FKBP10

Summary

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

FKBP10
Identifiers
AliasesFKBP10, FKBP65, OI11, OI6, PPIASE, hFKBP65, BRKS1, FK506 binding protein 10, FKBP prolyl isomerase 10
External IDsOMIM: 607063 MGI: 104769 HomoloGene: 7718 GeneCards: FKBP10
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_021939

NM_001163481
NM_010221

RefSeq (protein)

NP_068758

NP_001156953
NP_034351

Location (UCSC)Chr 17: 41.81 – 41.82 MbChr 11: 100.31 – 100.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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 edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141756 - Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: FKBP10 FK506 binding protein 10, 65 kDa".

Further reading edit

  • 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.