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Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1)

 IMPA1_HUMAN             Reviewed;         277 AA.
P29218; B2R733; B4DLN3; B7Z6Q4; J3KQT7; Q9UK71;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
27-SEP-2017, entry version 190.
RecName: Full=Inositol monophosphatase 1;
Short=IMP 1;
Short=IMPase 1;
EC=3.1.3.25 {ECO:0000269|PubMed:1377913, ECO:0000269|PubMed:17068342, ECO:0000269|PubMed:8068620, ECO:0000269|PubMed:8718889, ECO:0000269|PubMed:9462881};
AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000303|PubMed:9462881};
EC=3.1.3.94 {ECO:0000269|PubMed:9462881};
AltName: Full=Inositol-1(or 4)-monophosphatase 1;
AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
Name=IMPA1; Synonyms=IMPA;
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), AND CATALYTIC ACTIVITY.
TISSUE=Hippocampus;
PubMed=1377913; DOI=10.1042/bj2840749;
McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R.,
Bailey F.J., Maigetter R., Ragan C.I.;
"cDNA cloning of human and rat brain myo-inositol monophosphatase.
Expression and characterization of the human recombinant enzyme.";
Biochem. J. 284:749-754(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9339367; DOI=10.1006/geno.1997.4862;
Sjoeholt G., Molven A., Loevlie R., Wilcox A., Sikela J.M.,
Steen V.M.;
"Genomic structure and chromosomal localization of a human myo-
inositol monophosphatase gene (IMPA).";
Genomics 45:113-122(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Parthasarathy R., Parthasarathy L., Vadnal R.E.;
"Molecular cloning and expression of human cerebral cortex myo-
inositol monophosphatase A1 cDNA.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Thymus, and Umbilical cord blood;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
Parthasarathy L., Parthasarathy R.;
"Molecular cloning, genomic organization and promoter analysis of the
human brain lithium-sensitive myo-inositol monophosphatase A1
isoenzyme.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
SUBUNIT.
PubMed=9462881; DOI=10.1016/S0006-8993(97)01042-1;
Parthasarathy R., Parthasarathy L., Vadnal R.;
"Brain inositol monophosphatase identified as a galactose 1-
phosphatase.";
Brain Res. 778:99-106(1997).
[10]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
ENZYME REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-93.
PubMed=17068342; DOI=10.1074/jbc.M604474200;
Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y.,
Furuichi T., Chung S.-K., Yoshikawa T.;
"Spatial expression patterns and biochemical properties distinguish a
second myo-inositol monophosphatase IMPA2 from IMPA1.";
J. Biol. Chem. 282:637-646(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168, 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).
[15]
INVOLVEMENT IN MRT59.
PubMed=26416544; DOI=10.1038/mp.2015.150;
Figueiredo T., Melo U.S., Pessoa A.L., Nobrega P.R., Kitajima J.P.,
Rusch H., Vaz F., Lucato L.T., Zatz M., Kok F., Santos S.;
"A homozygous loss-of-function mutation in inositol monophosphatase 1
(IMPA1) causes severe intellectual disability.";
Mol. Psychiatry 21:1125-1129(2016).
[16]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GADOLINIUM IONS,
METAL-BINDING SITE, AND SUBUNIT.
PubMed=1332026; DOI=10.1073/pnas.89.21.10031;
Bone R., Springer J.P., Atack J.R.;
"Structure of inositol monophosphatase, the putative target of lithium
therapy.";
Proc. Natl. Acad. Sci. U.S.A. 89:10031-10035(1992).
[17]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MYO-INOSITOL
1-PHOSPHATE AND GADOLINIUM ION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, METAL-BINDING SITE, AND MUTAGENESIS OF SER-165
AND GLU-213.
PubMed=8068620; DOI=10.1021/bi00198a011;
Bone R., Frank L., Springer J.P., Pollack S.J., Osborne S.A.,
Atack J.R., Knowles M.R., McAllister G., Ragan C.I., Broughton H.B.;
"Structural analysis of inositol monophosphatase complexes with
substrates.";
Biochemistry 33:9460-9467(1994).
[18]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE
ANALOG AND MANGANESE, AND COFACTOR.
PubMed=8068621; DOI=10.1021/bi00198a012;
Bone R., Frank L., Springer J.P., Atack J.R.;
"Structural studies of metal binding by inositol monophosphatase:
evidence for two-metal ion catalysis.";
Biochemistry 33:9468-9476(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, MUTAGENESIS OF
LYS-36, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND ENZYME REGULATION.
PubMed=8718889; DOI=10.1021/bi9603837;
Ganzhorn A.J., Lepage P., Pelton P.D., Strasser F., Vincendon P.,
Rondeau J.-M.;
"The contribution of lysine-36 to catalysis by human myo-inositol
monophosphatase.";
Biochemistry 35:10957-10966(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 1D-MYO-INOSITOL
1-PHOSPHATE AND CALCIUM, AND METAL-BINDING SITE.
Ganzhorn A.J., Rondeau J.-M.;
"Structure of an enzyme-substrate complex and the catalytic mechanism
of human brain myo-inositol monophosphatase.";
Protein Eng. 10:61-70(1997).
[21]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM,
COFACTOR, AND SUBUNIT.
PubMed=23027737; DOI=10.1107/S1744309112035191;
Singh N., Halliday A.C., Knight M., Lack N.A., Lowe E.,
Churchill G.C.;
"Cloning, expression, purification, crystallization and X-ray analysis
of inositol monophosphatase from Mus musculus and Homo sapiens.";
Acta Crystallogr. F 68:1149-1152(2012).
-!- 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. Has broad substrate specificity and can use myo-
inositol monophosphates, myo-inositol 1,3-diphosphate, myo-
inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose
1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-
phosphate, beta-glycerophosphate, and 2'-AMP as substrates.
{ECO:0000269|PubMed:17068342, ECO:0000269|PubMed:8718889,
ECO:0000269|PubMed:9462881}.
-!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
+ phosphate. {ECO:0000269|PubMed:1377913,
ECO:0000269|PubMed:8068620, ECO:0000269|PubMed:8718889,
ECO:0000269|PubMed:9462881}.
-!- CATALYTIC ACTIVITY: Alpha-D-galactose 1-phosphate + H(2)O = D-
galactose + phosphate. {ECO:0000269|PubMed:9462881}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17068342,
ECO:0000269|PubMed:8718889, ECO:0000269|PubMed:9462881,
ECO:0000303|PubMed:23027737, ECO:0000303|PubMed:8068621};
-!- ENZYME REGULATION: Activity with myo-inositol monophosphate and D-
galactose 1-phosphate is inhibited by Li(+), Ca(2+) and Mn(2+),
but also by Mg(2+) at concentrations above 3 mM.
{ECO:0000269|PubMed:17068342, ECO:0000269|PubMed:8718889,
ECO:0000269|PubMed:9462881}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=42 uM for D-myo-inositol 1-phosphate
{ECO:0000269|PubMed:8068620};
KM=62 uM for L-myo-inositol 1-phosphate
{ECO:0000269|PubMed:8068620};
pH dependence:
Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:17068342};
-!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
inositol from D-glucose 6-phosphate: step 2/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1332026,
ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068620,
ECO:0000269|PubMed:8068621, ECO:0000269|PubMed:9462881}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-752410, EBI-752410;
O14732:IMPA2; NbExp=3; IntAct=EBI-752410, EBI-725233;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17068342}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P29218-1; Sequence=Displayed;
Name=2;
IsoId=P29218-2; Sequence=VSP_042521;
Note=No experimental confirmation available.;
Name=3;
IsoId=P29218-3; Sequence=VSP_046308;
Note=No experimental confirmation available. Ref.4 (BAH13340)
sequence is in conflict in position: 17:Q->R. {ECO:0000305};
-!- DISEASE: Mental retardation, autosomal recessive 59 (MRT59)
[MIM:617323]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRT59 transmission
pattern is consistent with autosomal recessive inheritance.
{ECO:0000269|PubMed:26416544}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the inositol monophosphatase family.
{ECO:0000305}.
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EMBL; X66922; CAA47359.1; -; mRNA.
EMBL; Y11360; CAA72195.1; -; Genomic_DNA.
EMBL; Y11361; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11362; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11367; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11363; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11364; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11365; CAA72195.1; JOINED; Genomic_DNA.
EMBL; Y11366; CAA72195.1; JOINED; Genomic_DNA.
EMBL; AF042729; AAB97468.1; -; mRNA.
EMBL; AK297078; BAG59595.1; -; mRNA.
EMBL; AK300750; BAH13340.1; -; mRNA.
EMBL; AK312823; BAG35680.1; -; mRNA.
EMBL; AC090255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471068; EAW87095.1; -; Genomic_DNA.
EMBL; BC008381; AAH08381.1; -; mRNA.
EMBL; BC009565; AAH09565.1; -; mRNA.
EMBL; AF178754; AAD52997.1; -; Genomic_DNA.
CCDS; CCDS47883.1; -. [P29218-3]
CCDS; CCDS47884.1; -. [P29218-2]
CCDS; CCDS6231.1; -. [P29218-1]
PIR; S23130; S23130.
RefSeq; NP_001138350.1; NM_001144878.1. [P29218-3]
RefSeq; NP_001138351.1; NM_001144879.1. [P29218-2]
RefSeq; NP_005527.1; NM_005536.3. [P29218-1]
UniGene; Hs.656694; -.
PDB; 1AWB; X-ray; 2.50 A; A/B=2-277.
PDB; 1IMA; X-ray; 2.30 A; A/B=1-277.
PDB; 1IMB; X-ray; 2.20 A; A/B=1-277.
PDB; 1IMC; X-ray; 2.60 A; A/B=1-277.
PDB; 1IMD; X-ray; 2.60 A; A/B=1-277.
PDB; 1IME; X-ray; 2.25 A; A/B=1-277.
PDB; 1IMF; X-ray; 2.50 A; A=1-277.
PDB; 2HHM; X-ray; 2.10 A; A/B=2-277.
PDB; 4AS4; X-ray; 1.70 A; A/B=1-277.
PDBsum; 1AWB; -.
PDBsum; 1IMA; -.
PDBsum; 1IMB; -.
PDBsum; 1IMC; -.
PDBsum; 1IMD; -.
PDBsum; 1IME; -.
PDBsum; 1IMF; -.
PDBsum; 2HHM; -.
PDBsum; 4AS4; -.
ProteinModelPortal; P29218; -.
SMR; P29218; -.
BioGrid; 109825; 23.
IntAct; P29218; 4.
MINT; MINT-1480285; -.
STRING; 9606.ENSP00000408526; -.
ChEMBL; CHEMBL1786; -.
DrugBank; DB03542; L-Myo-Inositol-1-Phosphate.
DrugBank; DB01356; Lithium.
GuidetoPHARMACOLOGY; 1463; -.
DEPOD; P29218; -.
iPTMnet; P29218; -.
PhosphoSitePlus; P29218; -.
SwissPalm; P29218; -.
BioMuta; IMPA1; -.
DMDM; 127717; -.
REPRODUCTION-2DPAGE; IPI00020906; -.
UCD-2DPAGE; P29218; -.
EPD; P29218; -.
MaxQB; P29218; -.
PaxDb; P29218; -.
PeptideAtlas; P29218; -.
PRIDE; P29218; -.
DNASU; 3612; -.
Ensembl; ENST00000256108; ENSP00000256108; ENSG00000133731. [P29218-1]
Ensembl; ENST00000311489; ENSP00000311803; ENSG00000133731. [P29218-2]
Ensembl; ENST00000449740; ENSP00000408526; ENSG00000133731. [P29218-3]
GeneID; 3612; -.
KEGG; hsa:3612; -.
UCSC; uc003ych.3; human. [P29218-1]
CTD; 3612; -.
DisGeNET; 3612; -.
EuPathDB; HostDB:ENSG00000133731.9; -.
GeneCards; IMPA1; -.
HGNC; HGNC:6050; IMPA1.
HPA; HPA037489; -.
MIM; 602064; gene.
MIM; 617323; phenotype.
neXtProt; NX_P29218; -.
OpenTargets; ENSG00000133731; -.
PharmGKB; PA29860; -.
eggNOG; KOG2951; Eukaryota.
eggNOG; COG0483; LUCA.
GeneTree; ENSGT00390000014699; -.
HOGENOM; HOG000282238; -.
HOVERGEN; HBG052123; -.
InParanoid; P29218; -.
KO; K01092; -.
OMA; NNYAEFC; -.
OrthoDB; EOG091G0D21; -.
PhylomeDB; P29218; -.
TreeFam; TF313194; -.
BioCyc; MetaCyc:HS05783-MONOMER; -.
Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RK; P29218; -.
UniPathway; UPA00823; UER00788.
ChiTaRS; IMPA1; human.
EvolutionaryTrace; P29218; -.
GeneWiki; IMPA1; -.
GenomeRNAi; 3612; -.
PRO; PR:P29218; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000133731; -.
CleanEx; HS_IMPA1; -.
ExpressionAtlas; P29218; baseline and differential.
Genevisible; P29218; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:MGI.
GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; TAS:Reactome.
GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; TAS:Reactome.
GO; GO:0052834; F:inositol monophosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0031403; F:lithium ion binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:UniProtKB.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IMP:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:UniProtKB.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
CDD; cd01639; IMPase; 1.
InterPro; IPR033942; IMPase.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR020552; Inositol_monoPase_Li-sen.
InterPro; IPR000760; Inositol_monophosphatase-like.
InterPro; IPR020550; Inositol_monophosphatase_CS.
PANTHER; PTHR20854; PTHR20854; 1.
Pfam; PF00459; Inositol_P; 1.
PRINTS; PR00377; IMPHPHTASES.
PRINTS; PR00378; LIIMPHPHTASE.
PROSITE; PS00629; IMP_1; 1.
PROSITE; PS00630; IMP_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Lithium; Magnesium; Mental retardation; Metal-binding;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 277 Inositol monophosphatase 1.
/FTId=PRO_0000142513.
REGION 92 95 Substrate binding.
{ECO:0000269|PubMed:8068620,
ECO:0000303|PubMed:8068621}.
REGION 194 196 Substrate binding.
{ECO:0000269|PubMed:8068620}.
METAL 70 70 Magnesium 1; catalytic.
{ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621,
ECO:0000303|PubMed:1332026,
ECO:0000303|PubMed:8068620}.
METAL 90 90 Magnesium 1; catalytic.
{ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621,
ECO:0000303|PubMed:1332026,
ECO:0000303|PubMed:8068620}.
METAL 90 90 Magnesium 2.
{ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621}.
METAL 92 92 Magnesium 1; via carbonyl oxygen;
catalytic. {ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621,
ECO:0000303|PubMed:1332026,
ECO:0000303|PubMed:8068620}.
METAL 93 93 Magnesium 2.
{ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621}.
METAL 220 220 Magnesium 2.
{ECO:0000269|PubMed:23027737,
ECO:0000269|PubMed:8068621}.
BINDING 70 70 Substrate. {ECO:0000269|PubMed:8068620,
ECO:0000303|PubMed:8068621}.
BINDING 213 213 Substrate. {ECO:0000269|PubMed:8068620,
ECO:0000303|PubMed:8068621}.
BINDING 220 220 Substrate. {ECO:0000269|PubMed:8068620}.
MOD_RES 168 168 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MGQRPGPVLPAVAVLGQVAKRKVAWLLRWKAVTRTE
TAGNSSGVYGFGKMKIFVKYFQKM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046308.
VAR_SEQ 153 277 DITKSLLVTELGSSRTPETVRMVLSNMEKLFCIPVHGIRSV
GTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGV
LMDVTGGPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDD
ED -> GSGVLEQQLLICALWQLAEQMHIMKWEFTAGMLQE
LALLLLKLVAC (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042521.
VARIANT 109 109 I -> V (in dbSNP:rs204781).
/FTId=VAR_049600.
MUTAGEN 36 36 K->Q: 50-fold reduction in activity.
{ECO:0000269|PubMed:8718889}.
MUTAGEN 93 93 D->N: Loss of activity.
{ECO:0000269|PubMed:17068342}.
MUTAGEN 165 165 S->A,I: Reduced enzyme activity with myo-
inositol 1-phosphate.
{ECO:0000269|PubMed:8068620}.
MUTAGEN 213 213 E->Q: Strongly reduced affinity for myo-
inositol 1-phosphate and strongly reduced
enzyme activity with myo-inositol 1-
phosphate. {ECO:0000269|PubMed:8068620}.
HELIX 4 26 {ECO:0000244|PDB:4AS4}.
STRAND 34 38 {ECO:0000244|PDB:4AS4}.
STRAND 41 43 {ECO:0000244|PDB:4AS4}.
HELIX 45 61 {ECO:0000244|PDB:4AS4}.
STRAND 66 69 {ECO:0000244|PDB:4AS4}.
HELIX 70 74 {ECO:0000244|PDB:4AS4}.
STRAND 86 93 {ECO:0000244|PDB:4AS4}.
HELIX 95 100 {ECO:0000244|PDB:4AS4}.
STRAND 106 113 {ECO:0000244|PDB:4AS4}.
STRAND 116 124 {ECO:0000244|PDB:4AS4}.
TURN 125 128 {ECO:0000244|PDB:4AS4}.
STRAND 129 134 {ECO:0000244|PDB:4AS4}.
TURN 135 137 {ECO:0000244|PDB:4AS4}.
STRAND 138 141 {ECO:0000244|PDB:4AS4}.
HELIX 154 156 {ECO:0000244|PDB:4AS4}.
STRAND 158 160 {ECO:0000244|PDB:4AS4}.
HELIX 169 183 {ECO:0000244|PDB:4AS4}.
TURN 184 186 {ECO:0000244|PDB:4AS4}.
STRAND 188 192 {ECO:0000244|PDB:4AS4}.
HELIX 196 204 {ECO:0000244|PDB:4AS4}.
STRAND 207 215 {ECO:0000244|PDB:4AS4}.
HELIX 218 230 {ECO:0000244|PDB:4AS4}.
STRAND 234 236 {ECO:0000244|PDB:4AS4}.
STRAND 240 242 {ECO:0000244|PDB:1IME}.
STRAND 247 255 {ECO:0000244|PDB:4AS4}.
HELIX 256 265 {ECO:0000244|PDB:4AS4}.
SEQUENCE 277 AA; 30189 MW; 861D5617E1C04627 CRC64;
MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG
VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRMVLSNME
KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG
GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED


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