S100A13

S100A13

S100A13

Protein-coding gene in the species Homo sapiens


S100 calcium-binding protein A13 (S100A13) is a protein that in humans is encoded by the S100A13 gene.[5][6]

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Function

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein is widely expressed in various types of tissues with a high expression level in thyroid gland. In smooth muscle cells, this protein co-expresses with other family members in the nucleus and in stress fibers, suggesting diverse functions in signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.[6]

Interactions

S100A13 has been shown to interact with SYT1[7][8] and FGF1.[7][8]

Pathology

Up-regulation of S100A13 was detected in cystic papillary thyroid carcinoma[9] and association of S100A13 expression and chemotherapy resistance was shown in proteomics study of melanoma.[10]


References

  1. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  2. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. Wicki R, Marenholz I, Mischke D, Schäfer BW, Heizmann CW (Dec 1996). "Characterization of the human S100A12 (calgranulin C, p6, CAAF1, CGRP) gene, a new member of the S100 gene cluster on chromosome 1q21". Cell Calcium. 20 (6): 459–64. doi:10.1016/S0143-4160(96)90087-1. PMID 8985590.
  4. Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, Hampton B, Burgess WH, Maciag T (Aug 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". The Journal of Biological Chemistry. 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. hdl:2158/26736. PMID 9712836.
  5. Landriscina M, Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (Jul 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". The Journal of Biological Chemistry. 276 (27): 25549–57. doi:10.1074/jbc.M102925200. PMID 11432880.
  6. Dinets A, Pernemalm M, Kjellin H, Sviatoha V, Sofiadis A, Juhlin CC, Zedenius J, Larsson C, Lehtiö J, Höög A (May 2015). "Differential protein expression profiles of cyst fluid from papillary thyroid carcinoma and benign thyroid lesions". PLOS ONE. 10 (5): e0126472. Bibcode:2015PLoSO..1026472D. doi:10.1371/journal.pone.0126472. PMC 4433121. PMID 25978681.
  7. Azimi A, Pernemalm M, Frostvik Stolt M, Hansson J, Lehtiö J, Egyházi Brage S, Hertzman Johansson C (2014). "Proteomics analysis of melanoma metastases: association between S100A13 expression and chemotherapy resistance". British Journal of Cancer. 110 (10): 2489–2495. doi:10.1038/bjc.2014.169. PMC 4021518. PMID 24722184.

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