FKBP10

FKBP10

Identifiers

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]
Band	17q21.2	End	41,823,213 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 D\|11 63.47 cM	Start	100,306,523 bp^[2]
Band	11 D\|11 63.47 cM	End	100,315,650 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

stromal cell of endometrium

ascending aorta

anterior pituitary

right coronary artery

canal of the cervix

left coronary artery

left uterine tube

gallbladder

right adrenal gland

smooth muscle tissue

Top expressed in

calvaria

internal carotid artery

external carotid artery

body of femur

fossa

molar

vas deferens

dermis

condyle

ascending aorta

More reference expression data

BioGPS


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: 100.31 – 100.32 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000141756 - Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b "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.

v t e Isomerases: geometric (EC 5.2)
5.2.1	FKBP: FKBP1A FKBP1B FKBP2 FKBP3 FKBP4 FKBP5 FKBP6 FKBP8 FKBP9 FKBP10 FKBPL other: Cyclophilin Parvulin Prolyl isomerase

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)

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This page was last edited on 13 October 2022, at 20:34

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References

Further reading