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UniProtKB - P49872 (F261_BOVIN)

Entry version 129 (11 Dec 2019)
Sequence version 1 (01 Oct 1996)
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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

PFKFB1

Organism
Bos taurus (Bovine)
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 transcript 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

Synthesis and degradation of fructose 2,6-bisphosphate.

<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 <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

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.By similarity

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 sitei82Fructose 6-phosphateBy similarity1
Binding sitei105Fructose 6-phosphateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei131Sequence analysis1
Binding sitei133Fructose 6-phosphateBy similarity1
Binding sitei139Fructose 6-phosphateBy similarity1
Active sitei161Sequence analysis1
Binding sitei175Fructose 6-phosphateBy similarity1
Binding sitei196Fructose 6-phosphateBy similarity1
Binding sitei200Fructose 6-phosphateBy similarity1
Binding sitei258Fructose 2,6-bisphosphateBy similarity1
Active sitei259Tele-phosphohistidine intermediateBy similarity1
Binding sitei265Fructose 2,6-bisphosphateBy similarity1
Binding sitei271Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Binding sitei308Fructose 2,6-bisphosphateBy similarity1
Active sitei328Proton donor/acceptorBy similarity1
Binding sitei339Fructose 2,6-bisphosphateBy similarity1
Binding sitei353Fructose 2,6-bisphosphateBy similarity1
Binding sitei357Fructose 2,6-bisphosphateBy similarity1
Binding sitei368Fructose 2,6-bisphosphateBy similarity1
<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>Sitei393Transition state stabilizerBy similarity1
Binding sitei394Fructose 2,6-bisphosphateBy similarity1
Binding sitei398Fructose 2,6-bisphosphateBy similarity1
Binding sitei430ATPBy similarity1

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 bindingi49 – 57ATPBy similarity9
Nucleotide bindingi170 – 175ATPBy similarity6
Nucleotide bindingi350 – 353ATPBy similarity4
Nucleotide bindingi394 – 398ATPBy similarity5

<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 functionHydrolase, Kinase, Multifunctional enzyme, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.46 908

<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:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Short name:
6PF-2-K/Fru-2,6-P2ase 1
Short name:
PFK/FBPase 1
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme
Including the following 2 domains:
6-phosphofructo-2-kinase (EC:2.7.1.105)
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
<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:PFKFB1
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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: Unplaced

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

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

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00001799592 – 4716-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1Add BLAST470

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-acetylserineBy similarity1
Modified residuei33Phosphoserine; by PKABy similarity1
Modified residuei141PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P49872

PRoteomics IDEntifications database

More...PRIDEi		P49872

<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

Liver.

<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

Homodimer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000000198

<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

3D structure databases

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

More...SMRi		P49872

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni2 – 2506-phosphofructo-2-kinaseAdd BLAST249
Regioni251 – 471Fructose-2,6-bisphosphataseAdd BLAST221

<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

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0234 Eukaryota
COG0406 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000181112

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P49872

KEGG Orthology (KO)

More...KOi		K19028

Database of Orthologous Groups

More...OrthoDBi		392001at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd07067 HP_PGM_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1240, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS

The PANTHER Classification System

More...PANTHERi		PTHR10606 PTHR10606, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00991 6PFRUCTKNASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00855 PGAM, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00175 PG_MUTASE, 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.

<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.

P49872-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQEMGELTQ TRLQKIWIPH NNGNSRLQRR RGSSIPQFTN SPTMVIMVGL 
        60         70         80         90        100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME 
       110        120        130        140        150
ALLIRKQCAL AALKDVHSYL SHEEGRVAVF DATNTTRERR SLILQFAKEH 
       160        170        180        190        200
GYKVFFIESI CNDPDVIAEN IRQVKLGSPD YIDCDREKVL EDFLKRIECY 
       210        220        230        240        250
EVNYQPLDDE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT VYYLMNIHVT 
       260        270        280        290        300
PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IQSQGISSLK 
       310        320        330        340        350
VGTSHMKRTI QTAEALGLPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF 
       360        370        380        390        400
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL 
       410        420        430        440        450
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCKVESIYLN VEAVNTHREK 
       460        470 
PENVDITREP EEALDTVPAH Y
Length:471
Mass (Da):54,657
Last modified:October 1, 1996 - v1
<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:i79C330B873B2D9EB
GO

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
M64323 mRNA Translation: AAA30696.1
S55569 mRNA Translation: AAB19845.1

Protein sequence database of the Protein Information Resource

More...PIRi		A44872

NCBI Reference Sequences

More...RefSeqi		NP_776997.3, NM_174572.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		282304

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:282304

<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
M64323 mRNA Translation: AAA30696.1
S55569 mRNA Translation: AAB19845.1
PIRiA44872
RefSeqiNP_776997.3, NM_174572.4

3D structure databases

SMRiP49872
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000198

Proteomic databases

PaxDbiP49872
PRIDEiP49872

Genome annotation databases

GeneIDi282304
KEGGibta:282304

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5207

Phylogenomic databases

eggNOGiKOG0234 Eukaryota
COG0406 LUCA
HOGENOMiHOG000181112
InParanoidiP49872
KOiK19028
OrthoDBi392001at2759

Enzyme and pathway databases

BRENDAi3.1.3.46 908

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS
PANTHERiPTHR10606 PTHR10606, 1 hit
PfamiView protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit
PRINTSiPR00991 6PFRUCTKNASE
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiF261_BOVIN
<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: P49872
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 11, 2019
This is version 129 of the entry and version 1 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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