FKBP8

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2AWG, 2D9F, 2F2D, 2MF9, 3EY6

Identifiers

Aliases

FKBP8, FKBP38, FKBPr38, FK506 binding protein 8

External IDs

MGI: 1341070 HomoloGene: 7720 GeneCards: FKBP8

Gene ontology
Molecular function	• FK506 binding • isomerase activity • peptidyl-prolyl cis-trans isomerase activity • metal ion binding • protein binding • identical protein binding
Cellular component	• integral component of membrane • endoplasmic reticulum membrane • membrane • mitochondrial membrane • integral component of endoplasmic reticulum membrane • mitochondrion • mitochondrial envelope
Biological process	• apoptotic process • intracellular signal transduction • multicellular organism growth • cell fate specification • negative regulation of apoptotic process • regulation of BMP signaling pathway • protein folding • neural tube development • positive regulation of BMP signaling pathway • regulation of gene expression • smoothened signaling pathway • camera-type eye development • dorsal/ventral neural tube patterning • viral process • dorsal/ventral pattern formation • chaperone-mediated protein folding • protein peptidyl-prolyl isomerization
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


23770


14232

Ensembl


ENSG00000105701


ENSMUSG00000019428

UniProt


Q14318


O35465

RefSeq (mRNA)


NM_001308373 NM_012181


NM_001111066 NM_001199631 NM_010223

RefSeq (protein)


NP_001295302.1 NP_036313.3 NP_001295302.1


NP_001104536.1 NP_001186560.1 NP_034353.2

Location (UCSC)

Chr 19: 18.53 – 18.54 Mb

Chr 8: 70.53 – 70.54 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

FK506-binding protein 8 is a protein that in humans is encoded by the FKBP8 gene.^[3]^[4]

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. Unlike the other members of the family, this encoded protein does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Lam E, Martin M, Wiederrecht G (Sep 1995). "Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs". Gene. 160 (2): 297–302. doi:10.1016/0378-1119(95)00216-S. PMID 7543869.
1 2 "Entrez Gene: FKBP8 FK506 binding protein 8, 38kDa".

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Pedersen KM, Finsen B, Celis JE, Jensen NA (1999). "muFKBP38: a novel murine immunophilin homolog differentially expressed in Schwannoma cells and central nervous system neurons in vivo.". Electrophoresis. 20 (2): 249–55. doi:10.1002/(SICI)1522-2683(19990201)20:2<249::AID-ELPS249>3.0.CO;2-F. PMID 10197430.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Shirane M, Nakayama KI (2003). "Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis.". Nat. Cell Biol. 5 (1): 28–37. doi:10.1038/ncb894. PMID 12510191.
Rosner M, Hofer K, Kubista M, Hengstschläger M (2003). "Cell size regulation by the human TSC tumor suppressor proteins depends on PI3K and FKBP38.". Oncogene. 22 (31): 4786–98. doi:10.1038/sj.onc.1206776. PMID 12894220.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature. 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Bulgakov OV, Eggenschwiler JT, Hong DH, et al. (2004). "FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural tissues.". Development. 131 (9): 2149–59. doi:10.1242/dev.01122. PMID 15105374.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Kang CB, Tai J, Chia J, Yoon HS (2005). "The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38).". FEBS Lett. 579 (6): 1469–76. doi:10.1016/j.febslet.2005.01.053. PMID 15733859.
Weiwad M, Edlich F, Erdmann F, et al. (2005). "A reassessment of the inhibitory capacity of human FKBP38 on calcineurin.". FEBS Lett. 579 (7): 1591–6. doi:10.1016/j.febslet.2004.12.098. PMID 15757646.
Edlich F, Weiwad M, Erdmann F, et al. (2005). "Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin.". EMBO J. 24 (14): 2688–99. doi:10.1038/sj.emboj.7600739. PMC 1176465. PMID 15990872.
Kang CB, Feng L, Chia J, Yoon HS (2005). "Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2.". Biochem. Biophys. Res. Commun. 337 (1): 30–8. doi:10.1016/j.bbrc.2005.09.023. PMID 16176796.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer.". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.

PDB gallery

2awg: Structure of the PPIase domain of the Human FK506-binding protein 8

2d9f: Solution structure of RUH-047, an FKBP domain from human cDNA

2f2d: Solution structure of the FK506-binding domain of human FKBP38

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)

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FKBP8

References

Further reading