UGCG: Difference between revisions

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{{Infobox_gene}}
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'''Ceramide glucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''UGCG'' [[gene]].<ref name="pmid8643456">{{cite journal |vauthors=Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y | title = Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis | journal = Proc Natl Acad Sci U S A | volume = 93 | issue = 10 | pages = 4638–43 |date=Jul 1996 | pmid = 8643456 | pmc = 39331 | doi =10.1073/pnas.93.10.4638 | bibcode=1996PNAS...93.4638I }}</ref><ref name="pmid9605861">{{cite journal |vauthors=Ichikawa S, Ozawa K, Hirabayashi Y | title = Assignment of a UDP-glucose:ceramide glucosyltransferase gene (UGCG) to human chromosome band 9q31 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 79 | issue = 3–4 | pages = 233–4 |date=Jun 1998 | pmid = 9605861 | pmc = | doi =10.1159/000134731  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UGCG UDP-glucose ceramide glucosyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7357| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{SWL|target=Glycosphingolipids|type=produces}} (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 biosynthesisThe product, glucosylceramide, is the core structure of more than 300 GSLs. UGCG is widely expressed and transcription is upregulated during keratinocyte differentiation.<ref name="entrez" />
{{GNF_Protein_box
| image =
| image_source =   
| PDB =
| Name = UDP-glucose ceramide glucosyltransferase
| HGNCid = 12524
| Symbol = UGCG
| AltSymbols =; GCS
| OMIM = 602874
| ECnumber = 
| Homologene = 37763
| MGIid = 1332243
| GeneAtlas_image1 = PBB_GE_UGCG_204881_s_at_tn.png
  | GeneAtlas_image2 = PBB_GE_UGCG_221765_at_tn.png
| Function = {{GNF_GO|id=GO:0008120 |text = ceramide glucosyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006679 |text = glucosylceramide biosynthetic process}} {{GNF_GO|id=GO:0006688 |text = glycosphingolipid biosynthetic process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7357
    | Hs_Ensembl = ENSG00000148154
    | Hs_RefseqProtein = NP_003349
    | Hs_RefseqmRNA = NM_003358
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 113698867
    | Hs_GenLoc_end = 113737470
    | Hs_Uniprot = Q16739
    | Mm_EntrezGene = 22234
    | Mm_Ensembl = ENSMUSG00000028381
    | Mm_RefseqmRNA = NM_011673
    | Mm_RefseqProtein = NP_035803
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 59283604
    | Mm_GenLoc_end = 59316887
    | Mm_Uniprot = O88693
  }}
}}
'''UDP-glucose ceramide glucosyltransferase''', also known as '''UGCG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UGCG UDP-glucose ceramide glucosyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7357| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
UGCG has been shown to [[Protein-protein interaction|interact]] with {{SWL|target=RTN1|type=PPI}}.<ref name=pmid12873973>{{cite journal |last=Di Sano |first=Federica |authorlink= |author2=Fazi Barbara |author3=Citro Gennaro |author4=Lovat Penny E |author5=Cesareni Gianni |author6=Piacentini Mauro  |date=Jul 2003 |title=Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells |journal=Cancer Res. |volume=63 |issue=14 |pages=3860–5 | issn = 0008-5472| pmid = 12873973 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: UGCG UDP-glucose ceramide glucosyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7357| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kohyama-Koganaya A, Hirabayashi Y |title=[Role of glucosylceramide synthase as negative regulator for ceramide] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 470-5 |year= 2002 |pmid= 11915344 |doi=  }}
*{{cite journal  |vauthors=Kohyama-Koganaya A, Hirabayashi Y |title=[Role of glucosylceramide synthase as negative regulator for ceramide] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 470–5 |year= 2002 |pmid= 11915344 |doi=  }}
*{{cite journal  | author=Matsuo N, Nomura T, Imokawa G |title=A rapid and simple assay method for UDP-glucose:ceramide glucosyltransferase. |journal=Biochim. Biophys. Acta |volume=1116 |issue= 2 |pages= 97-103 |year= 1992 |pmid= 1533793 |doi=  }}
*{{cite journal  |vauthors=Matsuo N, Nomura T, Imokawa G |title=A rapid and simple assay method for UDP-glucose:ceramide glucosyltransferase |journal=Biochim. Biophys. Acta |volume=1116 |issue= 2 |pages= 97–103 |year= 1992 |pmid= 1533793 |doi=  10.1016/0304-4165(92)90105-4}}
*{{cite journal | author=Ichikawa S, Sakiyama H, Suzuki G, ''et al.'' |title=Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4638-43 |year= 1996 |pmid= 8643456 |doi=  }}
*{{cite journal   |vauthors=Ichikawa S, Sakiyama H, Suzuki G, etal |title=Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 22 |pages= 12654 |year= 1996 |pmid= 8901638 |doi=  10.1073/pnas.93.22.12654| pmc=38048  |doi-broken-date=2018-10-20 }}
*{{cite journal  | author=Ichikawa S, Sakiyama H, Suzuki G, ''et al.'' |title=Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 22 |pages= 12654 |year= 1996 |pmid= 8901638 |doi= }}
*{{cite journal   |vauthors=Watanabe R, Wu K, Paul P, etal |title=Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation |journal=J. Biol. Chem. |volume=273 |issue= 16 |pages= 9651–5 |year= 1998 |pmid= 9545298 |doi=10.1074/jbc.273.16.9651 }}
*{{cite journal | author=Watanabe R, Wu K, Paul P, ''et al.'' |title=Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation. |journal=J. Biol. Chem. |volume=273 |issue= 16 |pages= 9651-5 |year= 1998 |pmid= 9545298 |doi= }}
*{{cite journal  |vauthors=Tepper AD, Diks SH, van Blitterswijk WJ, Borst J |title=Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34810–7 |year= 2000 |pmid= 10945987 |doi= 10.1074/jbc.M005142200 }}
*{{cite journal  | author=Ichikawa S, Ozawa K, Hirabayashi Y |title=Assignment of a UDP-glucose:ceramide glucosyltransferase gene (UGCG) to human chromosome band 9q31 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 3-4 |pages= 233-4 |year= 1998 |pmid= 9605861 |doi= }}
*{{cite journal   |vauthors=Ogretmen B, Schady D, Usta J, etal |title=Role of ceramide in mediating the inhibition of telomerase activity in A549 human lung adenocarcinoma cells |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24901–10 |year= 2001 |pmid= 11335714 |doi= 10.1074/jbc.M100314200 }}
*{{cite journal  | author=Tepper AD, Diks SH, van Blitterswijk WJ, Borst J |title=Glucosylceramide synthase does not attenuate the ceramide pool accumulating during apoptosis induced by CD95 or anti-cancer regimens. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34810-7 |year= 2000 |pmid= 10945987 |doi= 10.1074/jbc.M005142200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode = 2002PNAS...9916899M }}
*{{cite journal | author=Ogretmen B, Schady D, Usta J, ''et al.'' |title=Role of ceramide in mediating the inhibition of telomerase activity in A549 human lung adenocarcinoma cells. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24901-10 |year= 2001 |pmid= 11335714 |doi= 10.1074/jbc.M100314200 }}
*{{cite journal   |vauthors=Di Sano F, Fazi B, Citro G, etal |title=Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells |journal=Cancer Res. |volume=63 |issue= 14 |pages= 3860–5 |year= 2003 |pmid= 12873973 |doi=  }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Grazide S, Terrisse AD, Lerouge S, etal |title=Cytoprotective effect of glucosylceramide synthase inhibition against daunorubicin-induced apoptosis in human leukemic cell lines |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18256–61 |year= 2004 |pmid= 14766899 |doi= 10.1074/jbc.M314105200 }}
*{{cite journal | author=Di Sano F, Fazi B, Citro G, ''et al.'' |title=Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells. |journal=Cancer Res. |volume=63 |issue= 14 |pages= 3860-5 |year= 2003 |pmid= 12873973 |doi=  }}
*{{cite journal   |vauthors=Norris-Cervetto E, Callaghan R, Platt FM, etal |title=Inhibition of glucosylceramide synthase does not reverse drug resistance in cancer cells |journal=J. Biol. Chem. |volume=279 |issue= 39 |pages= 40412–8 |year= 2004 |pmid= 15263008 |doi= 10.1074/jbc.M404466200 }}
*{{cite journal | author=Grazide S, Terrisse AD, Lerouge S, ''et al.'' |title=Cytoprotective effect of glucosylceramide synthase inhibition against daunorubicin-induced apoptosis in human leukemic cell lines. |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18256-61 |year= 2004 |pmid= 14766899 |doi= 10.1074/jbc.M314105200 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Norris-Cervetto E, Callaghan R, Platt FM, ''et al.'' |title=Inhibition of glucosylceramide synthase does not reverse drug resistance in cancer cells. |journal=J. Biol. Chem. |volume=279 |issue= 39 |pages= 40412-8 |year= 2004 |pmid= 15263008 |doi= 10.1074/jbc.M404466200 }}
*{{cite journal   |vauthors=Turzanski J, Grundy M, Shang S, etal |title=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 |journal=Exp. Hematol. |volume=33 |issue= 1 |pages= 62–72 |year= 2005 |pmid= 15661399 |doi= 10.1016/j.exphem.2004.10.005 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Sun NN, Fastje CD, Wong SS, etal |title=Dose-dependent transcriptome changes by metal ores on a human acute lymphoblastic leukemia cell line |journal=Toxicology and Industrial Health |volume=19 |issue= 7–10 |pages= 157–63 |year= 2005 |pmid= 15747776 |doi=10.1191/0748233703th185oa }}
*{{cite journal | author=Turzanski J, Grundy M, Shang S, ''et al.'' |title=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. |journal=Exp. Hematol. |volume=33 |issue= 1 |pages= 62-72 |year= 2005 |pmid= 15661399 |doi= 10.1016/j.exphem.2004.10.005 }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode = 2005Natur.437.1173R }}
*{{cite journal | author=Sun NN, Fastje CD, Wong SS, ''et al.'' |title=Dose-dependent transcriptome changes by metal ores on a human acute lymphoblastic leukemia cell line. |journal=Toxicology and industrial health |volume=19 |issue= 7-10 |pages= 157-63 |year= 2005 |pmid= 15747776 |doi=  }}
*{{cite journal   |vauthors=Fazi B, Melino S, Di Sano F, etal |title=Cloning, expression, and preliminary structural characterization of RTN-1C |journal=Biochem. Biophys. Res. Commun. |volume=342 |issue= 3 |pages= 881–6 |year= 2006 |pmid= 16500619 |doi= 10.1016/j.bbrc.2006.02.036 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Fazi B, Melino S, Di Sano F, ''et al.'' |title=Cloning, expression, and preliminary structural characterization of RTN-1C. |journal=Biochem. Biophys. Res. Commun. |volume=342 |issue= 3 |pages= 881-6 |year= 2006 |pmid= 16500619 |doi= 10.1016/j.bbrc.2006.02.036 }}
}}
}}
{{refend}}
{{refend}}


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{{Glycolipid/sphingolipid metabolism enzymes}}
 
 
{{gene-9-stub}}

Latest revision as of 07:37, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ceramide glucosyltransferase is an enzyme that in humans is encoded by the UGCG gene.[1][2][3]

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.[3]

Interactions

UGCG has been shown to interact with RTN1 .[4]

References

  1. 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". Proc Natl Acad Sci U S A. 93 (10): 4638–43. Bibcode:1996PNAS...93.4638I. doi:10.1073/pnas.93.10.4638. PMC 39331. PMID 8643456.
  2. 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): 233–4. doi:10.1159/000134731. PMID 9605861.
  3. 3.0 3.1 "Entrez Gene: UGCG UDP-glucose ceramide glucosyltransferase".
  4. Di Sano, Federica; 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): 3860–5. ISSN 0008-5472. PMID 12873973.

Further reading