APBA3

Amyloid beta (A4) precursor protein-binding, family A, member 3
Rendering based on PDB 2YT7​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2YT7​, 2YT8​
Identifiers
Symbols	APBA3 ; MGC:15815; X11L2; mint3
External IDs	OMIM: 604262 MGI: 1888527 HomoloGene: 3591 GeneCards: APBA3 Gene
Gene ontology Molecular function • beta-amyloid binding • enzyme inhibitor activity • protein binding • enzyme binding Cellular component • perinuclear region of cytoplasm Biological process • in utero embryonic development • synaptic transmission • regulation of gene expression • protein transport • negative regulation of catalytic activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9546	57267
Ensembl	ENSG00000011132	ENSMUSG00000004931
UniProt	O96018	O88888
RefSeq (mRNA)	NM_004886	NM_018758
RefSeq (protein)	NP_004877	NP_061228
Location (UCSC)	Chr 19: 3.75 – 3.76 Mb	Chr 10: 81.27 – 81.27 Mb
PubMed search

Amyloid beta A4 precursor protein-binding family A member 3 is a protein that in humans is encoded by the APBA3 gene.^[1][2]

Function

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.^[2]

Interactions

APBA3 has been shown to interact with Amyloid precursor protein.^[1][3]

References

1. Tanahashi H, Tabira T (Apr 1999). "X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein". Biochem Biophys Res Commun 255 (3): 663–7. doi:10.1006/bbrc.1999.0265. PMID 10049767.
2. "Entrez Gene: APBA3 amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2)".
3. Biederer T, Cao X, Südhof TC, Liu X (Sep 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. PMID 12196555.

Further reading

• Kuriyan J, Cowburn D (1997). "Modular peptide recognition domains in eukaryotic signaling". Annual Review of Biophysics and Biomolecular Structure 26: 259–88. doi:10.1146/annurev.biophys.26.1.259. PMID 9241420.
• Morishima-Kawashima M, Ihara Y (2002). "[Recent advances in Alzheimer's disease]". Seikagaku 73 (11): 1297–307. PMID 11831025.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Okamoto M, Südhof TC (1999). "Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2". Eur. J. Cell Biol. 77 (3): 161–5. doi:10.1016/s0171-9335(98)80103-9. PMID 9860131.
• Tanahashi H, Tabira T (1999). "Genomic organization of the human X11L2 gene (APBA3), a third member of the X11 protein family interacting with Alzheimer's beta-amyloid precursor protein". NeuroReport 10 (12): 2575–8. doi:10.1097/00001756-199908200-00025. PMID 10574372.
• Okamoto M, Nakajima Y, Matsuyama T, Sugita M (2001). "Amyloid precursor protein associates independently and collaboratively with PTB and PDZ domains of mint on vesicles and at cell membrane". Neuroscience 104 (3): 653–65. doi:10.1016/S0306-4522(01)00124-5. PMID 11440799.
• Wang P, Wang X, Pei D (2004). "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". J. Biol. Chem. 279 (19): 20461–70. doi:10.1074/jbc.M400264200. PMID 14990567.
• Malmberg EK, Andersson CX, Gentzsch M, Chen JH, Mengos A, Cui L, Hansson GC, Riordan JR (2005). "Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold protein PDZK1 and vesicle coat protein Mint3". J. Cell. Sci. 117 (Pt 23): 5535–41. doi:10.1242/jcs.01472. PMID 15494376.