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P20839 (IMDH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase 1

Short name=IMP dehydrogenase 1
Short name=IMPD 1
Short name=IMPDH 1
EC=1.1.1.205
Alternative name(s):
IMPDH-I
Gene names
Name:IMPDH1
Synonyms:IMPD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03156

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_03156

Cofactor

Potassium By similarity. HAMAP-Rule MF_03156

Enzyme regulation

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. Ref.7

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_03156

Subunit structure

Homotetramer. Ref.7

Subcellular location

Cytoplasm. Nucleus Ref.10.

Tissue specificity

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

Induction

Constitutively expressed. Ref.7

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

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.

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Biophysicochemical properties

Kinetic parameters:

KM=18 µM for Inosine 5'-phosphate Ref.7 Ref.9

KM=46 µM for NAD+

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Leber congenital amaurosis
Retinitis pigmentosa
   DomainCBS domain
Repeat
   LigandDNA-binding
Metal-binding
NAD
Potassium
RNA-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

lymphocyte proliferation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

IMP dehydrogenase activity

Traceable author statement Ref.1. Source: ProtInc

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20839-1)

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.
Isoform 2 (identifier: P20839-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-108: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P20839-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESM
Isoform 4 (identifier: P20839-4)

The sequence of this isoform differs from the canonical sequence as follows:
     104-108: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P20839-5)

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.
Isoform 6 (identifier: P20839-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGPLTPPPL...QMDRLRRASM
Note: No experimental confirmation available.
Isoform 7 (identifier: P20839-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 514513Inosine-5'-monophosphate dehydrogenase 1 HAMAP-Rule MF_03156
PRO_0000093670

Regions

Domain114 – 17360CBS 1
Domain179 – 23759CBS 2
Nucleotide binding274 – 2763NAD By similarity
Nucleotide binding324 – 3263NAD By similarity
Region364 – 3663IMP binding HAMAP-Rule MF_03156
Region387 – 3882IMP binding HAMAP-Rule MF_03156
Region411 – 4155IMP binding By similarity

Sites

Active site3311Thioimidate intermediate By similarity
Metal binding3261Potassium; via carbonyl oxygen By similarity
Metal binding3281Potassium; via carbonyl oxygen By similarity
Metal binding3311Potassium; via carbonyl oxygen By similarity
Metal binding5001Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5011Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site3291IMP
Binding site4411IMP By similarity

Natural variations

Alternative sequence1 – 3333MADYL…GLTYN → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRAS in isoform 7.
VSP_046968
Alternative sequence11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESM in isoform 3.
VSP_014363
Alternative sequence11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESCFLLELSSVVL LAGVGVQMDRLRRASM in isoform 5.
VSP_046969
Alternative sequence11M → MEGPLTPPPLQGGGAAAVPE PGARQHPGHETAAQRYSARL LQAGYEPESPRLDLATHPTT PRSELSSVVLLAGVGVQMDR LRRASM in isoform 6.
VSP_046970
Alternative sequence84 – 10825Missing in isoform 2.
VSP_002674
Alternative sequence104 – 1085Missing in isoform 4.
VSP_043485
Natural variant1051R → 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. Ref.15
VAR_065616
Natural variant1161T → 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. Ref.15
VAR_065617
Natural variant1981N → 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. Ref.15
VAR_065618
Natural variant2241R → P in RP10. Ref.13
VAR_017031
Natural variant2261D → N in RP10. Ref.14 Ref.15
VAR_017032
Natural variant2681V → I in RP10. Ref.14 Ref.15
VAR_017033
Natural variant2851A → T. Ref.15
VAR_065619
Natural variant3241G → D Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid. Ref.15
VAR_065620
Natural variant3721H → P in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid. Ref.15
VAR_065621

Experimental info

Sequence conflict291G → D in AAA36114. Ref.1
Sequence conflict1091K → N in AAA36114. Ref.1
Sequence conflict273 – 2742LD → FH in AAA36114. Ref.1
Sequence conflict4191A → P in AAA36114. Ref.1
Sequence conflict4971A → P in AAA36114. Ref.1

Secondary structure

................................................................. 514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: ABAC654A9091BE62

FASTA51455,406
        10         20         30         40         50         60 
MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT 

        70         80         90        100        110        120 
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV 

       130        140        150        160        170        180 
LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT 

       190        200        210        220        230        240 
PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS 

       250        260        270        280        290        300 
QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 

       310        320        330        340        350        360 
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP 

       370        380        390        400        410        420 
IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM 

       430        440        450        460        470        480 
EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR 

       490        500        510 
SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY 

« Hide

Isoform 2 [UniParc].

Checksum: 47A1273662A8C39B
Show »

FASTA48952,598
Isoform 3 [UniParc].

Checksum: EB370370B77CD0DA
Show »

FASTA56360,437
Isoform 4 [UniParc].

Checksum: 83819A210AAAB3CA
Show »

FASTA50954,795
Isoform 5 [UniParc].

Checksum: 31E1ED04061B62F8
Show »

FASTA58963,253
Isoform 6 [UniParc].

Checksum: 7BED197A49991EA6
Show »

FASTA59964,320
Isoform 7 [UniParc].

Checksum: A10C18F253345FEA
Show »

FASTA56660,898

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Mutations of the IMPDH1 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35566.
RefSeqNP_000874.2. NM_000883.3.
NP_001096075.1. NM_001102605.1.
NP_001136045.1. NM_001142573.1.
NP_001136046.1. NM_001142574.1.
NP_001136047.1. NM_001142575.1.
NP_001136048.1. NM_001142576.1.
NP_899066.1. NM_183243.2.
XP_005250371.1. XM_005250314.1.
UniGeneHs.654401.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCNX-ray2.50A/B1-514[»]
ProteinModelPortalP20839.
SMRP20839. Positions 10-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109827. 8 interactions.
DIPDIP-60163N.
IntActP20839. 3 interactions.
MINTMINT-2801694.
STRING9606.ENSP00000345096.

Chemistry

BindingDBP20839.
ChEMBLCHEMBL1822.
DrugBankDB00688. Mycophenolate mofetil.
DB01024. Mycophenolic acid.
DB00157. NADH.
DB00811. Ribavirin.
DB00352. Thioguanine.
GuidetoPHARMACOLOGY2624.

PTM databases

PhosphoSiteP20839.

Polymorphism databases

DMDM25014074.

Proteomic databases

PaxDbP20839.
PRIDEP20839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338791; ENSP00000345096; ENSG00000106348. [P20839-6]
ENST00000343214; ENSP00000342438; ENSG00000106348. [P20839-2]
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]
GeneID3614.
KEGGhsa:3614.
UCSCuc003vmt.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

CTD3614.
GeneCardsGC07M128032.
HGNCHGNC:6052. IMPDH1.
HPAHPA001400.
MIM146690. gene.
180105. phenotype.
613837. phenotype.
neXtProtNX_P20839.
Orphanet65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
PharmGKBPA29862.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165752.
HOVERGENHBG052122.
InParanoidP20839.
KOK00088.
OMASSMGYCG.
OrthoDBEOG7VTDMM.
PhylomeDBP20839.
TreeFamTF300378.

Enzyme and pathway databases

BioCycMetaCyc:HS02896-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP20839.
UniPathwayUPA00601; UER00295.

Gene expression databases

ArrayExpressP20839.
BgeeP20839.
CleanExHS_IMPDH1.
GenevestigatorP20839.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIMPDH1. human.
EvolutionaryTraceP20839.
GeneWikiIMPDH1.
GenomeRNAi3614.
NextBio14135.
PROP20839.
SOURCESearch...

Entry information

Entry nameIMDH1_HUMAN
AccessionPrimary (citable) accession number: P20839
Secondary accession number(s): A4D0Z6 expand/collapse secondary AC list , A4D0Z7, A6NDW5, A6NNI6, B3KNP7, B3KVM8, B4DE09, C9JV30, J3KNX8, Q8N194, Q96NU2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 8, 2002
Last modified: April 16, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM