APBA2

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; OMA:APBA2 - orthologs
Gene location (Human)
Chr.	Chromosome 15 (human)
End	29,118,315 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	64,753,878 bp
RNA expression pattern
	Top expressed in
	superior frontal gyrus; ; right hemisphere of cerebellum; ; primary visual cortex; ; prefrontal cortex; ; right frontal lobe; ; Brodmann area 9; ; anterior cingulate cortex; ; hippocampus proper; ; ganglionic eminence; ; C1 segment;
	Top expressed in
	dentate gyrus of hippocampal formation granule cell; ; primary visual cortex; ; superior frontal gyrus; ; perirhinal cortex; ; CA3 field; ; entorhinal cortex; ; cerebellar cortex; ; hippocampus proper; ; primary motor cortex; ; cingulate gyrus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	amyloid-beta binding; protein binding; identical protein binding;
Cellular component	plasma 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
	321
	11784
	ENSG00000034053; ENSG00000276495
	ENSMUSG00000030519
	Q99767
	P98084
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
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
	Wikidata
View/Edit Human	View/Edit Mouse

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

Structure

This protein has phosphotyrosine-binding domain (PTB domain or PID) in the middle and two PDZ domains at C-terminal.

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

^ ^a ^b ^c ENSG00000276495 GRCh38: Ensembl release 89: ENSG00000034053, ENSG00000276495 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000030519 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)".
^ ^a ^b 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.
^ 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.
^ 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.
^ 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. PMC 6757996. PMID 12196555.
^ 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.

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. 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.
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. S2CID 42411043.
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. S2CID 54389955.
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.

This article on a gene on human chromosome 15 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] ENSG00000276495 GRCh38: Ensembl release 89: ENSG00000034053, ENSG00000276495 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8955346-5] 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.

[entrez-6] "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)".

[pmid12972431-7] 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.

[pmid15037614-8] 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.

[pmid10777610-9] 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.

[pmid12196555-10] 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. PMC 6757996. PMID 12196555.

[pmid9890987-11] 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.

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Structure

Function

Interactions

References

External links

Further reading