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UniProtKB - O00757 (F16P2_HUMAN)

Protein

Fructose-1,6-bisphosphatase isozyme 2

Gene

FBP2

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 and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.2 Publications

Miscellaneous

Specific for the alpha-anomer of the substrate (PubMed:22120740). The Arg-33 mutant form has been shown to act on the beta-anomer (PubMed:24086250).2 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+2 PublicationsNote: Binds 3 Mg2+ ions per subunit.2 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. Fructose 2,6-bisphosphate acts as competitive inhibitor. Strongly inhibited by Ca2+.3 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=1.3 µM for fructose 1,6-bisphosphate2 Publications
  2. KM=2.6 µM for fructose 1,6-bisphosphate2 Publications

    <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 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 sitei18AMP; via carbonyl oxygen1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei33Important for the conversion from active R-state to inactive T-state in the presence of AMP1
    <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
    Metal bindingi98Magnesium 11
    Metal bindingi98Magnesium 21
    Metal bindingi119Magnesium 21
    Metal bindingi119Magnesium 31
    Metal bindingi121Magnesium 2; via carbonyl oxygen1
    Metal bindingi122Magnesium 31
    Binding sitei122Substrate1
    Binding sitei141AMP1 Publication1
    Binding sitei265Substrate1
    Binding sitei275Substrate1
    Metal bindingi281Magnesium 31

    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 bindingi28 – 32AMP1 Publication5
    Nucleotide bindingi113 – 114AMP1 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

    • fructose 1,6-bisphosphate 1-phosphatase activity Source: GO_Central
    • identical protein binding Source: IntAct
    • metal ion binding Source: UniProtKB-KW
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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
    LigandCalcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS05462-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-70263 Gluconeogenesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		O00757

    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 isozyme 2 (EC:3.1.3.11)
    Short name:
    FBPase 2
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 2
    Muscle 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:FBP2
    <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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <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

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000130957.4

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:3607 FBP2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		603027 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_O00757

    <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

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Nucleus

    <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>Mutagenesisi1 – 10Missing : Greatly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA. 1 Publication10
    Mutagenesisi1 – 7Missing : Greatly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA. 7
    Mutagenesisi1 – 6Missing : Reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA. 6
    Mutagenesisi1 – 5Missing : Reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA. 5
    Mutagenesisi1 – 4Missing : Slightly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA. 4
    Mutagenesisi1 – 3Missing : No effect on kinetic properties but decreases binding to ALDOA. 3
    Mutagenesisi1 – 2Missing : No effect on kinetic properties and interaction with ALDOA. 2
    Mutagenesisi1Missing : No effect on kinetic properties and interaction with ALDOA. 1
    Mutagenesisi21K → E: Reduces sensitivity to AMP; when associated with M-178 and C-180. 1 Publication1
    Mutagenesisi33Q → R: Causes conformational change of N-terminal residues and decreased sensitivity towards AMP with lack of conversion to the inactive T-state in the presence of AMP. 1
    Mutagenesisi70E → Q: Greatly reduces affinity towards Ca(2+) and slightly reduces affinity towards Mg(2+). 1 Publication1
    Mutagenesisi178T → M: Reduces sensitivity to AMP; when associated with E-21 and C-180. 1 Publication1
    Mutagenesisi180Q → C: Reduces sensitivity to AMP; when associated with E-21 and M-178. 1 Publication1
    Mutagenesisi204 – 208KKKGK → AAAGA or EEEGE: Almost completely abolishes nuclear localization. 1 Publication5
    Mutagenesisi204K → E: Minor reduction in nuclear localization. 1
    Mutagenesisi205K → E: Minor reduction in nuclear localization. 1
    Mutagenesisi206K → E: Greatly reduces nuclear lozalization. 1
    Mutagenesisi208K → E: Significantly reduces nuclear localization. 1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		8789

    Open Targets

    More...    OpenTargetsi    		ENSG00000130957

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA28019

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		FBP2

    <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 ‘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_00002005041 – 339Fructose-1,6-bisphosphatase isozyme 2Add BLAST339

    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 residuei216PhosphotyrosineBy similarity1
    Modified residuei219PhosphotyrosineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		O00757

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		O00757

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

    More...    PaxDbi    		O00757

    PeptideAtlas

    More...    PeptideAtlasi    		O00757

    PRoteomics IDEntifications database

    More...    PRIDEi    		O00757

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		48020

    PTM databases

    DEPOD human dephosphorylation database

    More...    DEPODi    		O00757

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		O00757

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

    More...    PhosphoSitePlusi    		O00757

    SwissPalm database of S-palmitoylation events

    More...    SwissPalmi    		O00757

    <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 skeletal muscle (at protein level).1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000130957 Expressed in 93 organ(s), highest expression level in muscle of leg

    CleanEx database of gene expression profiles

    More...    CleanExi    		HS_FBP2

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		O00757 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA012513
    HPA055286

    <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. Interacts with ALDOA; the interaction blocks inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+. Interacts with alpha-actinin and F-actin.3 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

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		114317, 3 interactors

    Protein interaction database and analysis system

    More...    IntActi    		O00757, 20 interactors

    Molecular INTeraction database

    More...    MINTi    		O00757

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000364486

    <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

    1339
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		O00757

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

    More...    SMRi    		O00757

    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    		O00757

    <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>Regioni3 – 10Important for interaction with ALDOA1 Publication8
    Regioni213 – 216Substrate binding4
    Regioni245 – 249Substrate binding5

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi204 – 208Nuclear localization signal1 Publication5

    <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    		O00757

    KEGG Orthology (KO)

    More...    KOi    		K03841

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		HEKSECY

    Database of Orthologous Groups

    More...    OrthoDBi    		EOG091G0AZP

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		O00757

    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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <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.

    O00757-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR 
            60         70         80         90        100
    KAGLAHLYGI AGSVNVTGDE VKKLDVLSNS LVINMVQSSY STCVLVSEEN 
           110        120        130        140        150
    KDAIITAKEK RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE 
           160        170        180        190        200
    KDALQCGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD 
           210        220        230        240        250
    VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP YGARYVGSMV 
           260        270        280        290        300
    ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT 
           310        320        330 
    QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGS
    Length:339
    Mass (Da):36,743
    Last modified:September 27, 2005 - v2
    <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:i196B06D744710BC4
    GO

    Natural variant

    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_02444886V → L2 PublicationsCorresponds to variant dbSNP:rs573212Ensembl.1

    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
    		Y10812 mRNA Translation: CAA71772.1
    CR536483 mRNA Translation: CAG38722.1
    AL161728 Genomic DNA No translation available.
    BC113632 mRNA Translation: AAI13633.1
    BC117477 mRNA Translation: AAI17478.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS6711.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_003828.2, NM_003837.3

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.61255

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000375337; ENSP00000364486; ENSG00000130957

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		8789

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:8789

    UCSC genome browser

    More...    UCSCi    		uc004auv.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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		Y10812 mRNA Translation: CAA71772.1
    CR536483 mRNA Translation: CAG38722.1
    AL161728 Genomic DNA No translation available.
    BC113632 mRNA Translation: AAI13633.1
    BC117477 mRNA Translation: AAI17478.1
    CCDSiCCDS6711.1
    RefSeqiNP_003828.2, NM_003837.3
    UniGeneiHs.61255

    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
    3IFAX-ray1.93A/B/C/D2-339[»]
    3IFCX-ray1.97A/B/C/D2-339[»]
    4HE0X-ray2.69A2-339[»]
    4HE1X-ray2.23A2-339[»]
    4HE2X-ray1.60A2-339[»]
    5ET5X-ray1.67A2-339[»]
    5ET6X-ray1.84A/B/C/D2-339[»]
    5ET7X-ray2.99A/B/C/D2-339[»]
    5ET8X-ray1.92A2-339[»]
    5K54X-ray1.72A2-339[»]
    5K55X-ray1.98A2-339[»]
    5K56X-ray2.20A2-339[»]
    5L0AX-ray2.30A2-339[»]
    ProteinModelPortaliO00757
    SMRiO00757
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114317, 3 interactors
    IntActiO00757, 20 interactors
    MINTiO00757
    STRINGi9606.ENSP00000364486

    PTM databases

    DEPODiO00757
    iPTMnetiO00757
    PhosphoSitePlusiO00757
    SwissPalmiO00757

    Polymorphism and mutation databases

    BioMutaiFBP2

    Proteomic databases

    EPDiO00757
    MaxQBiO00757
    PaxDbiO00757
    PeptideAtlasiO00757
    PRIDEiO00757
    ProteomicsDBi48020

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		8789
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000375337; ENSP00000364486; ENSG00000130957
    GeneIDi8789
    KEGGihsa:8789
    UCSCiuc004auv.5 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		8789
    DisGeNETi8789
    EuPathDBiHostDB:ENSG00000130957.4

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		FBP2
    HGNCiHGNC:3607 FBP2
    HPAiHPA012513
    HPA055286
    MIMi603027 gene
    neXtProtiNX_O00757
    OpenTargetsiENSG00000130957
    PharmGKBiPA28019

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG1458 Eukaryota
    COG0158 LUCA
    GeneTreeiENSGT00390000015513
    HOGENOMiHOG000191265
    HOVERGENiHBG005627
    InParanoidiO00757
    KOiK03841
    OMAiHEKSECY
    OrthoDBiEOG091G0AZP
    PhylomeDBiO00757
    TreeFamiTF314824

    Enzyme and pathway databases

    UniPathwayi
    UPA00138

    BioCyciMetaCyc:HS05462-MONOMER
    ReactomeiR-HSA-70263 Gluconeogenesis
    SABIO-RKiO00757

    Miscellaneous databases

    EvolutionaryTraceiO00757

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

    More...    GenomeRNAii    		8789

    Protein Ontology

    More...    PROi    		PR:O00757

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000130957 Expressed in 93 organ(s), highest expression level in muscle of leg
    CleanExiHS_FBP2
    GenevisibleiO00757 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...

    <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 nameiF16P2_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: O00757
    Secondary accession number(s): Q17R39, Q6FI53
    <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 15, 1998
    Last sequence update: September 27, 2005
    Last modified: December 5, 2018
    This is version 163 of the entry and version 2 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, Reference proteome

    Documents

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