APBA3

Amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2), also known as APBA3, is a human gene.cite web | title = Entrez Gene: APBA3 amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9546| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a member of the X11 protein family. It is an adapter protein that interacts with the Alzheimer's disease amyloid precursor protein. This gene product is believed to be involved in signal transduction processes. This gene is a candidate gene for Alzheimer's disease.cite web | title = Entrez Gene: APBA3 amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9546| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Kuriyan J, Cowburn D |title=Modular peptide recognition domains in eukaryotic signaling. |journal=Annual review of biophysics and biomolecular structure |volume=26 |issue= |pages= 259–88 |year= 1997 |pmid= 9241420 |doi= 10.1146/annurev.biophys.26.1.259
*cite journal | author=Morishima-Kawashima M, Ihara Y |title= [Recent advances in Alzheimer's disease] |journal=Seikagaku |volume=73 |issue= 11 |pages= 1297–307 |year= 2002 |pmid= 11831025 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Okamoto M, Südhof TC |title=Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2. |journal=Eur. J. Cell Biol. |volume=77 |issue= 3 |pages= 161–5 |year= 1999 |pmid= 9860131 |doi=
*cite journal | author=Tanahashi H, Tabira T |title=X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein. |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 3 |pages= 663–7 |year= 1999 |pmid= 10049767 |doi= 10.1006/bbrc.1999.0265
*cite journal | author=Tanahashi H, Tabira T |title=Genomic organization of the human X11L2 gene (APBA3), a third member of the X11 protein family interacting with Alzheimer's beta-amyloid precursor protein. |journal=Neuroreport |volume=10 |issue= 12 |pages= 2575–8 |year= 1999 |pmid= 10574372 |doi=
*cite journal | author=Okamoto M, Nakajima Y, Matsuyama T, Sugita M |title=Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane. |journal=Neuroscience |volume=104 |issue= 3 |pages= 653–65 |year= 2001 |pmid= 11440799 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Wang P, Wang X, Pei D |title=Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20461–70 |year= 2004 |pmid= 14990567 |doi= 10.1074/jbc.M400264200
*cite journal | author=Grimwood J, Gordon LA, Olsen A, "et al." |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Malmberg EK, Andersson CX, Gentzsch M, "et al." |title=Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold protein PDZK1 and vesicle coat protein Mint3. |journal=J. Cell. Sci. |volume=117 |issue= Pt 23 |pages= 5535–41 |year= 2005 |pmid= 15494376 |doi= 10.1242/jcs.01472

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