Version 5.4
Homo sapiens Protein: FKBP2
Summary
InnateDB Protein IDBP-53313.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol FKBP2
Protein Name FK506 binding protein 2, 13kDa
Synonyms FKBP-13; PPIase;
Species Homo sapiens
Ensembl Protein ENSP00000310935
InnateDB Gene IDBG-53311 (FKBP2)
Protein Structure
UniProt Annotation
Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity T-cells and thymus.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 19 experimentally validated interaction(s) in this database.
Experimentally validated
Total 19 [view]
Protein-Protein 17 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0005528 FK506 binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0061077 chaperone-mediated protein folding
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR001179 Peptidyl-prolyl cis-trans isomerase, FKBP-type, domain
PFAM PF00254
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P26885
PhosphoSite PhosphoSite-P26885
TrEMBL Q53XJ5
UniProt Splice Variant
Entrez Gene 2286
UniGene
RefSeq NP_004461
HUGO HGNC:3718
OMIM 186946
CCDS CCDS8063
HPRD 01742
IMGT
EMBL AP001453 BC003384 BC091475 BT009861 CH471076 CR407636 M65128 M75099
GenPept AAA36563 AAA58473 AAH03384 AAH91475 AAP88863 CAG28564 EAW74224 EAW74225

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