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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-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 Mg2+ or Mn2+ ion per subunit.1 Publication

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
    Binding sitei77Substrate1
    Binding sitei82NADP1 Publication1
    Binding sitei109Substrate1
    Binding sitei132Substrate1
    Sitei139Critical for catalysis1
    Sitei212Critical for catalysis1
    Metal bindingi252Magnesium or manganese1
    Binding sitei260NADP1 Publication1
    Metal bindingi275Magnesium or manganese1
    Binding sitei328NADP; via amide nitrogen and carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi75 – 77NADP1 Publication3
    Nucleotide bindingi310 – 315NADP1 Publication6

    GO - Molecular functioni

    • (R)-2-hydroxyglutarate dehydrogenase activity Source: Reactome
    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • NAD binding Source: InterPro
    • NADP binding Source: Ensembl
    • protein homodimerization activity Source: UniProtKB
    • receptor binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06502-MONOMER.
    ZFISH: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.
    SABIO-RKO75874.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP] cytoplasmic (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    Cytosolic NADP-isocitrate dehydrogenase
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    Gene namesi
    Name:IDH1
    Synonyms:PICD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5382. IDH1.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Peroxisome 1 Publication

    GO - Cellular componenti

    • cell-cell adherens junction Source: BHF-UCL
    • cytoplasm Source: LIFEdb
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl
    • peroxisomal matrix Source: Reactome
    • peroxisome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    Pathology & Biotechi

    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.

    Organism-specific databases

    DisGeNETi3417.
    MalaCardsiIDH1.
    MIMi137800. phenotype.
    OpenTargetsiENSG00000138413.
    Orphaneti296. Enchondromatosis.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    163634. Maffucci syndrome.
    99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
    PharmGKBiPA29630.

    Chemistry databases

    ChEMBLiCHEMBL2007625.
    GuidetoPHARMACOLOGYi2884.

    Polymorphism and mutation databases

    BioMutaiIDH1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000835752 – 414Isocitrate dehydrogenase [NADP] cytoplasmicAdd BLAST413

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiO75874.
    PaxDbiO75874.
    PeptideAtlasiO75874.
    PRIDEiO75874.

    2D gel databases

    OGPiO75874.
    REPRODUCTION-2DPAGEIPI00027223.
    UCD-2DPAGEO75874.

    PTM databases

    iPTMnetiO75874.
    PhosphoSitePlusiO75874.
    SwissPalmiO75874.

    Expressioni

    Gene expression databases

    BgeeiENSG00000138413.
    CleanExiHS_IDH1.
    ExpressionAtlasiO75874. baseline and differential.
    GenevisibleiO75874. HS.

    Organism-specific databases

    HPAiCAB033218.
    CAB062556.
    HPA035248.
    HPA057936.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • protein homodimerization activity Source: UniProtKB
    • receptor binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi109643. 49 interactors.
    DIPiDIP-59311N.
    IntActiO75874. 4 interactors.
    MINTiMINT-4998878.
    STRINGi9606.ENSP00000260985.

    Chemistry databases

    BindingDBiO75874.

    Structurei

    Secondary structure

    1414
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 14Combined sources10
    Helixi17 – 29Combined sources13
    Turni30 – 34Combined sources5
    Beta strandi35 – 43Combined sources9
    Helixi46 – 51Combined sources6
    Turni52 – 54Combined sources3
    Helixi55 – 67Combined sources13
    Beta strandi68 – 72Combined sources5
    Helixi80 – 86Combined sources7
    Helixi95 – 103Combined sources9
    Beta strandi105 – 111Combined sources7
    Beta strandi126 – 134Combined sources9
    Helixi137 – 140Combined sources4
    Beta strandi142 – 146Combined sources5
    Beta strandi148 – 158Combined sources11
    Beta strandi165 – 172Combined sources8
    Beta strandi177 – 185Combined sources9
    Helixi186 – 203Combined sources18
    Beta strandi207 – 210Combined sources4
    Turni213 – 215Combined sources3
    Helixi219 – 234Combined sources16
    Helixi236 – 241Combined sources6
    Beta strandi246 – 248Combined sources3
    Helixi251 – 259Combined sources9
    Beta strandi263 – 269Combined sources7
    Helixi276 – 278Combined sources3
    Helixi280 – 284Combined sources5
    Helixi288 – 290Combined sources3
    Beta strandi291 – 296Combined sources6
    Beta strandi303 – 309Combined sources7
    Helixi313 – 320Combined sources8
    Helixi330 – 347Combined sources18
    Helixi350 – 368Combined sources19
    Helixi374 – 381Combined sources8
    Helixi383 – 385Combined sources3
    Helixi388 – 390Combined sources3
    Helixi394 – 413Combined sources20

    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[»]
    ProteinModelPortaliO75874.
    SMRiO75874.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75874.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni94 – 100Substrate binding7

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1526. Eukaryota.
    COG0538. LUCA.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiO75874.
    KOiK00031.
    OMAiHNFESCG.
    OrthoDBiEOG091G06IY.
    PhylomeDBiO75874.
    TreeFamiTF300428.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11822. PTHR11822. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000108. IDH_NADP. 1 hit.
    SMARTiSM01329. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    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
    Checksum:i60428B0B6E5851DC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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
    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 rs121913499dbSNPEnsembl.1
    Natural variantiVAR_055454132R → G in a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors. 2 Publications1
    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 rs121913500dbSNPEnsembl.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 Publications1
    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 rs121913499dbSNPEnsembl.1
    Natural variantiVAR_049780178V → I.Corresponds to variant rs34218846dbSNPEnsembl.1

    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.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    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[»]
    ProteinModelPortaliO75874.
    SMRiO75874.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109643. 49 interactors.
    DIPiDIP-59311N.
    IntActiO75874. 4 interactors.
    MINTiMINT-4998878.
    STRINGi9606.ENSP00000260985.

    Chemistry databases

    BindingDBiO75874.
    ChEMBLiCHEMBL2007625.
    GuidetoPHARMACOLOGYi2884.

    PTM databases

    iPTMnetiO75874.
    PhosphoSitePlusiO75874.
    SwissPalmiO75874.

    Polymorphism and mutation databases

    BioMutaiIDH1.

    2D gel databases

    OGPiO75874.
    REPRODUCTION-2DPAGEIPI00027223.
    UCD-2DPAGEO75874.

    Proteomic databases

    EPDiO75874.
    PaxDbiO75874.
    PeptideAtlasiO75874.
    PRIDEiO75874.

    Protocols and materials databases

    DNASUi3417.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi3417.
    DisGeNETi3417.
    GeneCardsiIDH1.
    H-InvDBHIX0161877.
    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.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1526. Eukaryota.
    COG0538. LUCA.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiO75874.
    KOiK00031.
    OMAiHNFESCG.
    OrthoDBiEOG091G06IY.
    PhylomeDBiO75874.
    TreeFamiTF300428.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06502-MONOMER.
    ZFISH: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.
    SABIO-RKO75874.

    Miscellaneous databases

    ChiTaRSiIDH1. human.
    EvolutionaryTraceiO75874.
    GeneWikiiIDH1.
    GenomeRNAii3417.
    PROiO75874.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000138413.
    CleanExiHS_IDH1.
    ExpressionAtlasiO75874. baseline and differential.
    GenevisibleiO75874. HS.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11822. PTHR11822. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000108. IDH_NADP. 1 hit.
    SMARTiSM01329. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiIDHC_HUMAN
    AccessioniPrimary (citable) accession number: O75874
    Secondary accession number(s): Q567U4
    , Q6FHQ6, Q7Z3V0, Q93090, Q9NTJ9, Q9UKW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 11, 2002
    Last modified: November 30, 2016
    This is version 180 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    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. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.