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Entry version 197 (29 Sep 2021)
Sequence version 1 (01 Aug 1998)
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Protein

UDP-glucose 6-dehydrogenase

Gene

UGDH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21961565, PubMed:21502315, PubMed:23106432, PubMed:22123821, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329).

Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity).

Required for proper brain and neuronal development (PubMed:32001716).

By similarity9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor. It binds at the same site as the substrate, but functions as allosteric inhibitor by triggering a conformation change that disrupts the active hexameric ring structure and gives rise to an inactive, horseshoe-shaped hexamer.5 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.55 sec(-1) with UDP-glucose as substrate.1 Publication
  1. KM=9.7 µM for UDP-glucose1 Publication
  2. KM=7.6 µM for UDP-glucose1 Publication
  3. KM=25 µM for UDP-glucose1 Publication
  4. KM=780 µM for NAD1 Publication
  5. KM=1160 µM for NAD+1 Publication
  6. KM=384 µM for NAD+1 Publication

pH dependencei

Optimum pH is 8.6.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UDP-alpha-D-glucuronate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose.8 Publications This subpathway is part of the pathway UDP-alpha-D-glucuronate biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-alpha-D-glucuronate from UDP-alpha-D-glucose, the pathway UDP-alpha-D-glucuronate biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei36NADCombined sources3 Publications1
Binding sitei41NADCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei161Proton donor/acceptor1 Publication1
Binding sitei165NADCombined sources1 Publication1
Active sitei220Proton donor/acceptor1 Publication1
Binding sitei260SubstrateCombined sources2 Publications2 Publications1
Active sitei276Nucleophile3 Publications1
Binding sitei346NADCombined sources4 Publications1
Binding sitei442SubstrateCombined sources2 Publications2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi11 – 16NADCombined sources3 Publications6
Nucleotide bindingi89 – 93NADCombined sources3 Publications5
Nucleotide bindingi130 – 132NAD2 Publications3
Nucleotide bindingi276 – 279NADCombined sources3 Publications4

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
Biological processCarbohydrate metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.22, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O60701

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-173599, Formation of the active cofactor, UDP-glucuronate

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O60701

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00038;UER00491

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
UDP-glucose 6-dehydrogenase (EC:1.1.1.227 Publications)
Short name:
UDP-Glc dehydrogenase
Short name:
UDP-GlcDH
Short name:
UDPGDH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:UGDH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12525, UGDH

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603370, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O60701

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000109814

<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

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Developmental and epileptic encephalopathy 84 (DEE84)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE84 is an autosomal recessive form characterized by onset of refractory seizures in the first months of life.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08375014Y → C in DEE84. 1 Publication1
Natural variantiVAR_08375124A → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_08375242I → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_08375344A → V in DEE84; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity. 1 PublicationCorresponds to variant dbSNP:rs749975104EnsemblClinVar.1
Natural variantiVAR_08375465 – 494Missing in DEE84. 1 PublicationCorresponds to variant dbSNP:rs200059198Add BLAST430
Natural variantiVAR_08375572S → A in DEE84. 1 Publication1
Natural variantiVAR_08375682A → T in DEE84; decreased function in glycosaminoglycan biosynthetic process in patient cells; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity. 1 Publication1
Natural variantiVAR_083757116I → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083758155 – 494Missing in DEE84. 1 PublicationCorresponds to variant dbSNP:rs1381665298Add BLAST340
Natural variantiVAR_083759175P → A in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs756467468EnsemblClinVar.1
Natural variantiVAR_083760217E → D in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083761255I → T in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1186496501EnsemblClinVar.1
Natural variantiVAR_083762271G → R in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083763303V → I in DEE84; unknown pathological significance; may affect splicing. 1 Publication1
Natural variantiVAR_083764306M → V in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083765317R → Q in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs775162839EnsemblClinVar.1
Natural variantiVAR_083766356 – 494Missing in DEE84. 1 PublicationAdd BLAST139
Natural variantiVAR_083767367Y → C in DEE84. 1 Publication1
Natural variantiVAR_083768393R → W in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs113094436EnsemblClinVar.1
Natural variantiVAR_083769410A → S in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770456604EnsemblClinVar.1
Natural variantiVAR_083770442R → W in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201894374EnsemblClinVar.1
Natural variantiVAR_083771443R → H in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083772449H → R in DEE84; unknown pathological significance. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi94K → E: Loss of hexamer formation. Causes formation of stable dimers. Strongly reduced affinity for NAD and UDP-glucose, and strongly decreased catalytic efficiency at pH 8.6. 2 Publications1
Mutagenesisi104A → G: Impairs protein folding. Decreases affinity for UDP-glucose. No effect on inhibition by UDP-xylose. No effect on hysteresis and cooperativity. 1 Publication1
Mutagenesisi104A → L: No significant effect on catalytic activity and on affinity for NAD and UDP-glucose. Decreases affinity for the inhibitor UDP-xylose. Disrupts hysteresis and cooperativity. 1 Publication1
Mutagenesisi131T → A: Reduced affinity for UDP-glucose, and reduced catalytic efficiency. 1 Publication1
Mutagenesisi132Missing : Nearly abolishes enzyme activity. Stabilizes the enzyme in a low-activity hexameric conformation. 1 Publication1
Mutagenesisi136A → M: Stabilizes the active conformation of the hexamer. Decreases affinity for UDP-xylose, but not for UDP-glucose. Disrupts hysteresis and cooperativity. 2 Publications1
Mutagenesisi161E → Q: Abolishes hydrolysis of the covalent intermediate between substrate and the catalytic cysteine residue. 1 Publication1
Mutagenesisi220K → A: Loss of ezyme activity. 1 Publication1
Mutagenesisi276C → A or S: Loss of enzyme activity. 1 Publication1
Mutagenesisi280D → A: Loss of ezyme activity. 1 Publication1
Mutagenesisi323 – 325FNT → TTD: Loss of hexamer formation. Causes formation of stable dimers. Strongly decreased specific activity at pH 8.4. 1 Publication3
Mutagenesisi465 – 494KVSSK…KKPKV → SSSSSSSSSSSSSSSSSSSS SSSSSSSSSS: No effect on the intrinsically disordered nature of the C-terminus. No effect on affinity for the inhibitor UDP-xylose. 1 PublicationAdd BLAST30
Mutagenesisi465 – 494Missing : Strongly decreases affinity for the inhibitor UDP-xylose. 1 PublicationAdd BLAST30

Keywords - Diseasei

Disease variant, Epilepsy

Organism-specific databases

DisGeNET

More...
DisGeNETi
7358

MalaCards human disease database

More...
MalaCardsi
UGDH
MIMi618792, phenotype

Open Targets

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OpenTargetsi
ENSG00000109814

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37170

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O60701, Tbio

Chemistry databases

Drug and drug target database

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DrugBanki
DB09130, Copper
DB00157, NADH

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
UGDH

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000740601 – 494UDP-glucose 6-dehydrogenaseAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei107N6-acetyllysineCombined sources1
Modified residuei476PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O60701

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O60701

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O60701

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O60701

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O60701

PeptideAtlas

More...
PeptideAtlasi
O60701

PRoteomics IDEntifications database

More...
PRIDEi
O60701

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
4666
49530 [O60701-1]
49531 [O60701-2]

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
O60701

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
O60701, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O60701

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
O60701

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O60701

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O60701

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in heart, placenta, liver, pancreas, spleen, thymus, prostate, ovary, small intestine and colon (PubMed:9737970). Widely expressed (PubMed:9737970).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000109814, Expressed in layer of synovial tissue and 231 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O60701, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O60701, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000109814, Tissue enriched (liver)

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

O60701
With#Exp.IntAct
itself4EBI-353006,EBI-353006

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
113205, 64 interactors

Protein interaction database and analysis system

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IntActi
O60701, 15 interactors

Molecular INTeraction database

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MINTi
O60701

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000319501

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O60701, protein

<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

1494
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O60701

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O60701

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni88 – 110Disordered1 PublicationAdd BLAST23
Regioni129 – 135Allosteric switch region6 Publications7
Regioni161 – 165Substrate bindingCombined sources2 Publications1 Publication5
Regioni220 – 224Substrate bindingCombined sources2 Publications1 Publication5
Regioni267 – 273Substrate bindingCombined sources2 Publications1 Publication7
Regioni321 – 325Important for formation of active hexamer structure1 Publication1 Publication5
Regioni338 – 339Substrate bindingCombined sources2 Publications1 Publication2
Regioni466 – 494Disordered1 Publication2 PublicationsAdd BLAST29

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The protein goes through several conformation states during the reaction cycle, giving rise to hysteresis. In the initial state, the ligand-free protein is in an inactive conformation (E*). Substrate binding triggers a change to the active conformation (E). UDP-xylose binding triggers the transition to a distinct, inhibited conformation. The presence of an intrinsically disordered C-terminus promotes a more dynamic protein structure and favors a conformation with high affinity for UPD-xylose.1 Publication
The allosteric switch region moves by about 5 Angstroms when UDP-xylose is bound, and occupies part of the UDP-glucose binding site. At the same time it promotes domain movements that disrupt the active hexameric ring structure and lead to the formation of a horseshoe-shaped, inactive hexamer.6 Publications

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2666, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000015355

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_023810_7_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O60701

Identification of Orthologs from Complete Genome Data

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OMAi
CLNLPEV

Database of Orthologous Groups

More...
OrthoDBi
915490at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O60701

TreeFam database of animal gene trees

More...
TreeFami
TF105671

Family and domain databases

Database of protein disorder

More...
DisProti
DP02338

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR036291, NAD(P)-bd_dom_sf
IPR017476, UDP-Glc/GDP-Man
IPR014027, UDP-Glc/GDP-Man_DH_C
IPR036220, UDP-Glc/GDP-Man_DH_C_sf
IPR014026, UDP-Glc/GDP-Man_DH_dimer
IPR001732, UDP-Glc/GDP-Man_DH_N
IPR028356, UDPglc_DH_euk

The PANTHER Classification System

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PANTHERi
PTHR11374, PTHR11374, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00984, UDPG_MGDP_dh, 1 hit
PF03720, UDPG_MGDP_dh_C, 1 hit
PF03721, UDPG_MGDP_dh_N, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF500133, UDPglc_DH_euk, 1 hit
PIRSF000124, UDPglc_GDPman_dh, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00984, UDPG_MGDP_dh_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit
SSF52413, SSF52413, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR03026, NDP-sugDHase, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O60701-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL
60 70 80 90 100
PIYEPGLKEV VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK
110 120 130 140 150
GRAADLKYIE ACARRIVQNS NGYKIVTEKS TVPVRAAESI RRIFDANTKP
160 170 180 190 200
NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI GGDETPEGQR AVQALCAVYE
210 220 230 240 250
HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL CEATGADVEE
260 270 280 290 300
VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW
310 320 330 340 350
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS
360 370 380 390 400
IYISKYLMDE GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD
410 420 430 440 450
PYEACDGAHA VVICTEWDMF KELDYERIHK KMLKPAFIFD GRRVLDGLHN
460 470 480 490
ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP KFSLQDPPNK KPKV
Length:494
Mass (Da):55,024
Last modified:August 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9C9DA5E1227D65CC
GO
Isoform 2 (identifier: O60701-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     89-155: Missing.

Show »
Length:427
Mass (Da):47,603
Checksum:iDC9E41480CA48E40
GO
Isoform 3 (identifier: O60701-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Show »
Length:397
Mass (Da):44,415
Checksum:i7CD01E38C0B0D6F5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RHF4D6RHF4_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
53Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ER83E7ER83_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
130Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ETF4E7ETF4_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
153Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ER95E7ER95_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
84Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EV97E7EV97_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
181Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PBD2E9PBD2_HUMAN
UDP-glucose 6-dehydrogenase
UGDH
55Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti338F → V in AAC05135 (Ref. 8) Curated1
Sequence conflicti377V → A in AAC05135 (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08375014Y → C in DEE84. 1 Publication1
Natural variantiVAR_08375124A → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_08375242I → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_08375344A → V in DEE84; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity. 1 PublicationCorresponds to variant dbSNP:rs749975104EnsemblClinVar.1
Natural variantiVAR_08375465 – 494Missing in DEE84. 1 PublicationCorresponds to variant dbSNP:rs200059198Add BLAST430
Natural variantiVAR_08375572S → A in DEE84. 1 Publication1
Natural variantiVAR_08375682A → T in DEE84; decreased function in glycosaminoglycan biosynthetic process in patient cells; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity. 1 Publication1
Natural variantiVAR_083757116I → T in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083758155 – 494Missing in DEE84. 1 PublicationCorresponds to variant dbSNP:rs1381665298Add BLAST340
Natural variantiVAR_083759175P → A in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs756467468EnsemblClinVar.1
Natural variantiVAR_083760217E → D in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083761255I → T in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1186496501EnsemblClinVar.1
Natural variantiVAR_083762271G → R in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083763303V → I in DEE84; unknown pathological significance; may affect splicing. 1 Publication1
Natural variantiVAR_083764306M → V in DEE84; unknown pathological significance. 1 Publication1
Natural variantiVAR_083765317R → Q in DEE84; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs775162839EnsemblClinVar.1
Natural variantiVAR_083766356 – 494Missing in DEE84. 1 PublicationAdd BLAST139
Natural variantiVAR_083767367Y → C in DEE84. 1 Publication1
Natural variantiVAR_083768393R → W in DEE84; unknown pathological significance. 1 Publication