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Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (IMPDH-I)

 IMDH1_HUMAN             Reviewed;         514 AA.
P20839; A4D0Z6; A4D0Z7; A6NDW5; A6NNI6; B3KNP7; B3KVM8; B4DE09;
C9JV30; J3KNX8; Q8N194; Q96NU2;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
08-NOV-2002, sequence version 2.
18-JUL-2018, entry version 210.
RecName: Full=Inosine-5'-monophosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMP dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPD 1 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPDH 1 {ECO:0000255|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156};
AltName: Full=IMPDH-I;
Name=IMPDH1 {ECO:0000255|HAMAP-Rule:MF_03156}; Synonyms=IMPD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=1969416;
Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.;
"Two distinct cDNAs for human IMP dehydrogenase.";
J. Biol. Chem. 265:5292-5295(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
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.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
ENZYME REGULATION.
PubMed=7903306;
Carr S.F., Papp E., Wu J.C., Natsumeda Y.;
"Characterization of human type I and type II IMP dehydrogenases.";
J. Biol. Chem. 268:27286-27290(1993).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R.,
Au-Young J., Stuve L.L.;
"PCR isolation and cloning of novel splice variant mRNAs from known
drug target genes.";
Genomics 83:566-571(2004).
[9]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7763314; DOI=10.1016/0006-2952(95)00026-V;
Hager P.W., Collart F.R., Huberman E., Mitchell B.S.;
"Recombinant human inosine monophosphate dehydrogenase type I and type
II proteins. Purification and characterization of inhibitor binding.";
Biochem. Pharmacol. 49:1323-1329(1995).
[10]
SUBCELLULAR LOCATION, AND NUCLEIC ACID-BINDING.
PubMed=14766016; DOI=10.1042/BJ20031585;
McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M.,
Hedstrom L.;
"Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro
and in vivo.";
Biochem. J. 379:243-251(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG.
Risal D., Strickler M.D., Goldstein B.M.;
"Crystal structure of the human type I inosine monophosphate
dehydrogenase and implications for isoform specificity.";
Submitted (FEB-2009) to the PDB data bank.
[14]
VARIANT RP10 PRO-224.
PubMed=11875049; DOI=10.1093/hmg/11.5.547;
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.;
"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.";
Hum. Mol. Genet. 11:547-557(2002).
[15]
VARIANTS RP10 ASN-226 AND ILE-268.
PubMed=11875050; DOI=10.1093/hmg/11.5.559;
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.;
"Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1)
cause the RP10 form of autosomal dominant retinitis pigmentosa.";
Hum. Mol. Genet. 11:559-568(2002).
[16]
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, AND CHARACTERIZATION OF VARIANT ASP-324.
PubMed=16384941; DOI=10.1167/iovs.05-0868;
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.;
"Spectrum and frequency of mutations in IMPDH1 associated with
autosomal dominant retinitis pigmentosa and Leber congenital
amaurosis.";
Invest. Ophthalmol. Vis. Sci. 47:34-42(2006).
-!- 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.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:7903306}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:7763314,
ECO:0000269|PubMed:7903306};
KM=46 uM for NAD(+) {ECO:0000269|PubMed:7763314,
ECO:0000269|PubMed:7903306};
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:7903306, ECO:0000269|Ref.13}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000255|HAMAP-
Rule:MF_03156, ECO:0000269|PubMed:14766016}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=P20839-1; Sequence=Displayed;
Name=2;
IsoId=P20839-2; Sequence=VSP_002674;
Note=No experimental confirmation available.;
Name=3;
IsoId=P20839-3; Sequence=VSP_014363;
Name=4;
IsoId=P20839-4; Sequence=VSP_043485;
Note=No experimental confirmation available.;
Name=5;
IsoId=P20839-5; Sequence=VSP_046969;
Note=Ref.2 (BAG53840) sequence has a frameshift in position 35.;
Name=6;
IsoId=P20839-6; Sequence=VSP_046970;
Note=No experimental confirmation available.;
Name=7;
IsoId=P20839-7; Sequence=VSP_046968;
-!- 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.
-!- 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. {ECO:0000269|PubMed:11875049,
ECO:0000269|PubMed:11875050, ECO:0000269|PubMed:16384941}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:16384941}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_03156}.
-!- WEB RESOURCE: Name=Mutations of the IMPDH1 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/impdhmut.htm";
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EMBL; J05272; AAA36114.1; -; mRNA.
EMBL; AK054640; BAB70780.1; -; mRNA.
EMBL; AK054667; BAG51409.1; -; mRNA.
EMBL; AK122994; BAG53840.1; ALT_FRAME; mRNA.
EMBL; AK293413; BAG56920.1; -; mRNA.
EMBL; AC010655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236947; EAL24310.1; -; Genomic_DNA.
EMBL; CH236947; EAL24311.1; -; Genomic_DNA.
EMBL; CH471070; EAW83652.1; -; Genomic_DNA.
EMBL; BC033622; AAH33622.2; -; mRNA.
EMBL; CD014008; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS34748.1; -. [P20839-3]
CCDS; CCDS34749.1; -. [P20839-6]
CCDS; CCDS43643.1; -. [P20839-5]
CCDS; CCDS47699.1; -. [P20839-7]
CCDS; CCDS47700.1; -. [P20839-2]
CCDS; CCDS55161.1; -. [P20839-4]
PIR; A35566; A35566.
RefSeq; NP_000874.2; NM_000883.3. [P20839-6]
RefSeq; NP_001096075.1; NM_001102605.1. [P20839-5]
RefSeq; NP_001136045.1; NM_001142573.1. [P20839-1]
RefSeq; NP_001136046.1; NM_001142574.1. [P20839-4]
RefSeq; NP_001136047.1; NM_001142575.1. [P20839-2]
RefSeq; NP_001136048.1; NM_001142576.1. [P20839-7]
RefSeq; NP_001291450.1; NM_001304521.1.
RefSeq; NP_899066.1; NM_183243.2. [P20839-3]
RefSeq; XP_016867661.1; XM_017012172.1.
UniGene; Hs.654401; -.
PDB; 1JCN; X-ray; 2.50 A; A/B=1-514.
PDBsum; 1JCN; -.
ProteinModelPortal; P20839; -.
SMR; P20839; -.
BioGrid; 109827; 89.
DIP; DIP-60163N; -.
IntAct; P20839; 18.
STRING; 9606.ENSP00000345096; -.
BindingDB; P20839; -.
ChEMBL; CHEMBL1822; -.
DrugBank; DB01033; Mercaptopurine.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB01024; Mycophenolic acid.
DrugBank; DB00157; NADH.
DrugBank; DB00811; Ribavirin.
DrugBank; DB06103; VX-148.
GuidetoPHARMACOLOGY; 2624; -.
iPTMnet; P20839; -.
PhosphoSitePlus; P20839; -.
BioMuta; IMPDH1; -.
DMDM; 25014074; -.
EPD; P20839; -.
MaxQB; P20839; -.
PaxDb; P20839; -.
PeptideAtlas; P20839; -.
PRIDE; P20839; -.
ProteomicsDB; 53811; -.
ProteomicsDB; 53812; -. [P20839-2]
ProteomicsDB; 53813; -. [P20839-3]
ProteomicsDB; 53814; -. [P20839-4]
Ensembl; ENST00000338791; ENSP00000345096; ENSG00000106348. [P20839-6]
Ensembl; ENST00000348127; ENSP00000265385; ENSG00000106348. [P20839-3]
Ensembl; ENST00000354269; ENSP00000346219; ENSG00000106348. [P20839-5]
Ensembl; ENST00000419067; ENSP00000399400; ENSG00000106348. [P20839-7]
Ensembl; ENST00000480861; ENSP00000420185; ENSG00000106348. [P20839-4]
Ensembl; ENST00000496200; ENSP00000420803; ENSG00000106348. [P20839-2]
GeneID; 3614; -.
KEGG; hsa:3614; -.
UCSC; uc003vmt.3; human. [P20839-1]
CTD; 3614; -.
DisGeNET; 3614; -.
EuPathDB; HostDB:ENSG00000106348.16; -.
GeneCards; IMPDH1; -.
GeneReviews; IMPDH1; -.
HGNC; HGNC:6052; IMPDH1.
MalaCards; IMPDH1; -.
MIM; 146690; gene.
MIM; 180105; phenotype.
MIM; 613837; phenotype.
neXtProt; NX_P20839; -.
OpenTargets; ENSG00000106348; -.
Orphanet; 65; Leber congenital amaurosis.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA29862; -.
eggNOG; ENOG410ISZP; Eukaryota.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00530000062923; -.
HOGENOM; HOG000165752; -.
HOVERGEN; HBG052122; -.
KO; K00088; -.
OMA; GIGIVHK; -.
OrthoDB; EOG091G0EAV; -.
PhylomeDB; P20839; -.
TreeFam; TF300378; -.
BioCyc; MetaCyc:HS02896-MONOMER; -.
BRENDA; 1.1.1.205; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK; P20839; -.
UniPathway; UPA00601; UER00295.
ChiTaRS; IMPDH1; human.
EvolutionaryTrace; P20839; -.
GeneWiki; IMPDH1; -.
GenomeRNAi; 3614; -.
PRO; PR:P20839; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106348; -.
CleanEx; HS_IMPDH1; -.
ExpressionAtlas; P20839; baseline and differential.
Genevisible; P20839; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003938; F:IMP dehydrogenase activity; EXP:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
GO; GO:0046651; P:lymphocyte proliferation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 2.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; CBS domain; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; DNA-binding;
GMP biosynthesis; Leber congenital amaurosis; Metal-binding;
Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein; Potassium;
Purine biosynthesis; Reference proteome; Repeat; Retinitis pigmentosa;
RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03156,
ECO:0000269|PubMed:7903306}.
CHAIN 2 514 Inosine-5'-monophosphate dehydrogenase 1.
/FTId=PRO_0000093670.
DOMAIN 114 173 CBS 1. {ECO:0000255|HAMAP-Rule:MF_03156}.
DOMAIN 179 237 CBS 2. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 274 276 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 324 326 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
REGION 364 366 IMP binding.
REGION 387 388 IMP binding.
REGION 411 415 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
ACT_SITE 331 331 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_03156}.
ACT_SITE 429 429 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03156}.
METAL 326 326 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 328 328 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 331 331 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 500 500 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 501 501 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 502 502 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 329 329 IMP.
BINDING 441 441 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 341 341 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P50096}.
MOD_RES 355 355 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P50096}.
VAR_SEQ 1 33 MADYLISGGTGYVPEDGLTAQQLFASADGLTYN -> MEGP
LTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGY
EPESPRLDLATHPTTPRSELSSVVLLAGVGVQMDRLRRAS
(in isoform 7). {ECO:0000305}.
/FTId=VSP_046968.
VAR_SEQ 1 1 M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRY
SARLLQAGYEPESM (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_014363.
VAR_SEQ 1 1 M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRY
SARLLQAGYEPESCFLLELSSVVLLAGVGVQMDRLRRASM
(in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046969.
VAR_SEQ 1 1 M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRY
SARLLQAGYEPESPRLDLATHPTTPRSELSSVVLLAGVGVQ
MDRLRRASM (in isoform 6). {ECO:0000305}.
/FTId=VSP_046970.
VAR_SEQ 84 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002674.
VAR_SEQ 104 108 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043485.
VARIANT 105 105 R -> 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). {ECO:0000269|PubMed:16384941}.
/FTId=VAR_065616.
VARIANT 116 116 T -> 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). {ECO:0000269|PubMed:16384941}.
/FTId=VAR_065617.
VARIANT 198 198 N -> 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). {ECO:0000269|PubMed:16384941}.
/FTId=VAR_065618.
VARIANT 224 224 R -> P (in RP10).
{ECO:0000269|PubMed:11875049}.
/FTId=VAR_017031.
VARIANT 226 226 D -> N (in RP10).
{ECO:0000269|PubMed:11875050,
ECO:0000269|PubMed:16384941}.
/FTId=VAR_017032.
VARIANT 268 268 V -> I (in RP10).
{ECO:0000269|PubMed:11875050,
ECO:0000269|PubMed:16384941}.
/FTId=VAR_017033.
VARIANT 285 285 A -> T. {ECO:0000269|PubMed:16384941}.
/FTId=VAR_065619.
VARIANT 324 324 G -> D (does not alter the enzymatic
affinity of the corresponding enzyme;
does not affect the affinity for single-
stranded nucleic acid).
{ECO:0000269|PubMed:16384941}.
/FTId=VAR_065620.
VARIANT 372 372 H -> P (in RP10; alters the affinity and/
or the specificity of single-stranded
nucleic acid).
{ECO:0000269|PubMed:16384941}.
/FTId=VAR_065621.
CONFLICT 29 29 G -> D (in Ref. 1; AAA36114).
{ECO:0000305}.
CONFLICT 109 109 K -> N (in Ref. 1; AAA36114).
{ECO:0000305}.
CONFLICT 273 274 LD -> FH (in Ref. 1; AAA36114).
{ECO:0000305}.
CONFLICT 419 419 A -> P (in Ref. 1; AAA36114).
{ECO:0000305}.
CONFLICT 497 497 A -> P (in Ref. 1; AAA36114).
{ECO:0000305}.
STRAND 12 14 {ECO:0000244|PDB:1JCN}.
HELIX 20 23 {ECO:0000244|PDB:1JCN}.
STRAND 26 28 {ECO:0000244|PDB:1JCN}.
HELIX 32 34 {ECO:0000244|PDB:1JCN}.
STRAND 35 37 {ECO:0000244|PDB:1JCN}.
HELIX 46 48 {ECO:0000244|PDB:1JCN}.
STRAND 53 58 {ECO:0000244|PDB:1JCN}.
STRAND 60 63 {ECO:0000244|PDB:1JCN}.
STRAND 65 67 {ECO:0000244|PDB:1JCN}.
TURN 71 73 {ECO:0000244|PDB:1JCN}.
HELIX 76 84 {ECO:0000244|PDB:1JCN}.
STRAND 88 91 {ECO:0000244|PDB:1JCN}.
HELIX 97 108 {ECO:0000244|PDB:1JCN}.
STRAND 142 144 {ECO:0000244|PDB:1JCN}.
TURN 160 163 {ECO:0000244|PDB:1JCN}.
TURN 195 199 {ECO:0000244|PDB:1JCN}.
HELIX 200 204 {ECO:0000244|PDB:1JCN}.
STRAND 211 216 {ECO:0000244|PDB:1JCN}.
STRAND 247 250 {ECO:0000244|PDB:1JCN}.
HELIX 256 265 {ECO:0000244|PDB:1JCN}.
STRAND 269 273 {ECO:0000244|PDB:1JCN}.
HELIX 281 293 {ECO:0000244|PDB:1JCN}.
STRAND 298 304 {ECO:0000244|PDB:1JCN}.
HELIX 307 316 {ECO:0000244|PDB:1JCN}.
STRAND 319 323 {ECO:0000244|PDB:1JCN}.
HELIX 343 354 {ECO:0000244|PDB:1JCN}.
HELIX 355 357 {ECO:0000244|PDB:1JCN}.
STRAND 361 365 {ECO:0000244|PDB:1JCN}.
HELIX 370 378 {ECO:0000244|PDB:1JCN}.
STRAND 382 387 {ECO:0000244|PDB:1JCN}.
TURN 388 392 {ECO:0000244|PDB:1JCN}.
HELIX 453 471 {ECO:0000244|PDB:1JCN}.
HELIX 476 484 {ECO:0000244|PDB:1JCN}.
STRAND 490 492 {ECO:0000244|PDB:1JCN}.
SEQUENCE 514 AA; 55406 MW; ABAC654A9091BE62 CRC64;
MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV
LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT
PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS
QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP
IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM
EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR
SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY


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