UniProtKB - O94923 (GLCE_HUMAN)

>sp|O94923|GLCE_HUMAN D-glucuronyl C5-epimerase OS=Homo sapiens OX=9606 GN=GLCE PE=1 SV=3
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSGFRVDGFEKRAAASE
SNNYMNHVAKQQSEEAFPQEQQKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIKGR
REGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGY
NVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAE
DRDKNKPNDWTVPKGCFMANVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKF
LTNGSVSVVLETTEKNQLFTIHYVSNAQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRK
GVGLSNTKAVKPTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKG
GWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFL
SEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYER
GMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPVFKE
FVKRWKSYLKGSRAKHN

Entry version 160 (07 Apr 2021)
Sequence version 3 (16 Jun 2009)
Previous versions | rss

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Protein

D-glucuronyl C5-epimerase

Gene

GLCE

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

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.3 Publications

Catalytic activityⁱ

[heparosan-N-sulfate]_(n)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
[heparan-N-sulfate]_(n)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- Ref.7
  "Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase."
  Debarnot C., Monneau Y.R., Roig-Zamboni V., Delauzun V., Le Narvor C., Richard E., Henault J., Goulet A., Fadel F., Vives R.R., Priem B., Bonnaffe D., Lortat-Jacob H., Bourne Y.
  Proc. Natl. Acad. Sci. U.S.A. 116:6760-6765(2019) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 98-617 OF WILD-TYPE AND MUTANT PHE-578 IN COMPLEXES WITH CALCIUM AND SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, GLYCOSYLATION AT ASN-225; ASN-303 AND ASN-393, MUTAGENESIS OF GLU-499; TYR-500 AND TYR-578.
EC:
5.1.3.17
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
- Ref.7
  "Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase."
  Debarnot C., Monneau Y.R., Roig-Zamboni V., Delauzun V., Le Narvor C., Richard E., Henault J., Goulet A., Fadel F., Vives R.R., Priem B., Bonnaffe D., Lortat-Jacob H., Bourne Y.
  Proc. Natl. Acad. Sci. U.S.A. 116:6760-6765(2019) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 98-617 OF WILD-TYPE AND MUTANT PHE-578 IN COMPLEXES WITH CALCIUM AND SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, GLYCOSYLATION AT ASN-225; ASN-303 AND ASN-393, MUTAGENESIS OF GLU-499; TYR-500 AND TYR-578.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
[heparosan-N-sulfate]_(n)
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=
[heparan-N-sulfate]_(n)
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Pathwayⁱ: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

Pathwayⁱ: heparin biosynthesis

This protein is involved in the pathway heparin biosynthesis, which is part of Glycan metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway heparin biosynthesis and in Glycan metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	180	SubstrateCombined sources1 Publication	1
Siteⁱ	180	Critical for catalysisBy similarity	1
Siteⁱ	187	Critical for catalysisBy similarity	1
Binding siteⁱ	202	SubstrateCombined sources1 Publication	1
Binding siteⁱ	210	SubstrateCombined sources1 Publication	1
Binding siteⁱ	213	SubstrateCombined sources1 Publication	1
Binding siteⁱ	216	SubstrateCombined sources1 Publication	1
Metal bindingⁱ	238	Calcium; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	240	CalciumCombined sources1 Publication	1
Metal bindingⁱ	268	CalciumCombined sources1 Publication	1
Metal bindingⁱ	269	Calcium; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	392	CalciumCombined sources1 Publication	1
Binding siteⁱ	510	SubstrateCombined sources1 Publication	1
Binding siteⁱ	514	SubstrateCombined sources1 Publication	1
Binding siteⁱ	560	SubstrateCombined sources1 Publication	1
Siteⁱ	560	Critical for catalysisBy similarity	1
Binding siteⁱ	563	SubstrateCombined sources1 Publication	1
Siteⁱ	578	Critical for catalysis1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	5.1.3.17, 2681
PathwayCommonsⁱ	O94923
Reactomeⁱ	R-HSA-2022928, HS-GAG biosynthesis
UniPathwayⁱ	UPA00756 UPA00862

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: D-glucuronyl C5-epimerase (EC:5.1.3.173 Publications) 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
Organismⁱ	Homo sapiens (Human)Imported
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17855, GLCE
MIMⁱ	612134, gene
neXtProtⁱ	NX_O94923
VEuPathDBⁱ	HostDB:ENSG00000138604.9

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 11	CytoplasmicSequence analysisAdd BLAST	11
Transmembraneⁱ	12 – 28	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	17
Topological domainⁱ	29 – 617	LumenalSequence analysisAdd BLAST	589

Keywords - Cellular componentⁱ

Golgi apparatus, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	146	Y → A: Reduces enzyme activity by about 60%. 1 Publication	1
Mutagenesisⁱ	162	Y → A: Reduces enzyme activity by about 75%. 1 Publication	1
Mutagenesisⁱ	168	Y → A: Almost abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	210	Y → A: Reduces enzyme activity by about 30%. 1 Publication	1
Mutagenesisⁱ	222	Y → A: Almost abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	499	E → Q: Loss of enzyme activity. 1 Publication	1
Mutagenesisⁱ	500	Y → F: Mildly decreased enzyme activity. 1 Publication	1
Mutagenesisⁱ	578	Y → F: Loss of enzyme activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	26035
Open Targets More...OpenTargetsⁱ	ENSG00000138604
PharmGKBⁱ	PA145148750

Miscellaneous databases

Pharosⁱ	O94923, Tbio

Pharosⁱ

O94923, Tbio

Genetic variation databases

BioMutaⁱ	GLCE

BioMutaⁱ

GLCE

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000192645	1 – 617	D-glucuronyl C5-epimeraseAdd BLAST		617

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	225	N-linked (GlcNAc...) asparagineCombined sources2 Publications	1
Glycosylationⁱ	303	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Glycosylationⁱ	393	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1

Keywords - PTMⁱ

Glycoprotein

Proteomic databases

EPDⁱ	O94923
jPOSTⁱ	O94923
MassIVEⁱ	O94923
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O94923
PaxDbⁱ	O94923
PeptideAtlas More...PeptideAtlasⁱ	O94923
PRIDEⁱ	O94923
ProteomicsDBⁱ	50559

PTM databases

GlyGenⁱ	O94923, 4 sites, 1 O-linked glycan (1 site)
iPTMnetⁱ	O94923
PhosphoSitePlusⁱ	O94923
SwissPalmⁱ	O94923

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000138604, Expressed in testis and 206 other tissues
ExpressionAtlasⁱ	O94923, baseline and differential
Genevisibleⁱ	O94923, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000138604, Tissue enhanced (brain)

HPAⁱ

ENSG00000138604, Tissue enhanced (brain)

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:30872481).

Interacts with HS2ST1.

By similarity1 Publication

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	117501, 27 interactors
IntActⁱ	O94923, 20 interactors
Molecular INTeraction database More...MINTⁱ	O94923
STRINGⁱ	9606.ENSP00000261858

Miscellaneous databases

RNActⁱ	O94923, protein

RNActⁱ

O94923, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	105 – 111	Combined sources	7
Turnⁱ	112 – 114	Combined sources	3
Beta strandⁱ	115 – 122	Combined sources	8
Beta strandⁱ	125 – 129	Combined sources	5
Helixⁱ	130 – 137	Combined sources	8
Beta strandⁱ	140 – 146	Combined sources	7
Beta strandⁱ	149 – 156	Combined sources	8
Helixⁱ	177 – 179	Combined sources	3
Turnⁱ	182 – 184	Combined sources	3
Beta strandⁱ	188 – 191	Combined sources	4
Turnⁱ	193 – 195	Combined sources	3
Beta strandⁱ	197 – 200	Combined sources	4
Beta strandⁱ	202 – 204	Combined sources	3
Helixⁱ	211 – 227	Combined sources	17
Beta strandⁱ	233 – 237	Combined sources	5
Beta strandⁱ	239 – 241	Combined sources	3
Beta strandⁱ	244 – 246	Combined sources	3
Beta strandⁱ	257 – 263	Combined sources	7
Turnⁱ	264 – 267	Combined sources	4
Beta strandⁱ	268 – 275	Combined sources	8
Beta strandⁱ	282 – 290	Combined sources	9
Beta strandⁱ	293 – 314	Combined sources	22
Beta strandⁱ	318 – 326	Combined sources	9
Beta strandⁱ	330 – 333	Combined sources	4
Beta strandⁱ	336 – 340	Combined sources	5
Beta strandⁱ	348 – 353	Combined sources	6
Helixⁱ	354 – 362	Combined sources	9
Beta strandⁱ	366 – 369	Combined sources	4
Beta strandⁱ	377 – 398	Combined sources	22
Helixⁱ	401 – 415	Combined sources	15
Beta strandⁱ	439 – 441	Combined sources	3
Helixⁱ	444 – 461	Combined sources	18
Helixⁱ	464 – 472	Combined sources	9
Helixⁱ	473 – 478	Combined sources	6
Helixⁱ	481 – 483	Combined sources	3
Beta strandⁱ	487 – 490	Combined sources	4
Turnⁱ	491 – 493	Combined sources	3
Beta strandⁱ	494 – 497	Combined sources	4
Helixⁱ	509 – 530	Combined sources	22
Helixⁱ	532 – 548	Combined sources	17
Helixⁱ	549 – 552	Combined sources	4
Beta strandⁱ	555 – 560	Combined sources	6
Helixⁱ	563 – 567	Combined sources	5
Helixⁱ	576 – 589	Combined sources	14
Turnⁱ	590 – 592	Combined sources	3
Helixⁱ	596 – 608	Combined sources	13
Turnⁱ	609 – 611	Combined sources	3

Show more details

3D structure databases

SMRⁱ	O94923
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	185 – 187	Substrate bindingCombined sources1 Publication	3
Regionⁱ	429 – 432	Substrate bindingBy similarity	4
Regionⁱ	499 – 500	Substrate bindingCombined sources1 Publication	2
Regionⁱ	572 – 581	Substrate bindingCombined sources1 Publication	10

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3760, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000006043
InParanoidⁱ	O94923
OMAⁱ	RGVFMYF
Database of Orthologous Groups More...OrthoDBⁱ	561819at2759
PhylomeDBⁱ	O94923
TreeFamⁱ	TF105869

Family and domain databases

InterProⁱ	View protein in InterPro IPR010598, C5-epim_C IPR039721, C5-epimerase
PANTHERⁱ	PTHR13174, PTHR13174, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06662, C5-epim_C, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

O94923-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MRCLAARVNY KTLIIICALF TLVTVLLWNK CSSDKAIQFP RRSSSGFRVD 
        60         70         80         90        100
GFEKRAAASE SNNYMNHVAK QQSEEAFPQE QQKAPPVVGG FNSNVGSKVL 
       110        120        130        140        150
GLKYEEIDCL INDEHTIKGR REGNEVFLPF TWVEKYFDVY GKVVQYDGYD 
       160        170        180        190        200
RFEFSHSYSK VYAQRAPYHP DGVFMSFEGY NVEVRDRVKC ISGVEGVPLS 
       210        220        230        240        250
TQWGPQGYFY PIQIAQYGLS HYSKNLTEKP PHIEVYETAE DRDKNKPNDW 
       260        270        280        290        300
TVPKGCFMAN VADKSRFTNV KQFIAPETSE GVSLQLGNTK DFIISFDLKF 
       310        320        330        340        350
LTNGSVSVVL ETTEKNQLFT IHYVSNAQLI AFKERDIYYG IGPRTSWSTV 
       360        370        380        390        400
TRDLVTDLRK GVGLSNTKAV KPTKIMPKKV VRLIAKGKGF LDNITISTTA 
       410        420        430        440        450
HMAAFFAASD WLVRNQDEKG GWPIMVTRKL GEGFKSLEPG WYSAMAQGQA 
       460        470        480        490        500
ISTLVRAYLL TKDHIFLNSA LRATAPYKFL SEQHGVKAVF MNKHDWYEEY 
       510        520        530        540        550
PTTPSSFVLN GFMYSLIGLY DLKETAGEKL GKEARSLYER GMESLKAMLP 
       560        570        580        590        600
LYDTGSGTIY DLRHFMLGIA PNLARWDYHT THINQLQLLS TIDESPVFKE 
       610 
FVKRWKSYLK GSRAKHN

Length:617

Mass (Da):70,101

Last modified:June 16, 2009 - v3

Checksum:ⁱ2F909A15FEA6DA05

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	H0YNP1	H0YNP1_HUMAN		Heparosan-N-sulfate-glucuronate 5-e... Heparosan-N-sulfate-glucuronate 5-epimerase, EC 5.1.3.17	GLCE	553	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_055837	65	M → V. Corresponds to variant dbSNP:rs12440300Ensembl.		1
Natural variantⁱVAR_057958	597	V → I1 PublicationCorresponds to variant dbSNP:rs3865014Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY635582 mRNA Translation: AAT48654.1 AC026992 mRNA No translation available. AB020643 mRNA Translation: BAA74859.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS32277.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001311022.1, NM_001324093.1 NP_001311023.1, NM_001324094.1 NP_056369.1, NM_015554.2 XP_005254355.1, XM_005254298.3

Genome annotation databases

Ensemblⁱ	ENST00000261858; ENSP00000261858; ENSG00000138604
GeneIDⁱ	26035
KEGGⁱ	hsa:26035
UCSC genome browser More...UCSCⁱ	uc002ary.2, human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O94923	Heparosan-N-sulfate-glucuronate 5-epimerase		HUMAN		553	UniRef100_O94923
+2

Protein	Similar proteins		Species	Score	Length	Source
O94923	Heparosan-N-sulfate-glucuronate 5-epimerase		HUMAN		553	UniRef90_O94923
Heparosan-N-sulfate-glucuronate 5-epimerase		PONAB		619
Heparosan-N-sulfate-glucuronate 5-epimerase		NOMLE		618
Heparosan-N-sulfate-glucuronate 5-epimerase		CALJA		618
Heparosan-N-sulfate-glucuronate 5-epimerase		CERAT		618
+49

Protein	Similar proteins		Species	Score	Length	Source
O94923	D-glucuronyl C5-epimerase B	)	DANRE		586	UniRef50_O94923
D-glucuronyl C5-epimerase		MOUSE		618
Heparosan-N-sulfate-glucuronate 5-epimerase		HUMAN		553
Heparosan-N-sulfate-glucuronate 5-epimerase		PONAB		619
Heparosan-N-sulfate-glucuronate 5-epimerase		NOMLE		618
+563

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY635582 mRNA Translation: AAT48654.1 AC026992 mRNA No translation available. AB020643 mRNA Translation: BAA74859.1
CCDSⁱ	CCDS32277.1
RefSeqⁱ	NP_001311022.1, NM_001324093.1 NP_001311023.1, NM_001324094.1 NP_056369.1, NM_015554.2 XP_005254355.1, XM_005254298.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	6HZZ	X-ray	2.52	A/B	98-617	[»]
	6I01	X-ray	2.10	A/B	98-617	[»]
	6I02	X-ray	2.45	A/B	98-617	[»]
SMRⁱ	O94923
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	117501, 27 interactors
IntActⁱ	O94923, 20 interactors
MINTⁱ	O94923
STRINGⁱ	9606.ENSP00000261858

PTM databases

GlyGenⁱ	O94923, 4 sites, 1 O-linked glycan (1 site)
iPTMnetⁱ	O94923
PhosphoSitePlusⁱ	O94923
SwissPalmⁱ	O94923

Genetic variation databases

BioMutaⁱ	GLCE

BioMutaⁱ

GLCE

Proteomic databases

EPDⁱ	O94923
jPOSTⁱ	O94923
MassIVEⁱ	O94923
MaxQBⁱ	O94923
PaxDbⁱ	O94923
PeptideAtlasⁱ	O94923
PRIDEⁱ	O94923
ProteomicsDBⁱ	50559

Protocols and materials databases

Antibodypediaⁱ	26368, 64 antibodies
The DNASU plasmid repository More...DNASUⁱ	26035

Genome annotation databases

Ensemblⁱ	ENST00000261858; ENSP00000261858; ENSG00000138604
GeneIDⁱ	26035
KEGGⁱ	hsa:26035
UCSCⁱ	uc002ary.2, human

Organism-specific databases

CTDⁱ	26035
DisGeNETⁱ	26035
GeneCardsⁱ	GLCE
HGNCⁱ	HGNC:17855, GLCE
HPAⁱ	ENSG00000138604, Tissue enhanced (brain)
MIMⁱ	612134, gene
neXtProtⁱ	NX_O94923
OpenTargetsⁱ	ENSG00000138604
PharmGKBⁱ	PA145148750
VEuPathDBⁱ	HostDB:ENSG00000138604.9
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3760, Eukaryota
GeneTreeⁱ	ENSGT00390000006043
InParanoidⁱ	O94923
OMAⁱ	RGVFMYF
OrthoDBⁱ	561819at2759
PhylomeDBⁱ	O94923
TreeFamⁱ	TF105869

Enzyme and pathway databases

UniPathwayⁱ	UPA00756 UPA00862
BRENDAⁱ	5.1.3.17, 2681
PathwayCommonsⁱ	O94923
Reactomeⁱ	R-HSA-2022928, HS-GAG biosynthesis

Miscellaneous databases

BioGRID-ORCSⁱ	26035, 10 hits in 961 CRISPR screens
ChiTaRSⁱ	GLCE, human
GeneWikiⁱ	GLCE
GenomeRNAiⁱ	26035
Pharosⁱ	O94923, Tbio
Protein Ontology More...PROⁱ	PR:O94923
RNActⁱ	O94923, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138604, Expressed in testis and 206 other tissues
ExpressionAtlasⁱ	O94923, baseline and differential
Genevisibleⁱ	O94923, HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR010598, C5-epim_C IPR039721, C5-epimerase
PANTHERⁱ	PTHR13174, PTHR13174, 1 hit
Pfamⁱ	View protein in Pfam PF06662, C5-epim_C, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GLCE_HUMAN
Accessionⁱ	O94923Primary (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:	April 7, 2021
	This is version 160 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

3D-structure, Reference proteome

Documents

Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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Supporting data

UniProtKB - O94923 (GLCE_HUMAN)

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D-glucuronyl C5-epimerase

GLCE

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: heparan sulfate biosynthesis

Pathwayi: heparin biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Golgi apparatus

Golgi apparatus

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Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: heparan sulfate biosynthesis

Pathwayⁱ: heparin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ