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Protein

Inositol monophosphatase 2

Gene

INM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 involved in the inositol cycle of calcium signaling.2 Publications

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by Li+ and Na+.1 Publication

Kineticsi

  1. KM=0.12 mM for inositol 1-phosphate1 Publication
  1. Vmax=16 µmol/min/mg enzyme for inositol 1-phosphate1 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 (INO1)
  2. Inositol monophosphatase 2 (INM2), Inositol monophosphatase 1 (INM1)
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 bindingi75 – 751Magnesium 1By similarity
Binding sitei75 – 751SubstrateBy similarity
Metal bindingi94 – 941Magnesium 1By similarity
Metal bindingi94 – 941Magnesium 2By similarity
Metal bindingi96 – 961Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi97 – 971Magnesium 2By similarity
Metal bindingi231 – 2311Magnesium 2By similarity
Binding sitei231 – 2311SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29851-MONOMER.
YEAST:MONOMER3O-11.
ReactomeiR-SCE-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
Gene namesi
Name:INM2
Synonyms:IMP2
Ordered Locus Names:YDR287W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR287W.
SGDiS000002695. INM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Inositol monophosphatase 2PRO_0000245568Add
BLAST

Proteomic databases

MaxQBiQ05533.

Interactioni

Protein-protein interaction databases

BioGridi32340. 18 interactions.
DIPiDIP-5626N.
MINTiMINT-508245.

Structurei

3D structure databases

ProteinModelPortaliQ05533.
SMRiQ05533. Positions 41-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 994Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000014699.
HOGENOMiHOG000282238.
InParanoidiQ05533.
KOiK01092.
OMAiTGGAMVH.
OrthoDBiEOG7RBZKG.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q05533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLTRQVLEE VENTFIELLR SKIGPLVKSH AGTNFCSYDD KANGVDLVTA
60 70 80 90 100
LDKQIESIIK ENLTAKYPSF KFIGEETYVK GVTKITNGPT FIVDPIDGTT
110 120 130 140 150
NFIHGYPYSC TSLGLAEMGK PVVGVVFNPH LNQLFHASKG NGAFLNDQEI
160 170 180 190 200
KVSKRPLILQ KSLIALEGGS ERTEGSQGNF DKKMNTYKNL LSESGAFVHG
210 220 230 240 250
FRSAGSAAMN ICYVASGMLD AYWEGGCWAW DVCAGWCILE EAGGIMVGGN
260 270 280 290
CGEWNIPLDR RCYLAIRGGC ESMEQKRFAE SFWPHVAGEL EY
Length:292
Mass (Da):32,093
Last modified:November 1, 1996 - v1
Checksum:iCEA9D943F69E2082
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64472.1.
AY557746 Genomic DNA. Translation: AAS56072.1.
BK006938 Genomic DNA. Translation: DAA12127.1.
PIRiS70117.
RefSeqiNP_010573.3. NM_001180595.3.

Genome annotation databases

EnsemblFungiiYDR287W; YDR287W; YDR287W.
GeneIDi851881.
KEGGisce:YDR287W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51031 Genomic DNA. Translation: AAB64472.1.
AY557746 Genomic DNA. Translation: AAS56072.1.
BK006938 Genomic DNA. Translation: DAA12127.1.
PIRiS70117.
RefSeqiNP_010573.3. NM_001180595.3.

3D structure databases

ProteinModelPortaliQ05533.
SMRiQ05533. Positions 41-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32340. 18 interactions.
DIPiDIP-5626N.
MINTiMINT-508245.

Proteomic databases

MaxQBiQ05533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR287W; YDR287W; YDR287W.
GeneIDi851881.
KEGGisce:YDR287W.

Organism-specific databases

EuPathDBiFungiDB:YDR287W.
SGDiS000002695. INM2.

Phylogenomic databases

GeneTreeiENSGT00390000014699.
HOGENOMiHOG000282238.
InParanoidiQ05533.
KOiK01092.
OMAiTGGAMVH.
OrthoDBiEOG7RBZKG.

Enzyme and pathway databases

UniPathwayiUPA00823; UER00788.
BioCyciYEAST:G3O-29851-MONOMER.
YEAST:MONOMER3O-11.
ReactomeiR-SCE-1855183. Synthesis of IP2, IP, and Ins in the cytosol.

Miscellaneous databases

PROiQ05533.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The yeast inositol monophosphatase is a lithium- and sodium-sensitive enzyme encoded by a non-essential gene pair."
    Lopez F., Leube M., Gil-Mascarell R., Navarro-Avino J.P., Serrano R.
    Mol. Microbiol. 31:1255-1264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "Yeast inositol mono- and trisphosphate levels are modulated by inositol monophosphatase activity and nutrients."
    Navarro-Avino J.P., Belles J.M., Serrano R.
    Biochem. Biophys. Res. Commun. 302:41-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiINM2_YEAST
AccessioniPrimary (citable) accession number: Q05533
Secondary accession number(s): D6VSR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.