APBA2

APBA2
Identifiers
AliasesAPBA2, D15S1518E, HsT16821, LIN-10, MGC:14091, MINT2, X11-BETA, X11L, amyloid beta precursor protein binding family A member 2
External IDsMGI: 1261791 HomoloGene: 4021 GeneCards: APBA2
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

321

11784

Ensembl

ENSG00000034053
ENSG00000276495

ENSMUSG00000030519

UniProt

Q99767

P98084

RefSeq (mRNA)

NM_001130414
NM_005503

NM_001291166
NM_001291167
NM_007461

RefSeq (protein)

NP_001123886
NP_005494

NP_001278095
NP_001278096
NP_031487

Location (UCSC)Chr 15: 28.88 – 29.12 MbChr 7: 64.5 – 64.75 Mb
PubMed search[1][2]
Wikidata
View/Edit HumanView/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

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

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

References

  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. PMID 8955346. doi:10.1016/S0014-5793(96)01128-3.
  4. 1 2 "Entrez Gene: APBA2 amyloid beta (A4) precursor protein-binding, family A, member 2 (X11-like)".
  5. 1 2 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. PMID 12972431. doi:10.1074/jbc.M306024200.
  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. PMID 15037614. doi:10.1074/jbc.M401925200.
  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. PMID 10777610. doi:10.1074/jbc.C000019200.
  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. PMID 9890987. doi:10.1074/jbc.274.4.2243.

Further reading


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.