Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inositol monophosphatase 2

Gene

IMPA2

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

Functioni

Can use myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Has been implicated as the pharmacological target for lithium Li+ action in brain.1 Publication

Catalytic activityi

Myo-inositol phosphate + H2O = myo-inositol + phosphate.

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by high Li+ and restricted Mg2+ concentrations.2 Publications

Kineticsi

  1. KM=5 mM for myo-inositol 1-monophosphate1 Publication

    pH dependencei

    Optimum pH is 7.5-8.0.1 Publication

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Metal bindingi81Magnesium 1By similarity1
    Binding sitei81Substrate1 Publication1
    Metal bindingi101Magnesium 1By similarity1
    Metal bindingi101Magnesium 2By similarity1
    Metal bindingi103Magnesium 1; via carbonyl oxygenBy similarity1
    Metal bindingi104Magnesium 2By similarity1
    Binding sitei224Substrate1 Publication1
    Metal bindingi231Magnesium 2By similarity1
    Binding sitei231SubstrateBy similarity1

    GO - Molecular functioni

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06822-MONOMER.
    ZFISH:HS06822-MONOMER.
    ReactomeiR-HSA-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
    UniPathwayiUPA00823; UER00788.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol monophosphatase 2 (EC:3.1.3.25)
    Short name:
    IMP 2
    Short name:
    IMPase 2
    Alternative name(s):
    Inositol-1(or 4)-monophosphatase 2
    Myo-inositol monophosphatase A2
    Gene namesi
    Name:IMPA2
    Synonyms:IMP.18P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6051. IMPA2.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: MGI
    • cytosol Source: Reactome
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi104D → N: Loss of activity. 1 Publication1

    Organism-specific databases

    DisGeNETi3613.
    OpenTargetsiENSG00000141401.
    PharmGKBiPA29861.

    Chemistry databases

    DrugBankiDB01356. Lithium.

    Polymorphism and mutation databases

    BioMutaiIMPA2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001425201 – 288Inositol monophosphatase 2Add BLAST288

    Proteomic databases

    EPDiO14732.
    MaxQBiO14732.
    PaxDbiO14732.
    PeptideAtlasiO14732.
    PRIDEiO14732.
    TopDownProteomicsiO14732-2. [O14732-2]

    PTM databases

    DEPODiO14732.
    iPTMnetiO14732.
    PhosphoSitePlusiO14732.

    Expressioni

    Inductioni

    Repressed by Li+.

    Gene expression databases

    BgeeiENSG00000141401.
    CleanExiHS_IMPA2.
    ExpressionAtlasiO14732. baseline and differential.
    GenevisibleiO14732. HS.

    Organism-specific databases

    HPAiHPA029561.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IMPA1P292183EBI-725233,EBI-752410
    UBA3Q8TBC43EBI-725233,EBI-717567

    GO - Molecular functioni

    • protein homodimerization activity Source: MGI

    Protein-protein interaction databases

    BioGridi109826. 35 interactors.
    IntActiO14732. 7 interactors.
    MINTiMINT-1413243.
    STRINGi9606.ENSP00000269159.

    Structurei

    Secondary structure

    1288
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi17 – 38Combined sources22
    Helixi56 – 70Combined sources15
    Beta strandi77 – 84Combined sources8
    Beta strandi97 – 104Combined sources8
    Helixi106 – 110Combined sources5
    Beta strandi117 – 124Combined sources8
    Beta strandi127 – 135Combined sources9
    Turni136 – 139Combined sources4
    Beta strandi140 – 145Combined sources6
    Turni146 – 148Combined sources3
    Beta strandi150 – 152Combined sources3
    Helixi165 – 167Combined sources3
    Beta strandi169 – 171Combined sources3
    Helixi180 – 195Combined sources16
    Beta strandi199 – 203Combined sources5
    Helixi207 – 215Combined sources9
    Beta strandi220 – 226Combined sources7
    Helixi229 – 231Combined sources3
    Helixi233 – 241Combined sources9
    Beta strandi245 – 247Combined sources3
    Beta strandi251 – 253Combined sources3
    Helixi256 – 258Combined sources3
    Beta strandi260 – 266Combined sources7
    Helixi267 – 275Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CZHX-ray2.70A/B1-288[»]
    2CZIX-ray3.00A1-288[»]
    2CZKX-ray2.90A1-288[»]
    2DDKX-ray2.70A/B1-288[»]
    2FVZX-ray2.40A/B/C/D16-288[»]
    ProteinModelPortaliO14732.
    SMRiO14732.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14732.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni103 – 106Substrate binding4
    Regioni205 – 207Substrate binding3

    Sequence similaritiesi

    Belongs to the inositol monophosphatase family.Curated

    Phylogenomic databases

    eggNOGiKOG2951. Eukaryota.
    COG0483. LUCA.
    GeneTreeiENSGT00390000014699.
    HOGENOMiHOG000282238.
    HOVERGENiHBG052123.
    InParanoidiO14732.
    KOiK01092.
    OMAiGDPWKEC.
    OrthoDBiEOG091G0D21.
    PhylomeDBiO14732.
    TreeFamiTF313194.

    Family and domain databases

    CDDicd01639. IMPase. 1 hit.
    InterProiIPR033942. IMPase.
    IPR020583. Inositol_monoP_metal-BS.
    IPR020552. Inositol_monoPase_Li-sen.
    IPR000760. Inositol_monophosphatase-like.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O14732-1) [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
    MKPSGEDQAA LAAGPWEECF QAAVQLALRA GQIIRKALTE EKRVSTKTSA
    60 70 80 90 100
    ADLVTETDHL VEDLIISELR ERFPSHRFIA EEAAASGAKC VLTHSPTWII
    110 120 130 140 150
    DPIDGTCNFV HRFPTVAVSI GFAVRQELEF GVIYHCTEER LYTGRRGRGA
    160 170 180 190 200
    FCNGQRLRVS GETDLSKALV LTEIGPKRDP ATLKLFLSNM ERLLHAKAHG
    210 220 230 240 250
    VRVIGSSTLA LCHLASGAAD AYYQFGLHCW DLAAATVIIR EAGGIVIDTS
    260 270 280
    GGPLDLMACR VVAASTREMA MLIAQALQTI NYGRDDEK
    Length:288
    Mass (Da):31,321
    Last modified:January 1, 1998 - v1
    Checksum:i30D83FA339AC69B4
    GO
    Isoform 2 (identifier: O14732-2) [UniParc]FASTAAdd to basket
    Also known as: A2b

    The sequence of this isoform differs from the canonical sequence as follows:
         6-34: EDQAALAAGPWEECFQAAVQLALRAGQII → QD

    Show »
    Length:261
    Mass (Da):28,512
    Checksum:iA9D2BC0A05D0DF2F
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04960188A → T.Corresponds to variant rs16976948dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0136746 – 34EDQAA…AGQII → QD in isoform 2. 1 PublicationAdd BLAST29

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF014398 mRNA. Translation: AAB70915.1.
    AF157102
    , AF157096, AF157097, AF157098, AF157099, AF157100, AF157101 Genomic DNA. Translation: AAD40683.1.
    AF200432 mRNA. Translation: AAF07824.1.
    BT007061 mRNA. Translation: AAP35710.1.
    EF444990 Genomic DNA. Translation: ACA06007.1.
    CH471113 Genomic DNA. Translation: EAX01559.1.
    BC017176 mRNA. Translation: AAH17176.1.
    CCDSiCCDS11855.1. [O14732-1]
    RefSeqiNP_055029.1. NM_014214.2. [O14732-1]
    UniGeneiHs.743311.

    Genome annotation databases

    EnsembliENST00000269159; ENSP00000269159; ENSG00000141401. [O14732-1]
    GeneIDi3613.
    KEGGihsa:3613.
    UCSCiuc002kqp.3. human. [O14732-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF014398 mRNA. Translation: AAB70915.1.
    AF157102
    , AF157096, AF157097, AF157098, AF157099, AF157100, AF157101 Genomic DNA. Translation: AAD40683.1.
    AF200432 mRNA. Translation: AAF07824.1.
    BT007061 mRNA. Translation: AAP35710.1.
    EF444990 Genomic DNA. Translation: ACA06007.1.
    CH471113 Genomic DNA. Translation: EAX01559.1.
    BC017176 mRNA. Translation: AAH17176.1.
    CCDSiCCDS11855.1. [O14732-1]
    RefSeqiNP_055029.1. NM_014214.2. [O14732-1]
    UniGeneiHs.743311.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CZHX-ray2.70A/B1-288[»]
    2CZIX-ray3.00A1-288[»]
    2CZKX-ray2.90A1-288[»]
    2DDKX-ray2.70A/B1-288[»]
    2FVZX-ray2.40A/B/C/D16-288[»]
    ProteinModelPortaliO14732.
    SMRiO14732.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109826. 35 interactors.
    IntActiO14732. 7 interactors.
    MINTiMINT-1413243.
    STRINGi9606.ENSP00000269159.

    Chemistry databases

    DrugBankiDB01356. Lithium.

    PTM databases

    DEPODiO14732.
    iPTMnetiO14732.
    PhosphoSitePlusiO14732.

    Polymorphism and mutation databases

    BioMutaiIMPA2.

    Proteomic databases

    EPDiO14732.
    MaxQBiO14732.
    PaxDbiO14732.
    PeptideAtlasiO14732.
    PRIDEiO14732.
    TopDownProteomicsiO14732-2. [O14732-2]

    Protocols and materials databases

    DNASUi3613.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000269159; ENSP00000269159; ENSG00000141401. [O14732-1]
    GeneIDi3613.
    KEGGihsa:3613.
    UCSCiuc002kqp.3. human. [O14732-1]

    Organism-specific databases

    CTDi3613.
    DisGeNETi3613.
    GeneCardsiIMPA2.
    HGNCiHGNC:6051. IMPA2.
    HPAiHPA029561.
    MIMi605922. gene.
    neXtProtiNX_O14732.
    OpenTargetsiENSG00000141401.
    PharmGKBiPA29861.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2951. Eukaryota.
    COG0483. LUCA.
    GeneTreeiENSGT00390000014699.
    HOGENOMiHOG000282238.
    HOVERGENiHBG052123.
    InParanoidiO14732.
    KOiK01092.
    OMAiGDPWKEC.
    OrthoDBiEOG091G0D21.
    PhylomeDBiO14732.
    TreeFamiTF313194.

    Enzyme and pathway databases

    UniPathwayiUPA00823; UER00788.
    BioCyciMetaCyc:HS06822-MONOMER.
    ZFISH:HS06822-MONOMER.
    ReactomeiR-HSA-1855183. Synthesis of IP2, IP, and Ins in the cytosol.

    Miscellaneous databases

    ChiTaRSiIMPA2. human.
    EvolutionaryTraceiO14732.
    GeneWikiiIMPA2.
    GenomeRNAii3613.
    PROiO14732.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000141401.
    CleanExiHS_IMPA2.
    ExpressionAtlasiO14732. baseline and differential.
    GenevisibleiO14732. HS.

    Family and domain databases

    CDDicd01639. IMPase. 1 hit.
    InterProiIPR033942. IMPase.
    IPR020583. Inositol_monoP_metal-BS.
    IPR020552. Inositol_monoPase_Li-sen.
    IPR000760. Inositol_monophosphatase-like.
    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...

    Entry informationi

    Entry nameiIMPA2_HUMAN
    AccessioniPrimary (citable) accession number: O14732
    Secondary accession number(s): B0YJ29, Q9UJT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: November 30, 2016
    This is version 150 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 18
      Human chromosome 18: 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

    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 one 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.