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P50096

- IMDH1_MOUSE

UniProt

P50096 - IMDH1_MOUSE

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Protein
Inosine-5'-monophosphate dehydrogenase 1
Gene
Impdh1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 By similarity.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Potassium; via carbonyl oxygen By similarity
Metal bindingi328 – 3281Potassium; via carbonyl oxygen By similarity
Binding sitei329 – 3291IMP By similarity
Active sitei331 – 3311Thioimidate intermediate By similarity
Metal bindingi331 – 3311Potassium; via carbonyl oxygen By similarity
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 – 2763NAD By similarity
Nucleotide bindingi324 – 3263NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. lymphocyte proliferation Source: MGI
  3. purine nucleotide biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase 1 (EC:1.1.1.205)
Short name:
IMP dehydrogenase 1
Short name:
IMPD 1
Short name:
IMPDH 1
Alternative name(s):
IMPDH-I
Gene namesi
Name:Impdh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:96567. Impdh1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 514513Inosine-5'-monophosphate dehydrogenase 1UniRule annotation
PRO_0000093671Add
BLAST

Proteomic databases

MaxQBiP50096.
PaxDbiP50096.
PRIDEiP50096.

PTM databases

PhosphoSiteiP50096.

Expressioni

Gene expression databases

ArrayExpressiP50096.
BgeeiP50096.
CleanExiMM_IMPDH1.
GenevestigatoriP50096.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi204791. 2 interactions.
IntActiP50096. 1 interaction.
MINTiMINT-4098666.
STRINGi10090.ENSMUSP00000077289.

Structurei

3D structure databases

ProteinModelPortaliP50096.
SMRiP50096. Positions 10-514.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3663IMP binding By similarity
Regioni387 – 3882IMP binding By similarity
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.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165752.
HOVERGENiHBG052122.
InParanoidiQ7TSG7.
KOiK00088.
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.

P50096-1 [UniParc]FASTAAdd to Basket

« Hide

MADYLISGGT GYVPEDGLTA QQLFANADGL TYNDFLILPG FIDFIADEVD    50
LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ 100
ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKIQHGFS GIPITATGTM 150
GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRVELVVAPA GVTLKEANEI 200
LQRSKKGKLP IVNDQDELVA IIARTDLKKN RDYPLASKDS HKQLLCGAAV 250
GTREDDKYRL DLLTQAGADV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI 300
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV 350
AEYARRFGVP VIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY 400
FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK 450
GSIQKFVPYL IAGIQHGCQD IGAQSLSVLR SMMYSGELKF EKRTMSAQIE 500
GGVHGLHSYE KRLY 514
Length:514
Mass (Da):55,279
Last modified:July 27, 2011 - v2
Checksum:i69E2DD40F03701F2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 222QQ → HE in AAA18285. 1 Publication
Sequence conflicti273 – 2731L → H in AAA18285. 1 Publication
Sequence conflicti414 – 4141M → I in AAA18285. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00978 mRNA. Translation: AAA18285.1.
AK171139 mRNA. Translation: BAE42272.1.
CH466533 Genomic DNA. Translation: EDL13790.1.
BC053416 mRNA. Translation: AAH53416.1.
CCDSiCCDS39449.1.
RefSeqiNP_035959.2. NM_011829.2.
UniGeneiMm.260707.

Genome annotation databases

EnsembliENSMUST00000078155; ENSMUSP00000077289; ENSMUSG00000003500.
ENSMUST00000159124; ENSMUSP00000124931; ENSMUSG00000003500.
ENSMUST00000162099; ENSMUSP00000124541; ENSMUSG00000003500.
GeneIDi23917.
KEGGimmu:23917.
UCSCiuc009bda.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00978 mRNA. Translation: AAA18285.1 .
AK171139 mRNA. Translation: BAE42272.1 .
CH466533 Genomic DNA. Translation: EDL13790.1 .
BC053416 mRNA. Translation: AAH53416.1 .
CCDSi CCDS39449.1.
RefSeqi NP_035959.2. NM_011829.2.
UniGenei Mm.260707.

3D structure databases

ProteinModelPortali P50096.
SMRi P50096. Positions 10-514.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204791. 2 interactions.
IntActi P50096. 1 interaction.
MINTi MINT-4098666.
STRINGi 10090.ENSMUSP00000077289.

Chemistry

BindingDBi P50096.

PTM databases

PhosphoSitei P50096.

Proteomic databases

MaxQBi P50096.
PaxDbi P50096.
PRIDEi P50096.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000078155 ; ENSMUSP00000077289 ; ENSMUSG00000003500 .
ENSMUST00000159124 ; ENSMUSP00000124931 ; ENSMUSG00000003500 .
ENSMUST00000162099 ; ENSMUSP00000124541 ; ENSMUSG00000003500 .
GeneIDi 23917.
KEGGi mmu:23917.
UCSCi uc009bda.1. mouse.

Organism-specific databases

CTDi 3614.
MGIi MGI:96567. Impdh1.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00530000062923.
HOGENOMi HOG000165752.
HOVERGENi HBG052122.
InParanoidi Q7TSG7.
KOi K00088.
TreeFami TF300378.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Miscellaneous databases

NextBioi 303685.
PROi P50096.
SOURCEi Search...

Gene expression databases

ArrayExpressi P50096.
Bgeei P50096.
CleanExi MM_IMPDH1.
Genevestigatori P50096.

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. "Type I inosine monophosphate dehydrogenase: evidence for a single functional gene in mammalian species."
    Dayton J.S., Mitchell B.S.
    Biochem. Biophys. Res. Commun. 195:897-901(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukemia.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain.

Entry informationi

Entry nameiIMDH1_MOUSE
AccessioniPrimary (citable) accession number: P50096
Secondary accession number(s): Q7TSG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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