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Q16739

- CEGT_HUMAN

UniProt

Q16739 - CEGT_HUMAN

Protein

Ceramide glucosyltransferase

Gene

UGCG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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.
    GenevestigatoriQ16739.

    Organism-specific databases

    HPAiHPA024124.

    Interactioni

    Protein-protein interaction databases

    BioGridi113204. 4 interactions.
    STRINGi9606.ENSP00000363397.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16739.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010LumenalSequence Analysis
    Topological domaini33 – 195163CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini216 – 28772LumenalSequence AnalysisAdd
    BLAST
    Topological domaini305 – 3095CytoplasmicSequence Analysis
    Topological domaini329 – 34820LumenalSequence AnalysisAdd
    BLAST
    Topological domaini370 – 39425CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 21520HelicalSequence AnalysisAdd
    BLAST
    Transmembranei288 – 30417HelicalSequence AnalysisAdd
    BLAST
    Transmembranei310 – 32819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei349 – 36921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1215.
    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

    MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL    50
    PGVSLLKPLK GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK 100
    LLGKYPNVDA RLFIGGKKVG INPKINNLMP GYEVAKYDLI WICDSGIRVI 150
    PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG TSHPRYYISA 200
    NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWRF 250
    AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS 300
    LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA 350
    VAWFIRESMT IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV 394
    Length:394
    Mass (Da):44,854
    Last modified:November 1, 1997 - v1
    Checksum:i3B998569F8A96449
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_003358.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6782.1.
    RefSeqi NP_003349.1. NM_003358.1.
    UniGenei Hs.304249.
    Hs.593014.

    3D structure databases

    ProteinModelPortali Q16739.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113204. 4 interactions.
    STRINGi 9606.ENSP00000363397.

    Chemistry

    BindingDBi Q16739.
    ChEMBLi CHEMBL2063.
    DrugBanki DB00419. Miglustat.
    GuidetoPHARMACOLOGYi 2528.

    Protein family/group databases

    CAZyi GT21. Glycosyltransferase Family 21.
    TCDBi 4.D.1.4.1. the putative vectorial glycosyl polymerization (vgp) family.

    PTM databases

    PhosphoSitei Q16739.

    Polymorphism databases

    DMDMi 2498228.

    Proteomic databases

    MaxQBi Q16739.
    PaxDbi Q16739.
    PRIDEi Q16739.

    Protocols and materials databases

    DNASUi 7357.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374279 ; ENSP00000363397 ; ENSG00000148154 .
    GeneIDi 7357.
    KEGGi hsa:7357.
    UCSCi uc004bft.3. human.

    Organism-specific databases

    CTDi 7357.
    GeneCardsi GC09P114659.
    HGNCi HGNC:12524. UGCG.
    HPAi HPA024124.
    MIMi 602874. gene.
    neXtProti NX_Q16739.
    PharmGKBi PA37169.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1215.
    HOGENOMi HOG000039663.
    HOVERGENi HBG003997.
    InParanoidi Q16739.
    KOi K00720.
    OMAi LVWICDS.
    OrthoDBi EOG70KGPR.
    PhylomeDBi Q16739.
    TreeFami TF314564.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    BRENDAi 2.4.1.80. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.

    Miscellaneous databases

    GeneWikii UGCG.
    GenomeRNAii 7357.
    NextBioi 28808.
    PROi Q16739.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16739.
    CleanExi HS_UGCG.
    Genevestigatori Q16739.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR025993. Ceramide_glucosylTrfase.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    Pfami PF13506. Glyco_transf_21. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 125 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