SGMS1

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Phosphatidylcholine:ceramide cholinephosphotransferase 1 is an enzyme that in humans is encoded by the SGMS1 gene.

Function

The protein encoded by this gene is predicted to be a five-pass transmembrane protein. This gene may be predominately expressed in brain.

Model organisms

Model organisms have been used in the study of SGMS1 function. A conditional knockout mouse line called Sgms1^{tm1a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping

Sgms1 knockout mouse phenotype

Characteristic	Phenotype
All data available at.	Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Abnormal
Heart weight	Normal
Salmonella infection	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Trichuris Challenge	Normal

Further reading

• Albi E, Magni MV (Oct 1999). "Sphingomyelin synthase in rat liver nuclear membrane and chromatin". FEBS Letters. 460 (2): 369–72. doi:10.1016/S0014-5793(99)01378-2. PMID 10544266.
• Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC (Jan 2004). "Identification of a family of animal sphingomyelin synthases". The EMBO Journal. 23 (1): 33–44. doi:10.1038/sj.emboj.7600034. PMC 1271672. PMID 14685263.
• Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA (Sep 2004). "Human gene MOB: structure specification and aspects of transcriptional activity". Gene. 338 (2): 257–65. doi:10.1016/j.gene.2004.06.003. PMID 15315829.
• Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC (Jun 2006). "Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice". Journal of Lipid Research. 47 (6): 1307–14. doi:10.1194/jlr.M600040-JLR200. PMID 16508036.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
• Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC (Jun 2007). "Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells". The Journal of Biological Chemistry. 282 (24): 17537–47. doi:10.1074/jbc.M702423200. PMID 17449912.
• Separovic D, Hanada K, Maitah MY, Nagy B, Hang I, Tainsky MA, Kraniak JM, Bielawski J (Jun 2007). "Sphingomyelin synthase 1 suppresses ceramide production and apoptosis post-photodamage". Biochemical and Biophysical Research Communications. 358 (1): 196–202. doi:10.1016/j.bbrc.2007.04.095. PMC 2701614. PMID 17467659.
• Li Z, Hailemariam TK, Zhou H, Li Y, Duckworth DC, Peake DA, Zhang Y, Kuo MS, Cao G, Jiang XC (Sep 2007). "Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization". Biochimica et Biophysica Acta. 1771 (9): 1186–94. doi:10.1016/j.bbalip.2007.05.007. PMC 2712822. PMID 17616479.