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P12268

- IMDH2_HUMAN

UniProt

P12268 - IMDH2_HUMAN

Protein

Inosine-5'-monophosphate dehydrogenase 2

Gene

IMPDH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (01 May 1991)
      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.

    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=9.3 µM for Inosine 5'-phosphate2 Publications
    2. KM=32 µM for NAD+2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi326 – 3261Potassium; via carbonyl oxygen1 PublicationUniRule annotation
    Metal bindingi328 – 3281Potassium; via carbonyl oxygen1 PublicationUniRule annotation
    Binding sitei329 – 3291IMPUniRule annotation
    Active sitei331 – 3311Thioimidate intermediate1 PublicationUniRule annotation
    Metal bindingi331 – 3311Potassium; via carbonyl oxygen1 PublicationUniRule 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 – 2763NAD
    Nucleotide bindingi324 – 3263NADUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. purine nucleobase metabolic process Source: Reactome
    4. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    5. 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:HS11242-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP12268.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 2UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 2UniRule annotation
    Short name:
    IMPD 2UniRule annotation
    Short name:
    IMPDH 2UniRule annotation
    Alternative name(s):
    IMPDH-II
    Gene namesi
    Name:IMPDH2UniRule annotation
    Synonyms:IMPD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6053. IMPDH2.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. peroxisomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29863.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 2PRO_0000093673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221Phosphoserine2 Publications
    Modified residuei400 – 4001Phosphotyrosine1 Publication
    Modified residuei416 – 4161Phosphoserine1 Publication
    Modified residuei511 – 5111N6-acetyllysine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP12268.
    PaxDbiP12268.
    PeptideAtlasiP12268.
    PRIDEiP12268.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00291510.
    P12268.
    UCD-2DPAGEP12268.

    PTM databases

    PhosphoSiteiP12268.

    Expressioni

    Tissue specificityi

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

    Inductioni

    Selectively up-regulated in neoplastic and replicating cells.

    Gene expression databases

    ArrayExpressiP12268.
    BgeeiP12268.
    CleanExiHS_IMPDH2.
    GenevestigatoriP12268.

    Organism-specific databases

    HPAiCAB020717.
    HPA001400.

    Interactioni

    Subunit structurei

    Homotetramer.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi109828. 35 interactions.
    IntActiP12268. 12 interactions.
    MINTiMINT-2860057.
    STRINGi9606.ENSP00000321584.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 193
    Helixi20 – 245
    Beta strandi25 – 273
    Helixi32 – 343
    Beta strandi35 – 373
    Helixi46 – 483
    Beta strandi53 – 586
    Beta strandi60 – 678
    Turni71 – 733
    Helixi77 – 859
    Beta strandi89 – 913
    Helixi97 – 10812
    Beta strandi112 – 1154
    Beta strandi147 – 1493
    Helixi161 – 1644
    Turni175 – 1773
    Beta strandi183 – 1853
    Helixi194 – 20310
    Beta strandi214 – 2163
    Beta strandi220 – 2223
    Beta strandi247 – 2504
    Helixi256 – 26510
    Beta strandi270 – 2734
    Helixi281 – 29313
    Beta strandi295 – 30410
    Helixi307 – 31610
    Beta strandi319 – 3235
    Beta strandi328 – 3314
    Helixi333 – 3364
    Helixi343 – 35412
    Helixi355 – 3573
    Beta strandi361 – 3655
    Helixi370 – 3789
    Beta strandi382 – 3876
    Helixi388 – 3903
    Beta strandi396 – 3983
    Beta strandi404 – 4063
    Beta strandi409 – 4124
    Turni417 – 4193
    Beta strandi444 – 4474
    Helixi453 – 47119
    Helixi476 – 4849
    Beta strandi490 – 4923
    Helixi495 – 5017

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B3OX-ray2.90A/B1-514[»]
    1NF7X-ray2.65A/B1-514[»]
    1NFBX-ray2.90A/B1-514[»]
    ProteinModelPortaliP12268.
    SMRiP12268. Positions 10-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12268.

    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.
    InParanoidiP12268.
    KOiK00088.
    OMAiFQAKARH.
    PhylomeDBiP12268.
    TreeFamiTF300378.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P12268-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD    50
    LTSALTKKIT LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ 100
    ANEVRKVKKY EQGFITDPVV LSPKDRVRDV FEAKARHGFC GIPITDTGRM 150
    GSRLVGIISS RDIDFLKEEE HDCFLEEIMT KREDLVVAPA GITLKEANEI 200
    LQRSKKGKLP IVNEDDELVA IIARTDLKKN RDYPLASKDA KKQLLCGAAI 250
    GTHEDDKYRL DLLAQAGVDV VVLDSSQGNS IFQINMIKYI KDKYPNLQVI 300
    GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV 350
    SEYARRFGVP VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY 400
    FFSDGIRLKK YRGMGSLDAM DKHLSSQNRY FSEADKIKVA QGVSGAVQDK 450
    GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR AMMYSGELKF EKRTSSAQVE 500
    GGVHSLHSYE KRLF 514
    Length:514
    Mass (Da):55,805
    Last modified:May 1, 1991 - v2
    Checksum:i876BEA0EC1DDBEE9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1912AG → RS in AAA36112. (PubMed:2902093)Curated

    Polymorphismi

    Genetic variants in the IMPDH2 gene may account for the large inter-individual variability in enzyme activity, immunosuppressive efficacy and side effects in transplant recipients receiving mycophenolic acid.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti263 – 2631L → F Found in transplant patients; functional polymorphism that results in 10-fold decrease of enzymatic activity. 1 Publication
    Corresponds to variant rs121434586 [ dbSNP | Ensembl ].
    VAR_070542

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04208 mRNA. Translation: AAA36112.1.
    L33842 Genomic DNA. Translation: AAA67054.1.
    L39210 Genomic DNA. Translation: AAB70699.1.
    BC006124 mRNA. Translation: AAH06124.1.
    BC012840 mRNA. Translation: AAH12840.1.
    BC015567 mRNA. Translation: AAH15567.1.
    L08114 Genomic DNA. Translation: AAA36113.1.
    CCDSiCCDS2786.1.
    PIRiI52303. A31997.
    RefSeqiNP_000875.2. NM_000884.2.
    UniGeneiHs.654400.

    Genome annotation databases

    EnsembliENST00000326739; ENSP00000321584; ENSG00000178035.
    GeneIDi3615.
    KEGGihsa:3615.
    UCSCiuc003cvt.3. human.

    Polymorphism databases

    DMDMi124419.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04208 mRNA. Translation: AAA36112.1 .
    L33842 Genomic DNA. Translation: AAA67054.1 .
    L39210 Genomic DNA. Translation: AAB70699.1 .
    BC006124 mRNA. Translation: AAH06124.1 .
    BC012840 mRNA. Translation: AAH12840.1 .
    BC015567 mRNA. Translation: AAH15567.1 .
    L08114 Genomic DNA. Translation: AAA36113.1 .
    CCDSi CCDS2786.1.
    PIRi I52303. A31997.
    RefSeqi NP_000875.2. NM_000884.2.
    UniGenei Hs.654400.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B3O X-ray 2.90 A/B 1-514 [» ]
    1NF7 X-ray 2.65 A/B 1-514 [» ]
    1NFB X-ray 2.90 A/B 1-514 [» ]
    ProteinModelPortali P12268.
    SMRi P12268. Positions 10-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109828. 35 interactions.
    IntActi P12268. 12 interactions.
    MINTi MINT-2860057.
    STRINGi 9606.ENSP00000321584.

    Chemistry

    BindingDBi P12268.
    ChEMBLi CHEMBL2111369.
    DrugBanki DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00157. NADH.
    GuidetoPHARMACOLOGYi 2625.

    PTM databases

    PhosphoSitei P12268.

    Polymorphism databases

    DMDMi 124419.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00291510.
    P12268.
    UCD-2DPAGE P12268.

    Proteomic databases

    MaxQBi P12268.
    PaxDbi P12268.
    PeptideAtlasi P12268.
    PRIDEi P12268.

    Protocols and materials databases

    DNASUi 3615.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326739 ; ENSP00000321584 ; ENSG00000178035 .
    GeneIDi 3615.
    KEGGi hsa:3615.
    UCSCi uc003cvt.3. human.

    Organism-specific databases

    CTDi 3615.
    GeneCardsi GC03M049061.
    HGNCi HGNC:6053. IMPDH2.
    HPAi CAB020717.
    HPA001400.
    MIMi 146691. gene.
    neXtProti NX_P12268.
    PharmGKBi PA29863.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165752.
    HOVERGENi HBG052122.
    InParanoidi P12268.
    KOi K00088.
    OMAi FQAKARH.
    PhylomeDBi P12268.
    TreeFami TF300378.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci MetaCyc:HS11242-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RK P12268.

    Miscellaneous databases

    ChiTaRSi IMPDH2. human.
    EvolutionaryTracei P12268.
    GeneWikii IMPDH2.
    GenomeRNAii 3615.
    NextBioi 14143.
    PROi P12268.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12268.
    Bgeei P12268.
    CleanExi HS_IMPDH2.
    Genevestigatori P12268.

    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. "Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs."
      Collart F.R., Huberman E.
      J. Biol. Chem. 263:15769-15772(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "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].
      Tissue: Spleen.
    3. "Cloning and sequence of the human type II IMP dehydrogenase gene."
      Glesne D.A., Huberman E.
      Biochem. Biophys. Res. Commun. 205:537-544(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    4. "Characterization of the human inosine-5'-monophosphate dehydrogenase type II gene."
      Zimmermann A.G., Spychala J., Mitchell B.S.
      J. Biol. Chem. 270:6808-6814(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
      Tissue: B-cell, Colon and Placenta.
    6. "Chromosomal localization and structure of the human type II IMP dehydrogenase gene."
      Glesne D.A., Collart F.R., Varkony T., Drabkin H., Huberman E.
      Genomics 16:274-277(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-514.
    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. "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: PROTEIN SEQUENCE OF N-TERMINUS, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "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.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity."
      Wang J., Zeevi A., Webber S., Girnita D.M., Addonizio L., Selby R., Hutchinson I.V., Burckart G.J.
      Pharmacogenet. Genomics 17:283-290(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM, VARIANT PHE-263.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-416, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design."
      Colby T.D., Vanderveen K., Strickler M.D., Markham G.D., Goldstein B.M.
      Proc. Natl. Acad. Sci. U.S.A. 96:3531-3536(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), ACTIVE SITE.
    19. "Crystal structure of human inosine monophosphate dehydrogenase type II complexed with the MPA/NAD analog C2-MAD."
      Risal D., Strickler M.D., Goldstein B.M.
      Submitted (DEC-2002) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND POTASSIUM.
    20. "The conformation of NAD bound to human inosine monophosphate Dehydrogenase Type II."
      Risal D., Strickler M.D., Goldstein B.M.
      Submitted (DEC-2002) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH NAD(+).

    Entry informationi

    Entry nameiIMDH2_HUMAN
    AccessioniPrimary (citable) accession number: P12268
    Secondary accession number(s): Q6LEF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 175 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 3
      Human chromosome 3: 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