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Peptidyl-prolyl cis-trans isomerase B

A eukaryotic peptidyl-prolyl cis-trans isomerase B that is encoded in the genome of human. [PRO:DNx, UniProtKB:P23284]

Synonyms

PPIase B;
EC 5.2.1.8;
CYP-S1;
Cyclophilin B;
Rotamase B;
S-cyclophilin;
SCYLP

Research

Bioassay Publications (4)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (25.00)29.6817
2010's2 (50.00)24.3611
2020's1 (25.00)2.80

Compounds (5)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
prolinalHomo sapiens (human)IC505,000.000011
cyclosporineHomo sapiens (human)IC500.008811
scy-635Homo sapiens (human)IC500.010311

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
cyclosporineHomo sapiens (human)Kd0.009811
(melle-4)cyclosporinHomo sapiens (human)Kd0.007411
scy-635Homo sapiens (human)Kd0.002911
alisporivirHomo sapiens (human)Kd0.001011

Enables

This protein enables 6 target(s):

TargetCategoryDefinition
RNA bindingmolecular functionBinding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah]
peptidyl-prolyl cis-trans isomerase activitymolecular functionCatalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). [EC:5.2.1.8]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
cyclosporin A bindingmolecular functionBinding to cyclosporin A, a cyclic undecapeptide that contains several N-methylated and unusual amino acids. [GOC:mb]
unfolded protein bindingmolecular functionBinding to an unfolded protein. [GOC:ai]
RNA polymerase bindingmolecular functionBinding to an RNA polymerase molecule or complex. [GOC:BHF, GOC:mah, GOC:txnOH]

Located In

This protein is located in 11 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
endoplasmic reticulumcellular componentThe irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732]
endoplasmic reticulum lumencellular componentThe volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684]
smooth endoplasmic reticulumcellular componentThe smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. [ISBN:0198506732]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
focal adhesioncellular componentA cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002]
membranecellular componentA lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]
melanosomecellular componentA tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. [GOC:jl, PMID:11584301]
perinuclear region of cytoplasmcellular componentCytoplasm situated near, or occurring around, the nucleus. [GOC:jid]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 2 target(s):

TargetCategoryDefinition
intracellular membrane-bounded organellecellular componentOrganized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Part Of

This protein is part of 2 target(s):

TargetCategoryDefinition
protein-containing complexcellular componentA stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]
endoplasmic reticulum chaperone complexcellular componentA protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1. [PMID:12475965]

Involved In

This protein is involved in 9 target(s):

TargetCategoryDefinition
protein peptidyl-prolyl isomerizationbiological processThe modification of a protein by cis-trans isomerization of a proline residue. [GOC:krc, PMID:16959570]
neutrophil chemotaxisbiological processThe directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. [GOC:jl, ISBN:0198506732]
positive regulation of multicellular organism growthbiological processAny process that activates or increases the frequency, rate or extent of growth of an organism to reach its usual body size. [GOC:dph, GOC:go_curators, GOC:tb]
positive regulation by host of viral processbiological processA process in which a host organism activates or increases the frequency, rate or extent of the release of a process being mediated by a virus with which it is infected. [GOC:jl]
positive regulation by host of viral genome replicationbiological processA process in which a host organism activates or increases the frequency, rate or extent of viral genome replication. [GOC:jl]
protein stabilizationbiological processAny process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. [GOC:ai]
bone developmentbiological processThe process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components. [GOC:dph]
chaperone-mediated protein foldingbiological processThe process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. [GOC:dph, GOC:vw]
protein foldingbiological processThe process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. [GOC:go_curators, GOC:rb]