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)

P09467

- F16P1_HUMAN

UniProt

P09467 - F16P1_HUMAN

Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

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 163 (01 Oct 2014)
      Sequence version 5 (02 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 3 magnesium 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

    Pathwayi

    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

    1. AMP binding Source: UniProtKB
    2. fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. metal ion binding Source: UniProtKB
    5. monosaccharide binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular response to drug Source: UniProtKB
    3. cellular response to magnesium ion Source: UniProtKB
    4. dephosphorylation Source: UniProtKB
    5. fructose 6-phosphate metabolic process Source: UniProtKB
    6. fructose metabolic process Source: ProtInc
    7. gluconeogenesis Source: UniProtKB
    8. glucose metabolic process Source: Reactome
    9. negative regulation of cell growth Source: UniProtKB
    10. negative regulation of glycolytic process Source: UniProtKB
    11. negative regulation of Ras protein signal transduction Source: UniProtKB
    12. protein homotetramerization Source: UniProtKB
    13. regulation of gluconeogenesis Source: UniProtKB
    14. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09189-MONOMER.
    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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:3606. FBP1.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Fructose-1,6-bisphosphatase deficiency (FBPD) [MIM:229700]: Inherited 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP09467.
    PaxDbiP09467.
    PRIDEiP09467.

    PTM databases

    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

    ArrayExpressiP09467.
    BgeeiP09467.
    CleanExiHS_FBP1.
    GenevestigatoriP09467.

    Organism-specific databases

    HPAiHPA005857.
    HPA012513.

    Interactioni

    Subunit structurei

    Homotetramer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-712740,EBI-712740
    BIN1O004994EBI-712740,EBI-719094

    Protein-protein interaction databases

    BioGridi108497. 20 interactions.
    IntActiP09467. 17 interactions.
    MINTiMINT-3006780.
    STRINGi9606.ENSP00000364475.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP09467.
    KOiK03841.
    OMAiSSFTTCV.
    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

    MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR    50
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED 100
    KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE 150
    KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD 200
    VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV 250
    ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK 300
    EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ 338
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi311033495.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Fructose bisphosphatase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6712.1.
    PIRi A46666.
    RefSeqi NP_000498.2. NM_000507.3.
    NP_001121100.1. NM_001127628.1.
    UniGenei Hs.494496.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FTA X-ray 2.30 A/B/C/D 2-338 [» ]
    2FHY X-ray 2.95 A/D/H/L 1-338 [» ]
    2FIE X-ray 2.81 A/D/H/L 1-338 [» ]
    2FIX X-ray 3.50 A/D/H/L 1-338 [» ]
    2JJK X-ray 2.00 A/B/C/D 1-338 [» ]
    2VT5 X-ray 2.20 A/B/C/D/E/F/G/H 1-338 [» ]
    2WBB X-ray 2.22 A/B/C/D/E/F/G/H 1-338 [» ]
    2WBD X-ray 2.40 A/B/C/D/E/F/G/H 1-338 [» ]
    2Y5K X-ray 2.10 A/B/C/D 1-338 [» ]
    2Y5L X-ray 2.20 A/B/C/D/E/F/G/H 1-338 [» ]
    3A29 X-ray 2.60 A/B/C/D 2-338 [» ]
    3KBZ X-ray 2.45 A/B/C/D 2-338 [» ]
    3KC0 X-ray 2.80 A/B/C/D 2-338 [» ]
    3KC1 X-ray 2.25 A/B/C/D 2-338 [» ]
    4MJO X-ray 2.40 A/B/C/D/E/F/G/H 1-338 [» ]
    ProteinModelPortali P09467.
    SMRi P09467. Positions 10-336.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108497. 20 interactions.
    IntActi P09467. 17 interactions.
    MINTi MINT-3006780.
    STRINGi 9606.ENSP00000364475.

    Chemistry

    BindingDBi P09467.
    ChEMBLi CHEMBL3975.
    DrugBanki DB00131. Adenosine monophosphate.

    PTM databases

    PhosphoSitei P09467.

    Polymorphism databases

    DMDMi 311033495.

    Proteomic databases

    MaxQBi P09467.
    PaxDbi P09467.
    PRIDEi P09467.

    Protocols and materials databases

    DNASUi 2203.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375326 ; ENSP00000364475 ; ENSG00000165140 .
    ENST00000415431 ; ENSP00000408025 ; ENSG00000165140 .
    GeneIDi 2203.
    KEGGi hsa:2203.
    UCSCi uc004auw.4. human.

    Organism-specific databases

    CTDi 2203.
    GeneCardsi GC09M097365.
    H-InvDB HIX0008191.
    HGNCi HGNC:3606. FBP1.
    HPAi HPA005857.
    HPA012513.
    MIMi 229700. phenotype.
    611570. gene.
    neXtProti NX_P09467.
    Orphaneti 348. Fructose-1,6-bisphosphatase deficiency.
    PharmGKBi PA28018.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0158.
    HOGENOMi HOG000191265.
    HOVERGENi HBG005627.
    InParanoidi P09467.
    KOi K03841.
    OMAi SSFTTCV.
    OrthoDBi EOG7GJ6D9.
    PhylomeDBi P09467.
    TreeFami TF314824.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci MetaCyc:HS09189-MONOMER.
    Reactomei REACT_1520. Gluconeogenesis.
    SABIO-RK P09467.

    Miscellaneous databases

    EvolutionaryTracei P09467.
    GenomeRNAii 2203.
    NextBioi 8907.
    PROi P09467.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09467.
    Bgeei P09467.
    CleanExi HS_FBP1.
    Genevestigatori P09467.

    Family and domain databases

    HAMAPi MF_01855. FBPase_class1.
    InterProi IPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view ]
    PANTHERi PTHR11556. PTHR11556. 1 hit.
    Pfami PF00316. FBPase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSi PR00115. F16BPHPHTASE.
    PROSITEi PS00124. FBPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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: October 1, 2014
    This is version 163 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