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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

    Pathwayi: XMP 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 (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH), 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)DescriptionActionsGraphical viewLength
    Metal bindingi326Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi328Potassium; via carbonyl oxygenUniRule annotation1
    Binding sitei329IMP1
    Active sitei331Thioimidate intermediateUniRule annotation1
    Metal bindingi331Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei429Proton acceptorUniRule annotation1
    Binding sitei441IMPUniRule annotation1
    Metal bindingi500Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi501Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi502Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi274 – 276NADUniRule annotation3
    Nucleotide bindingi324 – 326NADUniRule annotation3

    GO - Molecular functioni

    • DNA binding Source: UniProtKB
    • IMP dehydrogenase activity Source: Reactome
    • 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.
    ZFISH:HS02896-MONOMER.
    BRENDAi1.1.1.205. 2681.
    ReactomeiR-HSA-6798695. Neutrophil degranulation.
    R-HSA-73817. 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
    Proteomesi
    • UP000005640 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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065617116T → 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 Publication1
    Natural variantiVAR_017031224R → P in RP10. 1 Publication1
    Natural variantiVAR_017032226D → N in RP10. 2 Publications1
    Natural variantiVAR_017033268V → I in RP10. 2 Publications1
    Natural variantiVAR_065621372H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1
    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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065616105R → 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 Publication1
    Natural variantiVAR_065618198N → 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 Publication1

    Keywords - Diseasei

    Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

    Organism-specific databases

    DisGeNETi3614.
    MalaCardsiIMPDH1.
    MIMi180105. phenotype.
    613837. phenotype.
    OpenTargetsiENSG00000106348.
    Orphaneti65. Leber congenital amaurosis.
    791. Retinitis pigmentosa.
    PharmGKBiPA29862.

    Chemistry databases

    ChEMBLiCHEMBL1822.
    DrugBankiDB01033. Mercaptopurine.
    DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00811. Ribavirin.
    GuidetoPHARMACOLOGYi2624.

    Polymorphism and mutation databases

    BioMutaiIMPDH1.
    DMDMi25014074.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedUniRule annotation1 Publication
    ChainiPRO_00000936702 – 514Inosine-5'-monophosphate dehydrogenase 1Add BLAST513

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei160PhosphoserineCombined sources1
    Modified residuei341Omega-N-methylarginineBy similarity1
    Modified residuei355Omega-N-methylarginineBy similarity1

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    EPDiP20839.
    MaxQBiP20839.
    PaxDbiP20839.
    PeptideAtlasiP20839.
    PRIDEiP20839.

    PTM databases

    iPTMnetiP20839.
    PhosphoSitePlusiP20839.

    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

    BgeeiENSG00000106348.
    CleanExiHS_IMPDH1.
    ExpressionAtlasiP20839. baseline and differential.
    GenevisibleiP20839. HS.

    Organism-specific databases

    HPAiHPA058375.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi109827. 79 interactors.
    DIPiDIP-60163N.
    IntActiP20839. 12 interactors.
    MINTiMINT-2801694.
    STRINGi9606.ENSP00000345096.

    Chemistry databases

    BindingDBiP20839.

    Structurei

    Secondary structure

    1514
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi12 – 14Combined sources3
    Helixi20 – 23Combined sources4
    Beta strandi26 – 28Combined sources3
    Helixi32 – 34Combined sources3
    Beta strandi35 – 37Combined sources3
    Helixi46 – 48Combined sources3
    Beta strandi53 – 58Combined sources6
    Beta strandi60 – 63Combined sources4
    Beta strandi65 – 67Combined sources3
    Turni71 – 73Combined sources3
    Helixi76 – 84Combined sources9
    Beta strandi88 – 91Combined sources4
    Helixi97 – 108Combined sources12
    Beta strandi142 – 144Combined sources3
    Turni160 – 163Combined sources4
    Turni195 – 199Combined sources5
    Helixi200 – 204Combined sources5
    Beta strandi211 – 216Combined sources6
    Beta strandi247 – 250Combined sources4
    Helixi256 – 265Combined sources10
    Beta strandi269 – 273Combined sources5
    Helixi281 – 293Combined sources13
    Beta strandi298 – 304Combined sources7
    Helixi307 – 316Combined sources10
    Beta strandi319 – 323Combined sources5
    Helixi343 – 354Combined sources12
    Helixi355 – 357Combined sources3
    Beta strandi361 – 365Combined sources5
    Helixi370 – 378Combined sources9
    Beta strandi382 – 387Combined sources6
    Turni388 – 392Combined sources5
    Helixi453 – 471Combined sources19
    Helixi476 – 484Combined sources9
    Beta strandi490 – 492Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP20839.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini114 – 173CBS 1UniRule annotationAdd BLAST60
    Domaini179 – 237CBS 2UniRule annotationAdd BLAST59

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni364 – 366IMP binding3
    Regioni387 – 388IMP binding2
    Regioni411 – 415IMP bindingUniRule annotation5

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiENOG410ISZP. Eukaryota.
    COG0517. LUCA.
    GeneTreeiENSGT00530000062923.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    KOiK00088.
    OMAiDAMEKNN.
    OrthoDBiEOG091G0EAV.
    PhylomeDBiP20839.
    TreeFamiTF300378.

    Family and domain databases

    CDDicd00381. IMPDH. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH. 1 hit.
    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: PubMed:14702039 (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)DescriptionActionsGraphical viewLength
    Sequence conflicti29G → D in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti109K → N in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti273 – 274LD → FH in AAA36114 (PubMed:1969416).Curated2
    Sequence conflicti419A → P in AAA36114 (PubMed:1969416).Curated1
    Sequence conflicti497A → P in AAA36114 (PubMed:1969416).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065616105R → 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 Publication1
    Natural variantiVAR_065617116T → 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 Publication1
    Natural variantiVAR_065618198N → 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 Publication1
    Natural variantiVAR_017031224R → P in RP10. 1 Publication1
    Natural variantiVAR_017032226D → N in RP10. 2 Publications1
    Natural variantiVAR_017033268V → I in RP10. 2 Publications1
    Natural variantiVAR_065619285A → T.1 Publication1
    Natural variantiVAR_065620324G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. 1 Publication1
    Natural variantiVAR_065621372H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0469681 – 33MADYL…GLTYN → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRAS in isoform 7. CuratedAdd BLAST33
    Alternative sequenceiVSP_0143631M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3. 2 Publications1
    Alternative sequenceiVSP_0469691M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESCFLLELSSVVL LAGVGVQMDRLRRASM in isoform 5. 1 Publication1
    Alternative sequenceiVSP_0469701M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRASM in isoform 6. Curated1
    Alternative sequenceiVSP_00267484 – 108Missing in isoform 2. 1 PublicationAdd BLAST25
    Alternative sequenceiVSP_043485104 – 108Missing in isoform 4. 1 Publication5

    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_016867661.1. XM_017012172.1.
    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.3. human. [P20839-1]

    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_016867661.1. XM_017012172.1.
    UniGeneiHs.654401.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi109827. 79 interactors.
    DIPiDIP-60163N.
    IntActiP20839. 12 interactors.
    MINTiMINT-2801694.
    STRINGi9606.ENSP00000345096.

    Chemistry databases

    BindingDBiP20839.
    ChEMBLiCHEMBL1822.
    DrugBankiDB01033. Mercaptopurine.
    DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00811. Ribavirin.
    GuidetoPHARMACOLOGYi2624.

    PTM databases

    iPTMnetiP20839.
    PhosphoSitePlusiP20839.

    Polymorphism and mutation databases

    BioMutaiIMPDH1.
    DMDMi25014074.

    Proteomic databases

    EPDiP20839.
    MaxQBiP20839.
    PaxDbiP20839.
    PeptideAtlasiP20839.
    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.3. human. [P20839-1]

    Organism-specific databases

    CTDi3614.
    DisGeNETi3614.
    GeneCardsiIMPDH1.
    GeneReviewsiIMPDH1.
    HGNCiHGNC:6052. IMPDH1.
    HPAiHPA058375.
    MalaCardsiIMPDH1.
    MIMi146690. gene.
    180105. phenotype.
    613837. phenotype.
    neXtProtiNX_P20839.
    OpenTargetsiENSG00000106348.
    Orphaneti65. Leber congenital amaurosis.
    791. Retinitis pigmentosa.
    PharmGKBiPA29862.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410ISZP. Eukaryota.
    COG0517. LUCA.
    GeneTreeiENSGT00530000062923.
    HOGENOMiHOG000165752.
    HOVERGENiHBG052122.
    KOiK00088.
    OMAiDAMEKNN.
    OrthoDBiEOG091G0EAV.
    PhylomeDBiP20839.
    TreeFamiTF300378.

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.
    BioCyciMetaCyc:HS02896-MONOMER.
    ZFISH:HS02896-MONOMER.
    BRENDAi1.1.1.205. 2681.
    ReactomeiR-HSA-6798695. Neutrophil degranulation.
    R-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP20839.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000106348.
    CleanExiHS_IMPDH1.
    ExpressionAtlasiP20839. baseline and differential.
    GenevisibleiP20839. HS.

    Family and domain databases

    CDDicd00381. IMPDH. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH. 1 hit.
    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...

    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: November 30, 2016
    This is version 202 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

    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 one 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.