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UniProtKB - O00757 (F16P2_HUMAN)

Entry version 178 (29 Sep 2021)
Sequence version 2 (27 Sep 2005)
Previous versions | rss
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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 <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. 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 <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 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 <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 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 <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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.11, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O00757

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

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000130957

<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

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

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O00757, Tbio

Genetic variation 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 or proteolytic cleavage.<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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O00757

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		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: a multi-organism proteome resource

More...ProteomicsDBi		48020

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		FBP2

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 muscle of leg and 112 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O00757, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000130957, Group enriched (brain, skeletal muscle, tongue)

<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">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114317, 22 interactors

Protein interaction database and analysis system

More...IntActi		O00757, 24 interactors

Molecular INTeraction database

More...MINTi		O00757

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000364486

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O00757, protein

<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

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

More...SMRi		O00757

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		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

Ensembl GeneTree

More...GeneTreei		ENSGT00390000015513

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_039977_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O00757

Identification of Orthologs from Complete Genome Data

More...OMAi		HEKSECY

Database of Orthologous Groups

More...OrthoDBi		1381522at2759

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
IPR044015, FBPase_C_dom
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
PF18913, FBPase_C, 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>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

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

<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

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[»]
5Q0CX-ray2.40A/B/C/D/E/F/G/H1-339[»]
SMRiO00757
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114317, 22 interactors
IntActiO00757, 24 interactors
MINTiO00757
STRINGi9606.ENSP00000364486

PTM databases

DEPODiFBP2
iPTMnetiO00757
PhosphoSitePlusiO00757
SwissPalmiO00757

Genetic variation databases

BioMutaiFBP2

Proteomic databases

EPDiO00757
jPOSTiO00757
MassIVEiO00757
MaxQBiO00757
PaxDbiO00757
PeptideAtlasiO00757
PRIDEiO00757
ProteomicsDBi48020

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		2920, 242 antibodies

The DNASU plasmid repository

More...DNASUi		8789

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8789
DisGeNETi8789

GeneCards: human genes, protein and diseases

More...GeneCardsi		FBP2
HGNCiHGNC:3607, FBP2
HPAiENSG00000130957, Group enriched (brain, skeletal muscle, tongue)
MIMi603027, gene
neXtProtiNX_O00757
OpenTargetsiENSG00000130957
PharmGKBiPA28019
VEuPathDBiHostDB:ENSG00000130957

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1458, Eukaryota
GeneTreeiENSGT00390000015513
HOGENOMiCLU_039977_1_0_1
InParanoidiO00757
OMAiHEKSECY
OrthoDBi1381522at2759
PhylomeDBiO00757
TreeFamiTF314824

Enzyme and pathway databases

UniPathwayiUPA00138
BioCyciMetaCyc:HS05462-MONOMER
BRENDAi3.1.3.11, 2681
PathwayCommonsiO00757
ReactomeiR-HSA-70263, Gluconeogenesis
SABIO-RKiO00757

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8789, 19 hits in 1006 CRISPR screens
EvolutionaryTraceiO00757

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

More...GenomeRNAii		8789
PharosiO00757, Tbio

Protein Ontology

More...PROi		PR:O00757
RNActiO00757, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000130957, Expressed in muscle of leg and 112 other tissues
GenevisibleiO00757, HS

Family and domain databases

CDDicd00354, FBPase, 1 hit
HAMAPiMF_01855, FBPase_class1, 1 hit
InterProiView protein in InterPro
IPR044015, FBPase_C_dom
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
PF18913, FBPase_C, 1 hit
PIRSFiPIRSF500210, FBPtase, 1 hit
PIRSF000904, FBPtase_SBPase, 1 hit
PRINTSiPR00115, F16BPHPHTASE
PROSITEiView protein in PROSITE
PS00124, FBPASE, 1 hit

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 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: September 29, 2021
This is version 178 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, Reference proteome

Documents

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