APBB1

Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)
PDB rendering based on 2e45.
Available structures PDB 2E45, 2HO2, 2IDH, 2OEI, 3D8D, 3D8E, 3D8F, 3DXC, 3DXD, 3DXE
Identifiers
Symbols	APBB1; FE65; MGC:9072; RIR
External IDs	OMIM: 602709 MGI: 107765 HomoloGene: 898 GeneCards: APBB1 Gene
Gene Ontology Molecular function • beta-amyloid binding • beta-amyloid binding • chromatin binding • protein binding • transcription factor binding • histone binding • proline-rich region binding Cellular component • nucleus • nucleus • cytoplasm • plasma membrane • nuclear speck • lamellipodium • growth cone • synapse Biological process • regulation of transcription, DNA-dependent • response to DNA damage stimulus • cell cycle arrest • signal transduction • axonogenesis • chromatin modification • negative regulation of cell growth • positive regulation of apoptotic process • histone H4 acetylation • negative regulation of S phase of mitotic cell cycle • positive regulation of transcription, DNA-dependent • negative regulation of thymidylate synthase biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	322	11785
Ensembl	ENSG00000166313	ENSMUSG00000037032
UniProt	O00213	Q9QXJ1
RefSeq (mRNA)	NM_001164.2	NM_001253885.1
RefSeq (protein)	NP_001155.1	NP_001240814.1
Location (UCSC)	Chr 11: 6.42 – 6.44 Mb	Chr 7: 112.71 – 112.72 Mb
PubMed search	[1]	[2]

Amyloid beta A4 precursor protein-binding family B member 1 is a protein that in humans is encoded by the APBB1 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.

Interactions

APBB1 has been shown to interact with APLP2, TFCP2, LRP1 and Amyloid precursor protein.

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. doi:10.1016/S0014-5793(98)00941-7. PMID 9738440. 
• 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. doi:10.1097/00002281-200311000-00009. 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. PMC 231626. PMID 8887653. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231626. 
• 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. doi:10.1074/jbc.272.10.6399. PMID 9045663. 
• 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. doi:10.1074/jbc.272.52.32869. PMID 9407065. 
• 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) (Pt 1): 513–9. PMC 1219167. PMID 9461550. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219167. 
• 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. doi:10.1007/s003359900800. PMID 9585438. 
• 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. doi:10.1074/jbc.273.32.20128. PMID 9685356. 
• 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. doi:10.1007/s004390050820. PMID 9799084. 
• 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. doi:10.1074/jbc.273.50.33556. PMID 9837937. 
• 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. doi:10.1074/jbc.274.12.7952. PMID 10075692. 
• 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. doi:10.1002/(SICI)1097-4547(19991201)58:5<632::AID-JNR4>3.0.CO;2-P. PMID 10561691. 
• 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. 
• 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. 
• 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. doi:10.1097/00001756-200011090-00041. PMID 11095528. 
• 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. 
• 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.