APBB2

APBB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WGU, 2ROZ, 2YSZ, 2YT0, 2YT1
Identifiers
Aliases	APBB2 , FE65L, FE65L1, amyloid beta precursor protein binding family B member 2
External IDs	OMIM: 602710; MGI: 108405; HomoloGene: 32079; GeneCards: APBB2; OMA:APBB2 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4p14-p13 Start 40,810,027 bp [1] End 41,216,714 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 C3.1 Start 66,456,046 bp [2] End 66,776,127 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell Achilles tendon sural nerve dorsal motor nucleus of vagus nerve inferior olivary nucleus tendon of biceps brachii internal globus pallidus ventricular zone corpus callosum tibia Top expressed in genital tubercle lateral geniculate nucleus renal corpuscle medial dorsal nucleus pontine nuclei ankle triceps brachii muscle deep cerebellar nuclei lateral septal nucleus medial geniculate nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding transcription factor binding amyloid-beta binding Cellular component growth cone membrane cytoplasm lamellipodium synapse nucleus Biological process positive regulation of apoptotic process intracellular signal transduction negative regulation of cell growth negative regulation of apoptotic process extracellular matrix organization axon guidance neuron migration regulation of transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 323 11787 Ensembl ENSG00000163697 ENSMUSG00000029207 UniProt Q92870 Q9DBR4 RefSeq (mRNA) NM_001166050 NM_001166051 NM_001166052 NM_001166053 NM_001166054 NM_004307 NM_173075 NM_001330656 NM_001330658 NM_001201413 NM_001201414 NM_001201415 NM_001201416 NM_009686 NM_001310626 RefSeq (protein) NP_001159522 NP_001159523 NP_001159524 NP_001159525 NP_001159526 NP_001317585 NP_001317587 NP_004298 NP_775098 NP_001188342 NP_001188343 NP_001188344 NP_001188345 NP_001297555 NP_033816 Location (UCSC) Chr 4: 40.81 – 41.22 Mb Chr 5: 66.46 – 66.78 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Amyloid beta A4 precursor protein-binding family B member 2 is a protein that in humans is encoded by the APBB2 gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000163697 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029207 – 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. 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.
6. 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. S2CID   31066473.
7. "Entrez Gene: APBB2 amyloid beta (A4) precursor protein-binding, family B, member 2 (Fe65-like)".

External links

• Human APBB2 genome location and APBB2 gene details page in the UCSC Genome Browser .

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. Bibcode:1996PNAS...9310832G. 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. Bibcode:2002PNAS...9916899M. 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. S2CID   28343972.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.