Human Gene IMPA1 (ENST00000256108.10_7) from GENCODE V47lift37
  Description: inositol monophosphatase 1, transcript variant 1 (from RefSeq NM_005536.4)
Gencode Transcript: ENST00000256108.10_7
Gencode Gene: ENSG00000133731.10_12
Transcript (Including UTRs)
   Position: hg19 chr8:82,569,149-82,598,560 Size: 29,412 Total Exon Count: 9 Strand: -
Coding Region
   Position: hg19 chr8:82,571,586-82,593,795 Size: 22,210 Coding Exon Count: 8 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr8:82,569,149-82,598,560)mRNA (may differ from genome)Protein (277 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: IMPA1_HUMAN
DESCRIPTION: RecName: Full=Inositol monophosphatase 1; Short=IMP 1; Short=IMPase 1; EC=3.1.3.25; AltName: Full=Inositol-1(or 4)-monophosphatase 1; AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol- phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1- phosphate, beta-glycerophosphate, and 2'-AMP as substrates.
CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.
COFACTOR: Magnesium.
ENZYME REGULATION: Inhibited by Li(+).
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5;
PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo- inositol from D-glucose 6-phosphate: step 2/2.
SUBUNIT: Homodimer.
INTERACTION: Self; NbExp=2; IntAct=EBI-752410, EBI-752410;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the inositol monophosphatase family.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: IMPA1
Diseases sorted by gene-association score: mental retardation, autosomal recessive 59* (919), bipolar disorder (55), chronic intestinal vascular insufficiency (9), lip disease (6), evans' syndrome (6), galactosemia (6), gingival recession (6), mood disorder (3)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 15.90 RPKM in Testis
Total median expression: 371.08 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -19.2098-0.196 Picture PostScript Text
3' UTR -537.202437-0.220 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR020583 - Inositol_monoP_metal-BS
IPR020552 - Inositol_monoPase_Li-sen
IPR000760 - Inositol_monophosphatase
IPR020550 - Inositol_monophosphatase_CS

Pfam Domains:
PF00459 - Inositol monophosphatase family

SCOP Domains:
56655 - Carbohydrate phosphatase

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1AWB - X-ray MuPIT 1IMA - X-ray MuPIT 1IMB - X-ray MuPIT 1IMC - X-ray MuPIT 1IMD - X-ray MuPIT 1IME - X-ray MuPIT 1IMF - X-ray MuPIT 2HHM - X-ray MuPIT 4AS4 - X-ray MuPIT


ModBase Predicted Comparative 3D Structure on P29218
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologGenome Browser
Gene DetailsGene Details Gene Details Gene Details
Gene SorterGene Sorter Gene Sorter Gene Sorter
 RGDEnsembl  SGD
     Protein Sequence
     Alignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000287 magnesium ion binding
GO:0005515 protein binding
GO:0008934 inositol monophosphate 1-phosphatase activity
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0031403 lithium ion binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0052832 inositol monophosphate 3-phosphatase activity
GO:0052833 inositol monophosphate 4-phosphatase activity
GO:0052834 inositol monophosphate phosphatase activity

Biological Process:
GO:0006020 inositol metabolic process
GO:0006021 inositol biosynthetic process
GO:0006661 phosphatidylinositol biosynthetic process
GO:0006796 phosphate-containing compound metabolic process
GO:0007165 signal transduction
GO:0043647 inositol phosphate metabolic process
GO:0046854 phosphatidylinositol phosphorylation
GO:0046855 inositol phosphate dephosphorylation

Cellular Component:
GO:0005737 cytoplasm
GO:0005829 cytosol


-  Descriptions from all associated GenBank mRNAs
  BC008381 - Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1, mRNA (cDNA clone MGC:12464 IMAGE:3682305), complete cds.
AF042729 - Homo sapiens lithium-sensitive myo-inositol monophosphatase A1 (IMPA1) mRNA, complete cds.
BC009565 - Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1, mRNA (cDNA clone MGC:12163 IMAGE:3682657), complete cds.
AK297078 - Homo sapiens cDNA FLJ58981 complete cds, highly similar to Inositol monophosphatase (EC 3.1.3.25).
AK300750 - Homo sapiens cDNA FLJ54837 complete cds, highly similar to Inositol monophosphatase (EC 3.1.3.25).
HM005407 - Homo sapiens clone HTL-T-94 testicular tissue protein Li 94 mRNA, complete cds.
X66922 - H.sapiens mRNA for myo-insositol monophosphatase.
AK312823 - Homo sapiens cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA.
HQ447127 - Synthetic construct Homo sapiens clone IMAGE:100070415; CCSB006214_04 inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1) gene, encodes complete protein.
KJ891472 - Synthetic construct Homo sapiens clone ccsbBroadEn_00866 IMPA1 gene, encodes complete protein.
CU679403 - Synthetic construct Homo sapiens gateway clone IMAGE:100016955 5' read IMPA1 mRNA.
KJ905810 - Synthetic construct Homo sapiens clone ccsbBroadEn_15480 IMPA1 gene, encodes complete protein.
JD514298 - Sequence 495322 from Patent EP1572962.
JD119894 - Sequence 100918 from Patent EP1572962.
JD250535 - Sequence 231559 from Patent EP1572962.
JD259806 - Sequence 240830 from Patent EP1572962.
JD488775 - Sequence 469799 from Patent EP1572962.
JD538926 - Sequence 519950 from Patent EP1572962.
JD304199 - Sequence 285223 from Patent EP1572962.
JD103627 - Sequence 84651 from Patent EP1572962.
JD202699 - Sequence 183723 from Patent EP1572962.
JD552023 - Sequence 533047 from Patent EP1572962.
JD280503 - Sequence 261527 from Patent EP1572962.
JD206668 - Sequence 187692 from Patent EP1572962.
JD252691 - Sequence 233715 from Patent EP1572962.
JD491729 - Sequence 472753 from Patent EP1572962.
JD243059 - Sequence 224083 from Patent EP1572962.
JD368602 - Sequence 349626 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  BioCyc Knowledge Library
PWY-2301 - myo-inositol biosynthesis
PWY-6358 - superpathway of D-myo-inositol (1,4,5)-trisphosphate metabolism
PWY-6363 - D-myo-inositol (1,4,5)-trisphosphate degradation

Reactome (by CSHL, EBI, and GO)

Protein P29218 (Reactome details) participates in the following event(s):

R-HSA-1855211 I4P is dephosphorylated to Ins by IMPA1/2 in the cytosol
R-HSA-1855154 I1P is dephosphorylated to Ins by IMPA1/2 in the cytosol
R-HSA-1855210 I3P is dephosphorylated to Ins by IMPA1/2 in the cytosol
R-HSA-1855183 Synthesis of IP2, IP, and Ins in the cytosol
R-HSA-1483249 Inositol phosphate metabolism
R-HSA-1430728 Metabolism

-  Other Names for This Gene
  Alternate Gene Symbols: B2R733, B4DLN3, B7Z6Q4, ENST00000256108.1, ENST00000256108.2, ENST00000256108.3, ENST00000256108.4, ENST00000256108.5, ENST00000256108.6, ENST00000256108.7, ENST00000256108.8, ENST00000256108.9, IMPA, IMPA1_HUMAN, J3KQT7, NM_005536, P29218, Q9UK71, uc317ftp.1, uc317ftp.2
UCSC ID: ENST00000256108.10_7
RefSeq Accession: NM_005536.4
Protein: P29218 (aka IMPA1_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.