Alternative titles; symbols
HGNC Approved Gene Symbol: SSNA1
Cytogenetic location: 9q34.3 Genomic coordinates (GRCh38) : 9:137,188,676-137,190,366 (from NCBI)
Using serum from a patient with Sjogren syndrome to screen a human testis cDNA library, Ramos-Morales et al. (1998) isolated 2 clones encoding SSNA1, which they called NA14. The predicted 119-amino acid protein has a calculated molecular mass of 13.6 kD and has an N-terminal dimeric coiled-coil domain and a C-terminal basic domain. SSNA1 shares 96.6% amino acid identity with its mouse homolog. Northern blot analysis of adult human tissues detected strong expression in testes, with moderate to low expression in spleen, thymus, prostate, ovary, small intestine, colon, and peripheral blood leukocytes. Immunofluorescence microscopy of HeLa and mouse 3T3 cells transfected with SSNA1 showed numerous punctate structures scattered throughout the nucleus.
Pfannenschmid et al. (2003) cloned and characterized the Chlamydomonas reinhardtii homolog of NA14, which they named DIP13. By immunofluorescence in Chlamydomonas cells, the protein product was localized to microtubule structures, namely basal bodies, flagellar axonemes, and cytoplasmic microtubules. Anti-DIP13 antibody specifically recognized NA14, staining basal bodies and flagella of human sperm cells and the centrosome of HeLa cells. Expression of the DIP13 ORF in antisense orientation in Chlamydomonas resulted in multinucleate, multiflagellate cells, suggesting a role in microtubule function and cell division.
Andersen et al. (2003) performed mass spectrometry-based proteomic analysis of human centrosomes in the interphase of the cell cycle by quantitatively profiling hundreds of proteins across several centrifugation fractions. They validated 23 novel components and identified 41 likely candidates, including NA14.
Errico et al. (2004) demonstrated that spastin (SPAST; 604277) was enriched in cell regions containing dynamic microtubules. Spastin interacted with NA14 and cofractionated with gamma-tubulin (TUBG1; 191135). Deletion of the region required for binding to NA14 disrupted spastin interaction with microtubules, suggesting that NA14 may be an important adaptor to target spastin activity at the centrosome. Errico et al. (2004) hypothesized that spastin may play a role in cytoskeletal rearrangements and dynamics.
Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., Mann, M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426: 570-574, 2003. [PubMed: 14654843] [Full Text: https://doi.org/10.1038/nature02166]
Errico, A., Claudiani, P., D'Addio, M., Rugarli, E. I. Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon. Hum. Molec. Genet. 13: 2121-2132, 2004. [PubMed: 15269182] [Full Text: https://doi.org/10.1093/hmg/ddh223]
Pfannenschmid, F., Wimmer, V. C., Rios, R.-M., Geimer, S., Krockel, U., Leiherer, A., Haller, K., Nemcova, Y., Mages, W. Chlamydomonas DIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division. J. Cell Sci. 116: 1449-1462, 2003. [PubMed: 12640030] [Full Text: https://doi.org/10.1242/jcs.00337]
Ramos-Morales, F., Infante, C., Fedriani, C., Bornens, M., Rios, R. M. NA14 is a novel nuclear autoantigen with a coiled-coil domain. J. Biol. Chem. 273: 1634-1639, 1998. [PubMed: 9430706] [Full Text: https://doi.org/10.1074/jbc.273.3.1634]