Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NPH2

- INO1_HUMAN

UniProt

Q9NPH2 - INO1_HUMAN

Protein

Inositol-3-phosphate synthase 1

Gene

ISYNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Catalytic activityi

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

    Cofactori

    NAD.1 Publication

    Enzyme regulationi

    Inhibited by mood-stabilizing drugs such as valproate (VPA) and lithium.2 Publications

    Kineticsi

    1. KM=0.57 mM for 6-phosphate1 Publication
    2. KM=8 µM for NAD1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. inositol-3-phosphate synthase activity Source: Reactome

    GO - Biological processi

    1. inositol biosynthetic process Source: UniProtKB-UniPathway
    2. inositol phosphate metabolic process Source: Reactome
    3. phospholipid biosynthetic process Source: UniProtKB-KW
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_150352. 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
    Short name:
    hIPS
    Myo-inositol 1-phosphate synthase A1
    Short name:
    hINO1
    Gene namesi
    Name:ISYNA1
    Synonyms:INO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:29821. ISYNA1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164721116.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 558558Inositol-3-phosphate synthase 1PRO_0000324628Add
    BLAST

    Proteomic databases

    MaxQBiQ9NPH2.
    PaxDbiQ9NPH2.
    PRIDEiQ9NPH2.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00549569.

    PTM databases

    PhosphoSiteiQ9NPH2.

    Expressioni

    Tissue specificityi

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

    Inductioni

    By glucose and lovastain. Up-regulation is prevented by mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by E2F1.2 Publications

    Gene expression databases

    ArrayExpressiQ9NPH2.
    BgeeiQ9NPH2.
    CleanExiHS_ISYNA1.
    GenevestigatoriQ9NPH2.

    Organism-specific databases

    HPAiCAB020720.
    HPA007931.
    HPA008232.

    Interactioni

    Protein-protein interaction databases

    BioGridi119562. 4 interactions.
    IntActiQ9NPH2. 4 interactions.
    MINTiMINT-4942504.
    STRINGi9606.ENSP00000315147.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPH2.
    SMRiQ9NPH2. Positions 6-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1260.
    HOVERGENiHBG061200.
    InParanoidiQ9NPH2.
    KOiK01858.
    OMAiNPVLYAP.
    OrthoDBiEOG74J97N.
    PhylomeDBiQ9NPH2.
    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.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPH2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEAAAQFFVE SPDVVYGPEA IEAQYEYRTT RVSREGGVLK VHPTSTRFTF    50
    RTARQVPRLG VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR SGRKEANYYG 100
    SLTQAGTVSL GLDAEGQEVF VPFSAVLPMV APNDLVFDGW DISSLNLAEA 150
    MRRAKVLDWG LQEQLWPHME ALRPRPSVYI PEFIAANQSA RADNLIPGSR 200
    AQQLEQIRRD IRDFRSSAGL DKVIVLWTAN TERFCEVIPG LNDTAENLLR 250
    TIELGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQHRVFVG 300
    GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG ENLSAPLQFR 350
    SKEVSKSNVV DDMVQSNPVL YTPGEEPDHC VVIKYVPYVG DSKRALDEYT 400
    SELMLGGTNT LVLHNTCEDS LLAAPIMLDL ALLTELCQRV SFCTDMDPEP 450
    QTFHPVLSLL SFLFKAPLVP PGSPVVNALF RQRSCIENIL RACVGLPPQN 500
    HMLLEHKMER PGPSLKRVGP VAATYPMLNK KGPVPAATNG CTGDANGHLQ 550
    EEPPMPTT 558
    Length:558
    Mass (Da):61,068
    Last modified:October 1, 2000 - v1
    Checksum:i3A1009D941A5F87D
    GO
    Isoform 2 (identifier: Q9NPH2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-128: Missing.

    Show »
    Length:430
    Mass (Da):47,146
    Checksum:i8C21453E5B3E4D88
    GO
    Isoform 3 (identifier: Q9NPH2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-93: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:504
    Mass (Da):55,136
    Checksum:i84D7E719BBB98135
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171G → S in AAP97151. 1 PublicationCurated
    Sequence conflicti35 – 351E → K in AAP97151. 1 PublicationCurated
    Sequence conflicti57 – 571P → T in AAP97151. 1 PublicationCurated
    Sequence conflicti82 – 821R → Q in AAP97151. 1 PublicationCurated
    Sequence conflicti91 – 911Missing in AAP97151. 1 PublicationCurated
    Sequence conflicti155 – 1551K → N in AAG35698. (PubMed:12941308)Curated
    Sequence conflicti193 – 1931D → N in AAP97151. 1 PublicationCurated
    Sequence conflicti368 – 3681P → Q in AAH66902. (PubMed:15489334)Curated
    Sequence conflicti392 – 3921S → G in AAH66902. (PubMed:15489334)Curated
    Sequence conflicti414 – 4141H → R in BAG52493. (PubMed:14702039)Curated
    Sequence conflicti471 – 4711P → R in AAH66902. (PubMed:15489334)Curated
    Sequence conflicti514 – 5141S → C in BAA91626. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 128128Missing in isoform 2. 1 PublicationVSP_032324Add
    BLAST
    Alternative sequencei40 – 9354Missing in isoform 3. 1 PublicationVSP_046065Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207640 mRNA. Translation: AAG35698.1.
    AF220530 mRNA. Translation: AAF26444.1.
    AF220259
    , 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.
    CCDSiCCDS12379.1. [Q9NPH2-1]
    CCDS54234.1. [Q9NPH2-3]
    CCDS62603.1. [Q9NPH2-2]
    PIRiT46317.
    RefSeqiNP_001164409.1. NM_001170938.1. [Q9NPH2-3]
    NP_001240318.1. NM_001253389.1. [Q9NPH2-2]
    NP_057452.1. NM_016368.4. [Q9NPH2-1]
    UniGeneiHs.405873.

    Genome annotation databases

    GeneIDi51477.
    KEGGihsa:51477.
    UCSCiuc002nja.2. human. [Q9NPH2-1]
    uc002nje.2. human.

    Polymorphism databases

    DMDMi74734304.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207640 mRNA. Translation: AAG35698.1 .
    AF220530 mRNA. Translation: AAF26444.1 .
    AF220259
    , 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 .
    CCDSi CCDS12379.1. [Q9NPH2-1 ]
    CCDS54234.1. [Q9NPH2-3 ]
    CCDS62603.1. [Q9NPH2-2 ]
    PIRi T46317.
    RefSeqi NP_001164409.1. NM_001170938.1. [Q9NPH2-3 ]
    NP_001240318.1. NM_001253389.1. [Q9NPH2-2 ]
    NP_057452.1. NM_016368.4. [Q9NPH2-1 ]
    UniGenei Hs.405873.

    3D structure databases

    ProteinModelPortali Q9NPH2.
    SMRi Q9NPH2. Positions 6-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119562. 4 interactions.
    IntActi Q9NPH2. 4 interactions.
    MINTi MINT-4942504.
    STRINGi 9606.ENSP00000315147.

    PTM databases

    PhosphoSitei Q9NPH2.

    Polymorphism databases

    DMDMi 74734304.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00549569.

    Proteomic databases

    MaxQBi Q9NPH2.
    PaxDbi Q9NPH2.
    PRIDEi Q9NPH2.

    Protocols and materials databases

    DNASUi 51477.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 51477.
    KEGGi hsa:51477.
    UCSCi uc002nja.2. human. [Q9NPH2-1 ]
    uc002nje.2. human.

    Organism-specific databases

    CTDi 51477.
    GeneCardsi GC19M018545.
    HGNCi HGNC:29821. ISYNA1.
    HPAi CAB020720.
    HPA007931.
    HPA008232.
    MIMi 611670. gene.
    neXtProti NX_Q9NPH2.
    PharmGKBi PA164721116.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1260.
    HOVERGENi HBG061200.
    InParanoidi Q9NPH2.
    KOi K01858.
    OMAi NPVLYAP.
    OrthoDBi EOG74J97N.
    PhylomeDBi Q9NPH2.
    TreeFami TF300382.

    Enzyme and pathway databases

    UniPathwayi UPA00823 ; UER00787 .
    Reactomei REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.

    Miscellaneous databases

    ChiTaRSi ISYNA1. human.
    GenomeRNAii 51477.
    NextBioi 55121.
    PROi Q9NPH2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPH2.
    Bgeei Q9NPH2.
    CleanExi HS_ISYNA1.
    Genevestigatori Q9NPH2.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR002587. Myo-inos-1-P_Synthase.
    IPR013021. Myo-inos-1-P_Synthase_GAPDH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11510. PTHR11510. 1 hit.
    Pfami PF01658. Inos-1-P_synth. 1 hit.
    PF07994. NAD_binding_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015578. Myoinos-ppht_syn. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiINO1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPH2
    Secondary accession number(s): B3KRT1
    , G5E9U0, Q6NXT5, Q7Z525, Q9BT65, Q9H2Y2, Q9NSU0, Q9NVW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3