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P24547

- IMDH2_MOUSE

UniProt

P24547 - IMDH2_MOUSE

Protein

Inosine-5'-monophosphate dehydrogenase 2

Gene

Impdh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.UniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi326 – 3261Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei329 – 3291IMPUniRule annotation
    Active sitei331 – 3311Thioimidate intermediateUniRule annotation
    Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei441 – 4411IMPUniRule annotation
    Metal bindingi500 – 5001Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi274 – 2763NADUniRule annotation
    Nucleotide bindingi324 – 3263NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. IMP dehydrogenase activity Source: MGI
    4. metal ion binding Source: UniProtKB-HAMAP
    5. nucleotide binding Source: UniProtKB
    6. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. GMP biosynthetic process Source: UniProtKB-HAMAP
    3. lymphocyte proliferation Source: MGI
    4. purine nucleotide biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    DNA-binding, Metal-binding, NAD, Potassium, RNA-binding

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 2UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 2UniRule annotation
    Short name:
    IMPD 2UniRule annotation
    Short name:
    IMPDH 2UniRule annotation
    Alternative name(s):
    IMPDH-II
    Gene namesi
    Name:Impdh2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:109367. Impdh2.

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedUniRule annotation
    Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 2PRO_0000093674Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221PhosphoserineBy similarity
    Modified residuei400 – 4001PhosphotyrosineBy similarity
    Modified residuei416 – 4161PhosphoserineBy similarity
    Modified residuei511 – 5111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP24547.
    PaxDbiP24547.
    PRIDEiP24547.

    2D gel databases

    REPRODUCTION-2DPAGEP24547.

    PTM databases

    PhosphoSiteiP24547.

    Expressioni

    Gene expression databases

    BgeeiP24547.
    CleanExiMM_IMPDH2.
    GenevestigatoriP24547.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi204792. 2 interactions.
    IntActiP24547. 2 interactions.
    MINTiMINT-1869864.

    Structurei

    3D structure databases

    ProteinModelPortaliP24547.
    SMRiP24547. Positions 10-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini114 – 17360CBS 1UniRule annotationAdd
    BLAST
    Domaini179 – 23759CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni364 – 3663IMP bindingUniRule annotation
    Regioni387 – 3882IMP bindingUniRule annotation
    Regioni411 – 4155IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    InParanoidiP24547.
    KOiK00088.
    OMAiHAAKDEH.
    OrthoDBiEOG7VTDMM.
    PhylomeDBiP24547.
    TreeFamiTF300378.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24547-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD    50
    LTSALTKKIT LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ 100
    ANEVRKVKKY EQGFITDPVV LSPKDRVRDV FEAKARHGFC GIPITDTGRM 150
    GSRLVGIISS RDIDFLKEEE HDRFLEEIMT KREDLVVAPA GVTLKEANEI 200
    LQRSKKGKLP IVNENDELVA IIARTDLKKN RDYPLASKDA KKQLLCGAAI 250
    GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYI KEKYPSLQVI 300
    GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV 350
    SEYARRFGVP VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY 400
    FFSDGIRLKK YRGMGSLDAM DKHLSSQNRY FSEADKIKVA QGVSGAVQDK 450
    GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR AMMYSGELKF EKRTSSAQVE 500
    GGVHSLHSYE KRLF 514
    Length:514
    Mass (Da):55,815
    Last modified:October 3, 2003 - v2
    Checksum:i17D25A5C5EBCC439
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti458 – 4581P → L AA sequence (PubMed:2572589)Curated
    Sequence conflicti465 – 4651Q → S AA sequence (PubMed:2572589)Curated
    Sequence conflicti483 – 4831M → T in AAA39311. (PubMed:1671845)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti333 – 3331T → I in mycophenolic acid resistant cells.
    Natural varianti351 – 3511S → Y in mycophenolic acid resistant cells.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33934 mRNA. Translation: AAA39311.1.
    M98333 mRNA. Translation: AAA20181.1.
    BC010314 mRNA. Translation: AAH10314.1.
    BC052671 mRNA. Translation: AAH52671.1.
    CCDSiCCDS40768.1.
    PIRiJT0565.
    RefSeqiNP_035960.2. NM_011830.3.
    UniGeneiMm.6065.

    Genome annotation databases

    EnsembliENSMUST00000081111; ENSMUSP00000079888; ENSMUSG00000062867.
    GeneIDi23918.
    KEGGimmu:23918.
    UCSCiuc009rqg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33934 mRNA. Translation: AAA39311.1 .
    M98333 mRNA. Translation: AAA20181.1 .
    BC010314 mRNA. Translation: AAH10314.1 .
    BC052671 mRNA. Translation: AAH52671.1 .
    CCDSi CCDS40768.1.
    PIRi JT0565.
    RefSeqi NP_035960.2. NM_011830.3.
    UniGenei Mm.6065.

    3D structure databases

    ProteinModelPortali P24547.
    SMRi P24547. Positions 10-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204792. 2 interactions.
    IntActi P24547. 2 interactions.
    MINTi MINT-1869864.

    Chemistry

    BindingDBi P24547.
    ChEMBLi CHEMBL3169.

    PTM databases

    PhosphoSitei P24547.

    2D gel databases

    REPRODUCTION-2DPAGE P24547.

    Proteomic databases

    MaxQBi P24547.
    PaxDbi P24547.
    PRIDEi P24547.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081111 ; ENSMUSP00000079888 ; ENSMUSG00000062867 .
    GeneIDi 23918.
    KEGGi mmu:23918.
    UCSCi uc009rqg.1. mouse.

    Organism-specific databases

    CTDi 3615.
    MGIi MGI:109367. Impdh2.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165752.
    HOVERGENi HBG052122.
    InParanoidi P24547.
    KOi K00088.
    OMAi HAAKDEH.
    OrthoDBi EOG7VTDMM.
    PhylomeDBi P24547.
    TreeFami TF300378.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Miscellaneous databases

    ChiTaRSi IMPDH2. mouse.
    NextBioi 303689.
    PROi P24547.
    SOURCEi Search...

    Gene expression databases

    Bgeei P24547.
    CleanExi MM_IMPDH2.
    Genevestigatori P24547.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence of a cDNA encoding mouse IMP dehydrogenase."
      Tiedeman A.A., Smith J.M.
      Gene 97:289-293(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Gene amplification and dual point mutations of mouse IMP dehydrogenase associated with cellular resistance to mycophenolic acid."
      Lightfoot T., Snyder F.F.
      Biochim. Biophys. Acta 1217:156-162(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MYCOPHENOLIC ACID RESISTANT.
      Tissue: Brain.
    3. "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: C3H/He and Czech II.
      Tissue: Mammary gland and Osteoblast.
    4. "Increased activity, amount, and altered kinetic properties of IMP dehydrogenase from mycophenolic acid-resistant neuroblastoma cells."
      Hodges S.D., Fung E., McKay D.J., Renaux B.S., Snyder F.F.
      J. Biol. Chem. 264:18137-18141(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 125-133; 182-194; 289-290; 439-449; 456-466 AND 475-478.
    5. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 137-149.
      Tissue: Brain.

    Entry informationi

    Entry nameiIMDH2_MOUSE
    AccessioniPrimary (citable) accession number: P24547
    Secondary accession number(s): Q61734, Q91Z11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3