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UniProtKB/Swiss-Prot entry P29218


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IMPA1_HUMAN
Primary accession number P29218
Secondary accession number Q9UK71
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 95)
Name and origin of the protein
Protein name Inositol monophosphatase
Synonyms EC 3.1.3.25
Inositol-1(or 4)-monophosphatase
IMPase
IMP
Lithium-sensitive myo-inositol monophosphatase A1
Gene name
Name: IMPA1
Synonyms: IMPA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hippocampus;
PubMed=1377913 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/geno.1997.4862; PubMed=9339367 [NCBI, ExPASy, EBI, Israel, Japan]
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].
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].
TISSUE=Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
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.
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
PubMed=1332026 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
DOI=10.1021/bi00198a012; PubMed=8068621 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, AND MUTAGENESIS OF LYS-36.
DOI=10.1021/bi9603837; PubMed=8718889 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X66922; CAA47359.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11360; CAA72195.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11361; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11362; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11367; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11363; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11364; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11365; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11366; CAA72195.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF042729; AAB97468.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008381; AAH08381.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009565; AAH09565.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178754; AAD52997.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23130; S23130.
RefSeq NP_005527.1; -.
UniGene Hs.695965
3D structure databases
PDB
1AWB; X-ray; 2.50 A; A/B=2-277.[ExPASy / RCSB / EBI]
1IMA; X-ray; 2.30 A; A/B=1-277.[ExPASy / RCSB / EBI]
1IMB; X-ray; 2.20 A; A/B=1-277.[ExPASy / RCSB / EBI]
1IMC; X-ray; 2.60 A; A/B=1-277.[ExPASy / RCSB / EBI]
1IMD; X-ray; 2.60 A; A/B=1-277.[ExPASy / RCSB / EBI]
1IME; X-ray; 2.25 A; A/B=1-277.[ExPASy / RCSB / EBI]
1IMF; X-ray; 2.50 A; A=1-277.[ExPASy / RCSB / EBI]
2HHM; X-ray; 2.10 A; A/B=2-277.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AWB; -.
1IMA; -.
1IMB; -.
1IMC; -.
1IMD; -.
1IME; -.
1IMF; -.
2HHM; -.
ModBase P29218.
Protein-protein interaction databases
IntAct P29218; -.
PTM databases
PhosphoSite P29218; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00020906; -.
Organism-specific databases
H-InvDB HIX0007618; -.
HGNC HGNC:6050; IMPA1.
GenAtlas IMPA1.
MIM 602064; gene. [NCBI / EBI]
PharmGKB PA29860; -.
GeneCards P29218.
Gene expression databases
ArrayExpress P29218; -.
CleanEx HS_IMPA1; -.
GermOnline ENSG00000133731; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0008934; Molecular function: inositol-1(or 4)-monophosphatase activity (inferred from mutant phenotype from UniProtKB).
GO:0031403; Molecular function: lithium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
GO:0006796; Biological process: phosphate metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0006661; Biological process: phosphatidylinositol biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0007165; Biological process: signal transduction (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000146; In_FB_phphtase.
IPR000760; Inositol_P.
Graphical view of domain structure.
PANTHER PTHR20854; Inositol_P; 1.
Pfam PF00459; Inositol_P; 1.
Pfam graphical view of domain structure.
PRINTS PR00377; INFBPHPHTASE.
PR00378; INOSPHPHTASE.
ProDom PD023420; Inositol_P; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00629; IMP_1; 1.
PS00630; IMP_2; 1.
BLOCKS P29218.
ProtoNet P29218.
Proteomic databases
PeptideAtlas P29218; -.
Genome annotation databases
Ensembl ENSG00000133731; Homo sapiens. [Contig view]
GeneID 3612; -.
KEGG hsa:3612; -.
Phylogenomic databases
HOGENOM P29218; -.
HOVERGEN P29218; -.
Other
DrugBank DB01356; Lithium.
LinkHub P29218; -.
NextBio 14127; -.
SOURCE IMPA1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   277  277     Inositol monophosphatase. PRO_0000142513
METAL   70    70        Magnesium 1. 
METAL   90    90        Magnesium 1. 
METAL   90    90        Magnesium 2. 
METAL   92    92        Magnesium 1; via carbonyl oxygen. 
METAL   93    93        Magnesium 2. 
METAL   220   220        Magnesium 2. 
BINDING   93    93        Substrate. 
BINDING   220   220        Substrate. 
MUTAGEN   36    36        K->Q: 50-fold reduction in activity. 
HELIX   6    26  21      
STRAND   33    38  6      
STRAND   42    44  3      
HELIX   45    61  17      
STRAND   66    69  4      
HELIX   70    74  5      
STRAND   86    93  8      
HELIX   95   100  6      
STRAND   106   113  8      
STRAND   116   124  9      
TURN   125   128  4      
STRAND   129   134  6      
TURN   135   137  3      
STRAND   138   141  4      
HELIX   154   156  3      
STRAND   158   160  3      
HELIX   169   183  15      
TURN   184   186  3      
STRAND   188   192  5      
HELIX   196   204  9      
STRAND   207   215  9      
HELIX   218   221  4      
HELIX   224   230  7      
STRAND   234   236  3      
STRAND   247   255  9      
HELIX   256   265  10      
Sequence information
Length: 277 AA [This is the length of the unprocessed precursor] Molecular weight: 30189 Da [This is the MW of the unprocessed precursor] CRC64: 861D5617E1C04627 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE 

        70         80         90        100        110        120 
KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG 

       130        140        150        160        170        180 
VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRMVLSNME 

       190        200        210        220        230        240 
KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG 

       250        260        270 
GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED 

P29218 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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