APBA1

Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene.

APBA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AQC, 1U37, 1U38, 1U39, 1U3B, 1X11, 1X45, 1Y7N
Identifiers
Aliases	APBA1, D9S411E, LIN10, MINT1, X11, X11A, X11ALPHA, amyloid beta precursor protein binding family A member 1
External IDs	OMIM: 602414; MGI: 1860297; HomoloGene: 897; GeneCards: APBA1; OMA:APBA1 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q21.12 Start 69,427,532 bp End 69,672,371 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 B Start 23,736,251 bp End 23,926,960 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in superior frontal gyrus prefrontal cortex right frontal lobe temporal lobe amygdala anterior cingulate cortex dorsolateral prefrontal cortex hypothalamus Brodmann area 9 nucleus accumbens Top expressed in habenula ventral tegmental area visual cortex primary visual cortex dentate gyrus of hippocampal formation granule cell pontine nuclei inferior colliculi central gray substance of midbrain medial dorsal nucleus subiculum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function amyloid-beta binding protein binding Cellular component cytoplasm cytosol membrane synaptic vesicle perinuclear region of cytoplasm nucleus neuron projection Golgi apparatus presynaptic active zone membrane Schaffer collateral - CA1 synapse glutamatergic synapse plasma membrane dendritic spine synapse Biological process locomotory behavior multicellular organism growth axo-dendritic transport in utero embryonic development nervous system development glutamate secretion cell adhesion regulation of gene expression protein transport intracellular protein transport gamma-aminobutyric acid secretion neurotransmitter secretion chemical synaptic transmission protein-containing complex assembly regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 320 319924 Ensembl ENSG00000107282 ENSG00000276497 ENSMUSG00000024897 UniProt Q02410 B2RUJ5 RefSeq (mRNA) NM_001163 NM_177034 RefSeq (protein) NP_001154 NP_796008 Location (UCSC) Chr 9: 69.43 – 69.67 Mb Chr 19: 23.74 – 23.93 Mb PubMed search
Wikidata
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Function

The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.

Interactions

APBA1 has been shown to interact with KCNJ12, CCS, CASK and Amyloid precursor protein.

Further reading

• van der Geer P, Pawson T (1995). "The PTB domain: a new protein module implicated in signal transduction". Trends Biochem. Sci. 20 (7): 277–80. doi:10.1016/S0968-0004(00)89043-X. PMID 7545337.
• Chen WJ, Goldstein JL, Brown MS (1990). "NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor". J. Biol. Chem. 265 (6): 3116–23. doi:10.1016/S0021-9258(19)39742-X. PMID 1968060.
• Borg JP, Ooi J, Levy E, Margolis B (1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. doi:10.1128/mcb.16.11.6229. PMC 231626. PMID 8887653.
• Zhang Z, Lee CH, Mandiyan V, Borg JP, Margolis B, Schlessinger J, Kuriyan J (1997). "Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain". EMBO J. 16 (20): 6141–50. doi:10.1093/emboj/16.20.6141. PMC 1326298. PMID 9321393.
• Okamoto M, Südhof TC (1998). "Mints, Munc18-interacting proteins in synaptic vesicle exocytosis". J. Biol. Chem. 272 (50): 31459–64. doi:10.1074/jbc.272.50.31459. PMID 9395480.
• Blanco G, Irving NG, Brown SD, Miller CC, McLoughlin DM (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.
• Borg JP, Yang Y, De Taddéo-Borg M, Margolis B, Turner RS (1998). "The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion". J. Biol. Chem. 273 (24): 14761–6. doi:10.1074/jbc.273.24.14761. PMID 9614075.
• Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain". Cell. 94 (6): 773–82. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324. S2CID 12465062.
• Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B (1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620.
• Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B (1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. doi:10.1523/JNEUROSCI.19-04-01307.1999. PMC 6786035. PMID 9952408.
• Maximov A, Südhof TC, Bezprozvanny I (1999). "Association of neuronal calcium channels with modular adaptor proteins". J. Biol. Chem. 274 (35): 24453–6. doi:10.1074/jbc.274.35.24453. PMID 10455105.
• Mueller HT, Borg JP, Margolis B, Turner RS (2001). "Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains". J. Biol. Chem. 275 (50): 39302–6. doi:10.1074/jbc.M008453200. PMID 11010978.
• Biederer T, Südhof TC (2001). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–6. doi:10.1074/jbc.C000656200. PMID 11036064.
• Lau KF, McLoughlin DM, Standen C, Miller CC (2001). "X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains". Mol. Cell. Neurosci. 16 (5): 557–65. doi:10.1006/mcne.2000.0898. PMID 11083918. S2CID 54389955.
• McLoughlin DM, Standen CL, Lau KF, Ackerley S, Bartnikas TP, Gitlin JD, Miller CC (2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.
• Bécamel C, Alonso G, Galéotti N, Demey E, Jouin P, Ullmer C, Dumuis A, Bockaert J, Marin P (2002). "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332–42. doi:10.1093/emboj/21.10.2332. PMC 126011. PMID 12006486.
• Ho CS, Marinescu V, Steinhilb ML, Gaut JR, Turner RS, Stuenkel EL (2002). "Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism". J. Biol. Chem. 277 (30): 27021–8. doi:10.1074/jbc.M201823200. PMID 12016213.

External links

• Human APBA1 genome location and APBA1 gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: Q02410 (Amyloid-beta A4 precursor protein-binding family A member 1) at the PDBe-KB.