
additional information
three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
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three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
additional information
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three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview
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additional information
protein consists of a N-terminal RNA recognition motif and a C-terminal cyclophilin domain
additional information
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protein consists of a N-terminal RNA recognition motif and a C-terminal cyclophilin domain
additional information
PPIase domain and WW domain show weak interaction at their interface in solution, The flexible linker, connecting both domains, potomes binding
additional information
tertiary structure of hPAR14 is determined by 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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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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enzyme interacts with SNW1/SKI-binding protein and with stathmin
additional information
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
isoform Pin1 forms a complex with inhibitor of apoptosis protein, Survivin
additional information
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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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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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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the N-terminal WW domain is connected by a linker to the C-terminal catalytic isomerase domain, structure modeling, overview
additional information
recombinant enzyme is able to interact with nucleic acids, both single and double stranded DNA fragments as well as RNA
additional information
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recombinant enzyme is able to interact with nucleic acids, both single and double stranded DNA fragments as well as RNA
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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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
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CypB interacts with the endoplasmic reticulum stress-related chaperones, Bip and Grp94
additional information
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the N-terminal WW domain is connected by a linker to the C-terminal catalytic isomerase domain, structure modeling, overview
additional information
N-terminal sequence
additional information
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N-terminal sequence
additional information
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solution structure of the Fpr4 C-terminal PPIase domain by NMR spectroscopy, structure calculation, overview