SGMS1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2D8C

Identifiers

Aliases

SGMS1, MOB, MOB1, SMS1, TMEM23, hmob33, sphingomyelin synthase 1

External IDs

MGI: 2444110 HomoloGene: 27040 GeneCards: SGMS1

Gene ontology
Molecular function	• kinase activity • transferase activity • ceramide cholinephosphotransferase activity • sphingomyelin synthase activity
Cellular component	• integral component of membrane • integral component of Golgi membrane • Golgi trans cisterna • Golgi membrane • plasma membrane • Golgi apparatus • endoplasmic reticulum • nucleus • membrane
Biological process	• lipid metabolic process • cell growth • sphingomyelin biosynthetic process • sphingolipid biosynthetic process • phosphorylation • apoptotic process • sphingolipid metabolic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


259230


208449

Ensembl


ENSG00000198964


ENSMUSG00000040451

UniProt


Q86VZ5


Q8VCQ6

RefSeq (mRNA)


NM_147156


NM_001168525 NM_001168526 NM_144792

RefSeq (protein)


NP_671512.1


NP_001161997.1 NP_001161998.1 NP_659041.3

Location (UCSC)

Chr 10: 50.31 – 50.63 Mb

Chr 19: 32.12 – 32.39 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Phosphatidylcholine:ceramide cholinephosphotransferase 1 is an enzyme that in humans is encoded by the SGMS1 gene.^[3]^[4]^[5]

Function

The protein encoded by this gene is predicted to be a five-pass transmembrane protein. This gene may be predominately expressed in brain.^[5]

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.^[6] Male and female animals underwent a standardized phenotypic screen^[7] to determine the effects of deletion.^[8]^[9]^[10]^[11] Additional screens performed: - In-depth immunological phenotyping^[12]

*Sgms1* knockout mouse phenotype
Characteristic	Phenotype
All data available at.^[7]^[12]	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

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Vladychenskaya IP, Dergunova LV, Limborska SA (Feb 2002). "In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein". Biomolecular Engineering. 18 (6): 263–8. doi:10.1016/S1389-0344(01)00110-1. PMID 11841947.
↑ Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T (Apr 2004). "Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells". The Journal of Biological Chemistry. 279 (18): 18688–93. doi:10.1074/jbc.M401205200. PMID 14976195.
1 2 "Entrez Gene: TMEM23 transmembrane protein 23".
↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
1 2 "International Mouse Phenotyping Consortium".
↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".

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.

PDB gallery

2d8c: Solution structure of the sam-domain of mouse phosphatidyl ceramidecholinephosphotransferase 1

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SGMS1

Function

Model organisms

References

Further reading