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O94923 (GLCE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GLCE
Synonyms:KIAA0836
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 UniProtKB Q9EPS3

Catalytic activity

Heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate. Ref.5 Ref.6

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Glycan metabolism; heparin biosynthesis.

Subunit structure

Interacts with HS2ST1 By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the D-glucuronyl C5-epimerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 617617D-glucuronyl C5-epimerase
PRO_0000192645

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 2817Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 617589Lumenal Potential

Amino acid modifications

Glycosylation2251N-linked (GlcNAc...) Ref.4

Natural variations

Natural variant651M → V.
Corresponds to variant rs12440300 [ dbSNP | Ensembl ].
VAR_055837
Natural variant5971V → I. Ref.3
Corresponds to variant rs3865014 [ dbSNP | Ensembl ].
VAR_057958

Experimental info

Mutagenesis1461Y → A: Reduces enzyme activity by about 60%. Ref.5
Mutagenesis1621Y → A: Reduces enzyme activity by about 75%. Ref.5
Mutagenesis1681Y → A: Almost abolishes enzyme activity. Ref.5
Mutagenesis2101Y → A: Reduces enzyme activity by about 30%. Ref.5
Mutagenesis2221Y → A: Almost abolishes enzyme activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O94923 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 2F909A15FEA6DA05

FASTA61770,101
        10         20         30         40         50         60 
MRCLAARVNY KTLIIICALF TLVTVLLWNK CSSDKAIQFP RRSSSGFRVD GFEKRAAASE 

        70         80         90        100        110        120 
SNNYMNHVAK QQSEEAFPQE QQKAPPVVGG FNSNVGSKVL GLKYEEIDCL INDEHTIKGR 

       130        140        150        160        170        180 
REGNEVFLPF TWVEKYFDVY GKVVQYDGYD RFEFSHSYSK VYAQRAPYHP DGVFMSFEGY 

       190        200        210        220        230        240 
NVEVRDRVKC ISGVEGVPLS TQWGPQGYFY PIQIAQYGLS HYSKNLTEKP PHIEVYETAE 

       250        260        270        280        290        300 
DRDKNKPNDW TVPKGCFMAN VADKSRFTNV KQFIAPETSE GVSLQLGNTK DFIISFDLKF 

       310        320        330        340        350        360 
LTNGSVSVVL ETTEKNQLFT IHYVSNAQLI AFKERDIYYG IGPRTSWSTV TRDLVTDLRK 

       370        380        390        400        410        420 
GVGLSNTKAV KPTKIMPKKV VRLIAKGKGF LDNITISTTA HMAAFFAASD WLVRNQDEKG 

       430        440        450        460        470        480 
GWPIMVTRKL GEGFKSLEPG WYSAMAQGQA ISTLVRAYLL TKDHIFLNSA LRATAPYKFL 

       490        500        510        520        530        540 
SEQHGVKAVF MNKHDWYEEY PTTPSSFVLN GFMYSLIGLY DLKETAGEKL GKEARSLYER 

       550        560        570        580        590        600 
GMESLKAMLP LYDTGSGTIY DLRHFMLGIA PNLARWDYHT THINQLQLLS TIDESPVFKE 

       610 
FVKRWKSYLK GSRAKHN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY635582 mRNA. Translation: AAT48654.1.
AC026992 mRNA. No translation available.
AB020643 mRNA. Translation: BAA74859.1.
CCDSCCDS32277.1.
RefSeqNP_056369.1. NM_015554.1.
XP_005254355.1. XM_005254298.1.
UniGeneHs.183006.

3D structure databases

ProteinModelPortalO94923.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117501. 2 interactions.
STRING9606.ENSP00000261858.

PTM databases

PhosphoSiteO94923.

Proteomic databases

MaxQBO94923.
PaxDbO94923.
PRIDEO94923.

Protocols and materials databases

DNASU26035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261858; ENSP00000261858; ENSG00000138604.
GeneID26035.
KEGGhsa:26035.
UCSCuc002ary.1. human.

Organism-specific databases

CTD26035.
GeneCardsGC15P069452.
HGNCHGNC:17855. GLCE.
HPAHPA040481.
HPA048216.
MIM612134. gene.
neXtProtNX_O94923.
PharmGKBPA145148750.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86883.
HOGENOMHOG000230542.
HOVERGENHBG031576.
InParanoidO94923.
KOK01793.
OMAKPNDWTV.
PhylomeDBO94923.
TreeFamTF105869.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00756.
UPA00862.

Gene expression databases

ArrayExpressO94923.
BgeeO94923.
CleanExHS_GLCE.
GenevestigatorO94923.

Family and domain databases

InterProIPR010598. C5-epim.
[Graphical view]
PfamPF06662. C5-epim_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGLCE.
GenomeRNAi26035.
NextBio47849.
PROO94923.
SOURCESearch...

Entry information

Entry nameGLCE_HUMAN
AccessionPrimary (citable) accession number: O94923
Secondary accession number(s): Q6GUQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 107 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM