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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

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.

Catalytic activityi

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

Cofactori

K+UniRule annotation

Activity 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 1 (IMPDH1), Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2), Inosine-5'-monophosphate dehydrogenase (guaB), Inosine-5'-monophosphate dehydrogenase (DKFZp781N0678), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (IMPDH1), Inosine-5'-monophosphate dehydrogenase (IMPDH)
    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

    GO - Biological processi

    Keywordsi

    Molecular functionDNA-binding, Oxidoreductase, RNA-binding
    Biological processGMP biosynthesis, Purine biosynthesis
    LigandMetal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02896-MONOMER
    BRENDAi1.1.1.205 2681
    ReactomeiR-HSA-6798695 Neutrophil degranulation
    R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
    SABIO-RKiP20839
    UniPathwayi
    UPA00601;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

    EuPathDBiHostDB:ENSG00000106348.16
    HGNCiHGNC:6052 IMPDH1
    MIMi146690 gene
    neXtProtiNX_P20839

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    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
    GeneReviewsiIMPDH1
    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
    DB00157 NADH
    DB00811 Ribavirin
    DB06103 VX-148
    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
    ProteomicsDBi53811
    53812 [P20839-2]
    53813 [P20839-3]
    53814 [P20839-4]

    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 Expressed in 205 organ(s), highest expression level in blood
    CleanExiHS_IMPDH1
    ExpressionAtlasiP20839 baseline and differential
    GenevisibleiP20839 HS

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi109827, 89 interactors
    DIPiDIP-60163N
    IntActiP20839, 18 interactors
    STRINGi9606.ENSP00000345096

    Chemistry databases

    BindingDBiP20839

    Structurei

    Secondary structure

    1514
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiENOG410ISZP Eukaryota
    COG0517 LUCA
    GeneTreeiENSGT00530000062923
    HOGENOMiHOG000165752
    HOVERGENiHBG052122
    KOiK00088
    OMAiSSMGYCG
    OrthoDBiEOG091G0EAV
    PhylomeDBiP20839
    TreeFamiTF300378

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    Gene3Di3.20.20.70, 2 hits
    HAMAPiMF_01964 IMPDH, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt
    PfamiView protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit
    PIRSFiPIRSF000130 IMPDH, 1 hit
    SMARTiView protein in SMART
    SM00116 CBS, 2 hits
    TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
    PROSITEiView protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit

    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

    This entry has 7 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

    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

    Computationally mapped potential isoform sequencesi

    There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9J381C9J381_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1 IMPDH
    513Annotation score:
    C9K0R9C9K0R9_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    289Annotation score:
    H7C511H7C511_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    226Annotation score:
    C9J029C9J029_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    184Annotation score:
    H7C5T1H7C5T1_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    190Annotation score:
    F8WDE9F8WDE9_HUMAN
    Inosine-5'-monophosphate dehydrogen...
    IMPDH1
    69Annotation score:

    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 → T1 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

    Similar proteinsi

    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, 89 interactors
    DIPiDIP-60163N
    IntActiP20839, 18 interactors
    STRINGi9606.ENSP00000345096

    Chemistry databases

    BindingDBiP20839
    ChEMBLiCHEMBL1822
    DrugBankiDB01033 Mercaptopurine
    DB00688 Mycophenolate mofetil
    DB01024 Mycophenolic acid
    DB00157 NADH
    DB00811 Ribavirin
    DB06103 VX-148
    GuidetoPHARMACOLOGYi2624

    PTM databases

    iPTMnetiP20839
    PhosphoSitePlusiP20839

    Polymorphism and mutation databases

    BioMutaiIMPDH1
    DMDMi25014074

    Proteomic databases

    EPDiP20839
    MaxQBiP20839
    PaxDbiP20839
    PeptideAtlasiP20839
    PRIDEiP20839
    ProteomicsDBi53811
    53812 [P20839-2]
    53813 [P20839-3]
    53814 [P20839-4]

    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
    EuPathDBiHostDB:ENSG00000106348.16
    GeneCardsiIMPDH1
    GeneReviewsiIMPDH1
    HGNCiHGNC:6052 IMPDH1
    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
    OMAiSSMGYCG
    OrthoDBiEOG091G0EAV
    PhylomeDBiP20839
    TreeFamiTF300378

    Enzyme and pathway databases

    UniPathwayi
    UPA00601;UER00295

    BioCyciMetaCyc:HS02896-MONOMER
    BRENDAi1.1.1.205 2681
    ReactomeiR-HSA-6798695 Neutrophil degranulation
    R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
    SABIO-RKiP20839

    Miscellaneous databases

    ChiTaRSiIMPDH1 human
    EvolutionaryTraceiP20839
    GeneWikiiIMPDH1
    GenomeRNAii3614
    PROiPR:P20839
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000106348 Expressed in 205 organ(s), highest expression level in blood
    CleanExiHS_IMPDH1
    ExpressionAtlasiP20839 baseline and differential
    GenevisibleiP20839 HS

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    Gene3Di3.20.20.70, 2 hits
    HAMAPiMF_01964 IMPDH, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt
    PfamiView protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit
    PIRSFiPIRSF000130 IMPDH, 1 hit
    SMARTiView protein in SMART
    SM00116 CBS, 2 hits
    TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
    PROSITEiView protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit
    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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 8, 2002
    Last modified: November 7, 2018
    This is version 213 of the entry and version 2 of the sequence. See 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

    Keywords - Technical termi

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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    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. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
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