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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

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 conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.

Miscellaneous

Because IMPDH activity is tightly linked with cell proliferation, it has been recognized as a target for cancer and viral chemotherapy and as a target for immunosuppressive drugs. The activities of the antitumor drug tiazofurin, the antiviral drug ribavirin, and the immunosuppressive drugs mizoribine and mycophenolic acid (MPA) are attributed to the inhibition of IMPDH. In addition, bacterial and parasitic IMPDH's differ significantly from mammalian enzymes, which makes it a suitable target for anti-infective drugs.

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

K+UniRule annotation

<p>This subsection of the ‘Function’ 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

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Subject to product inhibition by XMP and NADH. Also inhibited by ADP.UniRule annotation1 Publication

<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

  1. KM=18 µM for Inosine 5'-phosphate2 Publications
  2. KM=46 µM for NAD+2 Publications

    <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: XMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase (DKFZp781N0678), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (guaB), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2), Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi326Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi328Potassium; via carbonyl oxygenUniRule annotation1
    <p>This subsection of the ‘Function’ 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 sitei329IMP1
    <p>This subsection of the ‘Function’ 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 sitei331Thioimidate intermediateUniRule annotation1
    Metal bindingi331Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei429Proton acceptorUniRule annotation1
    Binding sitei441IMPUniRule annotation1
    Metal bindingi500Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi274 – 276NADUniRule annotation3
    Nucleotide bindingi324 – 326NADUniRule annotation3

    <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 functionDNA-binding, Oxidoreductase, RNA-binding
    Biological processGMP biosynthesis, Purine biosynthesis
    LigandMetal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS02896-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.205 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-6798695 Neutrophil degranulation
    R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P20839

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

    More...
    UniPathwayi
    UPA00601;UER00295

    <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:
    Inosine-5'-monophosphate dehydrogenase 1UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 1UniRule annotation
    Short name:
    IMPD 1UniRule annotation
    Short name:
    IMPDH 1UniRule annotation
    Alternative name(s):
    IMPDH-I
    <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:IMPDH1UniRule annotation
    Synonyms:IMPD1
    <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 7

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000106348.16

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:6052 IMPDH1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    146690 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P20839

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <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

    Retinitis pigmentosa 10 (RP10)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
    See also OMIM:180105
    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_065617116T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_017031224R → P in RP10. 1 Publication1
    Natural variantiVAR_017032226D → N in RP10. 2 Publications1
    Natural variantiVAR_017033268V → I in RP10. 2 Publications1
    Natural variantiVAR_065621372H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Leber congenital amaurosis 11 (LCA11)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
    See also OMIM:613837
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065616105R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_065618198N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    3614

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    IMPDH1

    MalaCards human disease database

    More...
    MalaCardsi
    IMPDH1
    MIMi180105 phenotype
    613837 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000106348

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    65 Leber congenital amaurosis
    791 Retinitis pigmentosa

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA29862

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1822

    Drug and drug target database

    More...
    DrugBanki
    DB01033 Mercaptopurine
    DB00688 Mycophenolate mofetil
    DB01024 Mycophenolic acid
    DB00157 NADH
    DB00811 Ribavirin
    DB06103 VX-148

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2624

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    IMPDH1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    25014074

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedUniRule annotation1 Publication
    <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_00000936702 – 514Inosine-5'-monophosphate dehydrogenase 1Add BLAST513

    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 residuei160PhosphoserineCombined sources1
    Modified residuei341Omega-N-methylarginineBy similarity1
    Modified residuei355Omega-N-methylarginineBy similarity1

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P20839

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P20839

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

    More...
    PaxDbi
    P20839

    PeptideAtlas

    More...
    PeptideAtlasi
    P20839

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P20839

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    53811
    53812 [P20839-2]
    53813 [P20839-3]
    53814 [P20839-4]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P20839

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

    More...
    PhosphoSitePlusi
    P20839

    <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

    IMP type I is the main species in normal leukocytes and type II predominates over type I in the tumor.

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Constitutively expressed.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000106348 Expressed in 205 organ(s), highest expression level in blood

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_IMPDH1

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P20839 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P20839 HS

    <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

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    109827, 89 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-60163N

    Protein interaction database and analysis system

    More...
    IntActi
    P20839, 18 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000345096

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P20839

    <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

    1514
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P20839

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

    More...
    SMRi
    P20839

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P20839

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini114 – 173CBS 1UniRule annotationAdd BLAST60
    Domaini179 – 237CBS 2UniRule annotationAdd BLAST59

    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>Regioni364 – 366IMP binding3
    Regioni387 – 388IMP binding2
    Regioni411 – 415IMP bindingUniRule annotation5

    <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

    Belongs to the IMPDH/GMPR family.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410ISZP Eukaryota
    COG0517 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000154156

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000165752

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG052122

    KEGG Orthology (KO)

    More...
    KOi
    K00088

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SSMGYCG

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0EAV

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P20839

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300378

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00381 IMPDH, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 2 hits

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01964 IMPDH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000130 IMPDH, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00116 CBS, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01302 IMP_dehydrog, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (7+)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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 7 <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 7 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P20839-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' 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
    MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD
    60 70 80 90 100
    LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ
    110 120 130 140 150
    ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM
    160 170 180 190 200
    GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI
    210 220 230 240 250
    LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV
    260 270 280 290 300
    GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI
    310 320 330 340 350
    GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV
    360 370 380 390 400
    AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY
    410 420 430 440 450
    FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK
    460 470 480 490 500
    GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE
    510
    GGVHGLHSYE KRLY
    Length:514
    Mass (Da):55,406
    Last modified:November 8, 2002 - v2
    <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:iABAC654A9091BE62
    GO
    Isoform 2 (identifier: P20839-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-108: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:489
    Mass (Da):52,598
    Checksum:i47A1273662A8C39B
    GO
    Isoform 3 (identifier: P20839-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESM

    Show »
    Length:563
    Mass (Da):60,437
    Checksum:iEB370370B77CD0DA
    GO
    Isoform 4 (identifier: P20839-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-108: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:509
    Mass (Da):54,795
    Checksum:i83819A210AAAB3CA
    GO
    Isoform 5 (identifier: P20839-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPL...QMDRLRRASM

    Note: PubMed:14702039 (BAG53840) sequence has a frameshift in position 35.
    Show »
    Length:589
    Mass (Da):63,253
    Checksum:i31E1ED04061B62F8
    GO
    Isoform 6 (identifier: P20839-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPL...QMDRLRRASM

    Note: No experimental confirmation available.
    Show »
    Length:599
    Mass (Da):64,320
    Checksum:i7BED197A49991EA6
    GO
    Isoform 7 (identifier: P20839-7) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MADYLISGGTGYVPEDGLTAQQLFASADGLTYN → MEGPLTPPPL...VQMDRLRRAS

    Show »
    Length:566
    Mass (Da):60,898
    Checksum:iA10C18F253345FEA
    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
    C9J381C9J381_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1 IMPDH
    513Annotation score:

    Annotation score:4 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>
    C9K0R9C9K0R9_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    289Annotation 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>
    H7C511H7C511_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    226Annotation 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>
    C9J029C9J029_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    184Annotation 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>
    H7C5T1H7C5T1_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    190Annotation 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>
    F8WDE9F8WDE9_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    69Annotation 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 conflicti29G → D in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti109K → N in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti273 – 274LD → FH in AAA36114 (PubMed:1969416).Curated2
    Sequence conflicti419A → P in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti497A → P in AAA36114 (PubMed:1969416).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065616105R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_065617116T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_065618198N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_017031224R → P in RP10. 1 Publication1
    Natural variantiVAR_017032226D → N in RP10. 2 Publications1
    Natural variantiVAR_017033268V → I in RP10. 2 Publications1
    Natural variantiVAR_065619285A → T1 Publication1
    Natural variantiVAR_065620324G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_065621372H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1

    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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0469681 – 33MADYL…GLTYN → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRAS in isoform 7. CuratedAdd BLAST33
    Alternative sequenceiVSP_0143631M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3. 2 Publications1
    Alternative sequenceiVSP_0469691M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESCFLLELSSVVL LAGVGVQMDRLRRASM in isoform 5. 1 Publication1
    Alternative sequenceiVSP_0469701M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRASM in isoform 6. Curated1
    Alternative sequenceiVSP_00267484 – 108Missing in isoform 2. 1 PublicationAdd BLAST25
    Alternative sequenceiVSP_043485104 – 108Missing in isoform 4. 1 Publication5

    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
    J05272 mRNA Translation: AAA36114.1
    AK054640 mRNA Translation: BAB70780.1
    AK054667 mRNA Translation: BAG51409.1
    AK122994 mRNA Translation: BAG53840.1 Frameshift.
    AK293413 mRNA Translation: BAG56920.1
    AC010655 Genomic DNA No translation available.
    CH236947 Genomic DNA Translation: EAL24310.1
    CH236947 Genomic DNA Translation: EAL24311.1
    CH471070 Genomic DNA Translation: EAW83652.1
    BC033622 mRNA Translation: AAH33622.2
    CD014008 mRNA No translation available.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS34748.1 [P20839-3]
    CCDS34749.1 [P20839-6]
    CCDS43643.1 [P20839-5]
    CCDS47699.1 [P20839-7]
    CCDS47700.1 [P20839-2]
    CCDS55161.1 [P20839-4]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A35566

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000874.2, NM_000883.3 [P20839-6]
    NP_001096075.1, NM_001102605.1 [P20839-5]
    NP_001136045.1, NM_001142573.1 [P20839-1]
    NP_001136046.1, NM_001142574.1 [P20839-4]
    NP_001136047.1, NM_001142575.1 [P20839-2]
    NP_001136048.1, NM_001142576.1 [P20839-7]
    NP_001291450.1, NM_001304521.1
    NP_899066.1, NM_183243.2 [P20839-3]
    XP_016867661.1, XM_017012172.1

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.654401

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000338791; ENSP00000345096; ENSG00000106348 [P20839-6]
    ENST00000348127; ENSP00000265385; ENSG00000106348 [P20839-3]
    ENST00000354269; ENSP00000346219; ENSG00000106348 [P20839-5]
    ENST00000419067; ENSP00000399400; ENSG00000106348 [P20839-7]
    ENST00000480861; ENSP00000420185; ENSG00000106348 [P20839-4]
    ENST00000496200; ENSP00000420803; ENSG00000106348 [P20839-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3614

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:3614

    UCSC genome browser

    More...
    UCSCi
    uc003vmt.3 human [P20839-1]

    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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Mutations of the IMPDH1 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05272 mRNA Translation: AAA36114.1
    AK054640 mRNA Translation: BAB70780.1
    AK054667 mRNA Translation: BAG51409.1
    AK122994 mRNA Translation: BAG53840.1 Frameshift.
    AK293413 mRNA Translation: BAG56920.1
    AC010655 Genomic DNA No translation available.
    CH236947 Genomic DNA Translation: EAL24310.1
    CH236947 Genomic DNA Translation: EAL24311.1
    CH471070 Genomic DNA Translation: EAW83652.1
    BC033622 mRNA Translation: AAH33622.2
    CD014008 mRNA No translation available.
    CCDSiCCDS34748.1 [P20839-3]
    CCDS34749.1 [P20839-6]
    CCDS43643.1 [P20839-5]
    CCDS47699.1 [P20839-7]
    CCDS47700.1 [P20839-2]
    CCDS55161.1 [P20839-4]
    PIRiA35566
    RefSeqiNP_000874.2, NM_000883.3 [P20839-6]
    NP_001096075.1, NM_001102605.1 [P20839-5]
    NP_001136045.1, NM_001142573.1 [P20839-1]
    NP_001136046.1, NM_001142574.1 [P20839-4]
    NP_001136047.1, NM_001142575.1 [P20839-2]
    NP_001136048.1, NM_001142576.1 [P20839-7]
    NP_001291450.1, NM_001304521.1
    NP_899066.1, NM_183243.2 [P20839-3]
    XP_016867661.1, XM_017012172.1
    UniGeneiHs.654401

    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
    1JCNX-ray2.50A/B1-514[»]
    ProteinModelPortaliP20839
    SMRiP20839
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109827, 89 interactors
    DIPiDIP-60163N
    IntActiP20839, 18 interactors
    STRINGi9606.ENSP00000345096

    Chemistry databases

    BindingDBiP20839
    ChEMBLiCHEMBL1822
    DrugBankiDB01033 Mercaptopurine
    DB00688 Mycophenolate mofetil
    DB01024 Mycophenolic acid
    DB00157 NADH
    DB00811 Ribavirin
    DB06103 VX-148
    GuidetoPHARMACOLOGYi2624

    PTM databases

    iPTMnetiP20839
    PhosphoSitePlusiP20839

    Polymorphism and mutation databases

    BioMutaiIMPDH1
    DMDMi25014074

    Proteomic databases

    EPDiP20839
    MaxQBiP20839
    PaxDbiP20839
    PeptideAtlasiP20839
    PRIDEiP20839
    ProteomicsDBi53811
    53812 [P20839-2]
    53813 [P20839-3]
    53814 [P20839-4]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338791; ENSP00000345096; ENSG00000106348 [P20839-6]
    ENST00000348127; ENSP00000265385; ENSG00000106348 [P20839-3]
    ENST00000354269; ENSP00000346219; ENSG00000106348 [P20839-5]
    ENST00000419067; ENSP00000399400; ENSG00000106348 [P20839-7]
    ENST00000480861; ENSP00000420185; ENSG00000106348 [P20839-4]
    ENST00000496200; ENSP00000420803; ENSG00000106348 [P20839-2]
    GeneIDi3614
    KEGGihsa:3614
    UCSCiuc003vmt.3 human [P20839-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    3614
    DisGeNETi3614
    EuPathDBiHostDB:ENSG00000106348.16

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    IMPDH1
    GeneReviewsiIMPDH1
    HGNCiHGNC:6052 IMPDH1
    MalaCardsiIMPDH1
    MIMi146690 gene
    180105 phenotype
    613837 phenotype
    neXtProtiNX_P20839
    OpenTargetsiENSG00000106348
    Orphaneti65 Leber congenital amaurosis
    791 Retinitis pigmentosa
    PharmGKBiPA29862

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG410ISZP Eukaryota
    COG0517 LUCA
    GeneTreeiENSGT00940000154156
    HOGENOMiHOG000165752
    HOVERGENiHBG052122
    KOiK00088
    OMAiSSMGYCG
    OrthoDBiEOG091G0EAV
    PhylomeDBiP20839
    TreeFamiTF300378

    Enzyme and pathway databases

    UniPathwayi
    UPA00601;UER00295

    BioCyciMetaCyc:HS02896-MONOMER
    BRENDAi1.1.1.205 2681
    ReactomeiR-HSA-6798695 Neutrophil degranulation
    R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
    SABIO-RKiP20839

    Miscellaneous databases

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

    More...
    ChiTaRSi
    IMPDH1 human
    EvolutionaryTraceiP20839

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    IMPDH1

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

    More...
    GenomeRNAii
    3614

    Protein Ontology

    More...
    PROi
    PR:P20839

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000106348 Expressed in 205 organ(s), highest expression level in blood
    CleanExiHS_IMPDH1
    ExpressionAtlasiP20839 baseline and differential
    GenevisibleiP20839 HS

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    Gene3Di3.20.20.70, 2 hits
    HAMAPiMF_01964 IMPDH, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt
    PfamiView protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit
    PIRSFiPIRSF000130 IMPDH, 1 hit
    SMARTiView protein in SMART
    SM00116 CBS, 2 hits
    TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
    PROSITEiView protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiIMDH1_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: P20839
    Secondary accession number(s): A4D0Z6
    , A4D0Z7, A6NDW5, A6NNI6, B3KNP7, B3KVM8, B4DE09, C9JV30, J3KNX8, Q8N194, Q96NU2
    <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: February 1, 1991
    Last sequence update: November 8, 2002
    Last modified: December 5, 2018
    This is version 214 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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