Q64378 · FKBP5_MOUSE
- ProteinPeptidyl-prolyl cis-trans isomerase FKBP5
- GeneFkbp5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids456 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Inhibited by both FK506 and rapamycin.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | heat shock protein binding | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | chaperone-mediated protein folding | |
Biological Process | response to bacterium |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase FKBP5
- EC number
- Short namesPPIase FKBP5
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64378
Proteomes
Organism-specific databases
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000075325 | 1-456 | Peptidyl-prolyl cis-trans isomerase FKBP5 | |||
Sequence: MTTDEGTSNNGENPAATMTEQGEDITTKKDRGVLKIVKRVGTSDEAPMFGDKVYVHYKGMLSDGKKFDSSHDRKKPFAFSLGQGQVIKAWDIGVSTMKKGEICHLLCKPEYAYGSAGHLQKIPSNATLFFEIELLDFKGEDLFEDSGVIRRIKRKGEGYSNPNEGATVKVHLEGCCGGRTFDCRDVVFVVGEGEDHDIPIGIDKALVKMQREEQCILYLGPRYGFGEAGKPKFGIDPNAELMYEVTLKSFEKAKESWEMDTKEKLTQAAIVKEKGTVYFKGGKYTQAVIQYRKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYNKAVECCDKALGLDSANEKGLYRRGEAQLLMNDFESAKGDFEKVLAVNPQNRAARLQISMCQRKAKEHNERDRRVYANMFKKFAERDAKEEASKAGSKKAVEGAAGKQHESQAMEEGKAKGHV | ||||||
Modified residue | 28 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 155 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 444 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acetylation impairs ability to promote interaction between Akt/AKT1 and PHLPP1. Deacetylation by SIRT7 promotes interaction between Akt/AKT1 and PHLPP1, leading to suppress Akt/AKT1 activation.
Ubiquitinated, leading to degradation in a proteasome-dependent manner. Deubiquitinated by USP49, leading to stabilization.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, highest levels found in the liver, skeletal muscle, kidney and thymus. Expression is regulated during adipocyte differentiation.
Gene expression databases
Interaction
Subunit
Part of a heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B and steroid receptors (PubMed:11751894).
Upon ligand binding dissociates from the complex and FKBP4 takes its place (PubMed:11751894).
Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP (By similarity).
Interacts with NR3C1 (PubMed:21994940).
Interacts with Akt/AKT1 and PHLPP1; enhancing dephosphorylation and subsequent activation of Akt/AKT1 (By similarity).
Interacts with IFI44L; this interaction modulates the kinase activity of IKBKB and IKBKE (By similarity).
Interacts with IKBKB and IKBKE (By similarity).
Upon ligand binding dissociates from the complex and FKBP4 takes its place (PubMed:11751894).
Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP (By similarity).
Interacts with NR3C1 (PubMed:21994940).
Interacts with Akt/AKT1 and PHLPP1; enhancing dephosphorylation and subsequent activation of Akt/AKT1 (By similarity).
Interacts with IFI44L; this interaction modulates the kinase activity of IKBKB and IKBKE (By similarity).
Interacts with IKBKB and IKBKE (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q64378 | Nr3c1 P06537 | 2 | EBI-492796, EBI-492753 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MTTDEGTSNNGENPAATMTEQG | ||||||
Region | 1-24 | Disordered | ||||
Sequence: MTTDEGTSNNGENPAATMTEQGED | ||||||
Domain | 50-138 | PPIase FKBP-type 1 | ||||
Sequence: GDKVYVHYKGMLSDGKKFDSSHDRKKPFAFSLGQGQVIKAWDIGVSTMKKGEICHLLCKPEYAYGSAGHLQKIPSNATLFFEIELLDFK | ||||||
Domain | 165-251 | PPIase FKBP-type 2 | ||||
Sequence: GATVKVHLEGCCGGRTFDCRDVVFVVGEGEDHDIPIGIDKALVKMQREEQCILYLGPRYGFGEAGKPKFGIDPNAELMYEVTLKSFE | ||||||
Repeat | 268-301 | TPR 1 | ||||
Sequence: AAIVKEKGTVYFKGGKYTQAVIQYRKIVSWLEME | ||||||
Repeat | 317-350 | TPR 2 | ||||
Sequence: LAAFLNLAMCYLKLREYNKAVECCDKALGLDSAN | ||||||
Repeat | 351-384 | TPR 3 | ||||
Sequence: EKGLYRRGEAQLLMNDFESAKGDFEKVLAVNPQN | ||||||
Region | 421-456 | Disordered | ||||
Sequence: AKEEASKAGSKKAVEGAAGKQHESQAMEEGKAKGHV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length456
- Mass (Da)50,966
- Last updated1996-11-01 v1
- Checksum8FD0C9B61478EB46
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B2WBD2 | A0A3B2WBD2_MOUSE | Fkbp5 | 248 | ||
A0A3B2WCL4 | A0A3B2WCL4_MOUSE | Fkbp5 | 93 | ||
B8JJC2 | B8JJC2_MOUSE | Fkbp5 | 191 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MTTDEGTSNNGENPAATMTEQG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U36220 EMBL· GenBank· DDBJ | AAA89162.1 EMBL· GenBank· DDBJ | mRNA | ||
U16959 EMBL· GenBank· DDBJ | AAA86983.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015260 EMBL· GenBank· DDBJ | AAH15260.1 EMBL· GenBank· DDBJ | mRNA |