SGMS1

From Wikipedia, the free encyclopedia

Transmembrane protein 23

PDB rendering based on 2d8c.

Available structures: 2d8c

Identifiers

Symbol(s)

TMEM23; MOB1; MGC17342; MOB; SMS1

External IDs

MGI: 2444110 HomoloGene: 27040

Gene ontology
Molecular Function:	• kinase activity • transferase activity • ceramide cholinephosphotransferase activity
Cellular Component:	• Golgi trans cisterna • membrane • integral to membrane • integral to Golgi membrane
Biological Process:	• lipid metabolic process • sphingolipid metabolic process • sphingomyelin biosynthetic process • negative regulation of apoptosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_147156 (mRNA)
NP_671512 (protein)

NM_144792 (mRNA)
NP_659041 (protein)

Location

Chr 10: 51.74 - 52.05 Mb

Chr 19: 32.19 - 32.45 Mb

Pubmed search

[1]

[2]

Transmembrane protein 23, also known as TMEM23, is a human gene.^[1]

The protein encoded by this gene is predicted to be a five-pass transmembrane protein. This gene may be predominately expressed in brain.^[1]

[edit] References

^ ^a ^b Entrez Gene: TMEM23 transmembrane protein 23.

[edit] Further reading

Albi E, Magni MV (1999). "Sphingomyelin synthase in rat liver nuclear membrane and chromatin.". FEBS Lett. 460 (2): 369–72. PMID 10544266.
Vladychenskaya IP, Dergunova LV, Limborska SA (2002). "In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein.". Biomol. Eng. 18 (6): 263–8. PMID 11841947.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC (2004). "Identification of a family of animal sphingomyelin synthases.". EMBO J. 23 (1): 33–44. doi:10.1038/sj.emboj.7600034. PMID 14685263.
Yamaoka S, Miyaji M, Kitano T, et al. (2004). "Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells.". J. Biol. Chem. 279 (18): 18688–93. doi:10.1074/jbc.M401205200. PMID 14976195.
Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA (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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Dong J, Liu J, Lou B, et al. (2006). "Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice.". J. Lipid Res. 47 (6): 1307–14. doi:10.1194/jlr.M600040-JLR200. PMID 16508036.
Lim J, Hao T, Shaw C, et al. (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, et al. (2007). "Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells.". J. Biol. Chem. 282 (24): 17537–47. doi:10.1074/jbc.M702423200. PMID 17449912.
Separovic D, Hanada K, Maitah MY, et al. (2007). "Sphingomyelin synthase 1 suppresses ceramide production and apoptosis post-photodamage.". Biochem. Biophys. Res. Commun. 358 (1): 196–202. doi:10.1016/j.bbrc.2007.04.095. PMID 17467659.
Li Z, Hailemariam TK, Zhou H, et al. (2007). "Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization.". Biochim. Biophys. Acta 1771 (9): 1186–94. doi:10.1016/j.bbalip.2007.05.007. PMID 17616479.