FKBP2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2PBC, 4NNR

Identifiers

Aliases

FKBP2, FKBP-13, PPIase, FK506 binding protein 2

External IDs

MGI: 95542 HomoloGene: 40604 GeneCards: FKBP2

Gene ontology
Molecular function	• FK506 binding • protein binding • isomerase activity • peptidyl-prolyl cis-trans isomerase activity
Cellular component	• extracellular exosome • endoplasmic reticulum membrane • membrane • endoplasmic reticulum
Biological process	• protein folding • chaperone-mediated protein folding • protein peptidyl-prolyl isomerization
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

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

RefSeq (protein)


NP_001128680.1 NP_004461.2 NP_476433.1


NP_001159840.1 NP_032046.1

Location (UCSC)

Chr 11: 64.24 – 64.24 Mb

Chr 19: 6.98 – 6.98 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

FK506-binding protein 2 is a protein that in humans is encoded by the FKBP2 gene.^[3]^[4]

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.^[4]

Interactions

FKBP2 has been shown to interact with ARFGEF1^[5] and EPB41L2.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Jin YJ, Albers MW, Lane WS, Bierer BE, Schreiber SL, Burakoff SJ (Sep 1991). "Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13". Proc. Natl. Acad. Sci. U.S.A. 88 (15): 6677–81. doi:10.1073/pnas.88.15.6677. PMC 52151. PMID 1713687.
1 2 "Entrez Gene: FKBP2 FK506 binding protein 2, 13kDa".
↑ Padilla PI, Chang MJ, Pacheco-Rodriguez G, Adamik R, Moss J, Vaughan M (Mar 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. doi:10.1073/pnas.2628047100. PMC 151339. PMID 12606707.
↑ Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (Apr 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.

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. 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. doi:10.1126/science.1090389. PMID 14657499.
Won J, Kim M, Yi YW, Kim YH, Jung N, Kim TK (2005). "A magnetic nanoprobe technology for detecting molecular interactions in live cells". Science. 309 (5731): 121–5. doi:10.1126/science.1112869. PMID 15994554. (Retracted. If this is intentional, please replace {{Retracted}} with {{Retracted|intentional=yes}}.)
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. doi:10.1038/nature04209. PMID 16189514.
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.

PDB gallery

2pbc: FK506-binding protein 2

Isomerases: geometric (EC 5.2)

5.2.1	FKBP: FKBP1A FKBP1B FKBP2 FKBP3 FKBP5 FKBP6 FKBP8 FKBP9 FKBP10 FKBP52 FKBPL other: Cyclophilin Parvulin Prolyl isomerase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia - version of the 11/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

FKBP2

Function

Interactions

References

Further reading