Version 5.4
Mus musculus Protein: Fkbp11
Summary
InnateDB Protein IDBP-180997.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Fkbp11
Protein Name FK506 binding protein 11
Synonyms 1110002O23Rik; FKBP-11;
Species Mus musculus
Ensembl Protein ENSMUSP00000003445
InnateDB Gene IDBG-180995 (Fkbp11)
Protein Structure
UniProt Annotation
Function PPIases accelerate the folding of proteins during protein synthesis.
Subcellular Localization Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005528 FK506 binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0018208 peptidyl-proline modification
Cellular Component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1913370
InterPro IPR001179 Peptidyl-prolyl cis-trans isomerase, FKBP-type, domain
PFAM PF00254
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D1M7
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 66120
UniGene Mm.401838
RefSeq NP_077131
MGI ID
MGI Symbol Fkbp11
OMIM
CCDS CCDS27803
HPRD
IMGT
EMBL AK003331 AK019132 BC037596
GenPept AAH37596 BAB22719 BAB31559

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca