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P29218

- IMPA1_HUMAN

UniProt

P29218 - IMPA1_HUMAN

Protein

Inositol monophosphatase 1

Gene

IMPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    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. 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.1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Inhibited by Li+.1 Publication

    pH dependencei

    Optimum pH is 7.0-7.5.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Magnesium 1
    Binding sitei70 – 701Substrate1 Publication
    Metal bindingi90 – 901Magnesium 1
    Metal bindingi90 – 901Magnesium 2
    Metal bindingi92 – 921Magnesium 1; via carbonyl oxygen
    Metal bindingi93 – 931Magnesium 2
    Binding sitei213 – 2131Substrate1 Publication
    Metal bindingi220 – 2201Magnesium 2
    Binding sitei220 – 2201SubstrateBy similarity

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. inositol monophosphate 1-phosphatase activity Source: UniProtKB
    3. inositol monophosphate 3-phosphatase activity Source: UniProtKB-EC
    4. inositol monophosphate 4-phosphatase activity Source: UniProtKB-EC
    5. metal ion binding Source: UniProtKB-KW
    6. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. inositol biosynthetic process Source: UniProtKB-UniPathway
    2. inositol phosphate dephosphorylation Source: MGI
    3. inositol phosphate metabolic process Source: Reactome
    4. phosphate-containing compound metabolic process Source: UniProtKB
    5. phosphatidylinositol biosynthetic process Source: UniProtKB
    6. phosphatidylinositol phosphorylation Source: InterPro
    7. signal transduction Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Lithium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05783-MONOMER.
    BRENDAi3.1.3.25. 3474.
    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:3.1.3.25)
    Short name:
    IMP 1
    Short name:
    IMPase 1
    Alternative name(s):
    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:6050. IMPA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    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

    Organism-specific databases

    PharmGKBiPA29860.

    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

    PhosphoSiteiP29218.

    Expressioni

    Gene expression databases

    ArrayExpressiP29218.
    BgeeiP29218.
    CleanExiHS_IMPA1.
    GenevestigatoriP29218.

    Organism-specific databases

    HPAiHPA037489.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-752410,EBI-752410

    Protein-protein interaction databases

    BioGridi109825. 11 interactions.
    IntActiP29218. 1 interaction.
    MINTiMINT-1480285.
    STRINGi9606.ENSP00000408526.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 binding
    Regioni194 – 1963Substrate binding

    Sequence similaritiesi

    Belongs to the inositol monophosphatase family.Curated

    Phylogenomic databases

    eggNOGiCOG0483.
    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. Align

    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

    MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV    50
    EKMLISSIKE KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH 100
    RFPFVAVSIG FAVNKKIEFG VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ 150
    QEDITKSLLV TELGSSRTPE TVRMVLSNME KLFCIPVHGI RSVGTAAVNM 200
    CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG GPFDLMSRRV 250
    IAANNRILAE RIAKEIQVIP LQRDDED 277
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi127717.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS47883.1. [P29218-3 ]
    CCDS47884.1. [P29218-2 ]
    CCDS6231.1. [P29218-1 ]
    PIRi S23130.
    RefSeqi NP_001138350.1. NM_001144878.1. [P29218-3 ]
    NP_001138351.1. NM_001144879.1. [P29218-2 ]
    NP_005527.1. NM_005536.3. [P29218-1 ]
    UniGenei Hs.656694.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AWB X-ray 2.50 A/B 2-277 [» ]
    1IMA X-ray 2.30 A/B 1-277 [» ]
    1IMB X-ray 2.20 A/B 1-277 [» ]
    1IMC X-ray 2.60 A/B 1-277 [» ]
    1IMD X-ray 2.60 A/B 1-277 [» ]
    1IME X-ray 2.25 A/B 1-277 [» ]
    1IMF X-ray 2.50 A 1-277 [» ]
    2HHM X-ray 2.10 A/B 2-277 [» ]
    4AS4 X-ray 1.70 A/B 1-277 [» ]
    ProteinModelPortali P29218.
    SMRi P29218. Positions 3-276.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109825. 11 interactions.
    IntActi P29218. 1 interaction.
    MINTi MINT-1480285.
    STRINGi 9606.ENSP00000408526.

    Chemistry

    BindingDBi P29218.
    ChEMBLi CHEMBL1786.
    DrugBanki DB01356. Lithium.
    GuidetoPHARMACOLOGYi 1463.

    PTM databases

    PhosphoSitei P29218.

    Polymorphism databases

    DMDMi 127717.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00020906.
    UCD-2DPAGE P29218.

    Proteomic databases

    MaxQBi P29218.
    PaxDbi P29218.
    PeptideAtlasi P29218.
    PRIDEi P29218.

    Protocols and materials databases

    DNASUi 3612.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256108 ; ENSP00000256108 ; ENSG00000133731 . [P29218-1 ]
    ENST00000311489 ; ENSP00000311803 ; ENSG00000133731 . [P29218-2 ]
    ENST00000449740 ; ENSP00000408526 ; ENSG00000133731 . [P29218-3 ]
    GeneIDi 3612.
    KEGGi hsa:3612.
    UCSCi uc003ych.2. human. [P29218-1 ]
    uc011lfr.1. human. [P29218-2 ]

    Organism-specific databases

    CTDi 3612.
    GeneCardsi GC08M082569.
    HGNCi HGNC:6050. IMPA1.
    HPAi HPA037489.
    MIMi 602064. gene.
    neXtProti NX_P29218.
    PharmGKBi PA29860.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0483.
    HOGENOMi HOG000282238.
    HOVERGENi HBG052123.
    InParanoidi P29218.
    KOi K01092.
    OMAi KIEFGIV.
    OrthoDBi EOG7RJPS8.
    PhylomeDBi P29218.
    TreeFami TF313194.

    Enzyme and pathway databases

    UniPathwayi UPA00823 ; UER00788 .
    BioCyci MetaCyc:HS05783-MONOMER.
    BRENDAi 3.1.3.25. 3474.
    Reactomei REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RK P29218.

    Miscellaneous databases

    ChiTaRSi IMPA1. human.
    EvolutionaryTracei P29218.
    GeneWikii IMPA1.
    GenomeRNAii 3612.
    NextBioi 14127.
    PROi P29218.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29218.
    Bgeei P29218.
    CleanExi HS_IMPA1.
    Genevestigatori P29218.

    Family and domain databases

    InterProi IPR020583. Inositol_monoP_metal-BS.
    IPR020552. Inositol_monoPase_Li-sen.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view ]
    PANTHERi PTHR20854. PTHR20854. 1 hit.
    Pfami PF00459. Inositol_P. 1 hit.
    [Graphical view ]
    PRINTSi PR00377. IMPHPHTASES.
    PR00378. LIIMPHPHTASE.
    PROSITEi PS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).
      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. "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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF ASP-93.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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 MAGNESIUM IONS.
    14. "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 COMPLEX WITH SUBSTRATE.
    15. "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.
    16. "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).

    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: October 1, 2014
    This is version 160 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