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P20839

- IMDH1_HUMAN

UniProt

P20839 - IMDH1_HUMAN

Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (08 Nov 2002)
      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.

    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. Subject to product inhibition by XMP and NADH. Also inhibited by ADP.1 PublicationUniRule annotation

    Kineticsi

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

    Pathwayi

    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

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

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. lymphocyte proliferation Source: Ensembl
    3. nucleobase-containing small molecule metabolic process Source: Reactome
    4. purine nucleobase metabolic process Source: Reactome
    5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    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.
    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: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6052. IMPDH1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 10 (RP10) [MIM:180105]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:613837]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    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

    ArrayExpressiP20839.
    BgeeiP20839.
    CleanExiHS_IMPDH1.
    GenevestigatoriP20839.

    Organism-specific databases

    HPAiHPA001400.

    Interactioni

    Subunit structurei

    Homotetramer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi109827. 8 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 – 143
    Helixi20 – 234
    Beta strandi26 – 283
    Helixi32 – 343
    Beta strandi35 – 373
    Helixi46 – 483
    Beta strandi53 – 586
    Beta strandi60 – 634
    Beta strandi65 – 673
    Turni71 – 733
    Helixi76 – 849
    Beta strandi88 – 914
    Helixi97 – 10812
    Beta strandi142 – 1443
    Turni160 – 1634
    Turni195 – 1995
    Helixi200 – 2045
    Beta strandi211 – 2166
    Beta strandi247 – 2504
    Helixi256 – 26510
    Beta strandi269 – 2735
    Helixi281 – 29313
    Beta strandi298 – 3047
    Helixi307 – 31610
    Beta strandi319 – 3235
    Helixi343 – 35412
    Helixi355 – 3573
    Beta strandi361 – 3655
    Helixi370 – 3789
    Beta strandi382 – 3876
    Turni388 – 3925
    Helixi453 – 47119
    Helixi476 – 4849
    Beta strandi490 – 4923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    InParanoidiP20839.
    KOiK00088.
    OMAiHGHSKNI.
    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. Align

    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

    MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD    50
    LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ 100
    ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM 150
    GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI 200
    LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV 250
    GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 300
    GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV 350
    AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY 400
    FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK 450
    GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE 500
    GGVHGLHSYE KRLY 514
    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:
    EMBL
    GenBank
    DDBJ
    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_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]
    uc003vmv.2. human. [P20839-3]
    uc003vmx.2. human.
    uc011kol.1. human. [P20839-1]
    uc011kom.1. human. [P20839-4]

    Polymorphism databases

    DMDMi25014074.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS34748.1. [P20839-3 ]
    CCDS34749.1. [P20839-6 ]
    CCDS43643.1. [P20839-5 ]
    CCDS47699.1. [P20839-7 ]
    CCDS47700.1. [P20839-2 ]
    CCDS55161.1. [P20839-4 ]
    PIRi A35566.
    RefSeqi NP_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_899066.1. NM_183243.2. [P20839-3 ]
    XP_005250371.1. XM_005250314.1.
    UniGenei Hs.654401.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JCN X-ray 2.50 A/B 1-514 [» ]
    ProteinModelPortali P20839.
    SMRi P20839. Positions 10-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109827. 8 interactions.
    DIPi DIP-60163N.
    IntActi P20839. 3 interactions.
    MINTi MINT-2801694.
    STRINGi 9606.ENSP00000345096.

    Chemistry

    BindingDBi P20839.
    ChEMBLi CHEMBL1822.
    DrugBanki DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00157. NADH.
    DB00811. Ribavirin.
    DB00352. Thioguanine.
    GuidetoPHARMACOLOGYi 2624.

    PTM databases

    PhosphoSitei P20839.

    Polymorphism databases

    DMDMi 25014074.

    Proteomic databases

    MaxQBi P20839.
    PaxDbi P20839.
    PRIDEi P20839.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338791 ; 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 ]
    GeneIDi 3614.
    KEGGi hsa:3614.
    UCSCi uc003vmt.2. human. [P20839-2 ]
    uc003vmv.2. human. [P20839-3 ]
    uc003vmx.2. human.
    uc011kol.1. human. [P20839-1 ]
    uc011kom.1. human. [P20839-4 ]

    Organism-specific databases

    CTDi 3614.
    GeneCardsi GC07M128032.
    GeneReviewsi IMPDH1.
    HGNCi HGNC:6052. IMPDH1.
    HPAi HPA001400.
    MIMi 146690. gene.
    180105. phenotype.
    613837. phenotype.
    neXtProti NX_P20839.
    Orphaneti 65. Leber congenital amaurosis.
    791. Retinitis pigmentosa.
    PharmGKBi PA29862.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165752.
    HOVERGENi HBG052122.
    InParanoidi P20839.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG7VTDMM.
    PhylomeDBi P20839.
    TreeFami TF300378.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci MetaCyc:HS02896-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RK P20839.

    Miscellaneous databases

    ChiTaRSi IMPDH1. human.
    EvolutionaryTracei P20839.
    GeneWikii IMPDH1.
    GenomeRNAii 3614.
    NextBioi 14135.
    PROi P20839.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20839.
    Bgeei P20839.
    CleanExi HS_IMPDH1.
    Genevestigatori P20839.

    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. "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: October 1, 2014
    This is version 180 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