APBB1

Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65), also known as APBB1, is a human gene.cite web | title = Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=322| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=322| accessdate = ]

References

Further reading

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

PBB_Controls
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