CINAP antibody
- Known as:
- CINAP (anti-)
- Catalog number:
- orb100384
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- CINAP antibody
Related genes to: CINAP antibody
- Gene:
- AK6 NIH gene
- Name:
- adenylate kinase 6
- Previous symbol:
- -
- Synonyms:
- CINAP
- Chromosome:
- 5q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2013-09-19
- Date modifiied:
- 2019-02-25
- Gene:
- TSPYL2 NIH gene
- Name:
- TSPY like 2
- Previous symbol:
- -
- Synonyms:
- SE20-4, HRIHFB2216, CTCL, DENTT, CDA1, CINAP, TSPX
- Chromosome:
- Xp11.22
- Locus Type:
- gene with protein product
- Date approved:
- 2004-09-30
- Date modifiied:
- 2016-10-05
Related products to: CINAP antibody
Related articles to: CINAP antibody
- Dysfunctions in ribosome biogenesis cause developmental defects and increased cancer susceptibility; however, the connection between ribosome assembly and tumorigenesis remains unestablished. Here we show that hCINAP (also named AK6) is required for human 18S rRNA processing and 40S subunit assembly. Homozygous CINAP(-/-) mice show embryonic lethality. The heterozygotes are viable and show defects in 18S rRNA processing, whereas no delayed cell growth is observed. However, during rapid growth, CINAP haploinsufficiency impairs protein synthesis. Consistently, hCINAP depletion in fast-growing cancer cells inhibits ribosome assembly and abolishes tumorigenesis. These data demonstrate that hCINAP reduction is a specific rate-limiting controller during rapid growth. Notably, hCINAP is highly expressed in cancers and correlated with a worse prognosis. Genome-wide polysome profiling shows that hCINAP selectively modulates cancer-associated translatome to promote malignancy. Our results connect the role of hCINAP in ribosome assembly with tumorigenesis. Modulation of hCINAP expression may be a promising target for cancer therapy. - Source: PubMed
Publication date: 2016/08/01
Bai DongmeiZhang JinfangLi TingtingHang RunlaiLiu YongTian YongluHuang DaduQu LinglongCao XiaofengJi JiafuZheng Xiaofeng - Human coilin interacting nuclear ATPase protein (hCINAP) directly interacts with coilin, a marker protein of Cajal Bodies (CBs), nuclear organelles involved in the maturation of small nuclear ribonucleoproteins UsnRNPs and snoRNPs. hCINAP has previously been designated as an adenylate kinase (AK6), but is very atypical as it exhibits unusually broad substrate specificity, structural features characteristic of ATPase/GTPase proteins (Walker motifs A and B) and also intrinsic ATPase activity. Despite its intriguing structure, unique properties and cellular localization, the enzymatic mechanism and biological function of hCINAP have remained poorly characterized. Here, we offer the first high-resolution structure of hCINAP in complex with the substrate ADP (and dADP), the structure of hCINAP with a sulfate ion bound at the AMP binding site, and the structure of the ternary complex hCINAP-Mg(2+) ADP-Pi. Induced fit docking calculations are used to predict the structure of the hCINAP-Mg(2+) ATP-AMP ternary complex. Structural analysis suggested a functional role for His79 in the Walker B motif. Kinetic analysis of mutant hCINAP-H79G indicates that His79 affects both AK and ATPase catalytic efficiency and induces homodimer formation. Finally, we show that in vivo expression of hCINAP-H79G in human cells is toxic and drastically deregulates the number and appearance of CBs in the cell nucleus. Our findings suggest that hCINAP may not simply regulate nucleotide homeostasis, but may have broader functionality, including control of CB assembly and disassembly in the nucleus of human cells. - Source: PubMed
Publication date: 2011/10/31
Drakou Christina EMalekkou AnnaHayes Joseph MLederer Carsten WLeonidas Demetres DOikonomakos Nikos GLamond Angus ISantama NioviZographos Spyros E