Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.3 Publications

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme regulationi

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.5 Publications

Kineticsi

The kinetic constants are determined for the recombinant enzyme expressed in E.coli.

  1. KM=2.7 µM for fructose 1,6-biphosphate1 Publication

    Pathway:igluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi69 – 691Magnesium 1By similarity
    Metal bindingi98 – 981Magnesium 1By similarity
    Metal bindingi98 – 981Magnesium 2
    Metal bindingi119 – 1191Magnesium 2
    Metal bindingi119 – 1191Magnesium 3
    Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygen
    Metal bindingi122 – 1221Magnesium 3
    Binding sitei141 – 1411AMP1 Publication
    Binding sitei265 – 2651Substrate
    Metal bindingi281 – 2811Magnesium 3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 225AMP1 Publication
    Nucleotide bindingi28 – 325AMP1 Publication
    Nucleotide bindingi113 – 1142AMP1 Publication

    GO - Molecular functioni

    • AMP binding Source: UniProtKB
    • fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
    • identical protein binding Source: IntAct
    • metal ion binding Source: UniProtKB
    • monosaccharide binding Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: Reactome
    • cellular response to drug Source: UniProtKB
    • cellular response to magnesium ion Source: UniProtKB
    • dephosphorylation Source: UniProtKB
    • fructose 6-phosphate metabolic process Source: UniProtKB
    • fructose metabolic process Source: ProtInc
    • gluconeogenesis Source: UniProtKB
    • glucose metabolic process Source: Reactome
    • negative regulation of cell growth Source: UniProtKB
    • negative regulation of glycolytic process Source: UniProtKB
    • negative regulation of Ras protein signal transduction Source: UniProtKB
    • protein homotetramerization Source: UniProtKB
    • regulation of gluconeogenesis Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09189-MONOMER.
    BRENDAi3.1.3.11. 2681.
    ReactomeiREACT_1520. Gluconeogenesis.
    SABIO-RKP09467.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
    Short name:
    FBPase 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
    Liver FBPase
    Gene namesi
    Name:FBP1
    Synonyms:FBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:3606. FBP1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Involvement in diseasei

    Fructose-1,6-bisphosphatase deficiency (FBPD)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionInherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis (lactacidemia) in newborn infants or young children.

    See also OMIM:229700
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti164 – 1641G → S in FBPD. 1 Publication
    VAR_002380
    Natural varianti177 – 1771A → D in FBPD. 1 Publication
    VAR_002381
    Natural varianti194 – 1941F → S in FBPD. 1 Publication
    VAR_038812
    Natural varianti284 – 2841P → R in FBPD. 1 Publication
    VAR_038813

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701Q → E: Increased affinity towards Ca(2+) and Mg(2+). 1 Publication
    Mutagenesisi119 – 1191D → A: Reduced activity. 1 Publication
    Mutagenesisi122 – 1221D → A: Reduced activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi229700. phenotype.
    Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
    PharmGKBiPA28018.

    Chemistry

    DrugBankiDB00131. Adenosine monophosphate.

    Polymorphism and mutation databases

    BioMutaiFBP1.
    DMDMi311033495.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity1 Publication
    Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200498Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei151 – 1511N6-succinyllysineBy similarity
    Modified residuei216 – 2161PhosphotyrosineBy similarity
    Modified residuei265 – 2651Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09467.
    PaxDbiP09467.
    PRIDEiP09467.

    PTM databases

    DEPODiP09467.
    PhosphoSiteiP09467.

    Expressioni

    Tissue specificityi

    Expressed in pancreatic islets.1 Publication

    Inductioni

    Up-regulated in pancreatic islets of individuals with type 2 diabetes.1 Publication

    Gene expression databases

    BgeeiP09467.
    CleanExiHS_FBP1.
    ExpressionAtlasiP09467. baseline and differential.
    GenevisibleiP09467. HS.

    Organism-specific databases

    HPAiCAB033869.
    HPA005857.
    HPA012513.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-712740,EBI-712740
    BIN1O004994EBI-712740,EBI-719094
    FBP2O007576EBI-712740,EBI-719781

    Protein-protein interaction databases

    BioGridi108497. 24 interactions.
    DIPiDIP-46677N.
    IntActiP09467. 35 interactions.
    MINTiMINT-3006780.
    STRINGi9606.ENSP00000364475.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2411Combined sources
    Helixi30 – 4920Combined sources
    Turni50 – 534Combined sources
    Helixi54 – 574Combined sources
    Turni58 – 614Combined sources
    Helixi74 – 8714Combined sources
    Turni88 – 903Combined sources
    Beta strandi92 – 976Combined sources
    Helixi108 – 1103Combined sources
    Beta strandi111 – 12212Combined sources
    Helixi124 – 1296Combined sources
    Beta strandi133 – 1419Combined sources
    Beta strandi144 – 1474Combined sources
    Helixi150 – 1534Combined sources
    Helixi157 – 1593Combined sources
    Beta strandi161 – 17818Combined sources
    Beta strandi181 – 1888Combined sources
    Turni189 – 1924Combined sources
    Beta strandi193 – 1986Combined sources
    Beta strandi208 – 2125Combined sources
    Helixi214 – 2196Combined sources
    Helixi222 – 23211Combined sources
    Beta strandi235 – 2373Combined sources
    Helixi249 – 25911Combined sources
    Beta strandi262 – 2654Combined sources
    Beta strandi269 – 2713Combined sources
    Beta strandi275 – 2773Combined sources
    Turni278 – 2814Combined sources
    Helixi282 – 29110Combined sources
    Beta strandi295 – 2973Combined sources
    Beta strandi299 – 3024Combined sources
    Helixi303 – 3053Combined sources
    Beta strandi317 – 3215Combined sources
    Helixi322 – 33413Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FTAX-ray2.30A/B/C/D2-338[»]
    2FHYX-ray2.95A/D/H/L1-338[»]
    2FIEX-ray2.81A/D/H/L1-338[»]
    2FIXX-ray3.50A/D/H/L1-338[»]
    2JJKX-ray2.00A/B/C/D1-338[»]
    2VT5X-ray2.20A/B/C/D/E/F/G/H1-338[»]
    2WBBX-ray2.22A/B/C/D/E/F/G/H1-338[»]
    2WBDX-ray2.40A/B/C/D/E/F/G/H1-338[»]
    2Y5KX-ray2.10A/B/C/D1-338[»]
    2Y5LX-ray2.20A/B/C/D/E/F/G/H1-338[»]
    3A29X-ray2.60A/B/C/D2-338[»]
    3KBZX-ray2.45A/B/C/D2-338[»]
    3KC0X-ray2.80A/B/C/D2-338[»]
    3KC1X-ray2.25A/B/C/D2-338[»]
    4MJOX-ray2.40A/B/C/D/E/F/G/H1-338[»]
    ProteinModelPortaliP09467.
    SMRiP09467. Positions 10-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09467.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1254Substrate binding
    Regioni213 – 2164Substrate binding
    Regioni244 – 2496Substrate binding
    Regioni275 – 2773Substrate binding

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0158.
    GeneTreeiENSGT00390000015513.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP09467.
    KOiK03841.
    OMAiEANPMSW.
    OrthoDBiEOG7GJ6D9.
    PhylomeDBiP09467.
    TreeFamiTF314824.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09467-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR
    60 70 80 90 100
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED
    110 120 130 140 150
    KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE
    160 170 180 190 200
    KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD
    210 220 230 240 250
    VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV
    260 270 280 290 300
    ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK
    310 320 330
    EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ
    Length:338
    Mass (Da):36,842
    Last modified:November 2, 2010 - v5
    Checksum:iB3D270BCBB358B71
    GO

    Sequence cautioni

    The sequence AAC50207.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151G → A in AAA35817 (PubMed:8387495).Curated
    Sequence conflicti215 – 2151G → A in AAC25774 (PubMed:10222032).Curated
    Sequence conflicti337 – 3371A → G in AAC25774 (PubMed:10222032).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti164 – 1641G → S in FBPD. 1 Publication
    VAR_002380
    Natural varianti177 – 1771A → D in FBPD. 1 Publication
    VAR_002381
    Natural varianti194 – 1941F → S in FBPD. 1 Publication
    VAR_038812
    Natural varianti218 – 2181R → K.7 Publications
    Corresponds to variant rs1769259 [ dbSNP | Ensembl ].
    VAR_022212
    Natural varianti233 – 2331F → I.1 Publication
    Corresponds to variant rs2297085 [ dbSNP | Ensembl ].
    VAR_022213
    Natural varianti255 – 2551R → L.1 Publication
    Corresponds to variant rs28369761 [ dbSNP | Ensembl ].
    VAR_022214
    Natural varianti284 – 2841P → R in FBPD. 1 Publication
    VAR_038813
    Natural varianti325 – 3251V → A.1 Publication
    VAR_002382

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19922 mRNA. Translation: AAA35517.1.
    L10320 mRNA. Translation: AAA35817.1.
    D26054 mRNA. Translation: BAA05051.1.
    D26055 mRNA. Translation: BAA05052.1.
    D26056 mRNA. Translation: BAA05053.1.
    U21931
    , U21925, U21926, U21927, U21929, U21930 Genomic DNA. Translation: AAC50207.1. Sequence problems.
    AF073475 mRNA. Translation: AAC25774.1.
    AK223395 mRNA. Translation: BAD97115.1.
    AY866483 Genomic DNA. Translation: AAW34363.1.
    AL161728 Genomic DNA. Translation: CAH72692.1.
    BC012927 mRNA. Translation: AAH12927.1.
    U47919 mRNA. Translation: AAA89098.1.
    U47918 mRNA. Translation: AAA89097.1.
    CCDSiCCDS6712.1.
    PIRiA46666.
    RefSeqiNP_000498.2. NM_000507.3.
    NP_001121100.1. NM_001127628.1.
    UniGeneiHs.494496.

    Genome annotation databases

    EnsembliENST00000375326; ENSP00000364475; ENSG00000165140.
    ENST00000415431; ENSP00000408025; ENSG00000165140.
    GeneIDi2203.
    KEGGihsa:2203.
    UCSCiuc004auw.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Fructose bisphosphatase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19922 mRNA. Translation: AAA35517.1.
    L10320 mRNA. Translation: AAA35817.1.
    D26054 mRNA. Translation: BAA05051.1.
    D26055 mRNA. Translation: BAA05052.1.
    D26056 mRNA. Translation: BAA05053.1.
    U21931
    , U21925, U21926, U21927, U21929, U21930 Genomic DNA. Translation: AAC50207.1. Sequence problems.
    AF073475 mRNA. Translation: AAC25774.1.
    AK223395 mRNA. Translation: BAD97115.1.
    AY866483 Genomic DNA. Translation: AAW34363.1.
    AL161728 Genomic DNA. Translation: CAH72692.1.
    BC012927 mRNA. Translation: AAH12927.1.
    U47919 mRNA. Translation: AAA89098.1.
    U47918 mRNA. Translation: AAA89097.1.
    CCDSiCCDS6712.1.
    PIRiA46666.
    RefSeqiNP_000498.2. NM_000507.3.
    NP_001121100.1. NM_001127628.1.
    UniGeneiHs.494496.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FTAX-ray2.30A/B/C/D2-338[»]
    2FHYX-ray2.95A/D/H/L1-338[»]
    2FIEX-ray2.81A/D/H/L1-338[»]
    2FIXX-ray3.50A/D/H/L1-338[»]
    2JJKX-ray2.00A/B/C/D1-338[»]
    2VT5X-ray2.20A/B/C/D/E/F/G/H1-338[»]
    2WBBX-ray2.22A/B/C/D/E/F/G/H1-338[»]
    2WBDX-ray2.40A/B/C/D/E/F/G/H1-338[»]
    2Y5KX-ray2.10A/B/C/D1-338[»]
    2Y5LX-ray2.20A/B/C/D/E/F/G/H1-338[»]
    3A29X-ray2.60A/B/C/D2-338[»]
    3KBZX-ray2.45A/B/C/D2-338[»]
    3KC0X-ray2.80A/B/C/D2-338[»]
    3KC1X-ray2.25A/B/C/D2-338[»]
    4MJOX-ray2.40A/B/C/D/E/F/G/H1-338[»]
    ProteinModelPortaliP09467.
    SMRiP09467. Positions 10-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108497. 24 interactions.
    DIPiDIP-46677N.
    IntActiP09467. 35 interactions.
    MINTiMINT-3006780.
    STRINGi9606.ENSP00000364475.

    Chemistry

    BindingDBiP09467.
    ChEMBLiCHEMBL3975.
    DrugBankiDB00131. Adenosine monophosphate.

    PTM databases

    DEPODiP09467.
    PhosphoSiteiP09467.

    Polymorphism and mutation databases

    BioMutaiFBP1.
    DMDMi311033495.

    Proteomic databases

    MaxQBiP09467.
    PaxDbiP09467.
    PRIDEiP09467.

    Protocols and materials databases

    DNASUi2203.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000375326; ENSP00000364475; ENSG00000165140.
    ENST00000415431; ENSP00000408025; ENSG00000165140.
    GeneIDi2203.
    KEGGihsa:2203.
    UCSCiuc004auw.4. human.

    Organism-specific databases

    CTDi2203.
    GeneCardsiGC09M097365.
    H-InvDBHIX0008191.
    HGNCiHGNC:3606. FBP1.
    HPAiCAB033869.
    HPA005857.
    HPA012513.
    MIMi229700. phenotype.
    611570. gene.
    neXtProtiNX_P09467.
    Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
    PharmGKBiPA28018.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0158.
    GeneTreeiENSGT00390000015513.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP09467.
    KOiK03841.
    OMAiEANPMSW.
    OrthoDBiEOG7GJ6D9.
    PhylomeDBiP09467.
    TreeFamiTF314824.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciMetaCyc:HS09189-MONOMER.
    BRENDAi3.1.3.11. 2681.
    ReactomeiREACT_1520. Gluconeogenesis.
    SABIO-RKP09467.

    Miscellaneous databases

    ChiTaRSiFBP1. human.
    EvolutionaryTraceiP09467.
    GenomeRNAii2203.
    NextBioi8907.
    PROiP09467.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP09467.
    CleanExiHS_FBP1.
    ExpressionAtlasiP09467. baseline and differential.
    GenevisibleiP09467. HS.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Activation of the fructose 1,6-bisphosphatase gene by 1,25-dihydroxyvitamin D3 during monocytic differentiation."
      Solomon D.H., Raynal M.-C., Tejwani G.A., Cayre Y.E.
      Proc. Natl. Acad. Sci. U.S.A. 85:6904-6908(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-218.
    2. "Isolation of a human liver fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. Role of Asp-118 and Asp-121 in catalysis."
      El-Maghrabi M.R., Gidh-Jain M., Austin L.R., Pilkis S.J.
      J. Biol. Chem. 268:9466-9472(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, MUTAGENESIS OF ASP-119 AND ASP-122, VARIANT LYS-218.
      Tissue: Liver.
    3. "cDNA sequences encoding human fructose 1,6-bisphosphatase from monocytes, liver and kidney: application of monocytes to molecular analysis of human fructose 1,6-bisphosphatase deficiency."
      Kikawa Y., Inuzuka M., Takano T., Shigematsu Y., Nakai A., Yamamoto Y., Jin B.Y., Koga J., Taketo A., Sudo M.
      Biochem. Biophys. Res. Commun. 199:687-693(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-218.
      Tissue: Kidney, Liver and Monocyte.
    4. "Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron organization, localization to chromosome bands 9q22.2-q22.3, and mutation screening in subjects with fructose-1,6-bisphosphatase deficiency."
      El-Maghrabi M.R., Lang A.J., Jiang W., Yamagata K., Stoffel M., Takeda J., Fernald A.A., le Beau M.M., Bell G.I., Baker L., Pilkis S.J.
      Genomics 27:520-525(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-218.
      Tissue: Liver.
    5. "cDNA sequence and kinetic properties of human lung fructose(1, 6)bisphosphatase."
      Skalecki K., Rakus D., Wisniewski J.R., Kolodziej J., Dzugaj A.
      Arch. Biochem. Biophys. 365:1-9(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT LYS-218.
      Tissue: Lung.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-218.
      Tissue: Thymus.
    7. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-218; ILE-233 AND LEU-255.
    8. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Urinary bladder.
    10. "Liver fructose-1,6-bisphosphatase cDNA: trans-complementation of fission yeast and characterization of two human transcripts."
      Bertolotti R., Armbruster-Hilbert L., Okayama H.
      Differentiation 59:51-60(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 320-338.
      Tissue: Liver.
    11. "Expression of human fructose-1,6-bisphosphatase in the liver of transgenic mice results in increased glycerol gluconeogenesis."
      Lamont B.J., Visinoni S., Fam B.C., Kebede M., Weinrich B., Papapostolou S., Massinet H., Proietto J., Favaloro J., Andrikopoulos S.
      Endocrinology 147:2764-2772(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions."
      Zarzycki M., Maciaszczyk E., Dzugaj A.
      FEBS Lett. 581:1347-1350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-70.
    13. "Fructose-1,6-bisphosphatase overexpression in pancreatic beta-cells results in reduced insulin secretion: a new mechanism for fat-induced impairment of beta-cell function."
      Kebede M., Favaloro J., Gunton J.E., Laybutt D.R., Shaw M., Wong N., Fam B.C., Aston-Mourney K., Rantzau C., Zulli A., Proietto J., Andrikopoulos S.
      Diabetes 57:1887-1895(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    14. Cited for: FUNCTION.
    15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase."
      Zhang Y., Liang J.-Y., Huang S., Ke H., Lipscomb W.N.
      Biochemistry 32:1844-1857(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND SUBSTRATE ANALOGS, COFACTOR.
    17. "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors."
      Xue Y., Huang S., Liang J.-Y., Zhang Y., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 91:12482-12486(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE; AMP AND ZINC, SUBUNIT, COFACTOR, ENZYME REGULATION.
    18. "Benzoxazole benzenesulfonamides as allosteric inhibitors of fructose-1,6-bisphosphatase."
      Lai C., Gum R.J., Daly M., Fry E.H., Hutchins C., Abad-Zapatero C., von Geldern T.W.
      Bioorg. Med. Chem. Lett. 16:1807-1810(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH BENZOXAZOLE BENZENESULFONAMIDES, SUBUNIT, ENZYME REGULATION.
    19. "Benzoxazole benzenesulfonamides are novel allosteric inhibitors of fructose-1,6-bisphosphatase with a distinct binding mode."
      von Geldern T.W., Lai C., Gum R.J., Daly M., Sun C., Fry E.H., Abad-Zapatero C.
      Bioorg. Med. Chem. Lett. 16:1811-1815(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH BENZOXAZOLE BENZENESULFONAMIDES, SUBUNIT, ENZYME REGULATION.
    20. "Allosteric FBPase inhibitors gain 10(5) times in potency when simultaneously binding two neighboring AMP sites."
      Hebeisen P., Kuhn B., Kohler P., Gubler M., Huber W., Kitas E., Schott B., Benz J., Joseph C., Ruf A.
      Bioorg. Med. Chem. Lett. 18:4708-4712(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH AROMATIC SULFONYLUREA AMP ANALOGS, SUBUNIT, ENZYME REGULATION.
    21. "Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency."
      Kikawa Y., Inuzuka M., Jin B.Y., Kaji S., Koga J., Yamamoto Y., Fujisawa K., Hata I., Nakai A., Shigematsu Y., Mizunuma H., Taketo A., Mayumi M., Sudo M.
      Am. J. Hum. Genet. 61:852-861(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FBPD SER-164 AND ASP-177, VARIANT ALA-325.
    22. "Two newly identified genomic mutations in a Japanese female patient with fructose-1,6-bisphosphatase (FBPase) deficiency."
      Matsuura T., Chinen Y., Arashiro R., Katsuren K., Tamura T., Hyakuna N., Ohta T.
      Mol. Genet. Metab. 76:207-210(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FBPD SER-194 AND ARG-284.

    Entry informationi

    Entry nameiF16P1_HUMAN
    AccessioniPrimary (citable) accession number: P09467
    Secondary accession number(s): O75571, Q53F94, Q96E46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 2, 2010
    Last modified: July 22, 2015
    This is version 173 of the entry and version 5 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.