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Q9XSH5 (FKBP5_SAIBB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 8, 2011. Version 62. 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·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
OrganismSaimiri boliviensis boliviensis (Bolivian squirrel monkey)
Taxonomic identifier39432 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeSaimiriinaeSaimiri

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP By similarity. Interacts with the glucocorticoid receptor and modulates its response to glucocorticoids. Ref.1 Ref.2

Catalytic activity

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

Enzyme regulation

Inhibited by FK506 but not cyclosporin.

Subunit structure

Part of a heteromultimeric cytoplasmic complex with HSP90, HSP70 and steroid receptors. Dissociates from the complex when NR3C1 binds glucocorticoid By similarity.

Subcellular location

Cytoplasm Ref.1.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Miscellaneous

The relative resistance of squirrel monkeys to glucocorticoids is associated with a high level of expression of FKBP5, but is also due to intrinsic differences between the human and the monkey proteins. Human FKBP5 has a much lower effect on glucocorticoid sensitivity.

Sequence similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
TPR repeat
   Molecular functionChaperone
Isomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Peptidyl-prolyl cis-trans isomerase FKBP5
PRO_0000075328

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 residue4451Phosphoserine By similarity

Secondary structure

....................................................... 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9XSH5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DFF9E1D81F7759A8

FASTA45751,169
        10         20         30         40         50         60 
MTTDEGAKNS RGNPAATVAE QGEDVTSKKD RGVLKIVKRV GHGEETPMIG DRVYVHYNGK 

        70         80         90        100        110        120 
LANGKKFDSS HDRNEPFVFS IGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGATGSLP 

       130        140        150        160        170        180 
KIPSNATLFF EVELLDFKGE DLLEDGGIIR RTKRRGEGYS NPNEGARVQI HLEGRCGGRV 

       190        200        210        220        230        240 
FDCRDVAFTV GEGEDHDIPI GIDKALEKMQ REEQCILHLG PRYGFGEAGK PKFGIEPNAE 

       250        260        270        280        290        300 
LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYVQAVIQ YGKIVSWLEM 

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

       370        380        390        400        410        420 
QLLMNEFESA KGDFEKVLEV NPQNKAARLQ IFMCQKKAKE HNERDRRTYA NMFKKFAEQD 

       430        440        450 
AKEEANKAMS KKTSEGVTNE KLTASHAVEE EKPEGHV 

« Hide

References

[1]"Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding."
Denny W.B., Valentine D.L., Reynolds P.D., Smith D.F., Scammell J.G.
Endocrinology 141:4107-4113(2000) [PubMed: 11089542] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: B-cell.
[2]"Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes."
Sinars C.R., Cheung-Flynn J., Rimerman R.A., Scammell J.G., Smith D.F., Clardy J.
Proc. Natl. Acad. Sci. U.S.A. 100:868-873(2003) [PubMed: 12538866] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-421, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF140759 mRNA. Translation: AAD32678.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KT1X-ray2.80A1-457[»]
ProteinModelPortalQ9XSH5.
SMRQ9XSH5. Positions 28-421.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG051624.

Family and domain databases

InterProIPR023114. Elongated_TPR_rpt_dom.
IPR001179. PPIase_FKBP_dom.
IPR001440. TPR-1.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.10.150.160. Elongated_TPR_rpt_dom. 1 hit.
G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 2 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFKBP5_SAIBB
AccessionPrimary (citable) accession number: Q9XSH5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1999
Last modified: March 8, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families