APBA3

APBA3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2YT7, 2YT8
Identifiers
Aliases	APBA3, MGC:15815, X11L2, mint3, amyloid beta precursor protein binding family A member 3
External IDs	MGI: 1888527 HomoloGene: 3591 GeneCards: APBA3
Gene ontology Molecular function • enzyme binding • enzyme inhibitor activity • beta-amyloid binding • protein binding Cellular component • cytoplasm • perinuclear region of cytoplasm Biological process • regulation of gene expression • protein transport • regulation of catalytic activity • negative regulation of catalytic activity • in utero embryonic development • transport • chemical synaptic transmission 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_004877.1	NP_061228.1
Location (UCSC)	Chr 19: 3.75 – 3.76 Mb	Chr 10: 81.27 – 81.27 Mb
PubMed search	[1]	[2]
Wikidata

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Amyloid beta A4 precursor protein-binding family A member 3 is a protein that in humans is encoded by the APBA3 gene.^[3][4]

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.^[4]

Interactions

APBA3 has been shown to interact with Amyloid precursor protein.^[3][5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: APBA3 amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2)".
5. 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.