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P20839

- IMDH1_HUMAN

UniProt

P20839 - IMDH1_HUMAN

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Protein

Inosine-5'-monophosphate dehydrogenase 1

Gene

IMPDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.1 PublicationUniRule annotation

Kineticsi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi328 – 3281Potassium; via carbonyl oxygenUniRule annotation
Binding sitei329 – 3291IMP
Active sitei331 – 3311Thioimidate intermediateUniRule annotation
Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
Binding sitei441 – 4411IMPUniRule annotation
Metal bindingi500 – 5001Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi501 – 5011Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi502 – 5021Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. lymphocyte proliferation Source: Ensembl
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. purine nucleobase metabolic process Source: Reactome
  5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
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.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP20839.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 1UniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenase 1UniRule annotation
Short name:
IMPD 1UniRule annotation
Short name:
IMPDH 1UniRule annotation
Alternative name(s):
IMPDH-I
Gene namesi
Name:IMPDH1UniRule annotation
Synonyms:IMPD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6052. IMPDH1.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 10 (RP10) [MIM:180105]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065617
Natural varianti224 – 2241R → P in RP10. 1 Publication
VAR_017031
Natural varianti226 – 2261D → N in RP10. 2 Publications
VAR_017032
Natural varianti268 – 2681V → I in RP10. 2 Publications
VAR_017033
Natural varianti372 – 3721H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065621
Leber congenital amaurosis 11 (LCA11) [MIM:613837]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065616
Natural varianti198 – 1981N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065618

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 1PRO_0000093670Add
BLAST

Proteomic databases

MaxQBiP20839.
PaxDbiP20839.
PRIDEiP20839.

PTM databases

PhosphoSiteiP20839.

Expressioni

Tissue specificityi

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

Inductioni

Constitutively expressed.

Gene expression databases

BgeeiP20839.
CleanExiHS_IMPDH1.
ExpressionAtlasiP20839. baseline and differential.
GenevestigatoriP20839.

Organism-specific databases

HPAiHPA001400.

Interactioni

Subunit structurei

Homotetramer.2 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi109827. 17 interactions.
DIPiDIP-60163N.
IntActiP20839. 3 interactions.
MINTiMINT-2801694.
STRINGi9606.ENSP00000345096.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Helixi20 – 234Combined sources
Beta strandi26 – 283Combined sources
Helixi32 – 343Combined sources
Beta strandi35 – 373Combined sources
Helixi46 – 483Combined sources
Beta strandi53 – 586Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 673Combined sources
Turni71 – 733Combined sources
Helixi76 – 849Combined sources
Beta strandi88 – 914Combined sources
Helixi97 – 10812Combined sources
Beta strandi142 – 1443Combined sources
Turni160 – 1634Combined sources
Turni195 – 1995Combined sources
Helixi200 – 2045Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi247 – 2504Combined sources
Helixi256 – 26510Combined sources
Beta strandi269 – 2735Combined sources
Helixi281 – 29313Combined sources
Beta strandi298 – 3047Combined sources
Helixi307 – 31610Combined sources
Beta strandi319 – 3235Combined sources
Helixi343 – 35412Combined sources
Helixi355 – 3573Combined sources
Beta strandi361 – 3655Combined sources
Helixi370 – 3789Combined sources
Beta strandi382 – 3876Combined sources
Turni388 – 3925Combined sources
Helixi453 – 47119Combined sources
Helixi476 – 4849Combined sources
Beta strandi490 – 4923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCNX-ray2.50A/B1-514[»]
ProteinModelPortaliP20839.
SMRiP20839. Positions 10-514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20839.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
KOiK00088.
OMAiHGHSKNI.
OrthoDBiEOG7VTDMM.
PhylomeDBiP20839.
TreeFamiTF300378.

Family and domain databases

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

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20839-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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: Ref.2 (BAG53840) sequence has a frameshift in position 35.

Show »
Length:589
Mass (Da):63,253
Checksum:i31E1ED04061B62F8
GO
Isoform 6 (identifier: P20839-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGPLTPPPL...QMDRLRRASM

Note: No experimental confirmation available.

Show »
Length:599
Mass (Da):64,320
Checksum:i7BED197A49991EA6
GO
Isoform 7 (identifier: P20839-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MADYLISGGTGYVPEDGLTAQQLFASADGLTYN → MEGPLTPPPL...VQMDRLRRAS

Show »
Length:566
Mass (Da):60,898
Checksum:iA10C18F253345FEA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291G → D in AAA36114. (PubMed:1969416)Curated
Sequence conflicti109 – 1091K → N in AAA36114. (PubMed:1969416)Curated
Sequence conflicti273 – 2742LD → FH in AAA36114. (PubMed:1969416)Curated
Sequence conflicti419 – 4191A → P in AAA36114. (PubMed:1969416)Curated
Sequence conflicti497 – 4971A → P in AAA36114. (PubMed:1969416)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051R → W in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065616
Natural varianti116 – 1161T → M in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065617
Natural varianti198 – 1981N → K in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065618
Natural varianti224 – 2241R → P in RP10. 1 Publication
VAR_017031
Natural varianti226 – 2261D → N in RP10. 2 Publications
VAR_017032
Natural varianti268 – 2681V → I in RP10. 2 Publications
VAR_017033
Natural varianti285 – 2851A → T.1 Publication
VAR_065619
Natural varianti324 – 3241G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. 1 Publication
VAR_065620
Natural varianti372 – 3721H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. 1 Publication
VAR_065621

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MADYL…GLTYN → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRAS in isoform 7. CuratedVSP_046968Add
BLAST
Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3. 2 PublicationsVSP_014363
Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESCFLLELSSVVL LAGVGVQMDRLRRASM in isoform 5. 1 PublicationVSP_046969
Alternative sequencei1 – 11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRASM in isoform 6. CuratedVSP_046970
Alternative sequencei84 – 10825Missing in isoform 2. 1 PublicationVSP_002674Add
BLAST
Alternative sequencei104 – 1085Missing in isoform 4. 1 PublicationVSP_043485

Sequence databases

Select the link destinations:
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_899066.1. NM_183243.2. [P20839-3]
XP_005250371.1. XM_005250314.1.
UniGeneiHs.654401.

Genome annotation databases

EnsembliENST00000338791; ENSP00000345096; ENSG00000106348. [P20839-6]
ENST00000348127; ENSP00000265385; ENSG00000106348. [P20839-3]
ENST00000354269; ENSP00000346219; ENSG00000106348. [P20839-5]
ENST00000419067; ENSP00000399400; ENSG00000106348. [P20839-7]
ENST00000480861; ENSP00000420185; ENSG00000106348. [P20839-4]
ENST00000496200; ENSP00000420803; ENSG00000106348. [P20839-2]
GeneIDi3614.
KEGGihsa:3614.
UCSCiuc003vmt.2. human. [P20839-2]
uc003vmv.2. human. [P20839-3]
uc003vmx.2. human.
uc011kol.1. human. [P20839-1]
uc011kom.1. human. [P20839-4]

Polymorphism databases

DMDMi25014074.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Mutations of the IMPDH1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
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.
CCDSi CCDS34748.1. [P20839-3 ]
CCDS34749.1. [P20839-6 ]
CCDS43643.1. [P20839-5 ]
CCDS47699.1. [P20839-7 ]
CCDS47700.1. [P20839-2 ]
CCDS55161.1. [P20839-4 ]
PIRi A35566.
RefSeqi NP_000874.2. NM_000883.3. [P20839-6 ]
NP_001096075.1. NM_001102605.1. [P20839-5 ]
NP_001136045.1. NM_001142573.1. [P20839-1 ]
NP_001136046.1. NM_001142574.1. [P20839-4 ]
NP_001136047.1. NM_001142575.1. [P20839-2 ]
NP_001136048.1. NM_001142576.1. [P20839-7 ]
NP_899066.1. NM_183243.2. [P20839-3 ]
XP_005250371.1. XM_005250314.1.
UniGenei Hs.654401.

3D structure databases

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

Protein-protein interaction databases

BioGridi 109827. 17 interactions.
DIPi DIP-60163N.
IntActi P20839. 3 interactions.
MINTi MINT-2801694.
STRINGi 9606.ENSP00000345096.

Chemistry

BindingDBi P20839.
ChEMBLi CHEMBL2111369.
DrugBanki DB01033. Mercaptopurine.
DB00688. Mycophenolate mofetil.
DB01024. Mycophenolic acid.
DB00811. Ribavirin.
GuidetoPHARMACOLOGYi 2624.

PTM databases

PhosphoSitei P20839.

Polymorphism databases

DMDMi 25014074.

Proteomic databases

MaxQBi P20839.
PaxDbi P20839.
PRIDEi P20839.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338791 ; ENSP00000345096 ; ENSG00000106348 . [P20839-6 ]
ENST00000348127 ; ENSP00000265385 ; ENSG00000106348 . [P20839-3 ]
ENST00000354269 ; ENSP00000346219 ; ENSG00000106348 . [P20839-5 ]
ENST00000419067 ; ENSP00000399400 ; ENSG00000106348 . [P20839-7 ]
ENST00000480861 ; ENSP00000420185 ; ENSG00000106348 . [P20839-4 ]
ENST00000496200 ; ENSP00000420803 ; ENSG00000106348 . [P20839-2 ]
GeneIDi 3614.
KEGGi hsa:3614.
UCSCi uc003vmt.2. human. [P20839-2 ]
uc003vmv.2. human. [P20839-3 ]
uc003vmx.2. human.
uc011kol.1. human. [P20839-1 ]
uc011kom.1. human. [P20839-4 ]

Organism-specific databases

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

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00530000062923.
HOGENOMi HOG000165752.
HOVERGENi HBG052122.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG7VTDMM.
PhylomeDBi P20839.
TreeFami TF300378.

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

Bgeei P20839.
CleanExi HS_IMPDH1.
ExpressionAtlasi P20839. baseline and differential.
Genevestigatori P20839.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two distinct cDNAs for human IMP dehydrogenase."
    Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.
    J. Biol. Chem. 265:5292-5295(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Spleen.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
    Tissue: Brain.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Blood.
  7. "Characterization of human type I and type II IMP dehydrogenases."
    Carr S.F., Papp E., Wu J.C., Natsumeda Y.
    J. Biol. Chem. 268:27286-27290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
  8. "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes."
    Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., Stuve L.L.
    Genomics 83:566-571(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
  9. "Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding."
    Hager P.W., Collart F.R., Huberman E., Mitchell B.S.
    Biochem. Pharmacol. 49:1323-1329(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo."
    McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M., Hedstrom L.
    Biochem. J. 379:243-251(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEIC ACID-BINDING.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Crystal structure of the human type I inosine monophosphate dehydrogenase and implications for isoform specificity."
    Risal D., Strickler M.D., Goldstein B.M.
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
  13. "Identification of an IMPDH1 mutation in autosomal dominant retinitis pigmentosa (RP10) revealed following comparative microarray analysis of transcripts derived from retinas of wild-type and Rho(-/-) mice."
    Kennan A., Aherne A., Palfi A., Humphries M., McKee A., Stitt A., Simpson D.A., Demtroder K., Orntoft T., Ayuso C., Kenna P.F., Farrar G.J., Humphries P.
    Hum. Mol. Genet. 11:547-557(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP10 PRO-224.
  14. "Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa."
    Bowne S.J., Sullivan L.S., Blanton S.H., Cepko C.L., Blackshaw S., Birch D.G., Hughbanks-Wheaton D., Heckenlively J.R., Daiger S.P.
    Hum. Mol. Genet. 11:559-568(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP10 ASN-226 AND ILE-268.
  15. "Spectrum and frequency of mutations in IMPDH1 associated with autosomal dominant retinitis pigmentosa and Leber congenital amaurosis."
    Bowne S.J., Sullivan L.S., Mortimer S.E., Hedstrom L., Zhu J., Spellicy C.J., Gire A.I., Hughbanks-Wheaton D., Birch D.G., Lewis R.A., Heckenlively J.R., Daiger S.P.
    Invest. Ophthalmol. Vis. Sci. 47:34-42(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP10 MET-116; ASN-226; ILE-268 AND PRO-372, VARIANTS LCA11 TRP-105 AND LYS-198, VARIANTS THR-285 AND ASP-324, CHARACTERIZATION OF VARIANTS RP10 MET-116 AND PRO-372, CHARACTERIZATION OF VARIANTS LCA11 TRP-105 AND LYS-198, CHARACTERIZATION OF VARIANT ASP-324.

Entry informationi

Entry nameiIMDH1_HUMAN
AccessioniPrimary (citable) accession number: P20839
Secondary accession number(s): A4D0Z6
, A4D0Z7, A6NDW5, A6NNI6, B3KNP7, B3KVM8, B4DE09, C9JV30, J3KNX8, Q8N194, Q96NU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 8, 2002
Last modified: November 26, 2014
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Because IMPDH activity is tightly linked with cell proliferation, it has been recognized as a target for cancer and viral chemotherapy and as a target for immunosuppressive drugs. The activities of the antitumor drug tiazofurin, the antiviral drug ribavirin, and the immunosuppressive drugs mizoribine and mycophenolic acid (MPA) are attributed to the inhibition of IMPDH. In addition, bacterial and parasitic IMPDH's differ significantly from mammalian enzymes, which makes it a suitable target for anti-infective drugs.

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3