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P46926

- GNPI1_HUMAN

UniProt

P46926 - GNPI1_HUMAN

Protein

Glucosamine-6-phosphate isomerase 1

Gene

GNPDA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo By similarity.By similarity

    Catalytic activityi

    Alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei72 – 721Proton acceptor; for enolization stepBy similarity
    Active sitei141 – 1411For ring-opening stepBy similarity
    Active sitei143 – 1431Proton acceptor; for ring-opening stepBy similarity
    Active sitei148 – 1481For ring-opening stepBy similarity

    GO - Molecular functioni

    1. glucosamine-6-phosphate deaminase activity Source: UniProtKB
    2. hydrolase activity Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. generation of precursor metabolites and energy Source: UniProtKB
    3. glucosamine catabolic process Source: UniProtKB
    4. N-acetylglucosamine metabolic process Source: InterPro
    5. single fertilization Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    SABIO-RKP46926.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucosamine-6-phosphate isomerase 1 (EC:3.5.99.6)
    Alternative name(s):
    Glucosamine-6-phosphate deaminase 1
    Short name:
    GNPDA 1
    Short name:
    GlcN6P deaminase 1
    Oscillin
    Gene namesi
    Name:GNPDA1
    Synonyms:GNPI, HLN, KIAA0060
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4417. GNPDA1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28796.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Glucosamine-6-phosphate isomerase 1PRO_0000160122Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP46926.
    PaxDbiP46926.
    PeptideAtlasiP46926.
    PRIDEiP46926.

    PTM databases

    PhosphoSiteiP46926.

    Expressioni

    Gene expression databases

    ArrayExpressiP46926.
    BgeeiP46926.
    CleanExiHS_GNPDA1.
    GenevestigatoriP46926.

    Organism-specific databases

    HPAiHPA000499.
    HPA046891.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    BioGridi115325. 25 interactions.
    IntActiP46926. 1 interaction.
    STRINGi9606.ENSP00000311876.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87
    Helixi9 – 2719
    Beta strandi35 – 395
    Helixi43 – 5715
    Beta strandi66 – 749
    Helixi85 – 928
    Helixi94 – 963
    Helixi101 – 1033
    Helixi114 – 12714
    Beta strandi132 – 1365
    Beta strandi157 – 1615
    Helixi164 – 1707
    Helixi171 – 1733
    Turni174 – 1763
    Helixi178 – 1803
    Beta strandi183 – 1875
    Helixi190 – 1945
    Beta strandi199 – 2035
    Helixi206 – 2083
    Helixi209 – 2168
    Helixi225 – 2317
    Beta strandi233 – 2408
    Helixi241 – 2444
    Helixi249 – 2579
    Helixi259 – 2624
    Helixi263 – 2653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NE7X-ray1.75A/B/C/D/E/F1-289[»]
    ProteinModelPortaliP46926.
    SMRiP46926. Positions 1-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46926.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0363.
    HOGENOMiHOG000064979.
    HOVERGENiHBG002546.
    InParanoidiP46926.
    KOiK02564.
    PhylomeDBiP46926.
    TreeFamiTF300841.

    Family and domain databases

    HAMAPiMF_01241. GlcN6P_deamin.
    InterProiIPR006148. Glc/Gal-6P_isomerase.
    IPR004547. Glucosamine6P_isomerase.
    IPR018321. Glucosamine6P_isomerase_CS.
    [Graphical view]
    PANTHERiPTHR11280. PTHR11280. 1 hit.
    PfamiPF01182. Glucosamine_iso. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00502. nagB. 1 hit.
    PROSITEiPS01161. GLC_GALNAC_ISOMERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46926-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK    50
    KLIEYYKNGD LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH 100
    PENTHILDGN AVDLQAECDA FEEKIKAAGG IELFVGGIGP DGHIAFNEPG 150
    SSLVSRTRVK TLAMDTILAN ARFFDGELTK VPTMALTVGV GTVMDAREVM 200
    ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD EDATLELKVK 250
    TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD 289
    Length:289
    Mass (Da):32,669
    Last modified:November 1, 1995 - v1
    Checksum:i4111F655D574F74F
    GO

    Sequence cautioni

    The sequence BAA06544.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF048826 mRNA. Translation: AAC05123.1.
    AJ002231 mRNA. Translation: CAA05259.1.
    AF029914 mRNA. Translation: AAB84217.1.
    AF035809
    , AF035804, AF035805, AF035806, AF035807, AF035808 Genomic DNA. Translation: AAB88748.1.
    D31766 mRNA. Translation: BAA06544.2. Different initiation.
    AC005740 Genomic DNA. Translation: AAC62119.1.
    CH471062 Genomic DNA. Translation: EAW61890.1.
    CH471062 Genomic DNA. Translation: EAW61891.1.
    CH471062 Genomic DNA. Translation: EAW61892.1.
    CH471062 Genomic DNA. Translation: EAW61893.1.
    BC012853 mRNA. Translation: AAH12853.1.
    BC020769 mRNA. Translation: AAH20769.1.
    BC022322 mRNA. Translation: AAH22322.1.
    CCDSiCCDS4272.1.
    RefSeqiNP_005462.1. NM_005471.4.
    XP_006714810.1. XM_006714747.1.
    UniGeneiHs.633853.

    Genome annotation databases

    EnsembliENST00000311337; ENSP00000311876; ENSG00000113552.
    ENST00000500692; ENSP00000424275; ENSG00000113552.
    ENST00000503794; ENSP00000423485; ENSG00000113552.
    ENST00000508177; ENSP00000423674; ENSG00000113552.
    GeneIDi10007.
    KEGGihsa:10007.
    UCSCiuc003lmf.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF048826 mRNA. Translation: AAC05123.1 .
    AJ002231 mRNA. Translation: CAA05259.1 .
    AF029914 mRNA. Translation: AAB84217.1 .
    AF035809
    , AF035804 , AF035805 , AF035806 , AF035807 , AF035808 Genomic DNA. Translation: AAB88748.1 .
    D31766 mRNA. Translation: BAA06544.2 . Different initiation.
    AC005740 Genomic DNA. Translation: AAC62119.1 .
    CH471062 Genomic DNA. Translation: EAW61890.1 .
    CH471062 Genomic DNA. Translation: EAW61891.1 .
    CH471062 Genomic DNA. Translation: EAW61892.1 .
    CH471062 Genomic DNA. Translation: EAW61893.1 .
    BC012853 mRNA. Translation: AAH12853.1 .
    BC020769 mRNA. Translation: AAH20769.1 .
    BC022322 mRNA. Translation: AAH22322.1 .
    CCDSi CCDS4272.1.
    RefSeqi NP_005462.1. NM_005471.4.
    XP_006714810.1. XM_006714747.1.
    UniGenei Hs.633853.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NE7 X-ray 1.75 A/B/C/D/E/F 1-289 [» ]
    ProteinModelPortali P46926.
    SMRi P46926. Positions 1-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115325. 25 interactions.
    IntActi P46926. 1 interaction.
    STRINGi 9606.ENSP00000311876.

    PTM databases

    PhosphoSitei P46926.

    Proteomic databases

    MaxQBi P46926.
    PaxDbi P46926.
    PeptideAtlasi P46926.
    PRIDEi P46926.

    Protocols and materials databases

    DNASUi 10007.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311337 ; ENSP00000311876 ; ENSG00000113552 .
    ENST00000500692 ; ENSP00000424275 ; ENSG00000113552 .
    ENST00000503794 ; ENSP00000423485 ; ENSG00000113552 .
    ENST00000508177 ; ENSP00000423674 ; ENSG00000113552 .
    GeneIDi 10007.
    KEGGi hsa:10007.
    UCSCi uc003lmf.4. human.

    Organism-specific databases

    CTDi 10007.
    GeneCardsi GC05M141360.
    HGNCi HGNC:4417. GNPDA1.
    HPAi HPA000499.
    HPA046891.
    MIMi 601798. gene.
    neXtProti NX_P46926.
    PharmGKBi PA28796.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0363.
    HOGENOMi HOG000064979.
    HOVERGENi HBG002546.
    InParanoidi P46926.
    KOi K02564.
    PhylomeDBi P46926.
    TreeFami TF300841.

    Enzyme and pathway databases

    SABIO-RK P46926.

    Miscellaneous databases

    EvolutionaryTracei P46926.
    GeneWikii GNPDA1.
    GenomeRNAii 10007.
    NextBioi 37805.
    PROi P46926.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46926.
    Bgeei P46926.
    CleanExi HS_GNPDA1.
    Genevestigatori P46926.

    Family and domain databases

    HAMAPi MF_01241. GlcN6P_deamin.
    InterProi IPR006148. Glc/Gal-6P_isomerase.
    IPR004547. Glucosamine6P_isomerase.
    IPR018321. Glucosamine6P_isomerase_CS.
    [Graphical view ]
    PANTHERi PTHR11280. PTHR11280. 1 hit.
    Pfami PF01182. Glucosamine_iso. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00502. nagB. 1 hit.
    PROSITEi PS01161. GLC_GALNAC_ISOMERASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity."
      Wolosker H., Kline D., Bian Y., Blackshaw S., Cameron A.M., Fralich T.J., Schnaar R.L., Snyder S.H.
      FASEB J. 12:91-99(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization."
      Shevchenko V., Hogben M., Ekong R., Parrington J., Lai F.A.
      Gene 216:31-38(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    3. Hirata S., Koh T., Hoshi K.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Testis.
    4. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
      Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
      DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Ovary and Skin.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study."
      Arreola R., Valderrama B., Morante M.L., Horjales E.
      FEBS Lett. 551:63-70(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiGNPI1_HUMAN
    AccessioniPrimary (citable) accession number: P46926
    Secondary accession number(s): D3DQE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 139 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3