ID INO1_HUMAN Reviewed; 558 AA. AC Q9NPH2; B3KRT1; G5E9U0; Q6NXT5; Q7Z525; Q9BT65; Q9H2Y2; Q9NSU0; Q9NVW7; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Inositol-3-phosphate synthase 1; DE Short=IPS 1; DE EC=5.5.1.4 {ECO:0000269|PubMed:15024000, ECO:0000269|PubMed:23902760}; 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND 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; DOI=10.1007/0-387-27600-9_12; 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 of RT 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-inositol-3- RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 (ISYNA1) RT gene promoter."; RL Arch. Biochem. Biophys. 431:95-106(2004). RN [10] RP FUNCTION, ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL 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 ACTIVITY 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 ACTIVITY 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-phosphate RT (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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-279 AND SER-357, AND RP MUTAGENESIS OF SER-177; SER-279 AND SER-357. RX PubMed=23902760; DOI=10.1074/jbc.m113.479121; RA Deranieh R.M., He Q., Caruso J.A., Greenberg M.L.; RT "Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel RT regulatory mechanism of inositol biosynthesis."; RL J. Biol. Chem. 288:26822-26833(2013). CC -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that CC catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1- CC phosphate in a NAD-dependent manner (PubMed:15024000, PubMed:23902760). CC Rate-limiting enzyme in the synthesis of all inositol-containing CC compounds (PubMed:15024000). {ECO:0000269|PubMed:15024000, CC ECO:0000269|PubMed:23902760}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate; CC Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548; CC EC=5.5.1.4; Evidence={ECO:0000269|PubMed:15024000, CC ECO:0000269|PubMed:23902760}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000269|PubMed:15024000}; CC -!- ACTIVITY REGULATION: Inhibited by mood-stabilizing drugs such as CC valproate (VPA) and lithium. {ECO:0000269|PubMed:17901568, CC ECO:0000269|PubMed:17988368}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.57 mM for 6-phosphate {ECO:0000269|PubMed:15024000}; CC KM=8 uM for NAD {ECO:0000269|PubMed:15024000}; CC pH dependence: CC Optimum pH is 8.0. {ECO:0000269|PubMed:15024000}; CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol CC from D-glucose 6-phosphate: step 1/2. CC -!- INTERACTION: CC Q9NPH2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-720563, EBI-3867333; CC Q9NPH2; Q9NUX5: POT1; NbExp=2; IntAct=EBI-720563, EBI-752420; CC Q9NPH2; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-720563, EBI-3650647; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11986}. 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 -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, heart, placenta CC and pancreas. Weakly expressed in blood leukocyte, thymus, skeletal CC muscle and colon. {ECO:0000269|PubMed:12941308}. CC -!- INDUCTION: By glucose and lovastain. Up-regulation is prevented by CC mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by E2F1. CC {ECO:0000269|PubMed:12941308, ECO:0000269|PubMed:15464731}. CC -!- PTM: Phosphorylation at Ser-279 and Ser-357 may be associated with a CC decrease in activity. {ECO:0000269|PubMed:23902760}. CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP97151.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS12379.1; -. [Q9NPH2-1] DR CCDS; CCDS54234.1; -. [Q9NPH2-3] DR CCDS; CCDS62603.1; -. [Q9NPH2-2] DR PIR; T46317; T46317. DR RefSeq; NP_001164409.1; NM_001170938.1. [Q9NPH2-3] DR RefSeq; NP_001240318.1; NM_001253389.1. [Q9NPH2-2] DR RefSeq; NP_057452.1; NM_016368.4. [Q9NPH2-1] DR AlphaFoldDB; Q9NPH2; -. DR SMR; Q9NPH2; -. DR BioGRID; 119562; 65. DR IntAct; Q9NPH2; 26. DR MINT; Q9NPH2; -. DR STRING; 9606.ENSP00000337746; -. DR DrugBank; DB01840; 2-Deoxy-D-Glucitol 6-(E)-Vinylhomophosphonate. DR DrugBank; DB04516; 2-Deoxy-Glucitol-6-Phosphate. DR DrugBank; DB09462; Glycerin. DR GlyGen; Q9NPH2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NPH2; -. DR PhosphoSitePlus; Q9NPH2; -. DR BioMuta; ISYNA1; -. DR DMDM; 74734304; -. DR REPRODUCTION-2DPAGE; IPI00549569; -. DR CPTAC; CPTAC-227; -. DR CPTAC; CPTAC-228; -. DR EPD; Q9NPH2; -. DR jPOST; Q9NPH2; -. DR MassIVE; Q9NPH2; -. DR MaxQB; Q9NPH2; -. DR PaxDb; 9606-ENSP00000337746; -. DR PeptideAtlas; Q9NPH2; -. DR ProteomicsDB; 34039; -. DR ProteomicsDB; 81997; -. [Q9NPH2-1] DR ProteomicsDB; 81998; -. [Q9NPH2-2] DR Pumba; Q9NPH2; -. DR Antibodypedia; 28044; 105 antibodies from 23 providers. DR DNASU; 51477; -. DR Ensembl; ENST00000338128.13; ENSP00000337746.7; ENSG00000105655.19. [Q9NPH2-1] DR Ensembl; ENST00000457269.8; ENSP00000415458.3; ENSG00000105655.19. [Q9NPH2-3] DR Ensembl; ENST00000578963.5; ENSP00000475677.1; ENSG00000105655.19. [Q9NPH2-2] DR GeneID; 51477; -. DR KEGG; hsa:51477; -. DR MANE-Select; ENST00000338128.13; ENSP00000337746.7; NM_016368.5; NP_057452.1. DR UCSC; uc002nja.3; human. [Q9NPH2-1] DR AGR; HGNC:29821; -. DR CTD; 51477; -. DR DisGeNET; 51477; -. DR GeneCards; ISYNA1; -. DR HGNC; HGNC:29821; ISYNA1. DR HPA; ENSG00000105655; Tissue enhanced (choroid plexus, testis). DR MIM; 611670; gene. DR neXtProt; NX_Q9NPH2; -. DR OpenTargets; ENSG00000105655; -. DR PharmGKB; PA164721116; -. DR VEuPathDB; HostDB:ENSG00000105655; -. DR eggNOG; KOG0693; Eukaryota. DR GeneTree; ENSGT00390000018395; -. DR HOGENOM; CLU_021486_2_1_1; -. DR InParanoid; Q9NPH2; -. DR OMA; VPKVGMM; -. DR OrthoDB; 1201882at2759; -. DR PhylomeDB; Q9NPH2; -. DR TreeFam; TF300382; -. DR BRENDA; 5.5.1.4; 2681. DR PathwayCommons; Q9NPH2; -. DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol. DR SignaLink; Q9NPH2; -. DR SIGNOR; Q9NPH2; -. DR UniPathway; UPA00823; UER00787. DR BioGRID-ORCS; 51477; 56 hits in 1162 CRISPR screens. DR ChiTaRS; ISYNA1; human. DR GenomeRNAi; 51477; -. DR Pharos; Q9NPH2; Tbio. DR PRO; PR:Q9NPH2; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9NPH2; Protein. DR Bgee; ENSG00000105655; Expressed in right testis and 182 other cell types or tissues. DR ExpressionAtlas; Q9NPH2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IMP:CACAO. DR GO; GO:0006021; P:inositol biosynthetic process; IGI:UniProtKB. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR002587; Myo-inos-1-P_Synthase. DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR11510:SF5; INOSITOL-3-PHOSPHATE SYNTHASE 1; 1. DR PANTHER; PTHR11510; MYO-INOSITOL-1 PHOSPHATE SYNTHASE; 1. DR Pfam; PF01658; Inos-1-P_synth; 1. DR Pfam; PF07994; NAD_binding_5; 1. DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q9NPH2; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Inositol biosynthesis; Isomerase; KW Lipid biosynthesis; Lipid metabolism; NAD; Phospholipid biosynthesis; KW Phospholipid metabolism; Phosphoprotein; Reference proteome. FT CHAIN 1..558 FT /note="Inositol-3-phosphate synthase 1" FT /id="PRO_0000324628" FT REGION 537..558 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 67 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 68 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 69 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 70 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 141 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 177 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 178 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 188 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 191 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 228 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 229 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 230 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 231 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 278 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 279 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 303 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 306 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 337 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 338 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 339 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 352 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 390 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 391 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 419 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT BINDING 420 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P11986" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:23902760" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:23902760" FT VAR_SEQ 1..128 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_032324" FT VAR_SEQ 40..93 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046065" FT MUTAGEN 177 FT /note="S->A,D: Decreases activity." FT /evidence="ECO:0000269|PubMed:23902760" FT MUTAGEN 279 FT /note="S->A,D: Decreases activity." FT /evidence="ECO:0000269|PubMed:23902760" FT MUTAGEN 357 FT /note="S->D: Decreases activity." FT /evidence="ECO:0000269|PubMed:23902760" FT CONFLICT 17 FT /note="G -> S (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="E -> K (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="P -> T (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="R -> Q (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="Missing (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="K -> N (in Ref. 1; AAG35698)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="D -> N (in Ref. 3; AAP97151)" FT /evidence="ECO:0000305" FT CONFLICT 368 FT /note="P -> Q (in Ref. 8; AAH66902)" FT /evidence="ECO:0000305" FT CONFLICT 392 FT /note="S -> G (in Ref. 8; AAH66902)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="H -> R (in Ref. 4; BAG52493)" FT /evidence="ECO:0000305" FT CONFLICT 471 FT /note="P -> R (in Ref. 8; AAH66902)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="S -> C (in Ref. 4; BAA91626)" FT /evidence="ECO:0000305" 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 //