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Q64378 (FKBP5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP5

Short name=PPIase FKBP5
EC=5.2.1.8
Alternative name(s):
51 kDa FK506-binding protein
Short name=51 kDa FKBP
Short name=FKBP-51
FK506-binding protein 5
Short name=FKBP-5
Rotamase
Gene names
Name:Fkbp5
Synonyms:Fkbp51
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Part of a heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates from the complex and FKBP4 takes its place. Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP. Ref.4 Ref.5

Subcellular location

Cytoplasm. Nucleus Ref.4.

Tissue specificity

Widely expressed, highest levels found in the liver, skeletal muscle, kidney and thymus. Expression is regulated during adipocyte differentiation.

Sequence similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nr3c1P065372EBI-492796,EBI-492753

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Peptidyl-prolyl cis-trans isomerase FKBP5
PRO_0000075325

Regions

Domain50 – 13889PPIase FKBP-type 1
Domain165 – 25187PPIase FKBP-type 2
Repeat268 – 30134TPR 1
Repeat317 – 35034TPR 2
Repeat351 – 38434TPR 3

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue4441Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64378 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8FD0C9B61478EB46

FASTA45650,966
        10         20         30         40         50         60 
MTTDEGTSNN GENPAATMTE QGEDITTKKD RGVLKIVKRV GTSDEAPMFG DKVYVHYKGM 

        70         80         90        100        110        120 
LSDGKKFDSS HDRKKPFAFS LGQGQVIKAW DIGVSTMKKG EICHLLCKPE YAYGSAGHLQ 

       130        140        150        160        170        180 
KIPSNATLFF EIELLDFKGE DLFEDSGVIR RIKRKGEGYS NPNEGATVKV HLEGCCGGRT 

       190        200        210        220        230        240 
FDCRDVVFVV GEGEDHDIPI GIDKALVKMQ REEQCILYLG PRYGFGEAGK PKFGIDPNAE 

       250        260        270        280        290        300 
LMYEVTLKSF EKAKESWEMD TKEKLTQAAI VKEKGTVYFK GGKYTQAVIQ YRKIVSWLEM 

       310        320        330        340        350        360 
EYGLSEKESK ASESFLLAAF LNLAMCYLKL REYNKAVECC DKALGLDSAN EKGLYRRGEA 

       370        380        390        400        410        420 
QLLMNDFESA KGDFEKVLAV NPQNRAARLQ ISMCQRKAKE HNERDRRVYA NMFKKFAERD 

       430        440        450 
AKEEASKAGS KKAVEGAAGK QHESQAMEEG KAKGHV 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of an immunophilin expressed during the clonal expansion phase of adipocyte differentiation."
Yeh W.-C., Li T.-K., Bierer B.E., McKnight S.L.
Proc. Natl. Acad. Sci. U.S.A. 92:11081-11085(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition."
Baughman G., Wiederrecht G.J., Campbell N.F., Martin M.M., Bourgeois S.
Mol. Cell. Biol. 15:4395-4402(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[4]"A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins."
Davies T.H., Ning Y.M., Sanchez E.R.
J. Biol. Chem. 277:4597-4600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1, SUBCELLULAR LOCATION.
[5]"Protein phosphatase 5 mediates lipid metabolism through reciprocal control of glucocorticoid receptor and peroxisome proliferator-activated receptor-? (PPAR?)."
Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A., Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.
J. Biol. Chem. 286:42911-42922(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR3C1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36220 mRNA. Translation: AAA89162.1.
U16959 mRNA. Translation: AAA86983.1.
BC015260 mRNA. Translation: AAH15260.1.
CCDSCCDS37528.1.
RefSeqNP_034350.1. NM_010220.4.
UniGeneMm.276405.

3D structure databases

ProteinModelPortalQ64378.
SMRQ64378. Positions 13-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ64378. 6 interactions.
MINTMINT-1576439.

PTM databases

PhosphoSiteQ64378.

Proteomic databases

MaxQBQ64378.
PaxDbQ64378.
PRIDEQ64378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079413; ENSMUSP00000078382; ENSMUSG00000024222.
ENSMUST00000114792; ENSMUSP00000110440; ENSMUSG00000024222.
ENSMUST00000177939; ENSMUSP00000136245; ENSMUSG00000024222.
GeneID14229.
KEGGmmu:14229.
UCSCuc008bqz.2. mouse.

Organism-specific databases

CTD2289.
MGIMGI:104670. Fkbp5.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00550000074272.
HOGENOMHOG000256916.
HOVERGENHBG051624.
InParanoidQ64378.
KOK09571.
OMAHLEGCCG.
OrthoDBEOG725DHH.
PhylomeDBQ64378.

Gene expression databases

ArrayExpressQ64378.
BgeeQ64378.
CleanExMM_FKBP5.
GenevestigatorQ64378.

Family and domain databases

Gene3D1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
InterProIPR023114. Elongated_TPR_rpt_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 2 hits.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285495.
PROQ64378.
SOURCESearch...

Entry information

Entry nameFKBP5_MOUSE
AccessionPrimary (citable) accession number: Q64378
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot