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O94923

- GLCE_HUMAN

UniProt

O94923 - GLCE_HUMAN

Protein

D-glucuronyl C5-epimerase

Gene

GLCE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins.1 Publication

    Catalytic activityi

    Heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. heparosan-N-sulfate-glucuronate 5-epimerase activity Source: UniProtKB
    2. racemase and epimerase activity, acting on carbohydrates and derivatives Source: UniProtKB
    3. UDP-glucuronate 5'-epimerase activity Source: HGNC

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan biosynthetic process Source: Reactome
    3. glycosaminoglycan metabolic process Source: Reactome
    4. heparan sulfate proteoglycan biosynthetic process Source: UniProtKB
    5. heparin biosynthetic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_121248. HS-GAG biosynthesis.
    UniPathwayiUPA00756.
    UPA00862.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-glucuronyl C5-epimerase (EC:5.1.3.17)
    Alternative name(s):
    Heparan sulfate C5-epimerase
    Short name:
    Hsepi
    Heparin/heparan sulfate:glucuronic acid C5-epimerase
    Heparosan-N-sulfate-glucuronate 5-epimerase
    Gene namesi
    Name:GLCE
    Synonyms:KIAA0836Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:17855. GLCE.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi146 – 1461Y → A: Reduces enzyme activity by about 60%. 1 Publication
    Mutagenesisi162 – 1621Y → A: Reduces enzyme activity by about 75%. 1 Publication
    Mutagenesisi168 – 1681Y → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi210 – 2101Y → A: Reduces enzyme activity by about 30%. 1 Publication
    Mutagenesisi222 – 2221Y → A: Almost abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA145148750.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 617617D-glucuronyl C5-epimerasePRO_0000192645Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi225 – 2251N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiO94923.
    PaxDbiO94923.
    PRIDEiO94923.

    PTM databases

    PhosphoSiteiO94923.

    Expressioni

    Gene expression databases

    ArrayExpressiO94923.
    BgeeiO94923.
    CleanExiHS_GLCE.
    GenevestigatoriO94923.

    Organism-specific databases

    HPAiHPA040481.
    HPA048216.

    Interactioni

    Subunit structurei

    Interacts with HS2ST1.By similarity

    Protein-protein interaction databases

    BioGridi117501. 2 interactions.
    STRINGi9606.ENSP00000261858.

    Structurei

    3D structure databases

    ProteinModelPortaliO94923.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini29 – 617589LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 2817Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the D-glucuronyl C5-epimerase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG86883.
    HOGENOMiHOG000230542.
    HOVERGENiHBG031576.
    InParanoidiO94923.
    KOiK01793.
    OMAiKPNDWTV.
    PhylomeDBiO94923.
    TreeFamiTF105869.

    Family and domain databases

    InterProiIPR010598. C5-epim.
    [Graphical view]
    PfamiPF06662. C5-epim_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O94923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCLAARVNY KTLIIICALF TLVTVLLWNK CSSDKAIQFP RRSSSGFRVD    50
    GFEKRAAASE SNNYMNHVAK QQSEEAFPQE QQKAPPVVGG FNSNVGSKVL 100
    GLKYEEIDCL INDEHTIKGR REGNEVFLPF TWVEKYFDVY GKVVQYDGYD 150
    RFEFSHSYSK VYAQRAPYHP DGVFMSFEGY NVEVRDRVKC ISGVEGVPLS 200
    TQWGPQGYFY PIQIAQYGLS HYSKNLTEKP PHIEVYETAE DRDKNKPNDW 250
    TVPKGCFMAN VADKSRFTNV KQFIAPETSE GVSLQLGNTK DFIISFDLKF 300
    LTNGSVSVVL ETTEKNQLFT IHYVSNAQLI AFKERDIYYG IGPRTSWSTV 350
    TRDLVTDLRK GVGLSNTKAV KPTKIMPKKV VRLIAKGKGF LDNITISTTA 400
    HMAAFFAASD WLVRNQDEKG GWPIMVTRKL GEGFKSLEPG WYSAMAQGQA 450
    ISTLVRAYLL TKDHIFLNSA LRATAPYKFL SEQHGVKAVF MNKHDWYEEY 500
    PTTPSSFVLN GFMYSLIGLY DLKETAGEKL GKEARSLYER GMESLKAMLP 550
    LYDTGSGTIY DLRHFMLGIA PNLARWDYHT THINQLQLLS TIDESPVFKE 600
    FVKRWKSYLK GSRAKHN 617
    Length:617
    Mass (Da):70,101
    Last modified:June 16, 2009 - v3
    Checksum:i2F909A15FEA6DA05
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651M → V.
    Corresponds to variant rs12440300 [ dbSNP | Ensembl ].
    VAR_055837
    Natural varianti597 – 5971V → I.1 Publication
    Corresponds to variant rs3865014 [ dbSNP | Ensembl ].
    VAR_057958

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY635582 mRNA. Translation: AAT48654.1.
    AC026992 mRNA. No translation available.
    AB020643 mRNA. Translation: BAA74859.1.
    CCDSiCCDS32277.1.
    RefSeqiNP_056369.1. NM_015554.1.
    XP_005254355.1. XM_005254298.1.
    UniGeneiHs.183006.

    Genome annotation databases

    EnsembliENST00000261858; ENSP00000261858; ENSG00000138604.
    GeneIDi26035.
    KEGGihsa:26035.
    UCSCiuc002ary.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY635582 mRNA. Translation: AAT48654.1 .
    AC026992 mRNA. No translation available.
    AB020643 mRNA. Translation: BAA74859.1 .
    CCDSi CCDS32277.1.
    RefSeqi NP_056369.1. NM_015554.1.
    XP_005254355.1. XM_005254298.1.
    UniGenei Hs.183006.

    3D structure databases

    ProteinModelPortali O94923.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117501. 2 interactions.
    STRINGi 9606.ENSP00000261858.

    PTM databases

    PhosphoSitei O94923.

    Proteomic databases

    MaxQBi O94923.
    PaxDbi O94923.
    PRIDEi O94923.

    Protocols and materials databases

    DNASUi 26035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261858 ; ENSP00000261858 ; ENSG00000138604 .
    GeneIDi 26035.
    KEGGi hsa:26035.
    UCSCi uc002ary.1. human.

    Organism-specific databases

    CTDi 26035.
    GeneCardsi GC15P069452.
    HGNCi HGNC:17855. GLCE.
    HPAi HPA040481.
    HPA048216.
    MIMi 612134. gene.
    neXtProti NX_O94923.
    PharmGKBi PA145148750.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86883.
    HOGENOMi HOG000230542.
    HOVERGENi HBG031576.
    InParanoidi O94923.
    KOi K01793.
    OMAi KPNDWTV.
    PhylomeDBi O94923.
    TreeFami TF105869.

    Enzyme and pathway databases

    UniPathwayi UPA00756 .
    UPA00862 .
    Reactomei REACT_121248. HS-GAG biosynthesis.

    Miscellaneous databases

    GeneWikii GLCE.
    GenomeRNAii 26035.
    NextBioi 47849.
    PROi O94923.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94923.
    Bgeei O94923.
    CleanExi HS_GLCE.
    Genevestigatori O94923.

    Family and domain databases

    InterProi IPR010598. C5-epim.
    [Graphical view ]
    Pfami PF06662. C5-epim_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homo sapiens D-glucuronyl C5-epimerase (GLCE)."
      Ghiselli G.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-617, VARIANT ILE-597.
      Tissue: Brain.
    4. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
      Tissue: Liver.
    5. "Using engineered 2-O-sulfotransferase to determine the activity of heparan sulfate C5-epimerase and its mutants."
      Li K., Bethea H.N., Liu J.
      J. Biol. Chem. 285:11106-11113(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-146; TYR-162; TYR-168; TYR-210 AND TYR-222.
    6. "Uncovering a biphasic catalytic mode of C5-epimerase in heparan sulfate biosynthesis."
      Sheng J., Xu Y., Dulaney S.B., Huang X., Liu J.
      J. Biol. Chem. 287:20996-21002(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiGLCE_HUMAN
    AccessioniPrimary (citable) accession number: O94923
    Secondary accession number(s): Q6GUQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3