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Protein

Inositol-3-phosphate synthase 1

Gene

Isyna1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

NAD+By similarity

Pathwayi: myo-inositol biosynthesis

This protein is involved in step 1 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 1 (Isyna1)
  2. Inositol monophosphatase 1 (Impa1), Inositol monophosphatase 2 (Impa2), Inositol monophosphatase 3 (Impad1)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Inositol biosynthesis, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
UniPathwayiUPA00823; UER00787.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol-3-phosphate synthase 1 (EC:5.5.1.4)
Short name:
IPS 1
Alternative name(s):
Myo-inositol 1-phosphate synthase
Short name:
MI-1-P synthase
Short name:
MIP synthase
Gene namesi
Name:Isyna1
Synonyms:Ino1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1919030. Isyna1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557Inositol-3-phosphate synthase 1PRO_0000324630Add
BLAST

Proteomic databases

EPDiQ9JHU9.
MaxQBiQ9JHU9.
PaxDbiQ9JHU9.
PRIDEiQ9JHU9.

2D gel databases

REPRODUCTION-2DPAGEIPI00119886.
Q9JHU9.

PTM databases

iPTMnetiQ9JHU9.
PhosphoSiteiQ9JHU9.
SwissPalmiQ9JHU9.

Expressioni

Tissue specificityi

In testis, it is expressed in Sertoli cells. Highly expressed in 2 types of germ cells, pachytene spermatocytes and round spermatids.1 Publication

Gene expression databases

BgeeiQ9JHU9.
CleanExiMM_ISYNA1.
GenevisibleiQ9JHU9. MM.

Interactioni

Protein-protein interaction databases

BioGridi214923. 1 interaction.
IntActiQ9JHU9. 4 interactions.
MINTiMINT-4129716.
STRINGi10090.ENSMUSP00000019283.

Structurei

3D structure databases

ProteinModelPortaliQ9JHU9.
SMRiQ9JHU9. Positions 7-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0693. Eukaryota.
COG1260. LUCA.
GeneTreeiENSGT00390000018395.
HOGENOMiHOG000013469.
HOVERGENiHBG061200.
InParanoidiQ9JHU9.
KOiK01858.
OMAiNPVLYAP.
OrthoDBiEOG74J97N.
PhylomeDBiQ9JHU9.
TreeFamiTF300382.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002587. Myo-inos-1-P_Synthase.
IPR013021. Myo-inos-1-P_Synthase_GAPDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11510. PTHR11510. 1 hit.
PfamiPF01658. Inos-1-P_synth. 1 hit.
PF07994. NAD_binding_5. 1 hit.
[Graphical view]
PIRSFiPIRSF015578. Myoinos-ppht_syn. 1 hit.
SUPFAMiSSF51735. SSF51735. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9JHU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAAEILVD SPDVVYSPET IEARYEYRTT RVSREGGVLR VQPRATRFTF
60 70 80 90 100
RTARQVPRLG VMLVGWGGNN GSTLTAAVLA NRLRLTWPTR TGRKEANYYG
110 120 130 140 150
SLTQAGTVNL GLDENGREVF VPFSALLPMV APNDLVFDGW DISSLNLAEA
160 170 180 190 200
MRRAQVLDCG LQEQLWPHME SLRPRPSVYI PEFIAANQTA RADNLIPGTR
210 220 230 240 250
AQQLEQIRKD IRDFRSSAGL DKVIVLWTAN TERFCEVVPG RNDTAENLLH
260 270 280 290 300
TIQLGLEVSP STLFAVASIL EDCAFLNGSP QNTLVPGALE LASQRHVFVG
310 320 330 340 350
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPLQFR
360 370 380 390 400
SKEVTKSSVV DDMVHSNHVL YAPGERPDHC VVIKYVPYVG DSKRALDEYT
410 420 430 440 450
SELMLGGTNT LVLHNTCEDS LLAAPIMLDL VLLTELCQRV SFCTDSDPEP
460 470 480 490 500
QGFHTVLSLL SFLFKAPLVP PGSPVVNALF RQRSCIENIF RACVGLPPQN
510 520 530 540 550
HMLLEHKMER PGPGIKPGEV VATSPLPCKK EPTPATNGCT GDANGHPQAP

TPKLSTA
Length:557
Mass (Da):60,932
Last modified:October 1, 2000 - v1
Checksum:i91166BD2A2C53ADA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288525 mRNA. Translation: AAF90201.1.
AK005029 mRNA. Translation: BAB23756.1.
AK079323 mRNA. Translation: BAC37607.1.
BC003458 mRNA. Translation: AAH03458.1.
CCDSiCCDS22373.1.
RefSeqiNP_076116.1. NM_023627.1.
UniGeneiMm.29357.

Genome annotation databases

EnsembliENSMUST00000019283; ENSMUSP00000019283; ENSMUSG00000019139.
GeneIDi71780.
KEGGimmu:71780.
UCSCiuc009mav.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF288525 mRNA. Translation: AAF90201.1.
AK005029 mRNA. Translation: BAB23756.1.
AK079323 mRNA. Translation: BAC37607.1.
BC003458 mRNA. Translation: AAH03458.1.
CCDSiCCDS22373.1.
RefSeqiNP_076116.1. NM_023627.1.
UniGeneiMm.29357.

3D structure databases

ProteinModelPortaliQ9JHU9.
SMRiQ9JHU9. Positions 7-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214923. 1 interaction.
IntActiQ9JHU9. 4 interactions.
MINTiMINT-4129716.
STRINGi10090.ENSMUSP00000019283.

PTM databases

iPTMnetiQ9JHU9.
PhosphoSiteiQ9JHU9.
SwissPalmiQ9JHU9.

2D gel databases

REPRODUCTION-2DPAGEIPI00119886.
Q9JHU9.

Proteomic databases

EPDiQ9JHU9.
MaxQBiQ9JHU9.
PaxDbiQ9JHU9.
PRIDEiQ9JHU9.

Protocols and materials databases

DNASUi71780.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019283; ENSMUSP00000019283; ENSMUSG00000019139.
GeneIDi71780.
KEGGimmu:71780.
UCSCiuc009mav.1. mouse.

Organism-specific databases

CTDi51477.
MGIiMGI:1919030. Isyna1.

Phylogenomic databases

eggNOGiKOG0693. Eukaryota.
COG1260. LUCA.
GeneTreeiENSGT00390000018395.
HOGENOMiHOG000013469.
HOVERGENiHBG061200.
InParanoidiQ9JHU9.
KOiK01858.
OMAiNPVLYAP.
OrthoDBiEOG74J97N.
PhylomeDBiQ9JHU9.
TreeFamiTF300382.

Enzyme and pathway databases

UniPathwayiUPA00823; UER00787.
ReactomeiR-MMU-1855183. Synthesis of IP2, IP, and Ins in the cytosol.

Miscellaneous databases

ChiTaRSiIsyna1. mouse.
PROiQ9JHU9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHU9.
CleanExiMM_ISYNA1.
GenevisibleiQ9JHU9. MM.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR002587. Myo-inos-1-P_Synthase.
IPR013021. Myo-inos-1-P_Synthase_GAPDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11510. PTHR11510. 1 hit.
PfamiPF01658. Inos-1-P_synth. 1 hit.
PF07994. NAD_binding_5. 1 hit.
[Graphical view]
PIRSFiPIRSF015578. Myoinos-ppht_syn. 1 hit.
SUPFAMiSSF51735. SSF51735. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 [MRNA].
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Liver.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Characterization of the expression and regulation of genes necessary for myo-inositol biosynthesis and transport in the seminiferous epithelium."
    Chauvin T.R., Griswold M.D.
    Biol. Reprod. 70:744-751(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiINO1_MOUSE
AccessioniPrimary (citable) accession number: Q9JHU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.