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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

    Pathwayi: gluconeogenesis

    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)DescriptionActionsGraphical viewLength
    Metal bindingi69Magnesium 1By similarity1
    Metal bindingi98Magnesium 1By similarity1
    Metal bindingi98Magnesium 21
    Metal bindingi119Magnesium 21
    Metal bindingi119Magnesium 31
    Metal bindingi121Magnesium 2; via carbonyl oxygen1
    Metal bindingi122Magnesium 31
    Binding sitei141AMP1 Publication1
    Binding sitei265Substrate1
    Metal bindingi281Magnesium 31

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi18 – 22AMP1 Publication5
    Nucleotide bindingi28 – 32AMP1 Publication5
    Nucleotide bindingi113 – 114AMP1 Publication2

    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

    • cellular response to drug Source: UniProtKB
    • cellular response to magnesium ion Source: UniProtKB
    • dephosphorylation Source: UniProtKB
    • fructose 1,6-bisphosphate metabolic process Source: GO_Central
    • fructose 6-phosphate metabolic process Source: UniProtKB
    • fructose catabolic process Source: InterPro
    • fructose metabolic process Source: ProtInc
    • gluconeogenesis Source: UniProtKB
    • 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
    • sucrose biosynthetic process Source: GO_Central
    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.
    ZFISH:HS09189-MONOMER.
    BRENDAi3.1.3.11. 2681.
    ReactomeiR-HSA-70263. 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
    Proteomesi
    • UP000005640 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 (FBP1D)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive metabolic disorder characterized by impaired gluconeogenesis, and episodes of hypoglycemia and metabolic acidosis that can be lethal in newborn infants or young children.
    See also OMIM:229700
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_075492158R → W in FBP1D; unknown pathological significance. 1 PublicationCorresponds to variant rs766005419dbSNPEnsembl.1
    Natural variantiVAR_002380164G → S in FBP1D. 1 PublicationCorresponds to variant rs121918188dbSNPEnsembl.1
    Natural variantiVAR_002381177A → D in FBP1D. 1 PublicationCorresponds to variant rs121918189dbSNPEnsembl.1
    Natural variantiVAR_038812194F → S in FBP1D. 1 PublicationCorresponds to variant rs121918191dbSNPEnsembl.1
    Natural variantiVAR_038813284P → R in FBP1D. 1 PublicationCorresponds to variant rs121918192dbSNPEnsembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70Q → E: Increased affinity towards Ca(2+) and Mg(2+). 1 Publication1
    Mutagenesisi119D → A: Reduced activity. 1 Publication1
    Mutagenesisi122D → A: Reduced activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi2203.
    MalaCardsiFBP1.
    MIMi229700. phenotype.
    OpenTargetsiENSG00000165140.
    Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
    PharmGKBiPA28018.

    Chemistry databases

    ChEMBLiCHEMBL3975.
    DrugBankiDB00131. Adenosine monophosphate.

    Polymorphism and mutation databases

    BioMutaiFBP1.
    DMDMi311033495.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity1 Publication
    ChainiPRO_00002004982 – 338Fructose-1,6-bisphosphatase 1Add BLAST337

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineBy similarity1
    Modified residuei151N6-succinyllysineBy similarity1
    Modified residuei216PhosphotyrosineBy similarity1
    Modified residuei245PhosphotyrosineBy similarity1
    Modified residuei265PhosphotyrosineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP09467.
    MaxQBiP09467.
    PaxDbiP09467.
    PeptideAtlasiP09467.
    PRIDEiP09467.

    PTM databases

    DEPODiP09467.
    iPTMnetiP09467.
    PhosphoSitePlusiP09467.

    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

    BgeeiENSG00000165140.
    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
    itself8EBI-712740,EBI-712740
    BIN1O004994EBI-712740,EBI-719094
    FBP2O0075710EBI-712740,EBI-719781

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi108497. 28 interactors.
    DIPiDIP-46677N.
    IntActiP09467. 37 interactors.
    MINTiMINT-3006780.
    STRINGi9606.ENSP00000364475.

    Chemistry databases

    BindingDBiP09467.

    Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi14 – 24Combined sources11
    Helixi30 – 49Combined sources20
    Turni50 – 53Combined sources4
    Helixi54 – 57Combined sources4
    Turni58 – 61Combined sources4
    Helixi74 – 87Combined sources14
    Turni88 – 90Combined sources3
    Beta strandi92 – 97Combined sources6
    Helixi108 – 110Combined sources3
    Beta strandi111 – 122Combined sources12
    Helixi124 – 129Combined sources6
    Beta strandi133 – 141Combined sources9
    Beta strandi144 – 147Combined sources4
    Helixi150 – 153Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi161 – 178Combined sources18
    Beta strandi181 – 188Combined sources8
    Turni189 – 192Combined sources4
    Beta strandi193 – 198Combined sources6
    Beta strandi208 – 212Combined sources5
    Helixi214 – 219Combined sources6
    Helixi222 – 232Combined sources11
    Beta strandi235 – 237Combined sources3
    Helixi249 – 259Combined sources11
    Beta strandi262 – 265Combined sources4
    Beta strandi269 – 271Combined sources3
    Beta strandi275 – 277Combined sources3
    Turni278 – 281Combined sources4
    Helixi282 – 291Combined sources10
    Beta strandi295 – 297Combined sources3
    Beta strandi299 – 302Combined sources4
    Helixi303 – 305Combined sources3
    Beta strandi317 – 321Combined sources5
    Helixi322 – 334Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09467.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni122 – 125Substrate binding4
    Regioni213 – 216Substrate binding4
    Regioni244 – 249Substrate binding6
    Regioni275 – 277Substrate binding3

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiKOG1458. Eukaryota.
    COG0158. LUCA.
    GeneTreeiENSGT00390000015513.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP09467.
    KOiK03841.
    OMAiFNYIAAK.
    OrthoDBiEOG091G0AZP.
    PhylomeDBiP09467.
    TreeFamiTF314824.

    Family and domain databases

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    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 differs from that shown. Reason: Erroneous gene model prediction.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti215G → A in AAA35817 (PubMed:8387495).Curated1
    Sequence conflicti215G → A in AAC25774 (PubMed:10222032).Curated1
    Sequence conflicti337A → G in AAC25774 (PubMed:10222032).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_075492158R → W in FBP1D; unknown pathological significance. 1 PublicationCorresponds to variant rs766005419dbSNPEnsembl.1
    Natural variantiVAR_002380164G → S in FBP1D. 1 PublicationCorresponds to variant rs121918188dbSNPEnsembl.1
    Natural variantiVAR_002381177A → D in FBP1D. 1 PublicationCorresponds to variant rs121918189dbSNPEnsembl.1
    Natural variantiVAR_038812194F → S in FBP1D. 1 PublicationCorresponds to variant rs121918191dbSNPEnsembl.1
    Natural variantiVAR_022212218R → K.7 PublicationsCorresponds to variant rs1769259dbSNPEnsembl.1
    Natural variantiVAR_022213233F → I.1 PublicationCorresponds to variant rs2297085dbSNPEnsembl.1
    Natural variantiVAR_022214255R → L.1 PublicationCorresponds to variant rs28369761dbSNPEnsembl.1
    Natural variantiVAR_038813284P → R in FBP1D. 1 PublicationCorresponds to variant rs121918192dbSNPEnsembl.1
    Natural variantiVAR_002382325V → A.1 Publication1

    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.5. 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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108497. 28 interactors.
    DIPiDIP-46677N.
    IntActiP09467. 37 interactors.
    MINTiMINT-3006780.
    STRINGi9606.ENSP00000364475.

    Chemistry databases

    BindingDBiP09467.
    ChEMBLiCHEMBL3975.
    DrugBankiDB00131. Adenosine monophosphate.

    PTM databases

    DEPODiP09467.
    iPTMnetiP09467.
    PhosphoSitePlusiP09467.

    Polymorphism and mutation databases

    BioMutaiFBP1.
    DMDMi311033495.

    Proteomic databases

    EPDiP09467.
    MaxQBiP09467.
    PaxDbiP09467.
    PeptideAtlasiP09467.
    PRIDEiP09467.

    Protocols and materials databases

    DNASUi2203.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000375326; ENSP00000364475; ENSG00000165140.
    ENST00000415431; ENSP00000408025; ENSG00000165140.
    GeneIDi2203.
    KEGGihsa:2203.
    UCSCiuc004auw.5. human.

    Organism-specific databases

    CTDi2203.
    DisGeNETi2203.
    GeneCardsiFBP1.
    H-InvDBHIX0008191.
    HGNCiHGNC:3606. FBP1.
    HPAiCAB033869.
    HPA005857.
    HPA012513.
    MalaCardsiFBP1.
    MIMi229700. phenotype.
    611570. gene.
    neXtProtiNX_P09467.
    OpenTargetsiENSG00000165140.
    Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
    PharmGKBiPA28018.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1458. Eukaryota.
    COG0158. LUCA.
    GeneTreeiENSGT00390000015513.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP09467.
    KOiK03841.
    OMAiFNYIAAK.
    OrthoDBiEOG091G0AZP.
    PhylomeDBiP09467.
    TreeFamiTF314824.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciMetaCyc:HS09189-MONOMER.
    ZFISH:HS09189-MONOMER.
    BRENDAi3.1.3.11. 2681.
    ReactomeiR-HSA-70263. Gluconeogenesis.
    SABIO-RKP09467.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000165140.
    CleanExiHS_FBP1.
    ExpressionAtlasiP09467. baseline and differential.
    GenevisibleiP09467. HS.

    Family and domain databases

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    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...

    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: November 30, 2016
    This is version 187 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

    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 one 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.