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P29218

- IMPA1_HUMAN

UniProt

P29218 - IMPA1_HUMAN

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Protein

Inositol monophosphatase 1

Gene

IMPA1

Organism
Homo sapiens (Human)
Status
Reviewed - 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+3 Publications2 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

Pathwayi

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

  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. inositol monophosphate phosphatase activity Source: UniProtKB
  6. lithium ion binding Source: UniProtKB
  7. magnesium ion binding Source: UniProtKB
  8. manganese ion binding Source: UniProtKB
  9. protein homodimerization activity Source: MGI

GO - Biological processi

  1. inositol biosynthetic process Source: UniProtKB-UniPathway
  2. inositol phosphate dephosphorylation Source: UniProtKB
  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
Complete GO annotation...

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:3.1.3.255 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: Chromosome 8

Organism-specific databases

HGNCiHGNC:6050. IMPA1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

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

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

BgeeiP29218.
CleanExiHS_IMPA1.
ExpressionAtlasiP29218. baseline and differential.
GenevestigatoriP29218.

Organism-specific databases

HPAiHPA037489.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109825. 12 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 – 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. 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

        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]

Polymorphism databases

DMDMi127717.

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 .
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:
PDBei
RCSB PDBi
PDBji
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. 12 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.
GeneTreei ENSGT00390000014699.
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

Bgeei P29218.
CleanExi HS_IMPA1.
ExpressionAtlasi P29218. baseline and differential.
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

« 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: November 26, 2014
This is version 162 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