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Q9NPH2 (INO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol-3-phosphate synthase 1

Short name=IPS 1
EC=5.5.1.4
Alternative name(s):
Myo-inositol 1-phosphate synthase
Short name=MI-1-P synthase
Short name=MIP synthase
Short name=hIPS
Myo-inositol 1-phosphate synthase A1
Short name=hINO1
Gene names
Name:ISYNA1
Synonyms:INO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds. Ref.10

Catalytic activity

D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate. Ref.10

Cofactor

NAD. Ref.10

Enzyme regulation

Inhibited by mood-stabilizing drugs such as valproate (VPA) and lithium. Ref.11 Ref.12

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in testis, ovary, heart, placenta and pancreas. Weakly expressed in blood leukocyte, thymus, skeletal muscle and colon. Ref.1

Induction

By glucose and lovastain. Up-regulation is prevented by mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by E2F1. Ref.1 Ref.9 Ref.11 Ref.12

Sequence similarities

Belongs to the myo-inositol 1-phosphate synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.57 mM for 6-phosphate Ref.10

KM=8 µM for NAD

pH dependence:

Optimum pH is 8.0.

Sequence caution

The sequence AAP97151.1 differs from that shown. Reason: Frameshift at positions 82, 85 and 496.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NPH2-1)

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.
Isoform 2 (identifier: Q9NPH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.
Isoform 3 (identifier: Q9NPH2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-93: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Inositol-3-phosphate synthase 1
PRO_0000324628

Natural variations

Alternative sequence1 – 128128Missing in isoform 2.
VSP_032324
Alternative sequence40 – 9354Missing in isoform 3.
VSP_046065

Experimental info

Sequence conflict171G → S in AAP97151. Ref.3
Sequence conflict351E → K in AAP97151. Ref.3
Sequence conflict571P → T in AAP97151. Ref.3
Sequence conflict821R → Q in AAP97151. Ref.3
Sequence conflict911Missing in AAP97151. Ref.3
Sequence conflict1551K → N in AAG35698. Ref.1
Sequence conflict1931D → N in AAP97151. Ref.3
Sequence conflict3681P → Q in AAH66902. Ref.8
Sequence conflict3921S → G in AAH66902. Ref.8
Sequence conflict4141H → R in BAG52493. Ref.4
Sequence conflict4711P → R in AAH66902. Ref.8
Sequence conflict5141S → C in BAA91626. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3A1009D941A5F87D

FASTA55861,068
        10         20         30         40         50         60 
MEAAAQFFVE SPDVVYGPEA IEAQYEYRTT RVSREGGVLK VHPTSTRFTF RTARQVPRLG 

        70         80         90        100        110        120 
VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR SGRKEANYYG SLTQAGTVSL GLDAEGQEVF 

       130        140        150        160        170        180 
VPFSAVLPMV APNDLVFDGW DISSLNLAEA MRRAKVLDWG LQEQLWPHME ALRPRPSVYI 

       190        200        210        220        230        240 
PEFIAANQSA RADNLIPGSR AQQLEQIRRD IRDFRSSAGL DKVIVLWTAN TERFCEVIPG 

       250        260        270        280        290        300 
LNDTAENLLR TIELGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQHRVFVG 

       310        320        330        340        350        360 
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG ENLSAPLQFR SKEVSKSNVV 

       370        380        390        400        410        420 
DDMVQSNPVL YTPGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS 

       430        440        450        460        470        480 
LLAAPIMLDL ALLTELCQRV SFCTDMDPEP QTFHPVLSLL SFLFKAPLVP PGSPVVNALF 

       490        500        510        520        530        540 
RQRSCIENIL RACVGLPPQN HMLLEHKMER PGPSLKRVGP VAATYPMLNK KGPVPAATNG 

       550 
CTGDANGHLQ EEPPMPTT 

« Hide

Isoform 2 [UniParc].

Checksum: 8C21453E5B3E4D88
Show »

FASTA43047,146
Isoform 3 [UniParc].

Checksum: 84D7E719BBB98135
Show »

FASTA50455,136

References

« Hide 'large scale' references
[1]"cDNA cloning and gene expression analysis of human myo-inositol 1-phosphate synthase."
Guan G., Dai P., Shechter I.
Arch. Biochem. Biophys. 417:251-259(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
Tissue: Hepatoma.
[2]"Mammalian inositol 3-phosphate synthase: its role in the biosynthesis of brain inositol and its clinical use as a psychoactive agent."
Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F., Parthasarathy R.N.
Subcell. Biochem. 39:293-314(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[3]"Cloning of a novel human cDNA homology to S.polyrrhiza D-myo-inositol-3-phosphate synthase mRNA."
Zhou Y., Yu L., Zhao E.P., Hua Y.M., Xin Y.R., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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 AND 3).
Tissue: Embryo and Teratocarcinoma.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Brain and Uterus.
[9]"E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1) gene promoter."
Seelan R.S., Parthasarathy L.K., Parthasarathy R.N.
Arch. Biochem. Biophys. 431:95-106(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast."
Ju S., Shaltiel G., Shamir A., Agam G., Greenberg M.L.
J. Biol. Chem. 279:21759-21765(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[11]"Human MIP synthase splice variants in bipolar disorder."
Shamir A., Shaltiel G., Mark S., Bersudsky Y., Belmaker R.H., Agam G.
Bipolar Disord. 9:766-771(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[12]"Effects of valproate derivatives on human brain myo-inositol-1-phosphate (MIP) synthase activity and amphetamine-induced rearing."
Galit S., Shirley M., Ora K., Belmaker R.H., Galila A.
Pharmacol. Rep. 59:402-407(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF207640 mRNA. Translation: AAG35698.1.
AF220530 mRNA. Translation: AAF26444.1.
AF220259 expand/collapse EMBL AC list , AF220250, AF220251, AF220252, AF220253, AF220254, AF220255, AF220256, AF220257, AF220258 Genomic DNA. Translation: AAF26739.1.
AF086921 mRNA. Translation: AAP97151.1. Frameshift.
AK001325 mRNA. Translation: BAA91626.1.
AK021526 mRNA. Translation: BAB13837.1.
AK092179 mRNA. Translation: BAG52493.1.
AL137749 mRNA. Translation: CAB70904.1.
AC008397 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84703.1.
CH471106 Genomic DNA. Translation: EAW84705.1.
BC004320 mRNA. Translation: AAH04320.1.
BC018952 mRNA. Translation: AAH18952.1.
BC066902 mRNA. Translation: AAH66902.1.
PIRT46317.
RefSeqNP_001164409.1. NM_001170938.1.
NP_001240318.1. NM_001253389.1.
NP_057452.1. NM_016368.4.
UniGeneHs.405873.

3D structure databases

ProteinModelPortalQ9NPH2.
SMRQ9NPH2. Positions 6-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119562. 4 interactions.
IntActQ9NPH2. 4 interactions.
MINTMINT-4942504.
STRING9606.ENSP00000315147.

PTM databases

PhosphoSiteQ9NPH2.

Polymorphism databases

DMDM74734304.

2D gel databases

REPRODUCTION-2DPAGEIPI00549569.

Proteomic databases

PaxDbQ9NPH2.
PRIDEQ9NPH2.

Protocols and materials databases

DNASU51477.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338128; ENSP00000337746; ENSG00000105655. [Q9NPH2-1]
ENST00000457269; ENSP00000415458; ENSG00000105655. [Q9NPH2-3]
ENST00000578963; ENSP00000475677; ENSG00000105655. [Q9NPH2-2]
GeneID51477.
KEGGhsa:51477.
UCSCuc002nja.2. human. [Q9NPH2-1]
uc002nje.2. human.

Organism-specific databases

CTD51477.
GeneCardsGC19M018545.
HGNCHGNC:29821. ISYNA1.
HPACAB020720.
HPA007931.
HPA008232.
MIM611670. gene.
neXtProtNX_Q9NPH2.
PharmGKBPA164721116.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1260.
HOVERGENHBG061200.
InParanoidQ9NPH2.
KOK01858.
OMANPVLYAP.
OrthoDBEOG74J97N.
PhylomeDBQ9NPH2.
TreeFamTF300382.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00823; UER00787.

Gene expression databases

ArrayExpressQ9NPH2.
BgeeQ9NPH2.
CleanExHS_ISYNA1.
GenevestigatorQ9NPH2.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR002587. Myo-inos-1-P_Synthase.
IPR013021. Myo-inos-1-P_Synthase_GAPDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11510. PTHR11510. 1 hit.
PfamPF01658. Inos-1-P_synth. 1 hit.
PF07994. NAD_binding_5. 1 hit.
[Graphical view]
PIRSFPIRSF015578. Myoinos-ppht_syn. 1 hit.
ProtoNetSearch...

Other

ChiTaRSISYNA1. human.
GenomeRNAi51477.
NextBio55121.
PROQ9NPH2.
SOURCESearch...

Entry information

Entry nameINO1_HUMAN
AccessionPrimary (citable) accession number: Q9NPH2
Secondary accession number(s): B3KRT1 expand/collapse secondary AC list , G5E9U0, Q6NXT5, Q7Z525, Q9BT65, Q9H2Y2, Q9NSU0, Q9NVW7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM