Disease relevance of C11orf17

• The DNA sequence for one of these breast cancer associated genes was used to construct the larger 1319 bp BCA3 cDNA sequence using ESTs without assigned names or functions [1].

High impact information on C11orf17

• AAPK-dependent phosphorylation is required for the interaction of AKIP1 with messenger RNA that encodes dehydrin, a protein implicated in cell protection under stress conditions [2].
• Here we show that AAPK-interacting protein 1 (AKIP1), with sequence homology to heterogeneous nuclear RNA-binding protein A/B, is a substrate of AAPK [2].
• AAPK and AKIP1 are present in the guard-cell nucleus, and in vivo treatment of such cells with abscisic acid enhances the partitioning of AKIP1 into subnuclear foci which are reminiscent of nuclear speckles [2].
• Upon stimulation with forskolin, HeLa cells expressing AKIP1 accumulated higher levels of the endogenous C subunit in the nucleus [3].
• In silico study of breast cancer associated gene 3 using LION Target Engine and other tools [4].

Biological context of C11orf17

• Further analysis revealed possible functional domains and alternative splicing of BCA3 that we confirmed by RT-PCR analysis [1].
• As a test case, we investigated human breast cancer associated gene 3 (BCA3) with LION Target Engine and with other bioinformatics tools [4].
• LION Target Engine confirmed that the BCA3 gene is located on 11p15.4 and that the two most likely splice variants (lacking exon 3 and exons 3 and 5, respectively) exist [4].

Anatomical context of C11orf17

• High-level BCA3 mRNA expression was found in breast and prostate tumor cell lines whereas normal breast and prostate tissues have low-level expression [1].

Co-localisations of C11orf17

• In fact, we observed that AKIP1 colocalized with p65 within the cells and appeared to retain p65 in nucleus [5].

Analytical, diagnostic and therapeutic context of C11orf17

• Sequence conservation from multiple sequence alignments, splice variant identification, secondary structure predictions, and predicted phosphorylation sites suggest that the removal of interaction sites through alternative splicing might play a modulatory role in BCA3 [4].

References