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P12268

- IMDH2_HUMAN

UniProt

P12268 - IMDH2_HUMAN

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Protein

Inosine-5'-monophosphate dehydrogenase 2

Gene
IMPDH2, IMPD2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

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 Publication

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Potassium; via carbonyl oxygen
Metal bindingi328 – 3281Potassium; via carbonyl oxygen
Binding sitei329 – 3291IMP By similarity
Active sitei331 – 3311Thioimidate intermediate1 Publication
Metal bindingi331 – 3311Potassium; via carbonyl oxygen
Binding sitei441 – 4411IMP By similarity
Metal bindingi500 – 5001Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2763NADUniRule annotation
Nucleotide bindingi324 – 3263NAD By similarity

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
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:HS11242-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP12268.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 2 (EC:1.1.1.205)
Short name:
IMP dehydrogenase 2
Short name:
IMPD 2
Short name:
IMPDH 2
Alternative name(s):
IMPDH-II
Gene namesi
Name:IMPDH2
Synonyms:IMPD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6053. IMPDH2.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29863.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 2UniRule annotationPRO_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.UniRule annotation

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.1 Publication

Gene expression databases

ArrayExpressiP12268.
BgeeiP12268.
CleanExiHS_IMPDH2.
GenevestigatoriP12268.

Organism-specific databases

HPAiCAB020717.
HPA001400.

Interactioni

Subunit structurei

Homotetramer.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP12268.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 17360CBS 1Add
BLAST
Domaini179 – 23759CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663IMP bindingUniRule annotation
Regioni387 – 3882IMP bindingUniRule annotation
Regioni411 – 4155IMP binding By similarity

Sequence similaritiesi

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

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

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.UniRule annotation

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1912AG → RS in AAA36112. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 174 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

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