APBB1

Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)
PDB rendering based on 2e45.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2e45​
Identifiers
Symbols	APBB1 ; FE65; MGC:9072; RIR
External IDs	Template:OMIM5 Template:MGI HomoloGene: 898
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65), also known as APBB1, is a human gene.

The protein encoded by this gene is a member of the Fe65 protein family. It is an adaptor protein localized in the nucleus. It interacts with the Alzheimer's disease amyloid precursor protein (APP), transcription factor CP2/LSF/LBP1 and the low-density lipoprotein receptor-related protein. APP functions as a cytosolic anchoring site that can prevent the gene product's nuclear translocation. This encoded protein could play an important role in the pathogenesis of Alzheimer's disease. It is thought to regulate transcription. Also it is observed to block cell cycle progression by downregulating thymidylate synthase expression. Multiple alternatively spliced transcript variants have been described for this gene but some of their full length sequence is not known.

Further reading

• Russo T, Faraonio R, Minopoli G; et al. (1998). "Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein". FEBS Lett. 434 (1–2): 1–7. PMID 9738440.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Askanas V, Engel WK (2004). "Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging". Current opinion in rheumatology. 15 (6): 737–44. PMID 14569203.
• Borg JP, Ooi J, Levy E, Margolis B (1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. PMID 8887653.CS1 maint: Multiple names: authors list (link)
• Bressler SL, Gray MD, Sopher BL; et al. (1997). "cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein". Hum. Mol. Genet. 5 (10): 1589–98. PMID 8894693.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McLoughlin DM, Miller CC (1997). "The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system". FEBS Lett. 397 (2–3): 197–200. PMID 8955346.
• Zambrano N, Buxbaum JD, Minopoli G; et al. (1997). "Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins". J. Biol. Chem. 272 (10): 6399–405. PMID 9045663.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ermekova KS, Zambrano N, Linn H; et al. (1998). "The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled". J. Biol. Chem. 272 (52): 32869–77. PMID 9407065.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Duilio A, Faraonio R, Minopoli G; et al. (1998). "Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein". Biochem. J. 330 ( Pt 1): 513–9. PMID 9461550.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Blanco G, Irving NG, Brown SD; et al. (1998). "Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein". Mamm. Genome. 9 (6): 473–5. PMID 9585438.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zambrano N, Minopoli G, de Candia P, Russo T (1998). "The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1". J. Biol. Chem. 273 (32): 20128–33. PMID 9685356.CS1 maint: Multiple names: authors list (link)
• Hu Q, Kukull WA, Bressler SL; et al. (1998). "The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type". Hum. Genet. 103 (3): 295–303. PMID 9799084.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Trommsdorff M, Borg JP, Margolis B, Herz J (1999). "Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein". J. Biol. Chem. 273 (50): 33556–60. PMID 9837937.CS1 maint: Multiple names: authors list (link)
• Sabo SL, Lanier LM, Ikin AF; et al. (1999). "Regulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding protein". J. Biol. Chem. 274 (12): 7952–7. PMID 10075692.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hu Q, Hearn MG, Jin LW; et al. (2000). "Alternatively spliced isoforms of FE65 serve as neuron-specific and non-neuronal markers". J. Neurosci. Res. 58 (5): 632–40. PMID 10561691.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lambrechts A, Kwiatkowski AV, Lanier LM; et al. (2000). "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains". J. Biol. Chem. 275 (46): 36143–51. doi:10.1074/jbc.M006274200. PMID 10945997.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Minopoli G, de Candia P, Bonetti A; et al. (2001). "The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation". J. Biol. Chem. 276 (9): 6545–50. doi:10.1074/jbc.M007340200. PMID 11085987.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lau KF, McLoughlin DM, Standen CL; et al. (2001). "Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein". Neuroreport. 11 (16): 3607–10. PMID 11095528.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McLoughlin DM, Standen CL, Lau KF; et al. (2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zambrano N, Bruni P, Minopoli G; et al. (2001). "The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene". J. Biol. Chem. 276 (23): 19787–92. doi:10.1074/jbc.M100792200. PMID 11279131.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)