FKBP8

FK506-binding protein 8 is a protein that in humans is encoded by the FKBP8 gene.

FKBP8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2AWG, 2D9F, 2F2D, 2MF9, 3EY6
Identifiers
Aliases	FKBP8, FKBP38, FKBPr38, FK506 binding protein 8, FKBP prolyl isomerase 8
External IDs	OMIM: 604840; MGI: 1341070; HomoloGene: 7720; GeneCards: FKBP8; OMA:FKBP8 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.11 Start 18,531,751 bp End 18,544,077 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 B3.3 Start 70,980,374 bp End 70,987,978 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe right testis left testis right hemisphere of cerebellum anterior pituitary C1 segment cingulate gyrus anterior cingulate cortex muscle layer of sigmoid colon right uterine tube Top expressed in superior frontal gyrus dentate gyrus of hippocampal formation granule cell primary visual cortex spermatocyte neural layer of retina granulocyte lip perirhinal cortex entorhinal cortex ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function FK506 binding isomerase activity peptidyl-prolyl cis-trans isomerase activity metal ion binding protein binding identical protein binding disordered domain specific binding Cellular component integral component of membrane membrane mitochondrial membranes integral component of endoplasmic reticulum membrane mitochondrial envelope mitochondrion endoplasmic reticulum cytosol cytoplasm protein-containing complex Biological process apoptotic process intracellular signal transduction multicellular organism growth cell fate specification negative regulation of apoptotic process regulation of BMP signaling pathway 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 negative regulation of protein phosphorylation Sources:Amigo / QuickGO
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 NP_036313 NP_001295302.1 NP_001104536 NP_001186560 NP_034353 Location (UCSC) Chr 19: 18.53 – 18.54 Mb Chr 8: 70.98 – 70.99 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Further reading

• 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. S2CID 23007045.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 11653096.
• 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. Bibcode:2004Natur.428..529G. 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. S2CID 8203913.
• 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. S2CID 7200157.
• 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. hdl:10356/95126. PMID 15733859. S2CID 19114701.
• 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. S2CID 12995306.
• 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. hdl:10356/94816. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. S2CID 69278.
• 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.