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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Sus scrofa (Pig)
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.By similarity

Miscellaneous

The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with homocystine) but is not essential for enzyme activity.

<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+4 PublicationsNote: Binds 3 Mg2+ ions per subunit.4 Publications

<p>This subsection of the ‘Function’ 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.6 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

  1. KM=1.2 µM for fructose-1,6-diphosphate1 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 ‘Function’ 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 11 Publication1
    Metal bindingi98Magnesium 11 Publication1
    Metal bindingi98Magnesium 21 Publication1
    Metal bindingi119Magnesium 21 Publication1
    Metal bindingi119Magnesium 31 Publication1
    Metal bindingi121Magnesium 2; via carbonyl oxygen1 Publication1
    Metal bindingi122Magnesium 31 Publication1
    <p>This subsection of the ‘Function’ 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 sitei141AMP1 Publication1
    Binding sitei265SubstrateCombined sources9 Publications1
    Metal bindingi281Magnesium 31 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sources3 Publications5
    Nucleotide bindingi28 – 32AMPCombined sources3 Publications5
    Nucleotide bindingi113 – 114AMPCombined sources3 Publications2

    <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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.11 6170

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SSC-70263 Gluconeogenesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P00636

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

    More...
    UniPathwayi
    UPA00138

    <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:3.1.3.111 Publication1 Publication)
    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>OrganismiSus scrofa (Pig)
    <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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    <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
    • UP000008227 <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 10

    <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; 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

    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>Mutagenesisi55A → L: Destabilizes the inactive T-state and promotes transition to the R-state. 1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2263

    <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 methionineiRemoved2 Publications
    <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_00002005002 – 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-acetylthreonine2 Publications1
    Modified residuei151N6-succinyllysineBy similarity1
    Modified residuei208Phosphoserine; by PKA1 Publication1
    Modified residuei216PhosphotyrosineBy similarity1
    Modified residuei245PhosphotyrosineBy similarity1
    Modified residuei265PhosphotyrosineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    P00636

    PeptideAtlas

    More...
    PeptideAtlasi
    P00636

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00636

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P00636

    <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

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P00636 differential

    <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.9 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    9823.ENSSSCP00000011671

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P00636

    <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

    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
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P00636

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

    More...
    SMRi
    P00636

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00636

    <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 bindingCombined sources9 Publications4
    Regioni213 – 216Substrate bindingCombined sources9 Publications4
    Regioni244 – 249Substrate bindingCombined sources9 Publications6
    Regioni275 – 277Substrate bindingCombined sources9 Publications3

    <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

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG005627

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P00636

    KEGG Orthology (KO)

    More...
    KOi
    K03841

    Database of Orthologous Groups

    More...
    OrthoDBi
    1381522at2759

    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>.<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

    P00636-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR
    60 70 80 90 100
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED
    110 120 130 140 150
    KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE
    160 170 180 190 200
    KDALQPGRNL VAAGYALYGS ATMLVLAMVN GVNCFMLDPA IGEFILVDRD
    210 220 230 240 250
    VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP YGARYVGSMV
    260 270 280 290 300
    ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK
    310 320 330
    EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK
    Length:338
    Mass (Da):36,779
    Last modified:January 23, 2007 - v4
    <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:i610BF8D3C6D320F6
    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
    A0A287BJI2A0A287BJI2_PIG
    Fructose-1,6-bisphosphatase 1
    FBP1
    291Annotation 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>
    A0A286ZVB2A0A286ZVB2_PIG
    Fructose-1,6-bisphosphatase 1
    FBP1
    292Annotation 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>

    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 conflicti2T → A AA sequence (PubMed:6291465).Curated1
    Sequence conflicti4Q → E AA sequence (PubMed:6291465).Curated1
    Sequence conflicti21E → Q AA sequence (PubMed:6296821).Curated1
    Sequence conflicti97S → T AA sequence (PubMed:6296821).Curated1
    Sequence conflicti157G → E AA sequence (PubMed:6296821).Curated1
    Sequence conflicti200D → N AA sequence (PubMed:6296821).Curated1
    Sequence conflicti229Q → E AA sequence (PubMed:6296821).Curated1

    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
    M86347 mRNA Translation: AAA31035.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S37696 PAPGF

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_999144.1, NM_213979.1

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Ssc.5127

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSSSCT00000065852; ENSSSCP00000049752; ENSSSCG00000031174

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    397038

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ssc:397038

    <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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86347 mRNA Translation: AAA31035.1
    PIRiS37696 PAPGF
    RefSeqiNP_999144.1, NM_213979.1
    UniGeneiSsc.5127

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636
    SMRiP00636
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011671

    Chemistry databases

    BindingDBiP00636
    ChEMBLiCHEMBL2263

    PTM databases

    iPTMnetiP00636

    Proteomic databases

    PaxDbiP00636
    PeptideAtlasiP00636
    PRIDEiP00636

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSSSCT00000065852; ENSSSCP00000049752; ENSSSCG00000031174
    GeneIDi397038
    KEGGissc:397038

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2203

    Phylogenomic databases

    eggNOGiKOG1458 Eukaryota
    COG0158 LUCA
    GeneTreeiENSGT00390000015513
    HOGENOMiHOG000191265
    HOVERGENiHBG005627
    InParanoidiP00636
    KOiK03841
    OrthoDBi1381522at2759

    Enzyme and pathway databases

    UniPathwayi
    UPA00138

    BRENDAi3.1.3.11 6170
    ReactomeiR-SSC-70263 Gluconeogenesis
    SABIO-RKiP00636

    Miscellaneous databases

    EvolutionaryTraceiP00636

    Protein Ontology

    More...
    PROi
    PR:P00636

    Gene expression databases

    ExpressionAtlasiP00636 differential

    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...

    <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_PIG
    <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: P00636
    <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 21, 1986
    Last sequence update: January 23, 2007
    Last modified: January 16, 2019
    This is version 161 of the entry and version 4 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

    <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. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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