APBB2

Amyloid beta (A4) precursor protein-binding, family B, member 2
PDB rendering based on 1wgu.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1wgu​
Identifiers
Symbols	APBB2 ; FE65L; FE65L1
External IDs	OMIM: 602710 MGI: 108405 HomoloGene: 32079 GeneCards: APBB2 Gene
Gene ontology Molecular function • beta-amyloid binding • protein binding • transcription factor binding Cellular component • nucleus • cytoplasm • membrane • lamellipodium • growth cone • synapse Biological process • neuron migration • regulation of transcription, DNA-templated • cell cycle arrest • axon guidance • extracellular matrix organization • negative regulation of cell growth • intracellular signal transduction • positive regulation of apoptotic process • negative regulation of apoptotic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	323	11787
Ensembl	ENSG00000163697	ENSMUSG00000029207
UniProt	Q92870	Q9DBR4
RefSeq (mRNA)	NM_001166050	NM_001201413
RefSeq (protein)	NP_001159522	NP_001188342
Location (UCSC)	Chr 4: 40.81 – 41.22 Mb	Chr 5: 66.3 – 66.62 Mb
PubMed search

Amyloid beta A4 precursor protein-binding family B member 2 is a protein that in humans is encoded by the APBB2 gene.^[1][2][3]

The protein encoded by this gene interacts with the cytoplasmic domains of amyloid beta (A4) precursor protein and amyloid beta (A4) precursor-like protein 2. This protein contains two phosphotyrosine binding (PTB) domains, which are thought to function in signal transduction.^[3]

References

1. McLoughlin DM, Miller CC (Jan 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. doi:10.1016/S0014-5793(96)01128-3. PMID 8955346.
2. Blanco G, Irving NG, Brown SD, Miller CC, McLoughlin DM (Jun 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.
3. "Entrez Gene: APBB2 amyloid beta (A4) precursor protein-binding, family B, member 2 (Fe65-like)".

Further reading

• Guénette SY, Chen J, Jondro PD, Tanzi RE (1996). "Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein". Proc. Natl. Acad. Sci. U.S.A. 93 (20): 10832–7. doi:10.1073/pnas.93.20.10832. PMC 38241. PMID 8855266.
• Bruni P, Minopoli G, Brancaccio T; et al. (2002). "Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression". J. Biol. Chem. 277 (38): 35481–8. doi:10.1074/jbc.M205227200. PMID 12089154.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chang Y, Tesco G, Jeong WJ; et al. (2004). "Generation of the beta-amyloid peptide and the amyloid precursor protein C-terminal fragment gamma are potentiated by FE65L1". J. Biol. Chem. 278 (51): 51100–7. doi:10.1074/jbc.M309561200. PMID 14527950.
• 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.
• Li Y, Hollingworth P, Moore P; et al. (2006). "Genetic association of the APP binding protein 2 gene (APBB2) with late onset Alzheimer disease". Hum. Mutat. 25 (3): 270–7. doi:10.1002/humu.20138. PMID 15714520.
• Lange A, Thon L, Mathieu S, Adam D (2005). "The apoptosis inhibitory domain of FE65-like protein 1 regulates both apoptotic and caspase-independent programmed cell death mediated by tumor necrosis factor". Biochem. Biophys. Res. Commun. 335 (2): 575–83. doi:10.1016/j.bbrc.2005.07.125. PMID 16083851.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Hong Q, Hsu LJ, Schultz L; et al. (2007). "Zfra affects TNF-mediated cell death by interacting with death domain protein TRADD and negatively regulates the activation of NF-κB, JNK1, p53 and WOX1 during stress response". BMC Mol. Biol. 8: 50. doi:10.1186/1471-2199-8-50. PMC 1904229. PMID 17567906.