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Protein

Inositol monophosphatase 1

Gene

IMPA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Myo-inositol phosphate + H2O = myo-inositol + phosphate.4 Publications
Alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate.1 Publication

Cofactori

Mg2+2 Publications3 Publications

Enzyme regulationi

Activity with myo-inositol monophosphate and D-galactose 1-phosphate is inhibited by Li+, Ca2+ and Mn2+, but also by Mg2+ at concentrations above 3 mM.3 Publications

Kineticsi

  1. KM=42 µM for D-myo-inositol 1-phosphate1 Publication
  2. KM=62 µM for L-myo-inositol 1-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.0-7.5.1 Publication

    Pathway: myo-inositol biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Inositol-3-phosphate synthase 1 (ISYNA1)
    2. Inositol monophosphatase 1 (IMPA1), Inositol monophosphatase 2 (IMPA2), Inositol monophosphatase 3 (IMPAD1)
    This subpathway is part of the pathway myo-inositol biosynthesis, which is itself part of Polyol metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate, the pathway myo-inositol biosynthesis and in Polyol metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Magnesium 1; catalytic2 Publications2 Publications
    Binding sitei70 – 701Substrate1 Publication1 Publication
    Metal bindingi90 – 901Magnesium 1; catalytic2 Publications2 Publications
    Metal bindingi90 – 901Magnesium 22 Publications
    Metal bindingi92 – 921Magnesium 1; via carbonyl oxygen; catalytic2 Publications2 Publications
    Metal bindingi93 – 931Magnesium 22 Publications
    Binding sitei213 – 2131Substrate1 Publication1 Publication
    Metal bindingi220 – 2201Magnesium 22 Publications
    Binding sitei220 – 2201Substrate1 Publication

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • inositol monophosphate 1-phosphatase activity Source: UniProtKB
    • inositol monophosphate 3-phosphatase activity Source: UniProtKB-EC
    • inositol monophosphate 4-phosphatase activity Source: UniProtKB-EC
    • inositol monophosphate phosphatase activity Source: UniProtKB
    • lithium ion binding Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    • protein homodimerization activity Source: MGI

    GO - Biological processi

    • inositol biosynthetic process Source: UniProtKB-UniPathway
    • inositol phosphate dephosphorylation Source: UniProtKB
    • inositol phosphate metabolic process Source: Reactome
    • phosphate-containing compound metabolic process Source: UniProtKB
    • phosphatidylinositol biosynthetic process Source: UniProtKB
    • phosphatidylinositol phosphorylation Source: InterPro
    • signal transduction Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Lithium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05783-MONOMER.
    ReactomeiREACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP29218.
    UniPathwayiUPA00823; UER00788.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol monophosphatase 1 (EC:3.1.3.255 Publications)
    Short name:
    IMP 1
    Short name:
    IMPase 1
    Alternative name(s):
    D-galactose 1-phosphate phosphatase1 Publication (EC:3.1.3.941 Publication)
    Inositol-1(or 4)-monophosphatase 1
    Lithium-sensitive myo-inositol monophosphatase A1
    Gene namesi
    Name:IMPA1
    Synonyms:IMPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:6050. IMPA1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361K → Q: 50-fold reduction in activity. 1 Publication
    Mutagenesisi93 – 931D → N: Loss of activity. 1 Publication
    Mutagenesisi165 – 1651S → A or I: Reduced enzyme activity with myo-inositol 1-phosphate. 1 Publication
    Mutagenesisi213 – 2131E → Q: Strongly reduced affinity for myo-inositol 1-phosphate and strongly reduced enzyme activity with myo-inositol 1-phosphate. 1 Publication

    Organism-specific databases

    PharmGKBiPA29860.

    Chemistry

    DrugBankiDB01356. Lithium.

    Polymorphism and mutation databases

    BioMutaiIMPA1.
    DMDMi127717.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 277277Inositol monophosphatase 1PRO_0000142513Add
    BLAST

    Proteomic databases

    MaxQBiP29218.
    PaxDbiP29218.
    PeptideAtlasiP29218.
    PRIDEiP29218.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00020906.
    UCD-2DPAGEP29218.

    PTM databases

    DEPODiP29218.
    PhosphoSiteiP29218.

    Expressioni

    Gene expression databases

    BgeeiP29218.
    CleanExiHS_IMPA1.
    ExpressionAtlasiP29218. baseline and differential.
    GenevisibleiP29218. HS.

    Organism-specific databases

    HPAiHPA037489.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-752410,EBI-752410
    IMPA2O147323EBI-752410,EBI-725233

    Protein-protein interaction databases

    BioGridi109825. 13 interactions.
    IntActiP29218. 2 interactions.
    MINTiMINT-1480285.
    STRINGi9606.ENSP00000408526.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2623Combined sources
    Beta strandi34 – 385Combined sources
    Beta strandi41 – 433Combined sources
    Helixi45 – 6117Combined sources
    Beta strandi66 – 694Combined sources
    Helixi70 – 745Combined sources
    Beta strandi86 – 938Combined sources
    Helixi95 – 1006Combined sources
    Beta strandi106 – 1138Combined sources
    Beta strandi116 – 1249Combined sources
    Turni125 – 1284Combined sources
    Beta strandi129 – 1346Combined sources
    Turni135 – 1373Combined sources
    Beta strandi138 – 1414Combined sources
    Helixi154 – 1563Combined sources
    Beta strandi158 – 1603Combined sources
    Helixi169 – 18315Combined sources
    Turni184 – 1863Combined sources
    Beta strandi188 – 1925Combined sources
    Helixi196 – 2049Combined sources
    Beta strandi207 – 2159Combined sources
    Helixi218 – 23013Combined sources
    Beta strandi234 – 2363Combined sources
    Beta strandi240 – 2423Combined sources
    Beta strandi247 – 2559Combined sources
    Helixi256 – 26510Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AWBX-ray2.50A/B2-277[»]
    1IMAX-ray2.30A/B1-277[»]
    1IMBX-ray2.20A/B1-277[»]
    1IMCX-ray2.60A/B1-277[»]
    1IMDX-ray2.60A/B1-277[»]
    1IMEX-ray2.25A/B1-277[»]
    1IMFX-ray2.50A1-277[»]
    2HHMX-ray2.10A/B2-277[»]
    4AS4X-ray1.70A/B1-277[»]
    ProteinModelPortaliP29218.
    SMRiP29218. Positions 3-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29218.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni92 – 954Substrate binding1 Publication1 Publication
    Regioni194 – 1963Substrate binding1 Publication

    Sequence similaritiesi

    Belongs to the inositol monophosphatase family.Curated

    Phylogenomic databases

    eggNOGiCOG0483.
    GeneTreeiENSGT00390000014699.
    HOGENOMiHOG000282238.
    HOVERGENiHBG052123.
    InParanoidiP29218.
    KOiK01092.
    OMAiKIEFGIV.
    OrthoDBiEOG7RJPS8.
    PhylomeDBiP29218.
    TreeFamiTF313194.

    Family and domain databases

    InterProiIPR020583. Inositol_monoP_metal-BS.
    IPR020552. Inositol_monoPase_Li-sen.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view]
    PANTHERiPTHR20854. PTHR20854. 1 hit.
    PfamiPF00459. Inositol_P. 1 hit.
    [Graphical view]
    PRINTSiPR00377. IMPHPHTASES.
    PR00378. LIIMPHPHTASE.
    PROSITEiPS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P29218-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV
    60 70 80 90 100
    EKMLISSIKE KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH
    110 120 130 140 150
    RFPFVAVSIG FAVNKKIEFG VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ
    160 170 180 190 200
    QEDITKSLLV TELGSSRTPE TVRMVLSNME KLFCIPVHGI RSVGTAAVNM
    210 220 230 240 250
    CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG GPFDLMSRRV
    260 270
    IAANNRILAE RIAKEIQVIP LQRDDED
    Length:277
    Mass (Da):30,189
    Last modified:December 1, 1992 - v1
    Checksum:i861D5617E1C04627
    GO
    Isoform 2 (identifier: P29218-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-277: DITKSLLVTE...VIPLQRDDED → GSGVLEQQLL...ALLLLKLVAC

    Note: No experimental confirmation available.
    Show »
    Length:198
    Mass (Da):21,956
    Checksum:i59A26CFDC77422ED
    GO
    Isoform 3 (identifier: P29218-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGQRPGPVLPAVAVLGQVAKRKVAWLLRWKAVTRTETAGNSSGVYGFGKMKIFVKYFQKM

    Note: No experimental confirmation available.Curated
    Show »
    Length:336
    Mass (Da):36,695
    Checksum:i5838EB952D0C2FA6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 3 (identifier: P29218-3)
    Sequence conflicti17 – 171Q → R in BAH13340 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091I → V.
    Corresponds to variant rs204781 [ dbSNP | Ensembl ].
    VAR_049600

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGQRPGPVLPAVAVLGQVAK RKVAWLLRWKAVTRTETAGN SSGVYGFGKMKIFVKYFQKM in isoform 3. 1 PublicationVSP_046308
    Alternative sequencei153 – 277125DITKS…RDDED → GSGVLEQQLLICALWQLAEQ MHIMKWEFTAGMLQELALLL LKLVAC in isoform 2. 1 PublicationVSP_042521Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66922 mRNA. Translation: CAA47359.1.
    Y11360
    , Y11361, Y11362, Y11367, Y11363, Y11364, Y11365, Y11366 Genomic DNA. Translation: CAA72195.1.
    AF042729 mRNA. Translation: AAB97468.1.
    AK297078 mRNA. Translation: BAG59595.1.
    AK300750 mRNA. Translation: BAH13340.1.
    AK312823 mRNA. Translation: BAG35680.1.
    AC090255 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW87095.1.
    BC008381 mRNA. Translation: AAH08381.1.
    BC009565 mRNA. Translation: AAH09565.1.
    AF178754 Genomic DNA. Translation: AAD52997.1.
    CCDSiCCDS47883.1. [P29218-3]
    CCDS47884.1. [P29218-2]
    CCDS6231.1. [P29218-1]
    PIRiS23130.
    RefSeqiNP_001138350.1. NM_001144878.1. [P29218-3]
    NP_001138351.1. NM_001144879.1. [P29218-2]
    NP_005527.1. NM_005536.3. [P29218-1]
    UniGeneiHs.656694.

    Genome annotation databases

    EnsembliENST00000256108; ENSP00000256108; ENSG00000133731. [P29218-1]
    ENST00000311489; ENSP00000311803; ENSG00000133731. [P29218-2]
    ENST00000449740; ENSP00000408526; ENSG00000133731. [P29218-3]
    GeneIDi3612.
    KEGGihsa:3612.
    UCSCiuc003ych.2. human. [P29218-1]
    uc011lfr.1. human. [P29218-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X66922 mRNA. Translation: CAA47359.1.
    Y11360
    , Y11361, Y11362, Y11367, Y11363, Y11364, Y11365, Y11366 Genomic DNA. Translation: CAA72195.1.
    AF042729 mRNA. Translation: AAB97468.1.
    AK297078 mRNA. Translation: BAG59595.1.
    AK300750 mRNA. Translation: BAH13340.1.
    AK312823 mRNA. Translation: BAG35680.1.
    AC090255 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW87095.1.
    BC008381 mRNA. Translation: AAH08381.1.
    BC009565 mRNA. Translation: AAH09565.1.
    AF178754 Genomic DNA. Translation: AAD52997.1.
    CCDSiCCDS47883.1. [P29218-3]
    CCDS47884.1. [P29218-2]
    CCDS6231.1. [P29218-1]
    PIRiS23130.
    RefSeqiNP_001138350.1. NM_001144878.1. [P29218-3]
    NP_001138351.1. NM_001144879.1. [P29218-2]
    NP_005527.1. NM_005536.3. [P29218-1]
    UniGeneiHs.656694.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AWBX-ray2.50A/B2-277[»]
    1IMAX-ray2.30A/B1-277[»]
    1IMBX-ray2.20A/B1-277[»]
    1IMCX-ray2.60A/B1-277[»]
    1IMDX-ray2.60A/B1-277[»]
    1IMEX-ray2.25A/B1-277[»]
    1IMFX-ray2.50A1-277[»]
    2HHMX-ray2.10A/B2-277[»]
    4AS4X-ray1.70A/B1-277[»]
    ProteinModelPortaliP29218.
    SMRiP29218. Positions 3-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109825. 13 interactions.
    IntActiP29218. 2 interactions.
    MINTiMINT-1480285.
    STRINGi9606.ENSP00000408526.

    Chemistry

    BindingDBiP29218.
    ChEMBLiCHEMBL1786.
    DrugBankiDB01356. Lithium.
    GuidetoPHARMACOLOGYi1463.

    PTM databases

    DEPODiP29218.
    PhosphoSiteiP29218.

    Polymorphism and mutation databases

    BioMutaiIMPA1.
    DMDMi127717.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00020906.
    UCD-2DPAGEP29218.

    Proteomic databases

    MaxQBiP29218.
    PaxDbiP29218.
    PeptideAtlasiP29218.
    PRIDEiP29218.

    Protocols and materials databases

    DNASUi3612.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000256108; ENSP00000256108; ENSG00000133731. [P29218-1]
    ENST00000311489; ENSP00000311803; ENSG00000133731. [P29218-2]
    ENST00000449740; ENSP00000408526; ENSG00000133731. [P29218-3]
    GeneIDi3612.
    KEGGihsa:3612.
    UCSCiuc003ych.2. human. [P29218-1]
    uc011lfr.1. human. [P29218-2]

    Organism-specific databases

    CTDi3612.
    GeneCardsiGC08M082569.
    HGNCiHGNC:6050. IMPA1.
    HPAiHPA037489.
    MIMi602064. gene.
    neXtProtiNX_P29218.
    PharmGKBiPA29860.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0483.
    GeneTreeiENSGT00390000014699.
    HOGENOMiHOG000282238.
    HOVERGENiHBG052123.
    InParanoidiP29218.
    KOiK01092.
    OMAiKIEFGIV.
    OrthoDBiEOG7RJPS8.
    PhylomeDBiP29218.
    TreeFamiTF313194.

    Enzyme and pathway databases

    UniPathwayiUPA00823; UER00788.
    BioCyciMetaCyc:HS05783-MONOMER.
    ReactomeiREACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP29218.

    Miscellaneous databases

    ChiTaRSiIMPA1. human.
    EvolutionaryTraceiP29218.
    GeneWikiiIMPA1.
    GenomeRNAii3612.
    NextBioi14127.
    PROiP29218.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP29218.
    CleanExiHS_IMPA1.
    ExpressionAtlasiP29218. baseline and differential.
    GenevisibleiP29218. HS.

    Family and domain databases

    InterProiIPR020583. Inositol_monoP_metal-BS.
    IPR020552. Inositol_monoPase_Li-sen.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view]
    PANTHERiPTHR20854. PTHR20854. 1 hit.
    PfamiPF00459. Inositol_P. 1 hit.
    [Graphical view]
    PRINTSiPR00377. IMPHPHTASES.
    PR00378. LIIMPHPHTASE.
    PROSITEiPS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme."
      McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R., Bailey F.J., Maigetter R., Ragan C.I.
      Biochem. J. 284:749-754(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY.
      Tissue: Hippocampus.
    2. "Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA)."
      Sjoeholt G., Molven A., Loevlie R., Wilcox A., Sikela J.M., Steen V.M.
      Genomics 45:113-122(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Molecular cloning and expression of human cerebral cortex myo-inositol monophosphatase A1 cDNA."
      Parthasarathy R., Parthasarathy L., Vadnal R.E.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Thymus and Umbilical cord blood.
    5. "DNA sequence and analysis of human chromosome 8."
      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.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Urinary bladder.
    8. "Molecular cloning, genomic organization and promoter analysis of the human brain lithium-sensitive myo-inositol monophosphatase A1 isoenzyme."
      Parthasarathy L., Parthasarathy R.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    9. "Brain inositol monophosphatase identified as a galactose 1-phosphatase."
      Parthasarathy R., Parthasarathy L., Vadnal R.
      Brain Res. 778:99-106(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.
    10. "Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1."
      Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y., Furuichi T., Chung S.-K., Yoshikawa T.
      J. Biol. Chem. 282:637-646(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-93.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structure of inositol monophosphatase, the putative target of lithium therapy."
      Bone R., Springer J.P., Atack J.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:10031-10035(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GADOLINIUM IONS, METAL-BINDING SITE, SUBUNIT.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MYO-INOSITOL 1-PHOSPHATE AND GADOLINIUM ION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, METAL-BINDING SITE, MUTAGENESIS OF SER-165 AND GLU-213.
    16. "Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis."
      Bone R., Frank L., Springer J.P., Atack J.R.
      Biochemistry 33:9468-9476(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOG AND MANGANESE, COFACTOR.
    17. "The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase."
      Ganzhorn A.J., Lepage P., Pelton P.D., Strasser F., Vincendon P., Rondeau J.-M.
      Biochemistry 35:10957-10966(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, MUTAGENESIS OF LYS-36, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION.
    18. "Structure of an enzyme-substrate complex and the catalytic mechanism of human brain myo-inositol monophosphatase."
      Ganzhorn A.J., Rondeau J.-M.
      Protein Eng. 10:61-70(1997)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 1D-MYO-INOSITOL 1-PHOSPHATE AND CALCIUM, METAL-BINDING SITE.
    19. "Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens."
      Singh N., Halliday A.C., Knight M., Lack N.A., Lowe E., Churchill G.C.
      Acta Crystallogr. F 68:1149-1152(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiIMPA1_HUMAN
    AccessioniPrimary (citable) accession number: P29218
    Secondary accession number(s): B2R733
    , B4DLN3, B7Z6Q4, J3KQT7, Q9UK71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: June 24, 2015
    This is version 168 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.