Disease relevance of A2BP1

• The structural gene of FOX-1 (blaFOX-1) was cloned into a 2,270-bp PstI-PstI fragment and was expressed in E. coli TG1 [1].
• The deduced 382-amino-acid sequence of FOX-1 exhibited a high degree of similarity with chromosomally encoded AmpC beta-lactamases of Pseudomonas aeruginosa, Serratia marcescens, Enterobacter cloacae, E. coli, and Citrobacter freundii [1].

Psychiatry related information on A2BP1

• No mutations were found, suggesting that disruption of the A2BP1 gene is not a common cause of sporadic epilepsy or mental retardation [2].

High impact information on A2BP1

• Using the yeast two-hybrid system, we identified a novel protein, A2BP1 (ataxin-2 binding protein 1) which binds to the C-terminus of ataxin-2 [3].
• Western blot analysis of subcellular fractions indicated enrichment of A2BP1 in the same fractions as ataxin-2 [3].
• Immunocytochemistry showed that A2BP1 was expressed in the cytoplasm of Purkinje cells and dentate neurons in a pattern similar to that seen for ataxin-2 labeling [3].
• A2BP1 had striking homology with a human cDNA clone, P83A20, of unknown function and at least two copies of A2BP1 homologs are found in the Caenorhabditis elegans genome database [3].
• Sequencing of the corresponding DNA of K. oxytoca 1731 revealed 96 and 97% identities of the deduced amino acid sequence with FOX-1 and FOX-2, respectively [4].

Biological context of A2BP1

• It is proposed that disruption of the A2BP1 gene is a cause of the abnormal phenotype of the two patients [2].
• Ninety-six patients with sporadic epilepsy and 96 female patients with mental retardation were screened by SSCP for potential mutations of A2BP1 [2].
• The de novo chromosome 16 translocations of two patients with abnormal phenotypes (mental retardation and epilepsy) disrupt the A2BP1 gene [2].
• Here, we demonstrate that both mouse Fxh and A2BP1 transcripts undergo tissue-specific alternative splicing, generating protein isoforms specific to brain and muscle [5].
• Resistance could be transferred by conjugation or transformation into Escherichia coli K-12 via a 48.5-kb plasmid (pGLK1) that produced two FOX-1 molecular variants with isoelectric points of 6.8 and 7.2 and apparent molecular sizes of 37 and 35 kDa, respectively [1].

Anatomical context of A2BP1

• By immunocfluorescent staining, A2BP1 and ataxin-2 were both localized to the trans -Golgi network [3].

Associations of A2BP1 with chemical compounds

• By modified FOX-1 method, we estimated plasma hydroperoxide concentration of normal human subjects and of diabetic patients and compared with FOX-2 method [6].
• Measurement of plasma hydroperoxide concentration by FOX-1 assay in conjunction with triphenylphosphine [6].
• By modified FOX-1 method, the recovery percentage of cumene hydroperoxide was better in biological samples when compared to FOX-2 method [6].

Physical interactions of A2BP1

• Ataxin-2 interacts with ataxin-2-binding-protein 1 (A2BP1), a member of a novel family of putative RNA-binding proteins [7].

Other interactions of A2BP1

• The results presented here underline previous findings about the interaction of human ataxin-2 and A2BP1 [7].
• Measurement of urinary hydrogen peroxide by FOX-1 method in conjunction with catalase in diabetes mellitus--a sensitive and specific approach [8].

Analytical, diagnostic and therapeutic context of A2BP1

• Northern blot analysis showed that A2BP1 was predominantly expressed in muscle and brain [3].
• Sequence analysis of the A2BP1 cDNA revealed an RNP motif that is highly conserved among RNA-binding proteins [3].

References