APBA2

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APBA2
Protein APBA2 PDB 1u39.png
Identifiers
Aliases APBA2, D15S1518E, HsT16821, LIN-10, MGC:14091, MINT2, X11-BETA, X11L, amyloid beta precursor protein binding family A member 2
External IDs MGI: 1261791 HomoloGene: 4021 GeneCards: APBA2
RNA expression pattern
PBB GE APBA2 209870 s at fs.png

PBB GE APBA2 209871 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001130414
NM_005503

NM_001291166
NM_001291167
NM_007461

RefSeq (protein)

NP_001123886
NP_005494

Location (UCSC) Chr 15: 28.88 – 29.12 Mb Chr 7: 64.5 – 64.75 Mb
PubMed search [1] [2]
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.[3][4]

Function[edit]

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.[4]

Interactions[edit]

APBA2 has been shown to interact with CLSTN1,[5][6] RELA[7] and Amyloid precursor protein.[5][8][9]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. 
  4. ^ a b "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)". 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. PMID 12196555. 
  9. ^ 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[edit]

Further reading[edit]