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Amyloid beta (A4) precursor protein-binding, family A, member 2
Protein APBA2 PDB 1u39.png
PDB rendering based on 1u39.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols APBA2 ; D15S1518E; HsT16821; LIN-10; MGC:14091; MINT2; X11-BETA; X11L
External IDs OMIM602712 MGI1261791 HomoloGene4021 GeneCards: APBA2 Gene
RNA expression pattern
PBB GE APBA2 209871 s at tn.png
PBB GE APBA2 209870 s at tn.png
More reference expression data
Species Human Mouse
Entrez 321 11784
Ensembl ENSG00000034053 ENSMUSG00000030519
UniProt Q99767 P98084
RefSeq (mRNA) NM_001130414 NM_001291166
RefSeq (protein) NP_001123886 NP_001278095
Location (UCSC) Chr 15:
29.13 – 29.41 Mb
Chr 7:
64.5 – 64.75 Mb
PubMed search [1] [2]

Amyloid beta A4 precursor protein-binding family A member 2 is a protein that in humans is encoded by the APBA2 gene.[1][2]

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.[2]


APBA2 has been shown to interact with CLSTN1,[3][4] RELA[5] and Amyloid precursor protein.[3][6][7]


  1. ^ 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. 
  2. ^ a b "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)". 
  3. ^ a b Araki, Yoichi; Tomita Susumu; Yamaguchi Haruyasu; Miyagi Naomi; Sumioka Akio; Kirino Yutaka; Suzuki Toshiharu (December 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". J. Biol. Chem. (United States) 278 (49): 49448–58. doi:10.1074/jbc.M306024200. ISSN 0021-9258. PMID 12972431. 
  4. ^ Araki, Yoichi; Miyagi Naomi, Kato Naoko, Yoshida Tomohiro, Wada Sachiyo, Nishimura Masaki, Komano Hiroto, Yamamoto Tohru, De Strooper Bart, Yamamoto Kazuo, Suzuki Toshiharu (June 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". J. Biol. Chem. (United States) 279 (23): 24343–54. doi:10.1074/jbc.M401925200. ISSN 0021-9258. PMID 15037614. 
  5. ^ 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. (UNITED STATES) 275 (17): 13056–60. doi:10.1074/jbc.C000019200. ISSN 0021-9258. PMID 10777610. 
  6. ^ Biederer, Thomas; Cao Xinwei; Südhof Thomas C; Liu Xinran (September 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. (United States) 22 (17): 7340–51. PMID 12196555. 
  7. ^ 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. (UNITED STATES) 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. ISSN 0021-9258. PMID 9890987. 

Further reading[edit]