FKBP10

FKBP10
Identifiers
Aliases	FKBP10, FKBP65, OI11, OI6, PPIASE, hFKBP65, BRKS1, FK506 binding protein 10, FKBP prolyl isomerase 10
External IDs	OMIM: 607063; MGI: 104769; GeneCards: FKBP10
Enzyme activity
Gene location (Human)
Chr.	Chromosome 17 (human)
End	41,823,213 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	100,315,650 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; ascending aorta; ; Descending thoracic aorta; ; anterior pituitary; ; right coronary artery; ; right ovary; ; canal of the cervix; ; body of uterus; ; left ovary; ; left coronary artery;
	Top expressed in
	calvaria; ; internal carotid artery; ; external carotid artery; ; body of femur; ; fossa; ; molar; ; vas deferens; ; vestibular sensory epithelium; ; stroma of bone marrow; ; dermis;
	More reference expression data
	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
Databases	NCBI: entry; OMA: entry
	60681
	14230
	ENSG00000141756
	ENSMUSG00000001555
	Q96AY3
	Q61576
	NM_021939
	NM_001163481; NM_010221
	NP_068758
	NP_001156953; NP_034351
	Wikidata
View/Edit Human	View/Edit Mouse

FK506-binding protein 10 is a protein that in humans is encoded by the FKBP10 gene.

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.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000141756 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001555 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: FKBP10 FK506 binding protein 10, 65 kDa".

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. Bibcode:2002PNAS...9916899M. 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.

This article on a gene on human chromosome 17 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000141756 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid11071917-5] 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.

[pmid18786928-6] 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.

[entrez-7] 1 2 "Entrez Gene: FKBP10 FK506 binding protein 10, 65 kDa".

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

FKBP10

References

Further reading