APBA2

Amyloid beta A4 precursor protein-binding family A member 2 is a protein that in humans is encoded by the APBA2 gene.[5][6]

APBA2
Identifiers
Aliases	APBA2, D15S1518E, HsT16821, LIN-10, MGC:14091, MINT2, X11-BETA, X11L, amyloid beta precursor protein binding family A member 2
External IDs	OMIM: 602712 MGI: 1261791 HomoloGene: 4021 GeneCards: APBA2
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q13.1 Start 28,884,483 bp[1] End 29,118,315 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 C|7 34.65 cM Start 64,501,706 bp[2] End 64,753,878 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • amyloid-beta binding • GO:0001948 protein binding • identical protein binding Cellular component • cell membrane • synaptic vesicle • Schaffer collateral - CA1 synapse • cytoplasm • dendritic spine • synapse Biological process • regulation of gene expression • protein transport • in utero embryonic development • locomotory behavior • nervous system development • multicellular organism growth • chemical synaptic transmission • regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	321	11784
Ensembl	ENSG00000034053 ENSG00000276495	ENSMUSG00000030519
UniProt	Q99767	P98084
RefSeq (mRNA)	NM_001130414 NM_005503 NM_001353788 NM_001353789 NM_001353790 NM_001353791 NM_001353792 NM_001353793 NM_001353794 NM_001353795 NM_001353796 NM_001353797 NM_001379685	NM_001291166 NM_001291167 NM_007461
RefSeq (protein)	NP_001123886 NP_005494 NP_001340717 NP_001340718 NP_001340719 NP_001340720 NP_001340721 NP_001340722 NP_001340723 NP_001340724 NP_001340725 NP_001340726 NP_001366614	NP_001278095 NP_001278096 NP_031487
Location (UCSC)	Chr 15: 28.88 – 29.12 Mb	Chr 7: 64.5 – 64.75 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

APBA2 has been shown to interact with CLSTN1,[7][8] RELA[9] and Amyloid precursor protein.[7][10][11]

References

1. ENSG00000276495 GRCh38: Ensembl release 89: ENSG00000034053, ENSG00000276495 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030519 - 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 (January 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. "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)".
7. Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (December 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". J. Biol. Chem. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.
8. Araki Y, Miyagi N, Kato N, Yoshida T, Wada S, Nishimura M, Komano H, Yamamoto T, De Strooper B, Yamamoto K, Suzuki T (June 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". J. Biol. Chem. 279 (23): 24343–54. doi:10.1074/jbc.M401925200. PMID 15037614.
9. Tomita S, Fujita T, Kirino Y, Suzuki T (April 2000). "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. 275 (17): 13056–60. doi:10.1074/jbc.C000019200. PMID 10777610.
10. Biederer T, Cao X, Südhof TC, Liu X (September 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. doi:10.1523/JNEUROSCI.22-17-07340.2002. PMID 12196555.
11. Tomita S, Ozaki T, Taru H, Oguchi S, Takeda S, Yagi Y, Sakiyama S, Kirino Y, Suzuki T (January 1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. PMID 9890987.

External links

• Human APBA2 genome location and APBA2 gene details page in the UCSC Genome Browser.

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.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• 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.
• 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.
• 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.
• 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.
• Tomita S, Ozaki T, Taru H, Oguchi S, Takeda S, Yagi Y, Sakiyama S, Kirino Y, Suzuki T (1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. PMID 9890987.
• McLoughlin DM, Irving NG, Brownlees J, Brion JP, Leroy K, Miller CC (1999). "Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease". Eur. J. Neurosci. 11 (6): 1988–94. doi:10.1046/j.1460-9568.1999.00610.x. PMID 10336668.
• Tomita S, Fujita T, Kirino Y, Suzuki T (2000). "PDZ domain-dependent suppression of NF-kappaB/p65-induced Abeta42 production by a neuron-specific X11-like protein". J. Biol. Chem. 275 (17): 13056–60. doi:10.1074/jbc.C000019200. PMID 10777610.
• Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". J. Biol. Chem. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
• Lee DS, Tomita S, Kirino Y, Suzuki T (2000). "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein". J. Biol. Chem. 275 (30): 23134–8. doi:10.1074/jbc.C000302200. PMID 10833507.
• 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.
• Sutcliffe JS, Han MK, Amin T, Kesterson RA, Nurmi EL (2003). "Partial duplication of the APBA2 gene in chromosome 15q13 corresponds to duplicon structures". BMC Genomics. 4 (1): 15. doi:10.1186/1471-2164-4-15. PMC 156605. PMID 12720574.
• Sumioka A, Imoto S, Martins RN, Kirino Y, Suzuki T (2003). "XB51 isoforms mediate Alzheimer's beta-amyloid peptide production by X11L (X11-like protein)-dependent and -independent mechanisms". Biochem. J. 374 (Pt 1): 261–8. doi:10.1042/BJ20030489. PMC 1223589. PMID 12780348.