CETN2 Antibody

1. Multidisciplinary approach showed that HsPrp40Ap interacts with centrin in vitro, supporting a coupled functional role for these proteins in pre-mRNA splicing. PMID: 28636910
2. Cetn3 inhibits Mps1 autophosphorylation at Thr-676, a known site of T-loop autoactivation, and interferes with Mps1-dependent phosphorylation of Cetn2. The cellular overexpression of Cetn3 attenuates the incorporation of Cetn2 into centrioles and centrosome reduplication, whereas depletion of Cetn3 generates extra centrioles. PMID: 26354417
3. Centrin2 regulates primary ciliogenesis through controlling CP110 levels. PMID: 25753040
4. co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export, indicating the dominance of the centrin 2 phenotype. PMID: 24291146
5. Data indicate that overexpression of the centrin interactor POC5 leads to the assembly of linear, centrin-dependent structures. PMID: 23844208
6. Cen2 influences the binding of RPA and XPA with damaged DNA. PMID: 22809153
7. xeroderma pigmentosum complementation group C expression correlates with a decreased amount of CENTRIN 2 transcript and protein PMID: 21676658
8. The stability of centrin is regulated in part by Aurora A. PMID: 21731694
9. Mps1-dependent phosphorylation of Cetn2 stimulates the canonical centriole assembly pathway. PMID: 20980622
10. oxidative radicals induce high proportions of irreversible damages (polymerisation) centrin 2 is highly sensitive to ionising radiation. PMID: 20586543
11. required for centriole duplication in mammalian cells PMID: 12176356
12. The solution structure of the long C-terminal fragment of centrin 2 exhibits an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. PMID: 12578356
13. structural characterization of the complex formed by the C-terminal domain of Cen2 with a peptide of xeroderma pigmentosum group C protein PMID: 12890685
14. Results describe the self-assembly properties of purified human centrin-2 in vitro. PMID: 15356003
15. Centrin 2 stimulates nucleotide excision repair by interacting with XPC. PMID: 15964821
16. an 18-residue peptide, from the N-terminal unstructured fragment, has a significant affinity for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules. PMID: 16411764
17. the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide; a novel binding motif for centrin PMID: 16627479
18. A complex formed by a Ca2+-bound human centrin 2 with a 17-mer peptide derived from the XPC sequence was crystallized. PMID: 16820684
19. Centrin 2 is highly sensitive to ionizing radiation, which could have important consequences on its biological functions. PMID: 17603931
20. The present data confirm that the in vitro structural features of the centrin/XPC peptide complex are highly relevant to the cellular context. PMID: 17897675
21. CETN2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. PMID: 18172010
22. NMR analysis indicates that the physical interaction between C-XPC and centrin 2 induces only minor conformational changes into XPC, localized around the 17-mer segment (847-863), showed to be critically involved in the centrin binding. PMID: 18177054
23. lower centrin levels in oligoasthnozoospermic males resulted in lower pregnancy percentage in this group after ICSI. PMID: 19179680
24. The nucleocytoplasmic shuttling of centrin-2 depends on the SUMO system. PMID: 19706679
25. The structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 was determined. PMID: 19857500

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HGNC: 1867

OMIM: 300006

KEGG: hsa:1069

STRING: 9606.ENSP00000359300

UniGene: Hs.82794