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Entry version 183 (31 Jul 2019)
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).By similarity8 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
    Proteins known to be involved in this subpathway in this organism are:
    1. UDP-glucose 6-dehydrogenase (UGDH)
    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

    • NAD binding Source: InterPro
    • UDP-glucose 6-dehydrogenase activity Source: UniProtKB

    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

    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

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    <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

    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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    7358

    Open Targets

    More...
    OpenTargetsi
    ENSG00000109814

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA37170

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00157 NADH

    Polymorphism and mutation 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.<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

    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 human proteome resource

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

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    O60701

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    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 220 organ(s), highest expression level in layer of synovial tissue

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    O60701 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O60701 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB034444
    HPA036656
    HPA036657

    <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.

    10 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    113205, 52 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    O60701, 7 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000319501

    <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...

    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 – 110Intrinsically disordered; important for formation of active hexamer structure1 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 – 494Intrinsically disordered1 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
    COG1004 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000015355

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000153773

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O60701

    KEGG Orthology (KO)

    More...
    KOi
    K00012

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LCTEWDE

    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

    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

    More...
    PANTHERi
    PTHR11374 PTHR11374, 1 hit

    Pfam protein domain database

    More...
    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

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

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00984 UDPG_MGDP_dh_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48179 SSF48179, 1 hit
    SSF51735 SSF51735, 1 hit
    SSF52413 SSF52413, 1 hit

    TIGRFAMs; a protein family database

    More...
    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.

    Note: No experimental confirmation available.
    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.

    Note: No experimental confirmation available.
    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
    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>
    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>
    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>
    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>
    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>
    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

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0462341 – 97Missing in isoform 3. 1 PublicationAdd BLAST97
    Alternative sequenceiVSP_04255089 – 155Missing in isoform 2. 1 PublicationAdd BLAST67

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF061016 mRNA Translation: AAC36095.1
    AJ007702 mRNA Translation: CAA07609.1
    AJ272274
    , AJ272275, AJ272276, AJ272277, AJ272278, AJ272279, AJ272280, AJ272281 Genomic DNA Translation: CAB75891.1
    AK097930 mRNA Translation: BAG53554.1
    AK297737 mRNA Translation: BAG60087.1
    AC021148 Genomic DNA No translation available.
    CH471069 Genomic DNA Translation: EAW92937.1
    BC022781 mRNA Translation: AAH22781.1
    AF049126 mRNA Translation: AAC05135.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS3455.1 [O60701-1]
    CCDS54757.1 [O60701-3]
    CCDS54758.1 [O60701-2]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JE0353

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001171629.1, NM_001184700.1 [O60701-2]
    NP_001171630.1, NM_001184701.1 [O60701-3]
    NP_003350.1, NM_003359.3 [O60701-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000316423; ENSP00000319501; ENSG00000109814 [O60701-1]
    ENST00000501493; ENSP00000422909; ENSG00000109814 [O60701-2]
    ENST00000506179; ENSP00000421757; ENSG00000109814 [O60701-1]
    ENST00000507089; ENSP00000426560; ENSG00000109814 [O60701-3]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    7358

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:7358

    UCSC genome browser

    More...
    UCSCi
    uc003guk.3 human [O60701-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <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

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF061016 mRNA Translation: AAC36095.1
    AJ007702 mRNA Translation: CAA07609.1
    AJ272274
    , AJ272275, AJ272276, AJ272277, AJ272278, AJ272279, AJ272280, AJ272281 Genomic DNA Translation: CAB75891.1
    AK097930 mRNA Translation: BAG53554.1
    AK297737 mRNA Translation: BAG60087.1
    AC021148 Genomic DNA No translation available.
    CH471069 Genomic DNA Translation: EAW92937.1
    BC022781 mRNA Translation: AAH22781.1
    AF049126 mRNA Translation: AAC05135.1
    CCDSiCCDS3455.1 [O60701-1]
    CCDS54757.1 [O60701-3]
    CCDS54758.1 [O60701-2]
    PIRiJE0353
    RefSeqiNP_001171629.1, NM_001184700.1 [O60701-2]
    NP_001171630.1, NM_001184701.1 [O60701-3]
    NP_003350.1, NM_003359.3 [O60701-1]

    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 entryMethodResolution (Å)ChainPositionsPDBsum
    2Q3EX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-466[»]
    2QG4X-ray2.10A/B/C/D/E/F/G/H1-466[»]
    3ITKX-ray2.40A/B/C/D/E/F1-466[»]
    3KHUX-ray2.30A/B/C/D/E/F1-466[»]
    3PRJX-ray3.10A/B/C/D/E/F1-494[»]
    3PTZX-ray2.50A/B/C/D/E/F1-494[»]
    3TDKX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-487[»]
    3TF5X-ray2.30A/B/C1-494[»]
    4EDFX-ray2.08A/B/C/D1-494[»]
    4RJTX-ray2.70A/B/C1-494[»]
    5TJHX-ray2.05A/B/C/D/E/F1-494[»]
    5VR8X-ray2.00A/B/C/D/E/F1-466[»]
    5W4XX-ray2.65A/B/C1-494[»]
    6C4JX-ray2.53A/B/C/D/E/F/G/H/I/J/K/L1-494[»]
    6C4KX-ray2.65A/B/C1-494[»]
    6C58X-ray2.20A/B/C/D/E/F1-494[»]
    6C5AX-ray2.30A/B/C/D/E/F1-494[»]
    6C5ZX-ray2.95A/B/C/D/E/F1-494[»]
    SMRiO60701
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi113205, 52 interactors
    IntActiO60701, 7 interactors
    STRINGi9606.ENSP00000319501

    Chemistry databases

    DrugBankiDB00157 NADH

    PTM databases

    iPTMnetiO60701
    PhosphoSitePlusiO60701
    SwissPalmiO60701

    Polymorphism and mutation databases

    BioMutaiUGDH

    2D gel databases

    REPRODUCTION-2DPAGEiO60701

    Proteomic databases

    EPDiO60701
    jPOSTiO60701
    MaxQBiO60701
    PaxDbiO60701
    PeptideAtlasiO60701
    PRIDEiO60701
    ProteomicsDBi4666
    49530 [O60701-1]
    49531 [O60701-2]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    7358
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000316423; ENSP00000319501; ENSG00000109814 [O60701-1]
    ENST00000501493; ENSP00000422909; ENSG00000109814 [O60701-2]
    ENST00000506179; ENSP00000421757; ENSG00000109814 [O60701-1]
    ENST00000507089; ENSP00000426560; ENSG00000109814 [O60701-3]
    GeneIDi7358
    KEGGihsa:7358
    UCSCiuc003guk.3 human [O60701-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    7358
    DisGeNETi7358

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    UGDH
    HGNCiHGNC:12525 UGDH
    HPAiCAB034444
    HPA036656
    HPA036657
    MIMi603370 gene
    neXtProtiNX_O60701
    OpenTargetsiENSG00000109814
    PharmGKBiPA37170

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2666 Eukaryota
    COG1004 LUCA
    GeneTreeiENSGT00390000015355
    HOGENOMiHOG000153773
    InParanoidiO60701
    KOiK00012
    OMAiLCTEWDE
    OrthoDBi915490at2759
    PhylomeDBiO60701
    TreeFamiTF105671

    Enzyme and pathway databases

    UniPathwayiUPA00038;UER00491
    BRENDAi1.1.1.22 2681
    ReactomeiR-HSA-173599 Formation of the active cofactor, UDP-glucuronate
    SABIO-RKiO60701

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    UGDH human
    EvolutionaryTraceiO60701

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    UGDH

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    7358

    Protein Ontology

    More...
    PROi
    PR:O60701

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000109814 Expressed in 220 organ(s), highest expression level in layer of synovial tissue
    ExpressionAtlasiO60701 baseline and differential
    GenevisibleiO60701 HS

    Family and domain databases

    InterProiView 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
    PANTHERiPTHR11374 PTHR11374, 1 hit
    PfamiView protein in Pfam
    PF00984 UDPG_MGDP_dh, 1 hit
    PF03720 UDPG_MGDP_dh_C, 1 hit
    PF03721 UDPG_MGDP_dh_N, 1 hit
    PIRSFiPIRSF500133 UDPglc_DH_euk, 1 hit
    PIRSF000124 UDPglc_GDPman_dh, 1 hit
    SMARTiView protein in SMART
    SM00984 UDPG_MGDP_dh_C, 1 hit
    SUPFAMiSSF48179 SSF48179, 1 hit
    SSF51735 SSF51735, 1 hit
    SSF52413 SSF52413, 1 hit
    TIGRFAMsiTIGR03026 NDP-sugDHase, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUGDH_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O60701
    Secondary accession number(s): B3KUU2, B4DN25, O60589
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: July 31, 2019
    This is version 183 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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