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O75874

- IDHC_HUMAN

UniProt

O75874 - IDHC_HUMAN

Protein

Isocitrate dehydrogenase [NADP] cytoplasmic

Gene

IDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (11 Jul 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium or manganese 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

    1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. NAD binding Source: InterPro
    4. NADP binding Source: Ensembl
    5. protein homodimerization activity Source: UniProtKB
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. cellular lipid metabolic process Source: Reactome
    3. female gonad development Source: Ensembl
    4. glutathione metabolic process Source: Ensembl
    5. glyoxylate cycle Source: UniProtKB-KW
    6. isocitrate metabolic process Source: UniProtKB
    7. NADPH regeneration Source: Reactome
    8. response to oxidative stress Source: Ensembl
    9. response to steroid hormone Source: Ensembl
    10. small molecule metabolic process Source: Reactome
    11. tricarboxylic acid cycle Source: UniProtKB-KW

    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.
    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5382. IDH1.

    Subcellular locationi

    Cytoplasm 1 Publication. Peroxisome 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: Ensembl
    5. peroxisomal matrix Source: Reactome
    6. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Glioma (GLM) [MIM:137800]: Gliomas 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.
    Note: 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.

    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.

    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 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

    Proteomic databases

    MaxQBiO75874.
    PaxDbiO75874.
    PeptideAtlasiO75874.
    PRIDEiO75874.

    2D gel databases

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

    PTM databases

    PhosphoSiteiO75874.

    Expressioni

    Gene expression databases

    ArrayExpressiO75874.
    BgeeiO75874.
    CleanExiHS_IDH1.
    GenevestigatoriO75874.

    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 – 1410
    Helixi17 – 2913
    Turni30 – 345
    Beta strandi35 – 439
    Helixi46 – 516
    Turni52 – 543
    Helixi55 – 6713
    Beta strandi68 – 725
    Helixi80 – 867
    Helixi95 – 1039
    Beta strandi106 – 1116
    Beta strandi128 – 1336
    Helixi137 – 1404
    Beta strandi142 – 1465
    Beta strandi148 – 15811
    Beta strandi165 – 1728
    Beta strandi177 – 1859
    Helixi186 – 20318
    Beta strandi207 – 2115
    Turni213 – 2153
    Helixi219 – 23416
    Helixi236 – 2416
    Beta strandi246 – 2505
    Helixi251 – 26010
    Beta strandi265 – 2695
    Helixi271 – 28515
    Beta strandi290 – 2967
    Beta strandi303 – 3097
    Helixi313 – 3208
    Helixi330 – 34718
    Helixi350 – 36920
    Helixi374 – 3818
    Helixi383 – 3853
    Helixi388 – 3903
    Helixi394 – 40916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiO75874.
    KOiK00031.
    OMAiSCGGVAM.
    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

    MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD    50
    ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR 100
    NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG 150
    KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA 200
    LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL 250
    IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG 300
    KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK 350
    ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK 400
    LGENLKIKLA QAKL 414
    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. 2 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. 1 Publication
    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. 1 Publication
    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. 1 Publication
    VAR_055457
    Natural varianti178 – 1781V → I.
    Corresponds to variant rs34218846 [ dbSNP | Ensembl ].
    VAR_049780

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2381.1.
    PIRi T46280.
    RefSeqi NP_001269315.1. NM_001282386.1.
    NP_001269316.1. NM_001282387.1.
    NP_005887.2. NM_005896.3.
    UniGenei Hs.593422.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T09 X-ray 2.70 A/B 1-414 [» ]
    1T0L X-ray 2.41 A/B/C/D 1-414 [» ]
    3INM X-ray 2.10 A/B/C 1-414 [» ]
    3MAP X-ray 2.80 A/B 1-414 [» ]
    3MAR X-ray 3.41 A/B 1-414 [» ]
    3MAS X-ray 3.20 A/B 1-414 [» ]
    4I3K X-ray 3.31 A/B 1-414 [» ]
    4I3L X-ray 3.29 A/B 1-414 [» ]
    4KZO X-ray 2.20 A/B/C 1-414 [» ]
    4L03 X-ray 2.10 A/B/C 1-414 [» ]
    4L04 X-ray 2.87 A/B/C/D/E/F 1-414 [» ]
    4L06 X-ray 2.28 A/B/C/D/E/F 1-414 [» ]
    ProteinModelPortali O75874.
    SMRi O75874. Positions 3-414.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109643. 34 interactions.
    DIPi DIP-59311N.
    IntActi O75874. 4 interactions.
    MINTi MINT-4998878.
    STRINGi 9606.ENSP00000260985.

    Chemistry

    ChEMBLi CHEMBL2007625.

    PTM databases

    PhosphoSitei O75874.

    2D gel databases

    OGPi O75874.
    REPRODUCTION-2DPAGE IPI00027223.
    UCD-2DPAGE O75874.

    Proteomic databases

    MaxQBi O75874.
    PaxDbi O75874.
    PeptideAtlasi O75874.
    PRIDEi O75874.

    Protocols and materials databases

    DNASUi 3417.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345146 ; ENSP00000260985 ; ENSG00000138413 .
    ENST00000415913 ; ENSP00000390265 ; ENSG00000138413 .
    ENST00000446179 ; ENSP00000410513 ; ENSG00000138413 .
    GeneIDi 3417.
    KEGGi hsa:3417.
    UCSCi uc002vcs.3. human.

    Organism-specific databases

    CTDi 3417.
    GeneCardsi GC02M209100.
    H-InvDB HIX0161877.
    HGNCi HGNC:5382. IDH1.
    HPAi CAB033218.
    CAB062556.
    HPA035248.
    HPA057936.
    MIMi 137800. phenotype.
    147700. gene.
    neXtProti NX_O75874.
    Orphaneti 296. Enchondromatosis.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    163634. Maffucci syndrome.
    99646. Metaphyseal chondromatosis with D-2-hydroxyglutaric aciduria.
    PharmGKBi PA29630.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0538.
    HOGENOMi HOG000019858.
    HOVERGENi HBG006119.
    InParanoidi O75874.
    KOi K00031.
    OMAi SCGGVAM.
    OrthoDBi EOG7QNVKS.
    PhylomeDBi O75874.
    TreeFami TF300428.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06502-MONOMER.
    Reactomei REACT_160183. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
    REACT_16904. NADPH regeneration.
    SABIO-RK O75874.

    Miscellaneous databases

    ChiTaRSi IDH1. human.
    EvolutionaryTracei O75874.
    GeneWikii IDH1.
    GenomeRNAii 3417.
    NextBioi 13470.
    PROi O75874.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75874.
    Bgeei O75874.
    CleanExi HS_IDH1.
    Genevestigatori O75874.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR004790. Isocitrate_DH_NADP.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11822. PTHR11822. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000108. IDH_NADP. 1 hit.
    TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    15. 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.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-132.
    17. Cited for: VARIANTS HIS-132 AND SER-132.
    18. "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: October 1, 2014
    This is version 156 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