FKBP2

FKBP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2PBC, 4NNR
Identifiers
Aliases	FKBP2, FKBP-13, PPIase, FK506 binding protein 2, FKBP prolyl isomerase 2, FKBP13
External IDs	OMIM: 186946 MGI: 95542 HomoloGene: 40604 GeneCards: FKBP2
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.1 Start 64,241,003 bp End 64,244,134 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 A Start 6,955,109 bp End 6,957,869 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pituitary gland anterior pituitary body of pancreas right lobe of thyroid gland left lobe of thyroid gland right lobe of liver hypothalamus kidney substantia nigra renal cortex Top expressed in seminal vesicula supraoptic nucleus islet of Langerhans parotid gland medulla oblongata medial vestibular nucleus yolk sac lacrimal gland inferior colliculus superior frontal gyrus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function FK506 binding protein binding isomerase activity peptidyl-prolyl cis-trans isomerase activity Cellular component membrane endoplasmic reticulum endoplasmic reticulum membrane Biological process chaperone-mediated protein folding protein peptidyl-prolyl isomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2286 14227 Ensembl ENSG00000173486 ENSMUSG00000056629 UniProt P26885 P45878 RefSeq (mRNA) NM_001135208 NM_004470 NM_057092 NM_001166368 NM_008020 NM_001360286 NM_001360288 RefSeq (protein) NP_001128680 NP_004461 NP_476433 NP_001159840 NP_032046 NP_001347215 NP_001347217 Location (UCSC) Chr 11: 64.24 – 64.24 Mb Chr 19: 6.96 – 6.96 Mb PubMed search
Wikidata
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FK506-binding protein 2 is a protein that in humans is encoded by the FKBP2 gene.

Function

The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It is thought to function as an ER chaperone and may also act as a component of membrane cytoskeletal scaffolds. This gene has two alternatively spliced transcript variants that encode the same isoform. Multiple polyadenylation sites have been described for this gene, but the full length nature of this gene has not been determined.

Interactions

FKBP2 has been shown to interact with ARFGEF1 and EPB41L2.

Further reading

• DiLella AG, Hawkins A, Craig RJ, Schreiber SL, Griffin CA (1992). "Chromosomal band assignments of the genes encoding human FKBP12 and FKBP13". Biochem. Biophys. Res. Commun. 189 (2): 819–23. doi:10.1016/0006-291X(92)92276-4. PMID 1281998.
• Hendrickson BA, Zhang W, Craig RJ, Jin YJ, Bierer BE, Burakoff S, DiLella AG (1993). "Structural organization of the genes encoding human and murine FK506-binding protein (FKBP) 13 and comparison to FKBP1". Gene. 134 (2): 271–5. doi:10.1016/0378-1119(93)90106-D. PMID 7505249.
• Bush KT, Hendrickson BA, Nigam SK (1994). "Induction of the FK506-binding protein, FKBP13, under conditions which misfold proteins in the endoplasmic reticulum". Biochem. J. 303 (Pt 3): 705–8. doi:10.1042/bj3030705. PMC 1137603. PMID 7526846.
• Nigam SK, Jin YJ, Jin MJ, Bush KT, Bierer BE, Burakoff SJ (1993). "Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum". Biochem. J. 294 (Pt 2): 511–5. doi:10.1042/bj2940511. PMC 1134484. PMID 8373365.
• Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (1998). "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1". J. Cell Biol. 141 (1): 143–53. doi:10.1083/jcb.141.1.143. PMC 2132710. PMID 9531554.
• Padilla PI, Chang MJ, Pacheco-Rodriguez G, Adamik R, Moss J, Vaughan M (2003). "Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of FK506". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2322–7. Bibcode:2003PNAS..100.2322P. doi:10.1073/pnas.2628047100. PMC 151339. PMID 12606707.
• Willingham S, Outeiro TF, DeVit MJ, Lindquist SL, Muchowski PJ (2003). "Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein". Science. 302 (5651): 1769–72. Bibcode:2003Sci...302.1769W. doi:10.1126/science.1090389. PMID 14657499. S2CID 43221047.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.