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Entry version 210 (18 Sep 2019)
Sequence version 5 (02 Nov 2010)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi69Magnesium 1By similarity1
    Metal bindingi98Magnesium 1By similarity1
    Metal bindingi98Magnesium 2By similarity1
    Metal bindingi119Magnesium 2By similarity1
    Metal bindingi119Magnesium 3Combined sources1
    Metal bindingi121Magnesium 2; via carbonyl oxygenBy similarity1
    Metal bindingi122Magnesium 3Combined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei141AMPCombined sources1 Publication1
    Binding sitei265SubstrateBy similarity1
    Metal bindingi281Magnesium 3Combined sources1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 22AMPCombined sources1 Publication5
    Nucleotide bindingi28 – 32AMPCombined sources1 Publication5
    Nucleotide bindingi113 – 114AMPCombined sources1 Publication2

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAllosteric enzyme, Hydrolase
    Biological processCarbohydrate metabolism, Gluconeogenesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS09189-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.11 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-70263 Gluconeogenesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P09467

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00138

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    P09467

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase 1 (EC:3.1.3.112 Publications)
    Short name:
    FBPase 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
    Liver FBPase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:FBP1
    Synonyms:FBP
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:3606 FBP1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    611570 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P09467

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075492158R → W in FBP1D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766005419Ensembl.1
    Natural variantiVAR_002380164G → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918188EnsemblClinVar.1
    Natural variantiVAR_002381177A → D in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918189EnsemblClinVar.1
    Natural variantiVAR_038812194F → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918191EnsemblClinVar.1
    Natural variantiVAR_038813284P → R in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918192EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    DisGeNET

    More...
    DisGeNETi
    2203

    MalaCards human disease database

    More...
    MalaCardsi
    FBP1
    MIMi229700 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000165140

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    348 Fructose-1,6-bisphosphatase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA28018

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P09467

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3975

    Drug and drug target database

    More...
    DrugBanki
    DB02778 2,5-Anhydroglucitol-1,6-Biphosphate
    DB07312 2,5-DICHLORO-N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)BENZENESULFONAMIDE
    DB07321 2,5-DICHLORO-N-[5-METHOXY-7-(6-METHOXYPYRIDIN-3-YL)-1,3-BENZOXAZOL-2-YL]BENZENESULFONAMIDE
    DB08484 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE
    DB00131 Adenosine phosphate
    DB04493 Fructose-6-Phosphate
    DB05518 Managlinat dialanetil
    DB05053 MB-07803
    DB04175 Mdl-29951
    DB07270 N-[7-(3-AMINOPHENYL)-5-METHOXY-1,3-BENZOXAZOL-2-YL]-2,5-DICHLOROBENZENESULFONAMIDE
    DB02848 {4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanol

    DrugCentral

    More...
    DrugCentrali
    P09467

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    FBP1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    311033495

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002004982 – 338Fructose-1,6-bisphosphatase 1Add BLAST337

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
    Modified residuei151N6-succinyllysineBy similarity1
    Modified residuei216PhosphotyrosineBy similarity1
    Modified residuei245PhosphotyrosineBy similarity1
    Modified residuei265PhosphotyrosineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-200
    CPTAC-201

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P09467

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P09467

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P09467

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P09467

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P09467

    PeptideAtlas

    More...
    PeptideAtlasi
    P09467

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P09467

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    52223

    PTM databases

    DEPOD human dephosphorylation database

    More...
    DEPODi
    P09467

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P09467

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P09467

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in pancreatic islets.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000165140 Expressed in 153 organ(s), highest expression level in right lobe of liver

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P09467 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P09467 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB033869
    HPA005857
    HPA012513

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108497, 33 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-46677N

    Protein interaction database and analysis system

    More...
    IntActi
    P09467, 46 interactors

    Molecular INTeraction database

    More...
    MINTi
    P09467

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000408025

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P09467

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P09467

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P09467

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni122 – 125Substrate bindingBy similarity4
    Regioni213 – 216Substrate bindingBy similarity4
    Regioni244 – 249Substrate bindingBy similarity6
    Regioni275 – 277Substrate bindingBy similarity3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1458 Eukaryota
    COG0158 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000015513

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000191265

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P09467

    KEGG Orthology (KO)

    More...
    KOi
    K03841

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QSGLVCR

    Database of Orthologous Groups

    More...
    OrthoDBi
    1314660at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P09467

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF314824

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00354 FBPase, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01855 FBPase_class1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000146 FBPase_class-1
    IPR033391 FBPase_N
    IPR028343 FBPtase
    IPR020548 Fructose_bisphosphatase_AS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11556 PTHR11556, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00316 FBPase, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF500210 FBPtase, 1 hit
    PIRSF000904 FBPtase_SBPase, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00115 F16BPHPHTASE

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00124 FBPASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P09467-1 [UniParc]FASTAAdd to basket
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            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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB3D270BCBB358B71
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    Q5VZC3Q5VZC3_HUMAN
    Fructose-1,6-bisphosphatase 1
    FBP1
    151Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A3B3IUC7A0A3B3IUC7_HUMAN
    Fructose-1,6-bisphosphatase 1
    FBP1
    273Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 dbSNP:rs766005419Ensembl.1
    Natural variantiVAR_002380164G → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918188EnsemblClinVar.1
    Natural variantiVAR_002381177A → D in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918189EnsemblClinVar.1
    Natural variantiVAR_038812194F → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918191EnsemblClinVar.1
    Natural variantiVAR_022212218R → K7 PublicationsCorresponds to variant dbSNP:rs1769259EnsemblClinVar.1
    Natural variantiVAR_022213233F → I1 PublicationCorresponds to variant dbSNP:rs2297085EnsemblClinVar.1
    Natural variantiVAR_022214255R → L1 PublicationCorresponds to variant dbSNP:rs28369761Ensembl.1
    Natural variantiVAR_038813284P → R in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918192EnsemblClinVar.1
    Natural variantiVAR_002382325V → A1 Publication1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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 No translation available.
    BC012927 mRNA Translation: AAH12927.1
    U47919 mRNA Translation: AAA89098.1
    U47918 mRNA Translation: AAA89097.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS6712.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A46666

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000498.2, NM_000507.3
    NP_001121100.1, NM_001127628.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000375326; ENSP00000364475; ENSG00000165140
    ENST00000415431; ENSP00000408025; ENSG00000165140

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2203

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2203

    UCSC genome browser

    More...
    UCSCi
    uc004auw.5 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
    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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    5LDZX-ray2.20A/B/C/D/E/F1-338[»]
    SMRiP09467
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi108497, 33 interactors
    DIPiDIP-46677N
    IntActiP09467, 46 interactors
    MINTiP09467
    STRINGi9606.ENSP00000408025

    Chemistry databases

    BindingDBiP09467
    ChEMBLiCHEMBL3975
    DrugBankiDB02778 2,5-Anhydroglucitol-1,6-Biphosphate
    DB07312 2,5-DICHLORO-N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)BENZENESULFONAMIDE
    DB07321 2,5-DICHLORO-N-[5-METHOXY-7-(6-METHOXYPYRIDIN-3-YL)-1,3-BENZOXAZOL-2-YL]BENZENESULFONAMIDE
    DB08484 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE
    DB00131 Adenosine phosphate
    DB04493 Fructose-6-Phosphate
    DB05518 Managlinat dialanetil
    DB05053 MB-07803
    DB04175 Mdl-29951
    DB07270 N-[7-(3-AMINOPHENYL)-5-METHOXY-1,3-BENZOXAZOL-2-YL]-2,5-DICHLOROBENZENESULFONAMIDE
    DB02848 {4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanol
    DrugCentraliP09467

    Protein family/group databases

    MoonProtiP09467

    PTM databases

    DEPODiP09467
    iPTMnetiP09467
    PhosphoSitePlusiP09467

    Polymorphism and mutation databases

    BioMutaiFBP1
    DMDMi311033495

    Proteomic databases

    CPTACiCPTAC-200
    CPTAC-201
    EPDiP09467
    jPOSTiP09467
    MassIVEiP09467
    MaxQBiP09467
    PaxDbiP09467
    PeptideAtlasiP09467
    PRIDEiP09467
    ProteomicsDBi52223

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2203

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2203
    DisGeNETi2203

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    FBP1
    HGNCiHGNC:3606 FBP1
    HPAiCAB033869
    HPA005857
    HPA012513
    MalaCardsiFBP1
    MIMi229700 phenotype
    611570 gene
    neXtProtiNX_P09467
    OpenTargetsiENSG00000165140
    Orphaneti348 Fructose-1,6-bisphosphatase deficiency
    PharmGKBiPA28018

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1458 Eukaryota
    COG0158 LUCA
    GeneTreeiENSGT00390000015513
    HOGENOMiHOG000191265
    InParanoidiP09467
    KOiK03841
    OMAiQSGLVCR
    OrthoDBi1314660at2759
    PhylomeDBiP09467
    TreeFamiTF314824

    Enzyme and pathway databases

    UniPathwayiUPA00138
    BioCyciMetaCyc:HS09189-MONOMER
    BRENDAi3.1.3.11 2681
    ReactomeiR-HSA-70263 Gluconeogenesis
    SABIO-RKiP09467

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    FBP1 human
    EvolutionaryTraceiP09467

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    2203
    PharosiP09467

    Protein Ontology

    More...
    PROi
    PR:P09467

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000165140 Expressed in 153 organ(s), highest expression level in right lobe of liver
    ExpressionAtlasiP09467 baseline and differential
    GenevisibleiP09467 HS

    Family and domain databases

    CDDicd00354 FBPase, 1 hit
    HAMAPiMF_01855 FBPase_class1, 1 hit
    InterProiView protein in InterPro
    IPR000146 FBPase_class-1
    IPR033391 FBPase_N
    IPR028343 FBPtase
    IPR020548 Fructose_bisphosphatase_AS
    PANTHERiPTHR11556 PTHR11556, 1 hit
    PfamiView protein in Pfam
    PF00316 FBPase, 1 hit
    PIRSFiPIRSF500210 FBPtase, 1 hit
    PIRSF000904 FBPtase_SBPase, 1 hit
    PRINTSiPR00115 F16BPHPHTASE
    PROSITEiView protein in PROSITE
    PS00124 FBPASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiF16P1_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09467
    Secondary accession number(s): O75571, Q53F94, Q96E46
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 2, 2010
    Last modified: September 18, 2019
    This is version 210 of the entry and version 5 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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