Peptidyl-prolyl cis-trans isomerase FKBP5

A peptidyl-prolyl cis-trans isomerase FKBP5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q13451]

Synonyms

PPIase FKBP5;
EC 5.2.1.8;
51 kDa FK506-binding protein;
51 kDa FKBP;
FKBP-51;
54 kDa progesterone receptor-associated immunophilin;
Androgen-regulated protein 6;
FF1 antigen;
FK506-binding protein 5;
FKBP-5;
FKBP54

Research

Bioassay Publications (4)

Timeframe	Studies on this Protein(%)	All Drugs %
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	3 (75.00)	24.3611
2020's	1 (25.00)	2.80

Compounds (9)

Drugs with Inhibition Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
3-(3-pyridyl)-1-propyl-(2s)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-pyrrolidinecarboxylate	Homo sapiens (human)	IC50	100.0000	1	1
tacrolimus	Homo sapiens (human)	Ki	0.0795	2	2
biricodar	Homo sapiens (human)	IC50	8.5200	1	1
sirolimus	Homo sapiens (human)	Ki	0.0030	1	1
timcodar	Homo sapiens (human)	IC50	100.0000	1	1

Drugs with Activation Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
imidazole	Homo sapiens (human)	Kd	4,400.0000	1	1
2-hydroxypyridine	Homo sapiens (human)	Kd	1,300.0000	1	1
2-piperidone	Homo sapiens (human)	Kd	2,800.0000	1	1
4-methylimidazole	Homo sapiens (human)	Kd	2,900.0000	1	1

Enables

This protein enables 5 target(s):

Target	Category	Definition
peptidyl-prolyl cis-trans isomerase activity	molecular function	Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). [EC:5.2.1.8]
protein binding	molecular function	Binding to a protein. [GOC:go_curators]
FK506 binding	molecular function	Binding to a 23-membered macrolide lactone FK506. [GOC:jl]
protein-macromolecule adaptor activity	molecular function	The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid. [GOC:bf, GOC:mah, GOC:vw]
heat shock protein binding	molecular function	Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. [GOC:mah, GOC:vw]

Located In

This protein is located in 4 target(s):

Target	Category	Definition
nucleoplasm	cellular component	That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
cytosol	cellular component	The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
membrane	cellular component	A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]
extracellular exosome	cellular component	A 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 1 target(s):

Target	Category	Definition
cytoplasm	cellular component	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Involved In

This protein is involved in 4 target(s):

Target	Category	Definition
protein folding	biological process	The 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]
response to bacterium	biological process	Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium. [GOC:hb]
chaperone-mediated protein folding	biological process	The 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 peptidyl-prolyl isomerization	biological process	The modification of a protein by cis-trans isomerization of a proline residue. [GOC:krc, PMID:16959570]