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Q16739 (CEGT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UGCG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Found in all tissues examined. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Ceramide glucosyltransferase
PRO_0000059176

Regions

Topological domain1 – 1010Lumenal Potential
Transmembrane11 – 3222Helical; Potential
Topological domain33 – 195163Cytoplasmic Potential
Transmembrane196 – 21520Helical; Potential
Topological domain216 – 28772Lumenal Potential
Transmembrane288 – 30417Helical; Potential
Topological domain305 – 3095Cytoplasmic Potential
Transmembrane310 – 32819Helical; Potential
Topological domain329 – 34820Lumenal Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 39425Cytoplasmic Potential

Sites

Site1931May play an important role in binding to the inhibitors DEPC and PDMP By similarity

Amino acid modifications

Modified residue1171N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q16739 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 3B998569F8A96449

FASTA39444,854
        10         20         30         40         50         60 
MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK 

        70         80         90        100        110        120 
GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG 

       130        140        150        160        170        180 
INPKINNLMP GYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF 

       190        200        210        220        230        240 
AATLEQVYFG TSHPRYYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA 

       250        260        270        280        290        300 
KAIADRGWRF AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS 

       310        320        330        340        350        360 
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT 

       370        380        390 
IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6782.1.
RefSeqNP_003349.1. NM_003358.1.
UniGeneHs.304249.
Hs.593014.

3D structure databases

ProteinModelPortalQ16739.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113204. 4 interactions.
STRING9606.ENSP00000363397.

Chemistry

BindingDBQ16739.
ChEMBLCHEMBL2063.
DrugBankDB00419. Miglustat.
GuidetoPHARMACOLOGY2528.

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

PTM databases

PhosphoSiteQ16739.

Polymorphism databases

DMDM2498228.

Proteomic databases

MaxQBQ16739.
PaxDbQ16739.
PRIDEQ16739.

Protocols and materials databases

DNASU7357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374279; ENSP00000363397; ENSG00000148154.
GeneID7357.
KEGGhsa:7357.
UCSCuc004bft.3. human.

Organism-specific databases

CTD7357.
GeneCardsGC09P114659.
HGNCHGNC:12524. UGCG.
HPAHPA024124.
MIM602874. gene.
neXtProtNX_Q16739.
PharmGKBPA37169.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000039663.
HOVERGENHBG003997.
InParanoidQ16739.
KOK00720.
OMALVWICDS.
OrthoDBEOG70KGPR.
PhylomeDBQ16739.
TreeFamTF314564.

Enzyme and pathway databases

BRENDA2.4.1.80. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00222.

Gene expression databases

BgeeQ16739.
CleanExHS_UGCG.
GenevestigatorQ16739.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

GeneWikiUGCG.
GenomeRNAi7357.
NextBio28808.
PROQ16739.
SOURCESearch...

Entry information

Entry nameCEGT_HUMAN
AccessionPrimary (citable) accession number: Q16739
Secondary accession number(s): Q5T258
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM