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P48735

- IDHP_HUMAN

UniProt

P48735 - IDHP_HUMAN

Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

IDH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (03 Apr 2002)
      Previous versions | rss
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    Functioni

    Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171SubstrateBy similarity
    Binding sitei122 – 1221NADPBy similarity
    Binding sitei149 – 1491SubstrateBy similarity
    Binding sitei172 – 1721SubstrateBy similarity
    Sitei179 – 1791Critical for catalysisBy similarity
    Sitei251 – 2511Critical for catalysisBy similarity
    Metal bindingi291 – 2911Magnesium or manganeseBy similarity
    Binding sitei299 – 2991NADPBy similarity
    Metal bindingi314 – 3141Magnesium or manganeseBy similarity
    Binding sitei367 – 3671NADP; via amide nitrogen and carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi115 – 1173NADPBy similarity
    Nucleotide bindingi349 – 3546NADPBy similarity

    GO - Molecular functioni

    1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. NAD binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. carbohydrate metabolic process Source: ProtInc
    3. cellular metabolic process Source: Reactome
    4. glyoxylate cycle Source: UniProtKB-KW
    5. isocitrate metabolic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00021-MONOMER.
    ReactomeiREACT_1785. Citric acid cycle (TCA cycle).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP], mitochondrial (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    ICD-M
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    Gene namesi
    Name:IDH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:5383. IDH2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    D-2-hydroxyglutaric aciduria 2 (D2HGA2) [MIM:613657]: A neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401R → G in D2HGA2. 1 Publication
    VAR_065174
    Natural varianti140 – 1401R → Q in D2HGA2. 1 Publication
    VAR_065175

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi413 – 4131K → A: 44-fold loss in activity. 1 Publication
    Mutagenesisi413 – 4131K → Q: 20-fold decrease in Vmax. 1 Publication
    Mutagenesisi413 – 4131K → R: No appreciable difference in Km for isocitrate and NADP. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613657. phenotype.
    Orphaneti79315. D-2-hydroxyglutaric aciduria.
    296. Enchondromatosis.
    163634. Maffucci syndrome.
    PharmGKBiPA29631.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionBy similarityAdd
    BLAST
    Chaini40 – 452413Isocitrate dehydrogenase [NADP], mitochondrialPRO_0000014420Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451N6-acetyllysineBy similarity
    Modified residuei48 – 481N6-acetyllysineBy similarity
    Modified residuei67 – 671N6-acetyllysine1 Publication
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
    Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
    Modified residuei106 – 1061N6-acetyllysine; alternate1 Publication
    Modified residuei106 – 1061N6-succinyllysine; alternateBy similarity
    Modified residuei155 – 1551N6-acetyllysine1 Publication
    Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
    Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
    Modified residuei180 – 1801N6-acetyllysine; alternate1 Publication
    Modified residuei180 – 1801N6-succinyllysine; alternateBy similarity
    Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
    Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
    Modified residuei199 – 1991N6-acetyllysineBy similarity
    Modified residuei256 – 2561N6-acetyllysine; alternate1 Publication
    Modified residuei256 – 2561N6-succinyllysine; alternateBy similarity
    Modified residuei263 – 2631N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysine1 Publication
    Modified residuei275 – 2751N6-acetyllysine1 Publication
    Modified residuei280 – 2801N6-acetyllysineBy similarity
    Modified residuei282 – 2821N6-acetyllysine; alternate1 Publication
    Modified residuei282 – 2821N6-succinyllysine; alternateBy similarity
    Modified residuei384 – 3841N6-acetyllysine; alternateBy similarity
    Modified residuei384 – 3841N6-succinyllysine; alternateBy similarity
    Modified residuei400 – 4001N6-acetyllysineBy similarity
    Modified residuei413 – 4131N6-acetyllysine1 Publication
    Modified residuei442 – 4421N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48735.
    PaxDbiP48735.
    PeptideAtlasiP48735.
    PRIDEiP48735.

    2D gel databases

    OGPiP48735.
    UCD-2DPAGEP48735.

    PTM databases

    PhosphoSiteiP48735.

    Expressioni

    Gene expression databases

    ArrayExpressiP48735.
    BgeeiP48735.
    CleanExiHS_IDH2.
    GenevestigatoriP48735.

    Organism-specific databases

    HPAiHPA007831.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi109644. 8 interactions.
    IntActiP48735. 2 interactions.
    MINTiMINT-3016964.
    STRINGi9606.ENSP00000331897.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 545
    Helixi57 – 6913
    Turni70 – 745
    Beta strandi79 – 835
    Helixi86 – 916
    Turni92 – 943
    Helixi95 – 10713
    Beta strandi108 – 1125
    Helixi120 – 1267
    Helixi135 – 1439
    Beta strandi146 – 1516
    Beta strandi168 – 1725
    Helixi177 – 1804
    Beta strandi182 – 1865
    Beta strandi190 – 1989
    Beta strandi205 – 21410
    Beta strandi216 – 2249
    Helixi225 – 24218
    Beta strandi246 – 2505
    Turni252 – 2543
    Helixi258 – 27316
    Helixi275 – 2806
    Beta strandi285 – 2895
    Helixi290 – 29910
    Beta strandi304 – 3085
    Helixi310 – 32314
    Helixi327 – 3293
    Beta strandi330 – 3356
    Beta strandi342 – 3487
    Helixi352 – 3598
    Helixi369 – 38618
    Helixi389 – 40719
    Helixi413 – 4208
    Helixi422 – 4243
    Turni427 – 4293
    Helixi434 – 45219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JA8X-ray1.55A/B41-452[»]
    ProteinModelPortaliP48735.
    SMRiP48735. Positions 41-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 1407Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0538.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    InParanoidiP48735.
    KOiK00031.
    OMAiCFQYAIG.
    OrthoDBiEOG7QNVKS.
    PhylomeDBiP48735.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48735-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGYLRVVRS LCRASGSRPA WAPAALTAPT SQEQPRRHYA DKRIKVAKPV    50
    VEMDGDEMTR IIWQFIKEKL ILPHVDIQLK YFDLGLPNRD QTDDQVTIDS 100
    ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE 150
    PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVADRAG TFKMVFTPKD 200
    GSGVKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI QKKWPLYMST 250
    KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS 300
    SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT 350
    VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQMLEK 400
    VCVETVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG 450
    RQ 452
    Length:452
    Mass (Da):50,909
    Last modified:April 3, 2002 - v2
    Checksum:i4DDC830AFC06AB52
    GO
    Isoform 2 (identifier: P48735-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:400
    Mass (Da):45,180
    Checksum:iF1274A2EC2243D5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341Q → H in CAA49208. 1 PublicationCurated
    Sequence conflicti435 – 4351T → M in CAA49208. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401R → G in D2HGA2. 1 Publication
    VAR_065174
    Natural varianti140 – 1401R → Q in D2HGA2. 1 Publication
    VAR_065175

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_056278Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69433 mRNA. Translation: CAA49208.1.
    AK294148 mRNA. Translation: BAG57473.1.
    AK312627 mRNA. Translation: BAG35513.1.
    AK316388 mRNA. Translation: BAH14759.1.
    AC087284 Genomic DNA. No translation available.
    AC092769 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02082.1.
    BC009244 mRNA. Translation: AAH09244.1.
    BC071828 mRNA. Translation: AAH71828.1.
    CCDSiCCDS10359.1.
    PIRiS57499.
    RefSeqiNP_001276839.1. NM_001289910.1.
    NP_001277043.1. NM_001290114.1.
    NP_002159.2. NM_002168.3.
    UniGeneiHs.596461.

    Genome annotation databases

    EnsembliENST00000330062; ENSP00000331897; ENSG00000182054.
    ENST00000540499; ENSP00000446147; ENSG00000182054.
    GeneIDi3418.
    KEGGihsa:3418.
    UCSCiuc002box.3. human.

    Polymorphism databases

    DMDMi20141568.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69433 mRNA. Translation: CAA49208.1 .
    AK294148 mRNA. Translation: BAG57473.1 .
    AK312627 mRNA. Translation: BAG35513.1 .
    AK316388 mRNA. Translation: BAH14759.1 .
    AC087284 Genomic DNA. No translation available.
    AC092769 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02082.1 .
    BC009244 mRNA. Translation: AAH09244.1 .
    BC071828 mRNA. Translation: AAH71828.1 .
    CCDSi CCDS10359.1.
    PIRi S57499.
    RefSeqi NP_001276839.1. NM_001289910.1.
    NP_001277043.1. NM_001290114.1.
    NP_002159.2. NM_002168.3.
    UniGenei Hs.596461.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JA8 X-ray 1.55 A/B 41-452 [» ]
    ProteinModelPortali P48735.
    SMRi P48735. Positions 41-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109644. 8 interactions.
    IntActi P48735. 2 interactions.
    MINTi MINT-3016964.
    STRINGi 9606.ENSP00000331897.

    PTM databases

    PhosphoSitei P48735.

    Polymorphism databases

    DMDMi 20141568.

    2D gel databases

    OGPi P48735.
    UCD-2DPAGE P48735.

    Proteomic databases

    MaxQBi P48735.
    PaxDbi P48735.
    PeptideAtlasi P48735.
    PRIDEi P48735.

    Protocols and materials databases

    DNASUi 3418.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330062 ; ENSP00000331897 ; ENSG00000182054 .
    ENST00000540499 ; ENSP00000446147 ; ENSG00000182054 .
    GeneIDi 3418.
    KEGGi hsa:3418.
    UCSCi uc002box.3. human.

    Organism-specific databases

    CTDi 3418.
    GeneCardsi GC15M090626.
    HGNCi HGNC:5383. IDH2.
    HPAi HPA007831.
    MIMi 147650. gene.
    613657. phenotype.
    neXtProti NX_P48735.
    Orphaneti 79315. D-2-hydroxyglutaric aciduria.
    296. Enchondromatosis.
    163634. Maffucci syndrome.
    PharmGKBi PA29631.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0538.
    HOGENOMi HOG000019858.
    HOVERGENi HBG006119.
    InParanoidi P48735.
    KOi K00031.
    OMAi CFQYAIG.
    OrthoDBi EOG7QNVKS.
    PhylomeDBi P48735.
    TreeFami TF300428.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00021-MONOMER.
    Reactomei REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    ChiTaRSi IDH2. human.
    GeneWikii IDH2.
    GenomeRNAii 3418.
    NextBioi 13474.
    PROi P48735.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48735.
    Bgeei P48735.
    CleanExi HS_IDH2.
    Genevestigatori P48735.

    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. Huh T.-L., Oh I.-U., Kim Y.O., Huh J.-W., Song B.J.
      Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain cortex, Heart and Testis.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Colon and Skin.
    6. "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-67; LYS-106; LYS-155; LYS-166; LYS-180; LYS-256; LYS-263; LYS-272; LYS-275; LYS-282 AND LYS-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status."
      Yu W., Dittenhafer-Reed K.E., Denu J.M.
      J. Biol. Chem. 287:14078-14086(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-413, MUTAGENESIS OF LYS-413.
    9. Cited for: VARIANTS D2HGA2 GLN-140 AND GLY-140.

    Entry informationi

    Entry nameiIDHP_HUMAN
    AccessioniPrimary (citable) accession number: P48735
    Secondary accession number(s): B2R6L6, B4DFL2, Q96GT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: April 3, 2002
    Last modified: October 1, 2014
    This is version 144 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, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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