FKBP10

FK506-binding protein 10 is a protein that in humans is encoded by the FKBP10 gene.[5][6][7]

FKBP10
Identifiers
Aliases	FKBP10, FKBP65, OI11, OI6, PPIASE, hFKBP65, BRKS1, FK506 binding protein 10, FKBP prolyl isomerase 10
External IDs	OMIM: 607063 MGI: 104769 HomoloGene: 7718 GeneCards: FKBP10
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.2 Start 41,812,680 bp[1] End 41,823,213 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 D|11 63.47 cM Start 100,415,697 bp[2] End 100,424,824 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • isomerase activity • peptidyl-prolyl cis-trans isomerase activity • metal ion binding • FK506 binding Cellular component • endoplasmic reticulum lumen • endoplasmic reticulum • cytoplasm • nucleolus Biological process • chaperone-mediated protein folding • histone peptidyl-prolyl isomerization • peptidyl-proline modification • protein peptidyl-prolyl isomerization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	60681	14230
Ensembl	ENSG00000141756	ENSMUSG00000001555
UniProt	Q96AY3	Q61576
RefSeq (mRNA)	NM_021939	NM_001163481 NM_010221
RefSeq (protein)	NP_068758	NP_001156953 NP_034351
Location (UCSC)	Chr 17: 41.81 – 41.82 Mb	Chr 11: 100.42 – 100.42 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase family. It is located in endoplasmic reticulum and acts as molecular chaperones. Two alternatively spliced variants, which encode different isoform, are reported.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000141756 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001555 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Patterson CE, Schaub T, Coleman EJ, Davis EC (Feb 2001). "Developmental Regulation of FKBP65: An ER-localized Extracellular Matrix Binding-Protein". Mol Biol Cell. 11 (11): 3925–35. doi:10.1091/mbc.11.11.3925. PMC 15047. PMID 11071917.
6. Ishikawa Y, Vranka J, Wirz J, Nagata K, Bachinger HP (Nov 2008). "The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens". J Biol Chem. 283 (46): 31584–90. doi:10.1074/jbc.M802535200. PMID 18786928.
7. "Entrez Gene: FKBP10 FK506 binding protein 10, 65 kDa".

Further reading

• Patterson CE, Gao J, Rooney AP, Davis EC (2002). "Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family". Genomics. 79 (6): 881–9. doi:10.1006/geno.2002.6777. PMID 12036304.
• 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.
• Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519. S2CID 581283.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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.
• Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
• Foster LJ, Rudich A, Talior I, et al. (2006). "Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC)". J. Proteome Res. 5 (1): 64–75. doi:10.1021/pr0502626. PMID 16396496.