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Protein

Ceramide glucosyltransferase

Gene

UGCG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase".1 Publication

Catalytic activityi

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei193 – 1931May play an important role in binding to the inhibitors DEPC and PDMPBy similarity

GO - Molecular functioni

  1. ceramide glucosyltransferase activity Source: ProtInc

GO - Biological processi

  1. epidermis development Source: ProtInc
  2. glucosylceramide biosynthetic process Source: ProtInc
  3. glycosphingolipid biosynthetic process Source: ProtInc
  4. glycosphingolipid metabolic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.4.1.80. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
UniPathwayiUPA00222.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.
TCDBi4.D.1.4.1. the putative vectorial glycosyl polymerization (vgp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide glucosyltransferase (EC:2.4.1.80)
Alternative name(s):
GLCT-1
Glucosylceramide synthase
Short name:
GCS
UDP-glucose ceramide glucosyltransferase
UDP-glucose:N-acylsphingosine D-glucosyltransferase
Gene namesi
Name:UGCG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12524. UGCG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010LumenalSequence Analysis
Transmembranei11 – 3222HelicalSequence AnalysisAdd
BLAST
Topological domaini33 – 195163CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei196 – 21520HelicalSequence AnalysisAdd
BLAST
Topological domaini216 – 28772LumenalSequence AnalysisAdd
BLAST
Transmembranei288 – 30417HelicalSequence AnalysisAdd
BLAST
Topological domaini305 – 3095CytoplasmicSequence Analysis
Transmembranei310 – 32819HelicalSequence AnalysisAdd
BLAST
Topological domaini329 – 34820LumenalSequence AnalysisAdd
BLAST
Transmembranei349 – 36921HelicalSequence AnalysisAdd
BLAST
Topological domaini370 – 39425CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37169.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Ceramide glucosyltransferasePRO_0000059176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16739.
PaxDbiQ16739.
PRIDEiQ16739.

PTM databases

PhosphoSiteiQ16739.

Expressioni

Tissue specificityi

Found in all tissues examined.1 Publication

Gene expression databases

BgeeiQ16739.
CleanExiHS_UGCG.
ExpressionAtlasiQ16739. baseline and differential.
GenevestigatoriQ16739.

Organism-specific databases

HPAiHPA024124.

Interactioni

Protein-protein interaction databases

BioGridi113204. 9 interactions.
STRINGi9606.ENSP00000363397.

Structurei

3D structure databases

ProteinModelPortaliQ16739.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
HOVERGENiHBG003997.
InParanoidiQ16739.
KOiK00720.
OMAiLVWICDS.
OrthoDBiEOG70KGPR.
PhylomeDBiQ16739.
TreeFamiTF314564.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q16739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL
60 70 80 90 100
PGVSLLKPLK GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK
110 120 130 140 150
LLGKYPNVDA RLFIGGKKVG INPKINNLMP GYEVAKYDLI WICDSGIRVI
160 170 180 190 200
PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG TSHPRYYISA
210 220 230 240 250
NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWRF
260 270 280 290 300
AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS
310 320 330 340 350
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA
360 370 380 390
VAWFIRESMT IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV
Length:394
Mass (Da):44,854
Last modified:November 1, 1997 - v1
Checksum:i3B998569F8A96449
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50840 mRNA. Translation: BAA09451.1.
AK314847 mRNA. Translation: BAG37364.1.
AL442066 Genomic DNA. Translation: CAI15902.1.
CH471105 Genomic DNA. Translation: EAW59091.1.
BC038711 mRNA. Translation: AAH38711.1.
CCDSiCCDS6782.1.
RefSeqiNP_003349.1. NM_003358.2.
UniGeneiHs.304249.
Hs.593014.

Genome annotation databases

EnsembliENST00000374279; ENSP00000363397; ENSG00000148154.
GeneIDi7357.
KEGGihsa:7357.
UCSCiuc004bft.3. human.

Polymorphism databases

DMDMi2498228.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50840 mRNA. Translation: BAA09451.1.
AK314847 mRNA. Translation: BAG37364.1.
AL442066 Genomic DNA. Translation: CAI15902.1.
CH471105 Genomic DNA. Translation: EAW59091.1.
BC038711 mRNA. Translation: AAH38711.1.
CCDSiCCDS6782.1.
RefSeqiNP_003349.1. NM_003358.2.
UniGeneiHs.304249.
Hs.593014.

3D structure databases

ProteinModelPortaliQ16739.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113204. 9 interactions.
STRINGi9606.ENSP00000363397.

Chemistry

BindingDBiQ16739.
ChEMBLiCHEMBL2063.
DrugBankiDB00419. Miglustat.
GuidetoPHARMACOLOGYi2528.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.
TCDBi4.D.1.4.1. the putative vectorial glycosyl polymerization (vgp) family.

PTM databases

PhosphoSiteiQ16739.

Polymorphism databases

DMDMi2498228.

Proteomic databases

MaxQBiQ16739.
PaxDbiQ16739.
PRIDEiQ16739.

Protocols and materials databases

DNASUi7357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374279; ENSP00000363397; ENSG00000148154.
GeneIDi7357.
KEGGihsa:7357.
UCSCiuc004bft.3. human.

Organism-specific databases

CTDi7357.
GeneCardsiGC09P114659.
HGNCiHGNC:12524. UGCG.
HPAiHPA024124.
MIMi602874. gene.
neXtProtiNX_Q16739.
PharmGKBiPA37169.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
HOVERGENiHBG003997.
InParanoidiQ16739.
KOiK00720.
OMAiLVWICDS.
OrthoDBiEOG70KGPR.
PhylomeDBiQ16739.
TreeFamiTF314564.

Enzyme and pathway databases

UniPathwayiUPA00222.
BRENDAi2.4.1.80. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiUGCG. human.
GeneWikiiUGCG.
GenomeRNAii7357.
NextBioi28808.
PROiQ16739.
SOURCEiSearch...

Gene expression databases

BgeeiQ16739.
CleanExiHS_UGCG.
ExpressionAtlasiQ16739. baseline and differential.
GenevestigatoriQ16739.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis."
    Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.
    Proc. Natl. Acad. Sci. U.S.A. 93:4638-4643(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Melanoma.
  2. Erratum
    Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.
    Proc. Natl. Acad. Sci. U.S.A. 93:12654-12654(1996) [PubMed] [Europe PMC] [Abstract]
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiCEGT_HUMAN
AccessioniPrimary (citable) accession number: Q16739
Secondary accession number(s): Q5T258
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 4, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.