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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 Mg(2+) 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771Substrate
    Binding sitei82 – 821NADP1 Publication
    Binding sitei109 – 1091Substrate
    Binding sitei132 – 1321Substrate
    Sitei139 – 1391Critical for catalysis
    Sitei212 – 2121Critical for catalysis
    Metal bindingi252 – 2521Magnesium or manganese
    Binding sitei260 – 2601NADP1 Publication
    Metal bindingi275 – 2751Magnesium or manganese
    Binding sitei328 – 3281NADP; via amide nitrogen and carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi75 – 773NADP1 Publication
    Nucleotide bindingi310 – 3156NADP1 Publication

    GO - Molecular functioni

    • 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.
    BRENDAi1.1.1.42. 2681.
    ReactomeiREACT_160183. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
    REACT_16904. NADPH regeneration.
    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
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5382. IDH1.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Peroxisome 1 Publication

    GO - Cellular componenti

    • 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)

    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.

    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

    Organism-specific databases

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

    Polymorphism and mutation databases

    BioMutaiIDH1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 414413Isocitrate dehydrogenase [NADP] cytoplasmicPRO_0000083575Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei42 – 421Phosphotyrosine1 Publication
    Modified residuei81 – 811N6-acetyllysineBy similarity
    Modified residuei126 – 1261N6-succinyllysineBy similarity
    Modified residuei224 – 2241N6-acetyllysineBy similarity
    Modified residuei233 – 2331N6-acetyllysineBy similarity
    Modified residuei243 – 2431N6-acetyllysineBy similarity
    Modified residuei321 – 3211N6-acetyllysine1 Publication
    Modified residuei400 – 4001N6-succinyllysineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO75874.
    PeptideAtlasiO75874.
    PRIDEiO75874.

    2D gel databases

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

    PTM databases

    PhosphoSiteiO75874.

    Expressioni

    Gene expression databases

    BgeeiO75874.
    CleanExiHS_IDH1.
    ExpressionAtlasiO75874. baseline and differential.
    GenevisibleiO75874. HS.

    Organism-specific databases

    HPAiCAB033218.
    CAB062556.
    HPA035248.
    HPA057936.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi109643. 34 interactions.
    DIPiDIP-59311N.
    IntActiO75874. 4 interactions.
    MINTiMINT-4998878.
    STRINGi9606.ENSP00000260985.

    Structurei

    Secondary structure

    1
    414
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410Combined sources
    Helixi17 – 2913Combined sources
    Turni30 – 345Combined sources
    Beta strandi35 – 439Combined sources
    Helixi46 – 516Combined sources
    Turni52 – 543Combined sources
    Helixi55 – 6713Combined sources
    Beta strandi68 – 725Combined sources
    Helixi80 – 867Combined sources
    Helixi95 – 1039Combined sources
    Beta strandi105 – 1117Combined sources
    Beta strandi126 – 1349Combined sources
    Helixi137 – 1404Combined sources
    Beta strandi142 – 1465Combined sources
    Beta strandi148 – 15811Combined sources
    Beta strandi165 – 1728Combined sources
    Beta strandi177 – 1859Combined sources
    Helixi186 – 20318Combined sources
    Beta strandi207 – 2104Combined sources
    Turni213 – 2153Combined sources
    Helixi219 – 23416Combined sources
    Helixi236 – 2416Combined sources
    Beta strandi246 – 2483Combined sources
    Helixi251 – 2599Combined sources
    Beta strandi263 – 2697Combined sources
    Helixi276 – 2783Combined sources
    Helixi280 – 2845Combined sources
    Helixi288 – 2903Combined sources
    Beta strandi291 – 2966Combined sources
    Beta strandi303 – 3097Combined sources
    Helixi313 – 3208Combined sources
    Helixi330 – 34718Combined sources
    Helixi350 – 36819Combined sources
    Helixi374 – 3818Combined sources
    Helixi383 – 3853Combined sources
    Helixi388 – 3903Combined sources
    Helixi394 – 41320Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliO75874.
    SMRiO75874. Positions 3-414.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75874.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 1007Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0538.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiO75874.
    KOiK00031.
    OMAiLQGDEMT.
    OrthoDBiEOG7QNVKS.
    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.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321F → I in CAB66637 (PubMed:11230166).Curated
    Sequence conflicti126 – 1261K → E in CAB66637 (PubMed:11230166).Curated
    Sequence conflicti172 – 1721F → S in CAD97653 (PubMed:17974005).Curated
    Sequence conflicti174 – 1741E → G in CAD97653 (PubMed:17974005).Curated
    Sequence conflicti218 – 2181K → I in AAD02918 (PubMed:9866202).Curated
    Sequence conflicti307 – 3071A → S in AAH93020 (PubMed:15815621).Curated
    Sequence conflicti329 – 3291P → L in AAD02918 (PubMed:9866202).Curated
    Sequence conflicti381 – 3811K → R in AAD02918 (PubMed:9866202).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321R → C in colorectal cancer and glioma samples; 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. 3 Publications
    VAR_036013
    Natural varianti132 – 1321R → G in a glioma sample; glioblastoma multiforme; somatic mutation. 1 Publication
    VAR_055454
    Natural varianti132 – 1321R → H 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 Publications
    VAR_055455
    Natural varianti132 – 1321R → 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 Publications
    VAR_055456
    Natural varianti132 – 1321R → 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 Publications
    VAR_055457
    Natural varianti178 – 1781V → I.
    Corresponds to variant rs34218846 [ dbSNP | Ensembl ].
    VAR_049780

    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.
    UCSCiuc002vcs.3. human.

    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
    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[»]
    ProteinModelPortaliO75874.
    SMRiO75874. Positions 3-414.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109643. 34 interactions.
    DIPiDIP-59311N.
    IntActiO75874. 4 interactions.
    MINTiMINT-4998878.
    STRINGi9606.ENSP00000260985.

    Chemistry

    BindingDBiO75874.
    ChEMBLiCHEMBL2007625.

    PTM databases

    PhosphoSiteiO75874.

    Polymorphism and mutation databases

    BioMutaiIDH1.

    2D gel databases

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

    Proteomic databases

    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.
    UCSCiuc002vcs.3. human.

    Organism-specific databases

    CTDi3417.
    GeneCardsiGC02M209100.
    H-InvDBHIX0161877.
    HGNCiHGNC:5382. IDH1.
    HPAiCAB033218.
    CAB062556.
    HPA035248.
    HPA057936.
    MIMi137800. phenotype.
    147700. gene.
    neXtProtiNX_O75874.
    Orphaneti296. Enchondromatosis.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    163634. Maffucci syndrome.
    99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
    PharmGKBiPA29630.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0538.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiO75874.
    KOiK00031.
    OMAiLQGDEMT.
    OrthoDBiEOG7QNVKS.
    PhylomeDBiO75874.
    TreeFamiTF300428.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06502-MONOMER.
    BRENDAi1.1.1.42. 2681.
    ReactomeiREACT_160183. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
    REACT_16904. NADPH regeneration.
    SABIO-RKO75874.

    Miscellaneous databases

    ChiTaRSiIDH1. human.
    EvolutionaryTraceiO75874.
    GeneWikiiIDH1.
    GenomeRNAii3417.
    NextBioi13470.
    PROiO75874.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO75874.
    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.
    TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family."
      Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.
      Mol. Biol. Evol. 15:1674-1684(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase."
      Geisbrecht B.V., Gould S.J.
      J. Biol. Chem. 274:30527-30533(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Endometrium.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung and Placenta.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 5-20; 30-49; 101-109; 120-132; 141-212; 223-233; 250-270; 322-338 AND 389-400, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Differential gene expression in epithelial cells induced by bile salts: identification by RNA arbitrarily primed PCR."
      Kullmann F., Vogt T., Welsh J., McClelland M.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-253.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity."
      Xu X., Zhao J., Xu Z., Peng B., Huang Q., Arnold E., Ding J.
      J. Biol. Chem. 279:33946-33957(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH NADP; ISOCITRATE AND CALCIUM IONS, SUBUNIT.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GBM HIS-132 IN COMPLEX WITH NADP AND ALPHA-KETOGLUTARATE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS CYS-132; HIS-132; LEU-132 AND SER-132.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-132.
    18. Cited for: VARIANTS HIS-132 AND SER-132.
    19. "IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors."
      Bleeker F.E., Lamba S., Leenstra S., Troost D., Hulsebos T., Vandertop W.P., Frattini M., Molinari F., Knowles M., Cerrato A., Rodolfo M., Scarpa A., Felicioni L., Buttitta F., Malatesta S., Marchetti A., Bardelli A.
      Hum. Mutat. 30:7-11(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CYS-132; GLY-132 AND LEU-132, ROLE IN GLIOMAS.

    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: July 22, 2015
    This is version 166 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

    External Data

    Dasty 3

    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 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.