# UGCG

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Protein-coding gene in the species Homo sapiens

UGCG Identifiers Aliases UGCG, GCS, GLCT1, UDP-glucose ceramide glucosyltransferase External IDs OMIM: 602874; MGI: 1332243; HomoloGene: 37763; GeneCards: UGCG; OMA:UGCG - orthologs Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q31.3 Start 111,896,814 bp[1] End 111,935,369 bp[1] Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 32.44 cM|4 B3 Start 59,189,257 bp[2] End 59,222,833 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of thigh bronchial epithelial cell jejunal mucosa vena cava trabecular bone epithelium of nasopharynx pericardium cartilage tissue buccal mucosa cell bone marrow Top expressed in decidua morula morula gastrula esophagus lymph node jejunum tail of embryo ileum secondary oocyte More reference expression data BioGPS More reference expression data Gene ontology Molecular function glycosyltransferase activity transferase activity ceramide glucosyltransferase activity dihydroceramide glucosyltransferase activity protein binding Cellular component integral component of membrane Golgi membrane Golgi apparatus membrane Biological process glycosphingolipid biosynthetic process glycosphingolipid metabolic process glucosylceramide biosynthetic process epidermis development lipid metabolism sphingolipid metabolic process cell differentiation neuron development establishment of skin barrier intestinal lipid absorption protein lipidation regulation of signal transduction keratinocyte differentiation leptin-mediated signaling pathway cornified envelope assembly Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 7357 22234 Ensembl ENSG00000148154 ENSMUSG00000028381 UniProt Q16739 O88693 RefSeq (mRNA) NM_003358 NM_011673 RefSeq (protein) NP_003349 NP_003349.1 NP_035803 Location (UCSC) Chr 9: 111.9 – 111.94 Mb Chr 4: 59.19 – 59.22 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Ceramide glucosyltransferase** is an [enzyme](/source/Enzyme) that in humans is encoded by the *UGCG* [gene](/source/Gene).[5][6][7]

[Glycosphingolipids](/source/Glycosphingolipids) (GSLs) are a group of membrane components that contain lipid and sugar moieties. They are present in essentially all animal cells and are believed to have important roles in various cellular processes. UDP-glucose ceramide glucosyltransferase catalyzes the first glycosylation step in glycosphingolipid biosynthesis. The product, glucosylceramide, is the core structure of more than 300 GSLs. UGCG is widely expressed and transcription is upregulated during keratinocyte differentiation.[7]

## Interactions

UGCG has been shown to [interact](/source/Protein-protein_interaction) with [RTN1](/source/RTN1).[8]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000148154](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000148154) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000028381](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000028381) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=7357). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=22234). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid8643456_5-0)** Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y (Jul 1996). ["Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39331). *Proc Natl Acad Sci U S A*. **93** (10): 4638–4643. [Bibcode](/source/Bibcode_(identifier)):[1996PNAS...93.4638I](https://ui.adsabs.harvard.edu/abs/1996PNAS...93.4638I). [doi](/source/Doi_(identifier)):[10.1073/pnas.93.10.4638](https://doi.org/10.1073%2Fpnas.93.10.4638). [PMC](/source/PMC_(identifier)) [39331](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39331). [PMID](/source/PMID_(identifier)) [8643456](https://pubmed.ncbi.nlm.nih.gov/8643456).

1. **[^](#cite_ref-pmid9605861_6-0)** Ichikawa S, Ozawa K, Hirabayashi Y (Jun 1998). "Assignment of a UDP-glucose:ceramide glucosyltransferase gene (UGCG) to human chromosome band 9q31 by in situ hybridization". *Cytogenet Cell Genet*. **79** (3–4): 233–234. [doi](/source/Doi_(identifier)):[10.1159/000134731](https://doi.org/10.1159%2F000134731). [PMID](/source/PMID_(identifier)) [9605861](https://pubmed.ncbi.nlm.nih.gov/9605861).

1. ^ [***a***](#cite_ref-entrez_7-0) [***b***](#cite_ref-entrez_7-1) ["Entrez Gene: UGCG UDP-glucose ceramide glucosyltransferase"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=7357).

1. **[^](#cite_ref-pmid12873973_8-0)** Di Sano F, Fazi Barbara, Citro Gennaro, Lovat Penny E, Cesareni Gianni, Piacentini Mauro (Jul 2003). "Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells". *Cancer Res*. **63** (14): 3860–3865. [ISSN](/source/ISSN_(identifier)) [0008-5472](https://search.worldcat.org/issn/0008-5472). [PMID](/source/PMID_(identifier)) [12873973](https://pubmed.ncbi.nlm.nih.gov/12873973).

## Further reading

- Kohyama-Koganaya A, Hirabayashi Y (2002). "[Role of glucosylceramide synthase as negative regulator for ceramide]". *Tanpakushitsu Kakusan Koso*. **47** (4 Suppl): 470–475. [PMID](/source/PMID_(identifier)) [11915344](https://pubmed.ncbi.nlm.nih.gov/11915344).

- Matsuo N, Nomura T, Imokawa G (1992). "A rapid and simple assay method for UDP-glucose:ceramide glucosyltransferase". *Biochim. Biophys. Acta*. **1116** (2): 97–103. [doi](/source/Doi_(identifier)):[10.1016/0304-4165(92)90105-4](https://doi.org/10.1016%2F0304-4165%2892%2990105-4). [PMID](/source/PMID_(identifier)) [1533793](https://pubmed.ncbi.nlm.nih.gov/1533793).

- Ichikawa S, Sakiyama H, Suzuki G, et al. (1996). ["Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38048). *Proc. Natl. Acad. Sci. U.S.A*. **93** (22): 4638–4643. [Bibcode](/source/Bibcode_(identifier)):[1996PNAS...93.4638I](https://ui.adsabs.harvard.edu/abs/1996PNAS...93.4638I). [doi](/source/Doi_(identifier)):[10.1073/pnas.93.10.4638](https://doi.org/10.1073%2Fpnas.93.10.4638). [PMC](/source/PMC_(identifier)) [38048](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38048). [PMID](/source/PMID_(identifier)) [8901638](https://pubmed.ncbi.nlm.nih.gov/8901638).

- Watanabe R, Wu K, Paul P, et al. (1998). ["Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation"](https://doi.org/10.1074%2Fjbc.273.16.9651). *J. Biol. Chem*. **273** (16): 9651–9655. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.16.9651](https://doi.org/10.1074%2Fjbc.273.16.9651). [PMID](/source/PMID_(identifier)) [9545298](https://pubmed.ncbi.nlm.nih.gov/9545298).

- Tepper AD, Diks SH, van Blitterswijk WJ, Borst J (2000). ["Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens"](https://doi.org/10.1074%2Fjbc.M005142200). *J. Biol. Chem*. **275** (44): 34810–34817. [doi](/source/Doi_(identifier)):[10.1074/jbc.M005142200](https://doi.org/10.1074%2Fjbc.M005142200). [PMID](/source/PMID_(identifier)) [10945987](https://pubmed.ncbi.nlm.nih.gov/10945987).

- Ogretmen B, Schady D, Usta J, et al. (2001). ["Role of ceramide in mediating the inhibition of telomerase activity in A549 human lung adenocarcinoma cells"](https://doi.org/10.1074%2Fjbc.M100314200). *J. Biol. Chem*. **276** (27): 24901–24910. [doi](/source/Doi_(identifier)):[10.1074/jbc.M100314200](https://doi.org/10.1074%2Fjbc.M100314200). [PMID](/source/PMID_(identifier)) [11335714](https://pubmed.ncbi.nlm.nih.gov/11335714).

- 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–16903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/12477932).

- Di Sano F, Fazi B, Citro G, et al. (2003). "Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells". *Cancer Res*. **63** (14): 3860–3865. [PMID](/source/PMID_(identifier)) [12873973](https://pubmed.ncbi.nlm.nih.gov/12873973).

- Grazide S, Terrisse AD, Lerouge S, et al. (2004). ["Cytoprotective effect of glucosylceramide synthase inhibition against daunorubicin-induced apoptosis in human leukemic cell lines"](https://doi.org/10.1074%2Fjbc.M314105200). *J. Biol. Chem*. **279** (18): 18256–18261. [doi](/source/Doi_(identifier)):[10.1074/jbc.M314105200](https://doi.org/10.1074%2Fjbc.M314105200). [PMID](/source/PMID_(identifier)) [14766899](https://pubmed.ncbi.nlm.nih.gov/14766899).

- Norris-Cervetto E, Callaghan R, Platt FM, et al. (2004). ["Inhibition of glucosylceramide synthase does not reverse drug resistance in cancer cells"](https://doi.org/10.1074%2Fjbc.M404466200). *J. Biol. Chem*. **279** (39): 40412–40418. [doi](/source/Doi_(identifier)):[10.1074/jbc.M404466200](https://doi.org/10.1074%2Fjbc.M404466200). [PMID](/source/PMID_(identifier)) [15263008](https://pubmed.ncbi.nlm.nih.gov/15263008).

- 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)"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). *Genome Res*. **14** (10B): 2121–2127. [doi](/source/Doi_(identifier)):[10.1101/gr.2596504](https://doi.org/10.1101%2Fgr.2596504). [PMC](/source/PMC_(identifier)) [528928](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). [PMID](/source/PMID_(identifier)) [15489334](https://pubmed.ncbi.nlm.nih.gov/15489334).

- Turzanski J, Grundy M, Shang S, et al. (2005). ["P-glycoprotein is implicated in the inhibition of ceramide-induced apoptosis in TF-1 acute myeloid leukemia cells by modulation of the glucosylceramide synthase pathway"](https://doi.org/10.1016%2Fj.exphem.2004.10.005). *Exp. Hematol*. **33** (1): 62–72. [doi](/source/Doi_(identifier)):[10.1016/j.exphem.2004.10.005](https://doi.org/10.1016%2Fj.exphem.2004.10.005). [PMID](/source/PMID_(identifier)) [15661399](https://pubmed.ncbi.nlm.nih.gov/15661399).

- Sun NN, Fastje CD, Wong SS, et al. (2005). "Dose-dependent transcriptome changes by metal ores on a human acute lymphoblastic leukemia cell line". *Toxicology and Industrial Health*. **19** (7–10): 157–163. [doi](/source/Doi_(identifier)):[10.1191/0748233703th185oa](https://doi.org/10.1191%2F0748233703th185oa). [PMID](/source/PMID_(identifier)) [15747776](https://pubmed.ncbi.nlm.nih.gov/15747776). [S2CID](/source/S2CID_(identifier)) [14394243](https://api.semanticscholar.org/CorpusID:14394243).

- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". *Nature*. **437** (7062): 1173–1178. [Bibcode](/source/Bibcode_(identifier)):[2005Natur.437.1173R](https://ui.adsabs.harvard.edu/abs/2005Natur.437.1173R). [doi](/source/Doi_(identifier)):[10.1038/nature04209](https://doi.org/10.1038%2Fnature04209). [PMID](/source/PMID_(identifier)) [16189514](https://pubmed.ncbi.nlm.nih.gov/16189514). [S2CID](/source/S2CID_(identifier)) [4427026](https://api.semanticscholar.org/CorpusID:4427026).

- Fazi B, Melino S, Di Sano F, et al. (2006). "Cloning, expression, and preliminary structural characterization of RTN-1C". *Biochem. Biophys. Res. Commun*. **342** (3): 881–886. [doi](/source/Doi_(identifier)):[10.1016/j.bbrc.2006.02.036](https://doi.org/10.1016%2Fj.bbrc.2006.02.036). [PMID](/source/PMID_(identifier)) [16500619](https://pubmed.ncbi.nlm.nih.gov/16500619).

v t e Metabolism, lipid metabolism, glycolipid enzymes Sphingolipid To glycosphingolipid Glycosyltransferase Sulfotransferase To ceramide From ganglioside β-Galactosidase Hexosaminidase A Neuraminidase Glucocerebrosidase From globoside Hexosaminidase B α-Galactosidase β-Galactosidase Glucocerebrosidase From sphingomyelin Sphingomyelin phosphodiesterase Sphingomyelin phosphodiesterase 1 From sulfatide Arylsulfatase A Galactosylceramidase To sphingosine Ceramidase ACER1 ACER2 ACER3 ASAH1 ASAH2 ASAH2B ASAH2C Other Sphingosine kinase NCL Palmitoyl protein thioesterase Tripeptidyl peptidase I CLN3 CLN5 CLN6 CLN8 Ceramide synthesis Serine C-palmitoyltransferase (SPTLC1) Ceramide glucosyltransferase (UGCG)

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Adapted from the Wikipedia article [UGCG](https://en.wikipedia.org/wiki/UGCG) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/UGCG?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.