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Protein

Isocitrate dehydrogenase [NADP] cytoplasmic

Gene

IDH1

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

<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

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 Mg2+ or Mn2+ ion per subunit.1 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=49 µM for NADP1 Publication
  2. KM=29 µM for magnesium chloride1 Publication
  3. KM=65 µM for isocitrate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei77SubstrateCombined sources1 Publication1
    Binding sitei82NADPCombined sources2 Publications1
    Binding sitei109SubstrateCombined sources1 Publication1
    Binding sitei132SubstrateCombined sources1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei139Critical for catalysis1
    Binding sitei212Substrate; shared with neighboring subunitCombined sources1 Publication1
    Sitei212Critical for catalysis1
    <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 bindingi252Magnesium or manganese; shared with neighboring subunitCombined sources2 Publications1
    Binding sitei260NADPCombined sources2 Publications1
    Metal bindingi275Magnesium or manganeseCombined sources2 Publications1
    Metal bindingi279Magnesium or manganeseCombined sources2 Publications1
    Binding sitei328NADP; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1

    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 bindingi75 – 77NADPCombined sources2 Publications3
    Nucleotide bindingi310 – 315NADPCombined sources2 Publications6

    <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 functionOxidoreductase
    Biological processGlyoxylate bypass, Tricarboxylic acid cycle
    LigandMagnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS06502-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.42 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-2978092 Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate
    R-HSA-389542 NADPH regeneration
    R-HSA-6798695 Neutrophil degranulation
    R-HSA-9033241 Peroxisomal protein import

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O75874

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    O75874

    <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:
    Isocitrate dehydrogenase [NADP] cytoplasmic (EC:1.1.1.422 Publications)
    Short name:
    IDH
    Alternative name(s):
    Cytosolic NADP-isocitrate dehydrogenase
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    <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:IDH1
    Synonyms:PICD
    <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 2

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000138413.13

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:5382 IDH1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    147700 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_O75874

    <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, Peroxisome

    <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

    Glioma (GLM)2 Publications
    The gene represented in this entry is involved in disease pathogenesis. Mutations affecting Arg-132 are tissue-specific, and suggest that this residue plays a unique role in the development of high-grade gliomas. Mutations of Arg-132 to Cys, His, Leu or Ser abolish magnesium binding and abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. Elevated levels of R(-)-2-hydroxyglutarate are correlated with an elevated risk of malignant brain tumors.1 Publication
    Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
    See also OMIM:137800
    Genetic variations are associated with cartilaginous tumors such as enchondroma or chondrosarcoma. Mutations of Arg-132 to Cys, Gly or His abolish the conversion of isocitrate to alpha-ketoglutarate. Instead, alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate.1 Publication

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    3417

    MalaCards human disease database

    More...
    MalaCardsi
    IDH1
    MIMi137800 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000138413

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

    More...
    Orphaneti
    296 Enchondromatosis
    251579 Giant cell glioblastoma
    251576 Gliosarcoma
    163634 Maffucci syndrome
    99646 Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA29630

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2007625

    Drug and drug target database

    More...
    DrugBanki
    DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB09374 Indocyanine green
    DB01727 Isocitric Acid

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2884

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    IDH1

    <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 methionineiRemovedCombined sources
    <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_00000835752 – 414Isocitrate dehydrogenase [NADP] cytoplasmicAdd BLAST413

    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 residuei2N-acetylserineCombined sources1
    Modified residuei42PhosphotyrosineCombined sources1
    Modified residuei81N6-acetyllysineBy similarity1
    Modified residuei126N6-succinyllysineBy similarity1
    Modified residuei224N6-acetyllysineBy similarity1
    Modified residuei233N6-acetyllysineBy similarity1
    Modified residuei243N6-acetyllysineBy similarity1
    Modified residuei321N6-acetyllysineCombined sources1
    Modified residuei389PhosphoserineBy similarity1
    Modified residuei400N6-succinyllysineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Acetylation at Lys-374 dramatically reduces catalytic activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    O75874

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    O75874

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

    More...
    PaxDbi
    O75874

    PeptideAtlas

    More...
    PeptideAtlasi
    O75874

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O75874

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    50234

    2D gel databases

    USC-OGP 2-DE database

    More...
    OGPi
    O75874

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00027223

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    O75874

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    O75874

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

    More...
    PhosphoSitePlusi
    O75874

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    O75874

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000138413 Expressed in 235 organ(s), highest expression level in metanephros

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_IDH1

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    O75874 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O75874 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB033218
    CAB062556
    HPA035248
    HPA057936

    <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

    Homodimer.2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-715695,EBI-715695

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    109643, 65 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    O75874

    Database of interacting proteins

    More...
    DIPi
    DIP-59311N

    Protein interaction database and analysis system

    More...
    IntActi
    O75874, 6 interactors

    Molecular INTeraction database

    More...
    MINTi
    O75874

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000260985

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O75874

    <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

    1414
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1T09X-ray2.70A/B1-414[»]
    1T0LX-ray2.41A/B/C/D1-414[»]
    3INMX-ray2.10A/B/C1-414[»]
    3MAPX-ray2.80A/B1-414[»]
    3MARX-ray3.41A/B1-414[»]
    3MASX-ray3.20A/B1-414[»]
    4I3KX-ray3.31A/B1-414[»]
    4I3LX-ray3.29A/B1-414[»]
    4KZOX-ray2.20A/B/C1-414[»]
    4L03X-ray2.10A/B/C1-414[»]
    4L04X-ray2.87A/B/C/D/E/F1-414[»]
    4L06X-ray2.28A/B/C/D/E/F1-414[»]
    4UMXX-ray1.88A/B1-414[»]
    4UMYX-ray2.07A/B1-414[»]
    4XRXX-ray3.20A/B1-414[»]
    4XS3X-ray3.29A/B1-414[»]
    5DE1X-ray2.25A/B2-414[»]
    5GIRX-ray1.93C/D126-137[»]
    5K10electron microscopy3.80A/B3-413[»]
    5K11electron microscopy3.80A/B3-413[»]
    5L57X-ray2.69A1-414[»]
    5L58X-ray3.04A1-414[»]
    5LGEX-ray2.70A/B/C/D1-414[»]
    5SUNX-ray2.48A/B1-414[»]
    5SVFX-ray2.34A/B/C/D1-414[»]
    5TQHX-ray2.20A/B/C/D1-414[»]
    5YFMX-ray2.40A/B/C1-414[»]
    5YFNX-ray2.50A/B1-414[»]
    6ADGX-ray3.00A/B/C1-414[»]
    6B0ZX-ray2.33A/B/C/D1-414[»]
    6BKXX-ray1.65A/B/C1-414[»]
    6BKYX-ray2.17A/B/C/D/E/F1-414[»]
    6BKZX-ray2.01A/B1-414[»]
    6BL0X-ray2.17A/B/C1-414[»]
    6BL1X-ray2.02A/B/C1-414[»]
    6BL2X-ray1.92A/B/C1-414[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O75874

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

    More...
    SMRi
    O75874

    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
    O75874

    <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>Regioni94 – 100Substrate bindingCombined sources1 Publication7

    <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
    KOG1526 Eukaryota
    COG0538 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000012547

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000019858

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG006119

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O75874

    KEGG Orthology (KO)

    More...
    KOi
    K00031

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HGTVQRH

    Database of Orthologous Groups

    More...
    OrthoDBi
    769322at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O75874

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300428

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004790 Isocitrate_DH_NADP
    IPR024084 IsoPropMal-DH-like_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11822 PTHR11822, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00180 Iso_dh, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000108 IDH_NADP, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01329 Iso_dh, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00127 nadp_idh_euk, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00470 IDH_IMDH, 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>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

    O75874-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD
    60 70 80 90 100
    ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR
    110 120 130 140 150
    NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG
    160 170 180 190 200
    KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA
    210 220 230 240 250
    LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL
    260 270 280 290 300
    IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG
    310 320 330 340 350
    KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK
    360 370 380 390 400
    ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK
    410
    LGENLKIKLA QAKL
    Length:414
    Mass (Da):46,659
    Last modified:July 11, 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:i60428B0B6E5851DC
    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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9J4N6C9J4N6_HUMAN
    Isocitrate dehydrogenase [NADP] cyt...
    IDH1
    157Annotation 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>
    C9JJE5C9JJE5_HUMAN
    Isocitrate dehydrogenase [NADP] cyt...
    IDH1
    62Annotation 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>
    C9JLU6C9JLU6_HUMAN
    Isocitrate dehydrogenase [NADP] cyt...
    IDH1
    73Annotation 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 conflicti32F → I in CAB66637 (PubMed:11230166).Curated1
    Sequence conflicti126K → E in CAB66637 (PubMed:11230166).Curated1
    Sequence conflicti172F → S in CAD97653 (PubMed:17974005).Curated1
    Sequence conflicti174E → G in CAD97653 (PubMed:17974005).Curated1
    Sequence conflicti218K → I in AAD02918 (PubMed:9866202).Curated1
    Sequence conflicti307A → S in AAH93020 (PubMed:15815621).Curated1
    Sequence conflicti329P → L in AAD02918 (PubMed:9866202).Curated1
    Sequence conflicti381K → R in AAD02918 (PubMed:9866202).Curated1

    Natural variant

    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_036013132R → C in colorectal cancer and glioma samples; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate; induces histone methylation; enhances expression of chondrocyte-related genes; disturbs the formation of cartilaginous matrix; inhibits osteogenic differentiation. 4 PublicationsCorresponds to variant dbSNP:rs121913499EnsemblClinVar.1
    Natural variantiVAR_055454132R → G in a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors. 2 PublicationsCorresponds to variant dbSNP:rs121913499EnsemblClinVar.1
    Natural variantiVAR_055455132R → H in a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. 3 PublicationsCorresponds to variant dbSNP:rs121913500EnsemblClinVar.1
    Natural variantiVAR_055456132R → L in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. 2 PublicationsCorresponds to variant dbSNP:rs121913500EnsemblClinVar.1
    Natural variantiVAR_055457132R → S in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate. 2 PublicationsCorresponds to variant dbSNP:rs121913499EnsemblClinVar.1
    Natural variantiVAR_049780178V → I. Corresponds to variant dbSNP:rs34218846EnsemblClinVar.1

    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
    AF020038 mRNA Translation: AAD02918.1
    AF113917 mRNA Translation: AAD29284.1
    AL136702 mRNA Translation: CAB66637.1
    CR541695 mRNA Translation: CAG46496.1
    BX537411 mRNA Translation: CAD97653.1
    AC016697 Genomic DNA Translation: AAX93221.1
    CH471063 Genomic DNA Translation: EAW70439.1
    BC012846 mRNA Translation: AAH12846.1
    BC093020 mRNA Translation: AAH93020.1
    U62389 mRNA Translation: AAB17375.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS2381.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T46280

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001269315.1, NM_001282386.1
    NP_001269316.1, NM_001282387.1
    NP_005887.2, NM_005896.3

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.593422

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000345146; ENSP00000260985; ENSG00000138413
    ENST00000415913; ENSP00000390265; ENSG00000138413
    ENST00000446179; ENSP00000410513; ENSG00000138413

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3417

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:3417

    Keywords - Coding sequence diversityi

    Polymorphism

    <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

    Wikipedia

    Isocitrate dehydrogenase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF020038 mRNA Translation: AAD02918.1
    AF113917 mRNA Translation: AAD29284.1
    AL136702 mRNA Translation: CAB66637.1
    CR541695 mRNA Translation: CAG46496.1
    BX537411 mRNA Translation: CAD97653.1
    AC016697 Genomic DNA Translation: AAX93221.1
    CH471063 Genomic DNA Translation: EAW70439.1
    BC012846 mRNA Translation: AAH12846.1
    BC093020 mRNA Translation: AAH93020.1
    U62389 mRNA Translation: AAB17375.1
    CCDSiCCDS2381.1
    PIRiT46280
    RefSeqiNP_001269315.1, NM_001282386.1
    NP_001269316.1, NM_001282387.1
    NP_005887.2, NM_005896.3
    UniGeneiHs.593422

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1T09X-ray2.70A/B1-414[»]
    1T0LX-ray2.41A/B/C/D1-414[»]
    3INMX-ray2.10A/B/C1-414[»]
    3MAPX-ray2.80A/B1-414[»]
    3MARX-ray3.41A/B1-414[»]
    3MASX-ray3.20A/B1-414[»]
    4I3KX-ray3.31A/B1-414[»]
    4I3LX-ray3.29A/B1-414[»]
    4KZOX-ray2.20A/B/C1-414[»]
    4L03X-ray2.10A/B/C1-414[»]
    4L04X-ray2.87A/B/C/D/E/F1-414[»]
    4L06X-ray2.28A/B/C/D/E/F1-414[»]
    4UMXX-ray1.88A/B1-414[»]
    4UMYX-ray2.07A/B1-414[»]
    4XRXX-ray3.20A/B1-414[»]
    4XS3X-ray3.29A/B1-414[»]
    5DE1X-ray2.25A/B2-414[»]
    5GIRX-ray1.93C/D126-137[»]
    5K10electron microscopy3.80A/B3-413[»]
    5K11electron microscopy3.80A/B3-413[»]
    5L57X-ray2.69A1-414[»]
    5L58X-ray3.04A1-414[»]
    5LGEX-ray2.70A/B/C/D1-414[»]
    5SUNX-ray2.48A/B1-414[»]
    5SVFX-ray2.34A/B/C/D1-414[»]
    5TQHX-ray2.20A/B/C/D1-414[»]
    5YFMX-ray2.40A/B/C1-414[»]
    5YFNX-ray2.50A/B1-414[»]
    6ADGX-ray3.00A/B/C1-414[»]
    6B0ZX-ray2.33A/B/C/D1-414[»]
    6BKXX-ray1.65A/B/C1-414[»]
    6BKYX-ray2.17A/B/C/D/E/F1-414[»]
    6BKZX-ray2.01A/B1-414[»]
    6BL0X-ray2.17A/B/C1-414[»]
    6BL1X-ray2.02A/B/C1-414[»]
    6BL2X-ray1.92A/B/C1-414[»]
    ProteinModelPortaliO75874
    SMRiO75874
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109643, 65 interactors
    CORUMiO75874
    DIPiDIP-59311N
    IntActiO75874, 6 interactors
    MINTiO75874
    STRINGi9606.ENSP00000260985

    Chemistry databases

    BindingDBiO75874
    ChEMBLiCHEMBL2007625
    DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
    DB09374 Indocyanine green
    DB01727 Isocitric Acid
    GuidetoPHARMACOLOGYi2884

    PTM databases

    iPTMnetiO75874
    PhosphoSitePlusiO75874
    SwissPalmiO75874

    Polymorphism and mutation databases

    BioMutaiIDH1

    2D gel databases

    OGPiO75874
    REPRODUCTION-2DPAGEiIPI00027223
    UCD-2DPAGEiO75874

    Proteomic databases

    EPDiO75874
    jPOSTiO75874
    PaxDbiO75874
    PeptideAtlasiO75874
    PRIDEiO75874
    ProteomicsDBi50234

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    3417
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000345146; ENSP00000260985; ENSG00000138413
    ENST00000415913; ENSP00000390265; ENSG00000138413
    ENST00000446179; ENSP00000410513; ENSG00000138413
    GeneIDi3417
    KEGGihsa:3417

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    3417
    DisGeNETi3417
    EuPathDBiHostDB:ENSG00000138413.13

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    IDH1

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0161877
    HGNCiHGNC:5382 IDH1
    HPAiCAB033218
    CAB062556
    HPA035248
    HPA057936
    MalaCardsiIDH1
    MIMi137800 phenotype
    147700 gene
    neXtProtiNX_O75874
    OpenTargetsiENSG00000138413
    Orphaneti296 Enchondromatosis
    251579 Giant cell glioblastoma
    251576 Gliosarcoma
    163634 Maffucci syndrome
    99646 Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria
    PharmGKBiPA29630

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1526 Eukaryota
    COG0538 LUCA
    GeneTreeiENSGT00390000012547
    HOGENOMiHOG000019858
    HOVERGENiHBG006119
    InParanoidiO75874
    KOiK00031
    OMAiHGTVQRH
    OrthoDBi769322at2759
    PhylomeDBiO75874
    TreeFamiTF300428

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06502-MONOMER
    BRENDAi1.1.1.42 2681
    ReactomeiR-HSA-2978092 Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate
    R-HSA-389542 NADPH regeneration
    R-HSA-6798695 Neutrophil degranulation
    R-HSA-9033241 Peroxisomal protein import
    SABIO-RKiO75874
    SIGNORiO75874

    Miscellaneous databases

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

    More...
    ChiTaRSi
    IDH1 human
    EvolutionaryTraceiO75874

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    IDH1

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

    More...
    GenomeRNAii
    3417

    Protein Ontology

    More...
    PROi
    PR:O75874

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000138413 Expressed in 235 organ(s), highest expression level in metanephros
    CleanExiHS_IDH1
    ExpressionAtlasiO75874 baseline and differential
    GenevisibleiO75874 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR019818 IsoCit/isopropylmalate_DH_CS
    IPR004790 Isocitrate_DH_NADP
    IPR024084 IsoPropMal-DH-like_dom
    PANTHERiPTHR11822 PTHR11822, 1 hit
    PfamiView protein in Pfam
    PF00180 Iso_dh, 1 hit
    PIRSFiPIRSF000108 IDH_NADP, 1 hit
    SMARTiView protein in SMART
    SM01329 Iso_dh, 1 hit
    TIGRFAMsiTIGR00127 nadp_idh_euk, 1 hit
    PROSITEiView protein in PROSITE
    PS00470 IDH_IMDH, 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 nameiIDHC_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: O75874
    Secondary accession number(s): Q567U4
    , Q6FHQ6, Q7Z3V0, Q93090, Q9NTJ9, Q9UKW8
    <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: May 30, 2000
    Last sequence update: July 11, 2002
    Last modified: January 16, 2019
    This is version 199 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. SIMILARITY comments
      Index of protein domains and families
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
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