FKBP10
| FKBP10 | |||||||||||||||||
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| Identifiers | |||||||||||||||||
| Aliases | FKBP10, FKBP65, OI11, OI6, PPIASE, hFKBP65, BRKS1, FK506 binding protein 10 | ||||||||||||||||
| External IDs | MGI: 104769 HomoloGene: 7718 GeneCards: FKBP10 | ||||||||||||||||
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| More reference expression data | |||||||||||||||||
| Orthologs | |||||||||||||||||
| Species | Human | Mouse | |||||||||||||||
| Entrez | |||||||||||||||||
| Ensembl | |||||||||||||||||
| UniProt | |||||||||||||||||
| RefSeq (mRNA) | |||||||||||||||||
| RefSeq (protein) | |||||||||||||||||
| Location (UCSC) | Chr 17: 41.81 – 41.82 Mb | Chr 11: 100.42 – 100.42 Mb | |||||||||||||||
| PubMed search | [1] | [2] | |||||||||||||||
| Wikidata | |||||||||||||||||
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FK506-binding protein 10 is a protein that in humans is encoded by the FKBP10 gene.[3][4][5]
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.[5]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ 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. PMC 15047
. PMID 11071917. doi:10.1091/mbc.11.11.3925. - ↑ 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. PMID 18786928. doi:10.1074/jbc.M802535200.
- 1 2 "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. PMID 12036304. doi:10.1006/geno.2002.6777.
- 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- 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. PMID 12754519. doi:10.1038/nbt827.
- 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. PMID 14702039. doi:10.1038/ng1285.
- 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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
- Won J, Kim M, Yi YW, et al. (2005). "A magnetic nanoprobe technology for detecting molecular interactions in live cells". Science. 309 (5731): 121–5. PMID 15994554. doi:10.1126/science.1112869. (Retracted. If this is intentional, please replace
{{Retracted}}with{{Retracted|intentional=yes}}.) - 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. PMID 16303743. doi:10.1093/dnares/12.2.117.
- 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. PMID 16396496. doi:10.1021/pr0502626.
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