Sterile alpha motif domain-containing protein 9

Definition:

Double-stranded nucleic acid binding that acts as a an antiviral factor by playing an essential role in the formation of cytoplasmic antiviral granules. May play a role in the inflammatory response to tissue injury and the control of extra-osseous calcification, acting as a downstream target of TNF-alpha signaling. Involved in the regulation of EGR1, in coordination with RGL2. May be involved in endosome fusion.

References:

[1]. Orit Topaz, et al. A deleterious mutation in SAMD9 causes normophosphatemic familial tumoral calcinosis. Am J Hum Genet. 2006 Oct;79(4):759-64. [Content Brief]

[2]. Jia Liu, et al. SAMD9 is an innate antiviral host factor with stress response properties that can be antagonized by poxviruses. J Virol. 2015 Feb;89(3):1925-31. [Content Brief]

[3]. Dov Hershkovitz, et al. Functional characterization of SAMD9, a protein deficient in normophosphatemic familial tumoral calcinosis. J Invest Dermatol. 2011 Mar;131(3):662-9. [Content Brief]

[4]. Bernice Nounamo, et al. An interaction domain in human SAMD9 is essential for myxoma virus host-range determinant M062 antagonism of host anti-viral function. Virology. 2017 Mar;503:94-102. [Content Brief]

[5]. Ilana Chefetz, et al. Normophosphatemic familial tumoral calcinosis is caused by deleterious mutations in SAMD9, encoding a TNF-alpha responsive protein. J Invest Dermatol. 2008 Jun;128(6):1423-9. [Content Brief]

[6]. Akiko Nagamachi, et al. Haploinsufficiency of SAMD9L, an endosome fusion facilitator, causes myeloid malignancies in mice mimicking human diseases with monosomy 7. Cancer Cell. 2013 Sep 9;24(3):305-17. [Content Brief]

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