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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Cofactori

K(+)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. Subject to product inhibition by XMP and NADH. Also inhibited by ADP.UniRule annotation1 Publication

Kineticsi

  1. KM=18 µM for Inosine 5'-phosphate2 Publications
  2. KM=46 µM for NAD+2 Publications

    Pathway:iXMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase, Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase, Inosine-5'-monophosphate dehydrogenase, Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1), Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (DKFZp781N0678)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi326 – 3261Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei329 – 3291IMP
    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

    • DNA binding Source: UniProtKB
    • IMP dehydrogenase activity Source: ProtInc
    • metal ion binding Source: UniProtKB-HAMAP
    • nucleic acid binding Source: UniProtKB
    • nucleotide binding Source: UniProtKB-HAMAP
    • RNA binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    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

    BioCyciMetaCyc:HS02896-MONOMER.
    BRENDAi1.1.1.205. 2681.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP20839.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 1UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 1UniRule annotation
    Short name:
    IMPD 1UniRule annotation
    Short name:
    IMPDH 1UniRule annotation
    Alternative name(s):
    IMPDH-I
    Gene namesi
    Name:IMPDH1UniRule annotation
    Synonyms:IMPD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6052. IMPDH1.

    Subcellular locationi

    GO - Cellular componenti

    • cell junction Source: HPA
    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • nucleoplasm Source: HPA
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 10 (RP10)3 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

    See also OMIM:180105
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065617
    Natural varianti224 – 2241R → P in RP10. 1 Publication
    VAR_017031
    Natural varianti226 – 2261D → N in RP10. 2 Publications
    VAR_017032
    Natural varianti268 – 2681V → I in RP10. 2 Publications
    VAR_017033
    Natural varianti372 – 3721H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065621
    Leber congenital amaurosis 11 (LCA11)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.

    See also OMIM:613837
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065616
    Natural varianti198 – 1981N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065618

    Keywords - Diseasei

    Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

    Organism-specific databases

    MIMi180105. phenotype.
    613837. phenotype.
    Orphaneti65. Leber congenital amaurosis.
    791. Retinitis pigmentosa.
    PharmGKBiPA29862.

    Chemistry

    DrugBankiDB01033. Mercaptopurine.
    DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00811. Ribavirin.

    Polymorphism and mutation databases

    BioMutaiIMPDH1.
    DMDMi25014074.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedUniRule annotation1 Publication
    Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 1PRO_0000093670Add
    BLAST

    Proteomic databases

    MaxQBiP20839.
    PaxDbiP20839.
    PRIDEiP20839.

    PTM databases

    PhosphoSiteiP20839.

    Expressioni

    Tissue specificityi

    IMP type I is the main species in normal leukocytes and type II predominates over type I in the tumor.

    Inductioni

    Constitutively expressed.

    Gene expression databases

    BgeeiP20839.
    CleanExiHS_IMPDH1.
    ExpressionAtlasiP20839. baseline and differential.
    GenevisibleiP20839. HS.

    Organism-specific databases

    HPAiHPA058375.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi109827. 47 interactions.
    DIPiDIP-60163N.
    IntActiP20839. 3 interactions.
    MINTiMINT-2801694.
    STRINGi9606.ENSP00000345096.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 143Combined sources
    Helixi20 – 234Combined sources
    Beta strandi26 – 283Combined sources
    Helixi32 – 343Combined sources
    Beta strandi35 – 373Combined sources
    Helixi46 – 483Combined sources
    Beta strandi53 – 586Combined sources
    Beta strandi60 – 634Combined sources
    Beta strandi65 – 673Combined sources
    Turni71 – 733Combined sources
    Helixi76 – 849Combined sources
    Beta strandi88 – 914Combined sources
    Helixi97 – 10812Combined sources
    Beta strandi142 – 1443Combined sources
    Turni160 – 1634Combined sources
    Turni195 – 1995Combined sources
    Helixi200 – 2045Combined sources
    Beta strandi211 – 2166Combined sources
    Beta strandi247 – 2504Combined sources
    Helixi256 – 26510Combined sources
    Beta strandi269 – 2735Combined sources
    Helixi281 – 29313Combined sources
    Beta strandi298 – 3047Combined sources
    Helixi307 – 31610Combined sources
    Beta strandi319 – 3235Combined sources
    Helixi343 – 35412Combined sources
    Helixi355 – 3573Combined sources
    Beta strandi361 – 3655Combined sources
    Helixi370 – 3789Combined sources
    Beta strandi382 – 3876Combined sources
    Turni388 – 3925Combined sources
    Helixi453 – 47119Combined sources
    Helixi476 – 4849Combined sources
    Beta strandi490 – 4923Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCNX-ray2.50A/B1-514[»]
    ProteinModelPortaliP20839.
    SMRiP20839. Positions 10-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20839.

    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 binding
    Regioni387 – 3882IMP binding
    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.
    GeneTreeiENSGT00530000062923.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    KOiK00088.
    OMAiDAMEKNN.
    OrthoDBiEOG7VTDMM.
    PhylomeDBiP20839.
    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]

    Sequences (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P20839-1) [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

            10         20         30         40         50
    MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD
    60 70 80 90 100
    LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ
    110 120 130 140 150
    ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM
    160 170 180 190 200
    GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI
    210 220 230 240 250
    LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV
    260 270 280 290 300
    GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI
    310 320 330 340 350
    GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV
    360 370 380 390 400
    AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY
    410 420 430 440 450
    FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK
    460 470 480 490 500
    GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE
    510
    GGVHGLHSYE KRLY
    Length:514
    Mass (Da):55,406
    Last modified:November 8, 2002 - v2
    Checksum:iABAC654A9091BE62
    GO
    Isoform 2 (identifier: P20839-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-108: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:489
    Mass (Da):52,598
    Checksum:i47A1273662A8C39B
    GO
    Isoform 3 (identifier: P20839-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESM

    Show »
    Length:563
    Mass (Da):60,437
    Checksum:iEB370370B77CD0DA
    GO
    Isoform 4 (identifier: P20839-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-108: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:509
    Mass (Da):54,795
    Checksum:i83819A210AAAB3CA
    GO
    Isoform 5 (identifier: P20839-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPL...QMDRLRRASM

    Note: Ref.2 (BAG53840) sequence has a frameshift in position 35.
    Show »
    Length:589
    Mass (Da):63,253
    Checksum:i31E1ED04061B62F8
    GO
    Isoform 6 (identifier: P20839-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEGPLTPPPL...QMDRLRRASM

    Note: No experimental confirmation available.
    Show »
    Length:599
    Mass (Da):64,320
    Checksum:i7BED197A49991EA6
    GO
    Isoform 7 (identifier: P20839-7) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MADYLISGGTGYVPEDGLTAQQLFASADGLTYN → MEGPLTPPPL...VQMDRLRRAS

    Show »
    Length:566
    Mass (Da):60,898
    Checksum:iA10C18F253345FEA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291G → D in AAA36114 (PubMed:1969416).Curated
    Sequence conflicti109 – 1091K → N in AAA36114 (PubMed:1969416).Curated
    Sequence conflicti273 – 2742LD → FH in AAA36114 (PubMed:1969416).Curated
    Sequence conflicti419 – 4191A → P in AAA36114 (PubMed:1969416).Curated
    Sequence conflicti497 – 4971A → P in AAA36114 (PubMed:1969416).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065616
    Natural varianti116 – 1161T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065617
    Natural varianti198 – 1981N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065618
    Natural varianti224 – 2241R → P in RP10. 1 Publication
    VAR_017031
    Natural varianti226 – 2261D → N in RP10. 2 Publications
    VAR_017032
    Natural varianti268 – 2681V → I in RP10. 2 Publications
    VAR_017033
    Natural varianti285 – 2851A → T.1 Publication
    VAR_065619
    Natural varianti324 – 3241G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. 1 Publication
    VAR_065620
    Natural varianti372 – 3721H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
    VAR_065621

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333MADYL…GLTYN → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRAS in isoform 7. CuratedVSP_046968Add
    BLAST
    Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3. 2 PublicationsVSP_014363
    Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESCFLLELSSVVL LAGVGVQMDRLRRASM in isoform 5. 1 PublicationVSP_046969
    Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRASM in isoform 6. CuratedVSP_046970
    Alternative sequencei84 – 10825Missing in isoform 2. 1 PublicationVSP_002674Add
    BLAST
    Alternative sequencei104 – 1085Missing in isoform 4. 1 PublicationVSP_043485

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05272 mRNA. Translation: AAA36114.1.
    AK054640 mRNA. Translation: BAB70780.1.
    AK054667 mRNA. Translation: BAG51409.1.
    AK122994 mRNA. Translation: BAG53840.1. Frameshift.
    AK293413 mRNA. Translation: BAG56920.1.
    AC010655 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24310.1.
    CH236947 Genomic DNA. Translation: EAL24311.1.
    CH471070 Genomic DNA. Translation: EAW83652.1.
    BC033622 mRNA. Translation: AAH33622.2.
    CD014008 mRNA. No translation available.
    CCDSiCCDS34748.1. [P20839-3]
    CCDS34749.1. [P20839-6]
    CCDS43643.1. [P20839-5]
    CCDS47699.1. [P20839-7]
    CCDS47700.1. [P20839-2]
    CCDS55161.1. [P20839-4]
    PIRiA35566.
    RefSeqiNP_000874.2. NM_000883.3. [P20839-6]
    NP_001096075.1. NM_001102605.1. [P20839-5]
    NP_001136045.1. NM_001142573.1. [P20839-1]
    NP_001136046.1. NM_001142574.1. [P20839-4]
    NP_001136047.1. NM_001142575.1. [P20839-2]
    NP_001136048.1. NM_001142576.1. [P20839-7]
    NP_001291450.1. NM_001304521.1.
    NP_899066.1. NM_183243.2. [P20839-3]
    XP_005250371.1. XM_005250314.1.
    UniGeneiHs.654401.

    Genome annotation databases

    EnsembliENST00000338791; ENSP00000345096; ENSG00000106348. [P20839-6]
    ENST00000348127; ENSP00000265385; ENSG00000106348. [P20839-3]
    ENST00000354269; ENSP00000346219; ENSG00000106348. [P20839-5]
    ENST00000419067; ENSP00000399400; ENSG00000106348. [P20839-7]
    ENST00000480861; ENSP00000420185; ENSG00000106348. [P20839-4]
    ENST00000496200; ENSP00000420803; ENSG00000106348. [P20839-2]
    GeneIDi3614.
    KEGGihsa:3614.
    UCSCiuc003vmt.2. human. [P20839-2]
    uc003vmu.2. human.
    uc003vmv.2. human. [P20839-3]
    uc003vmx.2. human.
    uc011kol.1. human. [P20839-1]
    uc011kom.1. human. [P20839-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Mutations of the IMPDH1 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05272 mRNA. Translation: AAA36114.1.
    AK054640 mRNA. Translation: BAB70780.1.
    AK054667 mRNA. Translation: BAG51409.1.
    AK122994 mRNA. Translation: BAG53840.1. Frameshift.
    AK293413 mRNA. Translation: BAG56920.1.
    AC010655 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24310.1.
    CH236947 Genomic DNA. Translation: EAL24311.1.
    CH471070 Genomic DNA. Translation: EAW83652.1.
    BC033622 mRNA. Translation: AAH33622.2.
    CD014008 mRNA. No translation available.
    CCDSiCCDS34748.1. [P20839-3]
    CCDS34749.1. [P20839-6]
    CCDS43643.1. [P20839-5]
    CCDS47699.1. [P20839-7]
    CCDS47700.1. [P20839-2]
    CCDS55161.1. [P20839-4]
    PIRiA35566.
    RefSeqiNP_000874.2. NM_000883.3. [P20839-6]
    NP_001096075.1. NM_001102605.1. [P20839-5]
    NP_001136045.1. NM_001142573.1. [P20839-1]
    NP_001136046.1. NM_001142574.1. [P20839-4]
    NP_001136047.1. NM_001142575.1. [P20839-2]
    NP_001136048.1. NM_001142576.1. [P20839-7]
    NP_001291450.1. NM_001304521.1.
    NP_899066.1. NM_183243.2. [P20839-3]
    XP_005250371.1. XM_005250314.1.
    UniGeneiHs.654401.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCNX-ray2.50A/B1-514[»]
    ProteinModelPortaliP20839.
    SMRiP20839. Positions 10-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109827. 47 interactions.
    DIPiDIP-60163N.
    IntActiP20839. 3 interactions.
    MINTiMINT-2801694.
    STRINGi9606.ENSP00000345096.

    Chemistry

    BindingDBiP20839.
    ChEMBLiCHEMBL2111369.
    DrugBankiDB01033. Mercaptopurine.
    DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00811. Ribavirin.
    GuidetoPHARMACOLOGYi2624.

    PTM databases

    PhosphoSiteiP20839.

    Polymorphism and mutation databases

    BioMutaiIMPDH1.
    DMDMi25014074.

    Proteomic databases

    MaxQBiP20839.
    PaxDbiP20839.
    PRIDEiP20839.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338791; ENSP00000345096; ENSG00000106348. [P20839-6]
    ENST00000348127; ENSP00000265385; ENSG00000106348. [P20839-3]
    ENST00000354269; ENSP00000346219; ENSG00000106348. [P20839-5]
    ENST00000419067; ENSP00000399400; ENSG00000106348. [P20839-7]
    ENST00000480861; ENSP00000420185; ENSG00000106348. [P20839-4]
    ENST00000496200; ENSP00000420803; ENSG00000106348. [P20839-2]
    GeneIDi3614.
    KEGGihsa:3614.
    UCSCiuc003vmt.2. human. [P20839-2]
    uc003vmu.2. human.
    uc003vmv.2. human. [P20839-3]
    uc003vmx.2. human.
    uc011kol.1. human. [P20839-1]
    uc011kom.1. human. [P20839-4]

    Organism-specific databases

    CTDi3614.
    GeneCardsiGC07M128032.
    GeneReviewsiIMPDH1.
    HGNCiHGNC:6052. IMPDH1.
    HPAiHPA058375.
    MIMi146690. gene.
    180105. phenotype.
    613837. phenotype.
    neXtProtiNX_P20839.
    Orphaneti65. Leber congenital amaurosis.
    791. Retinitis pigmentosa.
    PharmGKBiPA29862.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0517.
    GeneTreeiENSGT00530000062923.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    KOiK00088.
    OMAiDAMEKNN.
    OrthoDBiEOG7VTDMM.
    PhylomeDBiP20839.
    TreeFamiTF300378.

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.
    BioCyciMetaCyc:HS02896-MONOMER.
    BRENDAi1.1.1.205. 2681.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP20839.

    Miscellaneous databases

    ChiTaRSiIMPDH1. human.
    EvolutionaryTraceiP20839.
    GeneWikiiIMPDH1.
    GenomeRNAii3614.
    NextBioi14135.
    PROiP20839.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP20839.
    CleanExiHS_IMPDH1.
    ExpressionAtlasiP20839. baseline and differential.
    GenevisibleiP20839. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Two distinct cDNAs for human IMP dehydrogenase."
      Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.
      J. Biol. Chem. 265:5292-5295(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Spleen.
    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 2; 3; 4 AND 5).
      Tissue: Brain.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3).
      Tissue: Blood.
    7. "Characterization of human type I and type II IMP dehydrogenases."
      Carr S.F., Papp E., Wu J.C., Natsumeda Y.
      J. Biol. Chem. 268:27286-27290(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
    8. "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes."
      Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., Stuve L.L.
      Genomics 83:566-571(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    9. "Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding."
      Hager P.W., Collart F.R., Huberman E., Mitchell B.S.
      Biochem. Pharmacol. 49:1323-1329(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo."
      McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M., Hedstrom L.
      Biochem. J. 379:243-251(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEIC ACID-BINDING.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of the human type I inosine monophosphate dehydrogenase and implications for isoform specificity."
      Risal D., Strickler M.D., Goldstein B.M.
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
    13. "Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice."
      Kennan A., Aherne A., Palfi A., Humphries M., McKee A., Stitt A., Simpson D.A., Demtroder K., Orntoft T., Ayuso C., Kenna P.F., Farrar G.J., Humphries P.
      Hum. Mol. Genet. 11:547-557(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RP10 PRO-224.
    14. "Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa."
      Bowne S.J., Sullivan L.S., Blanton S.H., Cepko C.L., Blackshaw S., Birch D.G., Hughbanks-Wheaton D., Heckenlively J.R., Daiger S.P.
      Hum. Mol. Genet. 11:559-568(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RP10 ASN-226 AND ILE-268.
    15. "Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and Leber congenital amaurosis."
      Bowne S.J., Sullivan L.S., Mortimer S.E., Hedstrom L., Zhu J., Spellicy C.J., Gire A.I., Hughbanks-Wheaton D., Birch D.G., Lewis R.A., Heckenlively J.R., Daiger S.P.
      Invest. Ophthalmol. Vis. Sci. 47:34-42(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RP10 MET-116; ASN-226; ILE-268 AND PRO-372, VARIANTS LCA11 TRP-105 AND LYS-198, VARIANTS THR-285 AND ASP-324, CHARACTERIZATION OF VARIANTS RP10 MET-116 AND PRO-372, CHARACTERIZATION OF VARIANTS LCA11 TRP-105 AND LYS-198, CHARACTERIZATION OF VARIANT ASP-324.

    Entry informationi

    Entry nameiIMDH1_HUMAN
    AccessioniPrimary (citable) accession number: P20839
    Secondary accession number(s): A4D0Z6
    , A4D0Z7, A6NDW5, A6NNI6, B3KNP7, B3KVM8, B4DE09, C9JV30, J3KNX8, Q8N194, Q96NU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 8, 2002
    Last modified: July 22, 2015
    This is version 189 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

    Miscellaneous

    Because IMPDH activity is tightly linked with cell proliferation, it has been recognized as a target for cancer and viral chemotherapy and as a target for immunosuppressive drugs. The activities of the antitumor drug tiazofurin, the antiviral drug ribavirin, and the immunosuppressive drugs mizoribine and mycophenolic acid (MPA) are attributed to the inhibition of IMPDH. In addition, bacterial and parasitic IMPDH's differ significantly from mammalian enzymes, which makes it a suitable target for anti-infective drugs.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.