Full text data of ISYNA1
ISYNA1
(INO1)
[Confidence: low (only semi-automatic identification from reviews)]
Inositol-3-phosphate synthase 1; IPS 1; 5.5.1.4 (Myo-inositol 1-phosphate synthase; MI-1-P synthase; MIP synthase; hIPS; Myo-inositol 1-phosphate synthase A1; hINO1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Inositol-3-phosphate synthase 1; IPS 1; 5.5.1.4 (Myo-inositol 1-phosphate synthase; MI-1-P synthase; MIP synthase; hIPS; Myo-inositol 1-phosphate synthase A1; hINO1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NPH2
ID INO1_HUMAN Reviewed; 558 AA.
AC Q9NPH2; B3KRT1; G5E9U0; Q6NXT5; Q7Z525; Q9BT65; Q9H2Y2; Q9NSU0;
read moreAC Q9NVW7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Inositol-3-phosphate synthase 1;
DE Short=IPS 1;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase;
DE Short=MI-1-P synthase;
DE Short=MIP synthase;
DE Short=hIPS;
DE AltName: Full=Myo-inositol 1-phosphate synthase A1;
DE Short=hINO1;
GN Name=ISYNA1; Synonyms=INO1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Hepatoma;
RX PubMed=12941308; DOI=10.1016/S0003-9861(03)00388-6;
RA Guan G., Dai P., Shechter I.;
RT "cDNA cloning and gene expression analysis of human myo-inositol 1-
RT phosphate synthase.";
RL Arch. Biochem. Biophys. 417:251-259(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=17121280;
RA Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F.,
RA Parthasarathy R.N.;
RT "Mammalian inositol 3-phosphate synthase: its role in the biosynthesis
RT of brain inositol and its clinical use as a psychoactive agent.";
RL Subcell. Biochem. 39:293-314(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou Y., Yu L., Zhao E.P., Hua Y.M., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to S.polyrrhiza D-myo-
RT inositol-3-phosphate synthase mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryo, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INDUCTION.
RX PubMed=15464731; DOI=10.1016/j.abb.2004.08.002;
RA Seelan R.S., Parthasarathy L.K., Parthasarathy R.N.;
RT "E2F1 regulation of the human myo-inositol 1-phosphate synthase
RT (ISYNA1) gene promoter.";
RL Arch. Biochem. Biophys. 431:95-106(2004).
RN [10]
RP FUNCTION, ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15024000; DOI=10.1074/jbc.M312078200;
RA Ju S., Shaltiel G., Shamir A., Agam G., Greenberg M.L.;
RT "Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.";
RL J. Biol. Chem. 279:21759-21765(2004).
RN [11]
RP ENZYME REGULATION.
RX PubMed=17988368; DOI=10.1111/j.1399-5618.2007.00440.x;
RA Shamir A., Shaltiel G., Mark S., Bersudsky Y., Belmaker R.H., Agam G.;
RT "Human MIP synthase splice variants in bipolar disorder.";
RL Bipolar Disord. 9:766-771(2007).
RN [12]
RP ENZYME REGULATION.
RX PubMed=17901568;
RA Galit S., Shirley M., Ora K., Belmaker R.H., Galila A.;
RT "Effects of valproate derivatives on human brain myo-inositol-1-
RT phosphate (MIP) synthase activity and amphetamine-induced rearing.";
RL Pharmacol. Rep. 59:402-407(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol
CC 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC synthesis of all inositol-containing compounds.
CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = 1D-myo-inositol 3-
CC phosphate.
CC -!- COFACTOR: NAD.
CC -!- ENZYME REGULATION: Inhibited by mood-stabilizing drugs such as
CC valproate (VPA) and lithium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 mM for 6-phosphate;
CC KM=8 uM for NAD;
CC pH dependence:
CC Optimum pH is 8.0;
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC inositol from D-glucose 6-phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NPH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPH2-2; Sequence=VSP_032324;
CC Name=3;
CC IsoId=Q9NPH2-3; Sequence=VSP_046065;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, heart,
CC placenta and pancreas. Weakly expressed in blood leukocyte,
CC thymus, skeletal muscle and colon.
CC -!- INDUCTION: By glucose and lovastain. Up-regulation is prevented by
CC mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by
CC E2F1.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97151.1; Type=Frameshift; Positions=82, 85, 496;
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DR EMBL; AF207640; AAG35698.1; -; mRNA.
DR EMBL; AF220530; AAF26444.1; -; mRNA.
DR EMBL; AF220259; AAF26739.1; -; Genomic_DNA.
DR EMBL; AF220250; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220251; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220252; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220253; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220254; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220255; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220256; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220257; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220258; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF086921; AAP97151.1; ALT_FRAME; mRNA.
DR EMBL; AK001325; BAA91626.1; -; mRNA.
DR EMBL; AK021526; BAB13837.1; -; mRNA.
DR EMBL; AK092179; BAG52493.1; -; mRNA.
DR EMBL; AL137749; CAB70904.1; -; mRNA.
DR EMBL; AC008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84703.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84705.1; -; Genomic_DNA.
DR EMBL; BC004320; AAH04320.1; -; mRNA.
DR EMBL; BC018952; AAH18952.1; -; mRNA.
DR EMBL; BC066902; AAH66902.1; -; mRNA.
DR PIR; T46317; T46317.
DR RefSeq; NP_001164409.1; NM_001170938.1.
DR RefSeq; NP_001240318.1; NM_001253389.1.
DR RefSeq; NP_057452.1; NM_016368.4.
DR UniGene; Hs.405873; -.
DR ProteinModelPortal; Q9NPH2; -.
DR SMR; Q9NPH2; 6-512.
DR IntAct; Q9NPH2; 4.
DR MINT; MINT-4942504; -.
DR STRING; 9606.ENSP00000315147; -.
DR PhosphoSite; Q9NPH2; -.
DR DMDM; 74734304; -.
DR REPRODUCTION-2DPAGE; IPI00549569; -.
DR PaxDb; Q9NPH2; -.
DR PRIDE; Q9NPH2; -.
DR DNASU; 51477; -.
DR Ensembl; ENST00000338128; ENSP00000337746; ENSG00000105655.
DR Ensembl; ENST00000457269; ENSP00000415458; ENSG00000105655.
DR Ensembl; ENST00000578963; ENSP00000475677; ENSG00000105655.
DR GeneID; 51477; -.
DR KEGG; hsa:51477; -.
DR UCSC; uc002nje.2; human.
DR CTD; 51477; -.
DR GeneCards; GC19M018545; -.
DR HGNC; HGNC:29821; ISYNA1.
DR HPA; CAB020720; -.
DR HPA; HPA007931; -.
DR HPA; HPA008232; -.
DR MIM; 611670; gene.
DR neXtProt; NX_Q9NPH2; -.
DR PharmGKB; PA164721116; -.
DR eggNOG; COG1260; -.
DR HOVERGEN; HBG061200; -.
DR InParanoid; Q9NPH2; -.
DR KO; K01858; -.
DR OMA; NPVLYAP; -.
DR OrthoDB; EOG74J97N; -.
DR PhylomeDB; Q9NPH2; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00823; UER00787.
DR ChiTaRS; ISYNA1; human.
DR GenomeRNAi; 51477; -.
DR NextBio; 55121; -.
DR PRO; PR:Q9NPH2; -.
DR ArrayExpress; Q9NPH2; -.
DR Bgee; Q9NPH2; -.
DR CleanEx; HS_ISYNA1; -.
DR Genevestigator; Q9NPH2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; TAS:Reactome.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 2.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR11510; PTHR11510; 1.
DR Pfam; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; NAD; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1 558 Inositol-3-phosphate synthase 1.
FT /FTId=PRO_0000324628.
FT VAR_SEQ 1 128 Missing (in isoform 2).
FT /FTId=VSP_032324.
FT VAR_SEQ 40 93 Missing (in isoform 3).
FT /FTId=VSP_046065.
FT CONFLICT 17 17 G -> S (in Ref. 3; AAP97151).
FT CONFLICT 35 35 E -> K (in Ref. 3; AAP97151).
FT CONFLICT 57 57 P -> T (in Ref. 3; AAP97151).
FT CONFLICT 82 82 R -> Q (in Ref. 3; AAP97151).
FT CONFLICT 91 91 Missing (in Ref. 3; AAP97151).
FT CONFLICT 155 155 K -> N (in Ref. 1; AAG35698).
FT CONFLICT 193 193 D -> N (in Ref. 3; AAP97151).
FT CONFLICT 368 368 P -> Q (in Ref. 8; AAH66902).
FT CONFLICT 392 392 S -> G (in Ref. 8; AAH66902).
FT CONFLICT 414 414 H -> R (in Ref. 4; BAG52493).
FT CONFLICT 471 471 P -> R (in Ref. 8; AAH66902).
FT CONFLICT 514 514 S -> C (in Ref. 4; BAA91626).
SQ SEQUENCE 558 AA; 61068 MW; 3A1009D941A5F87D CRC64;
MEAAAQFFVE SPDVVYGPEA IEAQYEYRTT RVSREGGVLK VHPTSTRFTF RTARQVPRLG
VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR SGRKEANYYG SLTQAGTVSL GLDAEGQEVF
VPFSAVLPMV APNDLVFDGW DISSLNLAEA MRRAKVLDWG LQEQLWPHME ALRPRPSVYI
PEFIAANQSA RADNLIPGSR AQQLEQIRRD IRDFRSSAGL DKVIVLWTAN TERFCEVIPG
LNDTAENLLR TIELGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQHRVFVG
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG ENLSAPLQFR SKEVSKSNVV
DDMVQSNPVL YTPGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
LLAAPIMLDL ALLTELCQRV SFCTDMDPEP QTFHPVLSLL SFLFKAPLVP PGSPVVNALF
RQRSCIENIL RACVGLPPQN HMLLEHKMER PGPSLKRVGP VAATYPMLNK KGPVPAATNG
CTGDANGHLQ EEPPMPTT
//
ID INO1_HUMAN Reviewed; 558 AA.
AC Q9NPH2; B3KRT1; G5E9U0; Q6NXT5; Q7Z525; Q9BT65; Q9H2Y2; Q9NSU0;
read moreAC Q9NVW7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Inositol-3-phosphate synthase 1;
DE Short=IPS 1;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase;
DE Short=MI-1-P synthase;
DE Short=MIP synthase;
DE Short=hIPS;
DE AltName: Full=Myo-inositol 1-phosphate synthase A1;
DE Short=hINO1;
GN Name=ISYNA1; Synonyms=INO1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Hepatoma;
RX PubMed=12941308; DOI=10.1016/S0003-9861(03)00388-6;
RA Guan G., Dai P., Shechter I.;
RT "cDNA cloning and gene expression analysis of human myo-inositol 1-
RT phosphate synthase.";
RL Arch. Biochem. Biophys. 417:251-259(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=17121280;
RA Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F.,
RA Parthasarathy R.N.;
RT "Mammalian inositol 3-phosphate synthase: its role in the biosynthesis
RT of brain inositol and its clinical use as a psychoactive agent.";
RL Subcell. Biochem. 39:293-314(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou Y., Yu L., Zhao E.P., Hua Y.M., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to S.polyrrhiza D-myo-
RT inositol-3-phosphate synthase mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryo, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INDUCTION.
RX PubMed=15464731; DOI=10.1016/j.abb.2004.08.002;
RA Seelan R.S., Parthasarathy L.K., Parthasarathy R.N.;
RT "E2F1 regulation of the human myo-inositol 1-phosphate synthase
RT (ISYNA1) gene promoter.";
RL Arch. Biochem. Biophys. 431:95-106(2004).
RN [10]
RP FUNCTION, ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15024000; DOI=10.1074/jbc.M312078200;
RA Ju S., Shaltiel G., Shamir A., Agam G., Greenberg M.L.;
RT "Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.";
RL J. Biol. Chem. 279:21759-21765(2004).
RN [11]
RP ENZYME REGULATION.
RX PubMed=17988368; DOI=10.1111/j.1399-5618.2007.00440.x;
RA Shamir A., Shaltiel G., Mark S., Bersudsky Y., Belmaker R.H., Agam G.;
RT "Human MIP synthase splice variants in bipolar disorder.";
RL Bipolar Disord. 9:766-771(2007).
RN [12]
RP ENZYME REGULATION.
RX PubMed=17901568;
RA Galit S., Shirley M., Ora K., Belmaker R.H., Galila A.;
RT "Effects of valproate derivatives on human brain myo-inositol-1-
RT phosphate (MIP) synthase activity and amphetamine-induced rearing.";
RL Pharmacol. Rep. 59:402-407(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol
CC 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC synthesis of all inositol-containing compounds.
CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = 1D-myo-inositol 3-
CC phosphate.
CC -!- COFACTOR: NAD.
CC -!- ENZYME REGULATION: Inhibited by mood-stabilizing drugs such as
CC valproate (VPA) and lithium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 mM for 6-phosphate;
CC KM=8 uM for NAD;
CC pH dependence:
CC Optimum pH is 8.0;
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC inositol from D-glucose 6-phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NPH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPH2-2; Sequence=VSP_032324;
CC Name=3;
CC IsoId=Q9NPH2-3; Sequence=VSP_046065;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, heart,
CC placenta and pancreas. Weakly expressed in blood leukocyte,
CC thymus, skeletal muscle and colon.
CC -!- INDUCTION: By glucose and lovastain. Up-regulation is prevented by
CC mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by
CC E2F1.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97151.1; Type=Frameshift; Positions=82, 85, 496;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF207640; AAG35698.1; -; mRNA.
DR EMBL; AF220530; AAF26444.1; -; mRNA.
DR EMBL; AF220259; AAF26739.1; -; Genomic_DNA.
DR EMBL; AF220250; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220251; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220252; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220253; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220254; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220255; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220256; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220257; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220258; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF086921; AAP97151.1; ALT_FRAME; mRNA.
DR EMBL; AK001325; BAA91626.1; -; mRNA.
DR EMBL; AK021526; BAB13837.1; -; mRNA.
DR EMBL; AK092179; BAG52493.1; -; mRNA.
DR EMBL; AL137749; CAB70904.1; -; mRNA.
DR EMBL; AC008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84703.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84705.1; -; Genomic_DNA.
DR EMBL; BC004320; AAH04320.1; -; mRNA.
DR EMBL; BC018952; AAH18952.1; -; mRNA.
DR EMBL; BC066902; AAH66902.1; -; mRNA.
DR PIR; T46317; T46317.
DR RefSeq; NP_001164409.1; NM_001170938.1.
DR RefSeq; NP_001240318.1; NM_001253389.1.
DR RefSeq; NP_057452.1; NM_016368.4.
DR UniGene; Hs.405873; -.
DR ProteinModelPortal; Q9NPH2; -.
DR SMR; Q9NPH2; 6-512.
DR IntAct; Q9NPH2; 4.
DR MINT; MINT-4942504; -.
DR STRING; 9606.ENSP00000315147; -.
DR PhosphoSite; Q9NPH2; -.
DR DMDM; 74734304; -.
DR REPRODUCTION-2DPAGE; IPI00549569; -.
DR PaxDb; Q9NPH2; -.
DR PRIDE; Q9NPH2; -.
DR DNASU; 51477; -.
DR Ensembl; ENST00000338128; ENSP00000337746; ENSG00000105655.
DR Ensembl; ENST00000457269; ENSP00000415458; ENSG00000105655.
DR Ensembl; ENST00000578963; ENSP00000475677; ENSG00000105655.
DR GeneID; 51477; -.
DR KEGG; hsa:51477; -.
DR UCSC; uc002nje.2; human.
DR CTD; 51477; -.
DR GeneCards; GC19M018545; -.
DR HGNC; HGNC:29821; ISYNA1.
DR HPA; CAB020720; -.
DR HPA; HPA007931; -.
DR HPA; HPA008232; -.
DR MIM; 611670; gene.
DR neXtProt; NX_Q9NPH2; -.
DR PharmGKB; PA164721116; -.
DR eggNOG; COG1260; -.
DR HOVERGEN; HBG061200; -.
DR InParanoid; Q9NPH2; -.
DR KO; K01858; -.
DR OMA; NPVLYAP; -.
DR OrthoDB; EOG74J97N; -.
DR PhylomeDB; Q9NPH2; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00823; UER00787.
DR ChiTaRS; ISYNA1; human.
DR GenomeRNAi; 51477; -.
DR NextBio; 55121; -.
DR PRO; PR:Q9NPH2; -.
DR ArrayExpress; Q9NPH2; -.
DR Bgee; Q9NPH2; -.
DR CleanEx; HS_ISYNA1; -.
DR Genevestigator; Q9NPH2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; TAS:Reactome.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 2.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR11510; PTHR11510; 1.
DR Pfam; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; NAD; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1 558 Inositol-3-phosphate synthase 1.
FT /FTId=PRO_0000324628.
FT VAR_SEQ 1 128 Missing (in isoform 2).
FT /FTId=VSP_032324.
FT VAR_SEQ 40 93 Missing (in isoform 3).
FT /FTId=VSP_046065.
FT CONFLICT 17 17 G -> S (in Ref. 3; AAP97151).
FT CONFLICT 35 35 E -> K (in Ref. 3; AAP97151).
FT CONFLICT 57 57 P -> T (in Ref. 3; AAP97151).
FT CONFLICT 82 82 R -> Q (in Ref. 3; AAP97151).
FT CONFLICT 91 91 Missing (in Ref. 3; AAP97151).
FT CONFLICT 155 155 K -> N (in Ref. 1; AAG35698).
FT CONFLICT 193 193 D -> N (in Ref. 3; AAP97151).
FT CONFLICT 368 368 P -> Q (in Ref. 8; AAH66902).
FT CONFLICT 392 392 S -> G (in Ref. 8; AAH66902).
FT CONFLICT 414 414 H -> R (in Ref. 4; BAG52493).
FT CONFLICT 471 471 P -> R (in Ref. 8; AAH66902).
FT CONFLICT 514 514 S -> C (in Ref. 4; BAA91626).
SQ SEQUENCE 558 AA; 61068 MW; 3A1009D941A5F87D CRC64;
MEAAAQFFVE SPDVVYGPEA IEAQYEYRTT RVSREGGVLK VHPTSTRFTF RTARQVPRLG
VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR SGRKEANYYG SLTQAGTVSL GLDAEGQEVF
VPFSAVLPMV APNDLVFDGW DISSLNLAEA MRRAKVLDWG LQEQLWPHME ALRPRPSVYI
PEFIAANQSA RADNLIPGSR AQQLEQIRRD IRDFRSSAGL DKVIVLWTAN TERFCEVIPG
LNDTAENLLR TIELGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQHRVFVG
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG ENLSAPLQFR SKEVSKSNVV
DDMVQSNPVL YTPGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
LLAAPIMLDL ALLTELCQRV SFCTDMDPEP QTFHPVLSLL SFLFKAPLVP PGSPVVNALF
RQRSCIENIL RACVGLPPQN HMLLEHKMER PGPSLKRVGP VAATYPMLNK KGPVPAATNG
CTGDANGHLQ EEPPMPTT
//
MIM
611670
*RECORD*
*FIELD* NO
611670
*FIELD* TI
*611670 INOSITOL-3-PHOSPHATE SYNTHASE 1; ISYNA1
;;MYOINOSITOL 1-PHOSPHATE SYNTHASE A1;;
read moreIPS
*FIELD* TX
DESCRIPTION
Myoinositol, the most common naturally occurring form of inositol, is a
component of plasma membrane phospholipids and functions as a cell
signaling molecule. ISYNA1 (EC 5.5.1.4), or IPS, is a rate-limiting
enzyme that catalyzes the de novo synthesis of myoinositol 1-phosphate
from glucose 6-phosphate (Seelan et al., 2004).
CLONING
By searching an EST database for homologs of yeast and plant Ips,
followed by RT-PCR and 3-prime RACE of HepG2 hepatoma cell line RNA,
Guan et al. (2003) cloned human IPS. The deduced 558-amino acid protein
has a calculated molecular mass of 61.1 kD and shares 66% and 86%
identity with yeast and mouse Ips, respectively. Northern blot analysis
detected a major 1.8-kb IPS transcript in all tissues examined. Highest
expression was in testis, followed by heart, pancreas, and placenta, and
lowest expression was in leukocytes, thymus, skeletal muscle, and colon.
GENE FUNCTION
Guan et al. (2003) found that glucose elevated expression of IPS mRNA 2-
to 4-fold in HepG2 cells. Lovastatin, an inhibitor of G protein
activation, upregulated IPS mRNA 2- to 3-fold in a time- and
concentration-dependent manner, suggesting that IPS expression is
regulated by a G protein-mediated signal transduction mechanism.
Seelan et al. (2004) identified the minimal promoter of ISYNA1 and
showed that it was upregulated in a dose-dependent manner by the
transcription factor E2F1 (189971), a cell cycle regulator, in
transfected HeLa cells. ISYNA1 induction was suppressed by ectopic
expression of RB1 (614041), which prevents cell progression through G1/S
phase when complexed with E2F1.
GENE STRUCTURE
Seelan et al. (2004) determined that the ISYNA1 gene contains 11 exons.
The promoter region contains a TATA-like element, but no canonical TATA
box. EMSA and antibody supershift analysis identified a functional
E2F-binding motif that overlaps an SP1 (189906) motif.
MAPPING
Seelan et al. (2004) stated that the ISYNA1 gene maps to chromosome
19p13.1 and that a related processed pseudogene maps to chromosome 4p15.
*FIELD* RF
1. Guan, G.; Dai, P.; Shechter, I.: cDNA cloning and gene expression
analysis of human myo-inositol 1-phosphate synthase. Arch. Biochem.
Biophys. 417: 251-259, 2003.
2. Seelan, R. S.; Parthasarathy, L. K.; Parthasarathy, R. N.: E2F1
regulation of the human myo-inositol 1-phosphate synthase (ISYNA1)
gene promoter. Arch. Biochem. Biophys. 431: 95-106, 2004.
*FIELD* CD
Patricia A. Hartz: 12/13/2007
*FIELD* ED
alopez: 06/17/2011
alopez: 10/21/2008
mgross: 12/13/2007
*RECORD*
*FIELD* NO
611670
*FIELD* TI
*611670 INOSITOL-3-PHOSPHATE SYNTHASE 1; ISYNA1
;;MYOINOSITOL 1-PHOSPHATE SYNTHASE A1;;
read moreIPS
*FIELD* TX
DESCRIPTION
Myoinositol, the most common naturally occurring form of inositol, is a
component of plasma membrane phospholipids and functions as a cell
signaling molecule. ISYNA1 (EC 5.5.1.4), or IPS, is a rate-limiting
enzyme that catalyzes the de novo synthesis of myoinositol 1-phosphate
from glucose 6-phosphate (Seelan et al., 2004).
CLONING
By searching an EST database for homologs of yeast and plant Ips,
followed by RT-PCR and 3-prime RACE of HepG2 hepatoma cell line RNA,
Guan et al. (2003) cloned human IPS. The deduced 558-amino acid protein
has a calculated molecular mass of 61.1 kD and shares 66% and 86%
identity with yeast and mouse Ips, respectively. Northern blot analysis
detected a major 1.8-kb IPS transcript in all tissues examined. Highest
expression was in testis, followed by heart, pancreas, and placenta, and
lowest expression was in leukocytes, thymus, skeletal muscle, and colon.
GENE FUNCTION
Guan et al. (2003) found that glucose elevated expression of IPS mRNA 2-
to 4-fold in HepG2 cells. Lovastatin, an inhibitor of G protein
activation, upregulated IPS mRNA 2- to 3-fold in a time- and
concentration-dependent manner, suggesting that IPS expression is
regulated by a G protein-mediated signal transduction mechanism.
Seelan et al. (2004) identified the minimal promoter of ISYNA1 and
showed that it was upregulated in a dose-dependent manner by the
transcription factor E2F1 (189971), a cell cycle regulator, in
transfected HeLa cells. ISYNA1 induction was suppressed by ectopic
expression of RB1 (614041), which prevents cell progression through G1/S
phase when complexed with E2F1.
GENE STRUCTURE
Seelan et al. (2004) determined that the ISYNA1 gene contains 11 exons.
The promoter region contains a TATA-like element, but no canonical TATA
box. EMSA and antibody supershift analysis identified a functional
E2F-binding motif that overlaps an SP1 (189906) motif.
MAPPING
Seelan et al. (2004) stated that the ISYNA1 gene maps to chromosome
19p13.1 and that a related processed pseudogene maps to chromosome 4p15.
*FIELD* RF
1. Guan, G.; Dai, P.; Shechter, I.: cDNA cloning and gene expression
analysis of human myo-inositol 1-phosphate synthase. Arch. Biochem.
Biophys. 417: 251-259, 2003.
2. Seelan, R. S.; Parthasarathy, L. K.; Parthasarathy, R. N.: E2F1
regulation of the human myo-inositol 1-phosphate synthase (ISYNA1)
gene promoter. Arch. Biochem. Biophys. 431: 95-106, 2004.
*FIELD* CD
Patricia A. Hartz: 12/13/2007
*FIELD* ED
alopez: 06/17/2011
alopez: 10/21/2008
mgross: 12/13/2007