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P54071

- IDHP_MOUSE

UniProt

P54071 - IDHP_MOUSE

Protein

Isocitrate dehydrogenase [NADP], mitochondrial

Gene

Idh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (11 Sep 2007)
      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. glyoxylate cycle Source: UniProtKB-KW
    3. isocitrate metabolic process Source: UniProtKB
    4. response to stress Source: UniProtKB-KW
    5. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Stress response, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:96414. Idh2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionBy similarityAdd
    BLAST
    Chaini40 – 452413Isocitrate dehydrogenase [NADP], mitochondrialPRO_0000014421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451N6-acetyllysine1 Publication
    Modified residuei48 – 481N6-acetyllysine1 Publication
    Modified residuei67 – 671N6-acetyllysineBy similarity
    Modified residuei69 – 691N6-acetyllysine1 Publication
    Modified residuei80 – 801N6-acetyllysine; alternate1 Publication
    Modified residuei80 – 801N6-succinyllysine; alternate1 Publication
    Modified residuei106 – 1061N6-acetyllysine; alternate1 Publication
    Modified residuei106 – 1061N6-succinyllysine; alternate1 Publication
    Modified residuei155 – 1551N6-acetyllysine1 Publication
    Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
    Modified residuei166 – 1661N6-succinyllysine; alternate1 Publication
    Modified residuei180 – 1801N6-acetyllysine; alternate1 Publication
    Modified residuei180 – 1801N6-succinyllysine; alternate1 Publication
    Modified residuei193 – 1931N6-acetyllysine; alternate1 Publication
    Modified residuei193 – 1931N6-succinyllysine; alternate1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei256 – 2561N6-acetyllysine; alternate1 Publication
    Modified residuei256 – 2561N6-succinyllysine; alternate1 Publication
    Modified residuei263 – 2631N6-acetyllysine2 Publications
    Modified residuei272 – 2721N6-acetyllysine1 Publication
    Modified residuei275 – 2751N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-acetyllysine1 Publication
    Modified residuei282 – 2821N6-acetyllysine; alternate1 Publication
    Modified residuei282 – 2821N6-succinyllysine; alternate1 Publication
    Modified residuei384 – 3841N6-acetyllysine; alternate1 Publication
    Modified residuei384 – 3841N6-succinyllysine; alternate1 Publication
    Modified residuei400 – 4001N6-acetyllysine1 Publication
    Modified residuei413 – 4131N6-acetyllysineBy similarity
    Modified residuei442 – 4421N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation at Lys-413 dramatically reduces catalytic activity. Deacetylated by SIRT3 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54071.
    PaxDbiP54071.
    PRIDEiP54071.

    PTM databases

    PhosphoSiteiP54071.

    Expressioni

    Tissue specificityi

    Heart > kidney >> other tissues.1 Publication

    Inductioni

    By oxidative stress (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP54071.
    BgeeiP54071.
    CleanExiMM_IDH2.
    GenevestigatoriP54071.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi234733. 2 interactions.
    IntActiP54071. 4 interactions.
    MINTiMINT-4114220.

    Structurei

    3D structure databases

    ProteinModelPortaliP54071.
    SMRiP54071. Positions 40-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0538.
    GeneTreeiENSGT00390000012547.
    HOGENOMiHOG000019858.
    HOVERGENiHBG006119.
    KOiK00031.
    OMAiFKDEFQR.
    OrthoDBiEOG7QNVKS.
    PhylomeDBiP54071.
    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.

    P54071-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGYLRAVSS LCRASGSART WAPAALTVPS WPEQPRRHYA EKRIKVEKPV    50
    VEMDGDEMTR IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS 100
    ALATQKYSVA VKCATITPDE ARVEEFKLKK MWKSPNGTIR NILGGTVFRE 150
    PIICKNIPRL VPGWTKPITI GRHAHGDQYK ATDFVVDRAG TFKLVFTPKD 200
    GSSAKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYSI QKKWPLYLST 250
    KNTILKAYDG RFKDIFQEIF DKHYKTDFDK NKIWYEHRLI DDMVAQVLKS 300
    SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT 350
    VTRHYREHQK GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK 400
    VCVQTVESGA MTKDLAGCIH GLSNVKLNEH FLNTTDFLDT IKSNLDRALG 450
    KQ 452
    Length:452
    Mass (Da):50,906
    Last modified:September 11, 2007 - v3
    Checksum:i19BB5CF78512ECAB
    GO

    Sequence cautioni

    The sequence AAC52473.1 differs from that shown. Reason: Frameshift at positions 5 and 11.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti104 – 1041T → A in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti109 – 1091V → M in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti152 – 1521I → S in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti200 – 2001D → N in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti214 – 2141A → G in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti280 – 2801K → R in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti280 – 2801K → R in AAG43538. (PubMed:11278619)Curated
    Sequence conflicti322 – 3232QG → SR in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti367 – 3682NP → KG in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti398 – 3981L → R in AAC52473. (PubMed:8867815)Curated
    Sequence conflicti408 – 4081Missing in AAC52473. (PubMed:8867815)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51167 mRNA. Translation: AAC52473.1. Frameshift.
    AF212319 mRNA. Translation: AAG43538.1.
    AK088110 mRNA. Translation: BAC40149.1.
    AK145753 mRNA. Translation: BAE26628.1.
    AK161640 mRNA. Translation: BAE36505.1.
    AK169395 mRNA. Translation: BAE41142.1.
    BC060030 mRNA. Translation: AAH60030.1.
    CCDSiCCDS39994.1.
    RefSeqiNP_766599.2. NM_173011.2.
    UniGeneiMm.246432.
    Mm.290925.

    Genome annotation databases

    EnsembliENSMUST00000107384; ENSMUSP00000103007; ENSMUSG00000030541.
    GeneIDi269951.
    KEGGimmu:269951.
    UCSCiuc009hzm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51167 mRNA. Translation: AAC52473.1 . Frameshift.
    AF212319 mRNA. Translation: AAG43538.1 .
    AK088110 mRNA. Translation: BAC40149.1 .
    AK145753 mRNA. Translation: BAE26628.1 .
    AK161640 mRNA. Translation: BAE36505.1 .
    AK169395 mRNA. Translation: BAE41142.1 .
    BC060030 mRNA. Translation: AAH60030.1 .
    CCDSi CCDS39994.1.
    RefSeqi NP_766599.2. NM_173011.2.
    UniGenei Mm.246432.
    Mm.290925.

    3D structure databases

    ProteinModelPortali P54071.
    SMRi P54071. Positions 40-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 234733. 2 interactions.
    IntActi P54071. 4 interactions.
    MINTi MINT-4114220.

    Chemistry

    ChEMBLi CHEMBL2176829.

    PTM databases

    PhosphoSitei P54071.

    Proteomic databases

    MaxQBi P54071.
    PaxDbi P54071.
    PRIDEi P54071.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107384 ; ENSMUSP00000103007 ; ENSMUSG00000030541 .
    GeneIDi 269951.
    KEGGi mmu:269951.
    UCSCi uc009hzm.2. mouse.

    Organism-specific databases

    CTDi 3418.
    MGIi MGI:96414. Idh2.

    Phylogenomic databases

    eggNOGi COG0538.
    GeneTreei ENSGT00390000012547.
    HOGENOMi HOG000019858.
    HOVERGENi HBG006119.
    KOi K00031.
    OMAi FKDEFQR.
    OrthoDBi EOG7QNVKS.
    PhylomeDBi P54071.
    TreeFami TF300428.

    Miscellaneous databases

    ChiTaRSi IDH2. mouse.
    NextBioi 393111.
    PROi P54071.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54071.
    Bgeei P54071.
    CleanExi MM_IDH2.
    Genevestigatori P54071.

    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. "Molecular cloning of the cDNA of mouse mitochondrial NADP-dependent isocitrate dehydrogenase and the expression of the gene during lymphocyte activation."
      Yang L., Luo H., Vinay P., Wu J.
      J. Cell. Biochem. 60:400-410(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Heart.
    2. "Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase."
      Jo S.-H., Son M.-K., Koh H.-J., Lee S.-M., Song I.-H., Kim Y.-O., Lee Y.-S., Jeong K.-S., Kim W.B., Park J.-W., Song B.J., Huhe T.-L.
      J. Biol. Chem. 276:16168-16176(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Embryo, Heart and Thymus.
    4. "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].
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-60 AND 81-89, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-106; LYS-166; LYS-180; LYS-193; LYS-256; LYS-282 AND LYS-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-45; LYS-48; LYS-69; LYS-80; LYS-106; LYS-155; LYS-166; LYS-180; LYS-193; LYS-199; LYS-256; LYS-263; LYS-272; LYS-280; LYS-282; LYS-384; LYS-400 AND LYS-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiIDHP_MOUSE
    AccessioniPrimary (citable) accession number: P54071
    Secondary accession number(s): Q8C2R9, Q9EQK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3