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UniProtKB - P17858 (PFKAL_HUMAN)

Entry version 240 (25 May 2022)
Sequence version 6 (06 Mar 2007)
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Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

PFKL

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 phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:22923583).

Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).

UniRule annotationBy similarity1 Publication

Miscellaneous

In human PFK exists as a system of 3 types of subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.
Glycosylation may play a role in cancer cell proliferation: inhibition of 6-phosphofructokinase activity and subsequent redirection of the glucose flux through the oxidative pentose phosphate pathway confers a selective growth advantage on cancer cells. Moreover GlcNAcylation is observed in multiple cancer cell lines and tissue samples and GlcNAcylation leads to larger xenografts tunors in mice (PubMed:22923583).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei25ATP; via amide nitrogenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi119Magnesium; catalyticUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei166Proton acceptorUniRule annotation1
Binding sitei201Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Binding sitei292Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei470Fructose 2,6-bisphosphate; allosteric activatorUniRule annotation1
Binding sitei565Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partnerUniRule annotation1
Binding sitei628Fructose 2,6-bisphosphate; allosteric activatorUniRule annotation1
Binding sitei654Fructose 2,6-bisphosphate; allosteric activator; shared with dimeric partnerUniRule annotation1
Binding sitei734Fructose 2,6-bisphosphate; allosteric activatorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi88 – 89ATPUniRule annotation2
Nucleotide bindingi118 – 121ATPUniRule annotation4

<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, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P17858

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-6798695, Neutrophil degranulation
R-HSA-70171, Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P17858

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P17858

SIGNOR Signaling Network Open Resource

More...SIGNORi		P17858

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

More...UniPathwayi		UPA00109;UER00182

<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%5Fand%5Ftaxonomy%5Fsection">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:
ATP-dependent 6-phosphofructokinase, liver typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-L
Alternative name(s):
6-phosphofructokinase type B
Phosphofructo-1-kinase isozyme B
Short name:
PFK-B
PhosphohexokinaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:PFKLImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 21

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:8876, PFKL

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		171860, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P17858

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000141959

<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

Cytoplasm

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi527T → A: Does not affect GlcNAcylation. 1 Publication1
Mutagenesisi529S → A: Prevents GlcNAcylation and enhance enzyme activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5211

Open Targets

More...OpenTargetsi		ENSG00000141959

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33215

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P17858, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2191

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PFKL

Domain mapping of disease mutations (DMDM)

More...DMDMi		134048493

<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%5Fprocessing%5Fsection">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 methionineiRemovedCombined sources1 Publication
<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_00001120212 – 780ATP-dependent 6-phosphofructokinase, liver typeAdd BLAST779

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-acetylalanineCombined sources1 Publication1
Modified residuei377PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi529O-linked (GlcNAc) serine1 Publication1
Modified residuei640PhosphotyrosineBy similarity1
Modified residuei775PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-425
CPTAC-426

Encyclopedia of Proteome Dynamics

More...EPDi		P17858

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17858

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P17858

MaxQB - The MaxQuant DataBase

More...MaxQBi		P17858

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

More...PaxDbi		P17858

PeptideAtlas

More...PeptideAtlasi		P17858

PRoteomics IDEntifications database

More...PRIDEi		P17858

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53520 [P17858-1]
53521 [P17858-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P17858-1 [P17858-1]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2022, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P17858, 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17858

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P17858

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

More...PhosphoSitePlusi		P17858

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P17858

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000141959, Expressed in adult mammalian kidney and 240 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P17858, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17858, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000141959, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (where M stands for Muscle), PFKL (Liver) and PFKP (Platelet). The composition of the PFK tetramer differs according to the tissue type it is present in. In muscles, it is composed of 4 PFKM subunits (also called M4). In the liver, the predominant form is a tetramer of PFKL subunits (L4). In erythrocytes, both PFKM and PFKL subunits randomly tetramerize to form M4, L4 and other combinations (ML3, M2L2, M3L). The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable).

UniRule annotationCurated

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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		111232, 135 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1998, 6-phosphofructokinase, L4 homotetramer
CPX-2000, 6-phosphofructokinase, ML3 heterotetramer
CPX-2001, 6-phosphofructokinase, M2L2 heterotetramer
CPX-2002, 6-phosphofructokinase, M3L heterotetramer

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P17858

Protein interaction database and analysis system

More...IntActi		P17858, 46 interactors

Molecular INTeraction database

More...MINTi		P17858

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000269848

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P17858, 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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P17858

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

More...SMRi		P17858

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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 – 390N-terminal catalytic PFK domain 1Add BLAST389
Regioni164 – 166Substrate bindingUniRule annotation3
Regioni208 – 210Substrate bindingUniRule annotation3
Regioni298 – 301Substrate bindingUniRule annotation4
Regioni391 – 400Interdomain linker10
Regioni401 – 780C-terminal regulatory PFK domain 2Add BLAST380
Regioni527 – 531Fructose 2,6-bisphosphate binding; allosteric activatorUniRule annotation5
Regioni572 – 574Fructose 2,6-bisphosphate binding; allosteric activatorUniRule annotation3
Regioni660 – 663Fructose 2,6-bisphosphate binding; allosteric activatorUniRule annotation4

<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 phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2440, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159292

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_011053_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17858

Identification of Orthologs from Complete Genome Data

More...OMAi		WFNLRPM

Database of Orthologous Groups

More...OrthoDBi		172878at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17858

TreeFam database of animal gene trees

More...TreeFami		TF300411

Family and domain databases

Conserved Domains Database

More...CDDi		cd00764, Eukaryotic_PFK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.460, 2 hits

HAMAP database of protein families

More...HAMAPi		MF_03184, Phosphofructokinase_I_E, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009161, 6-Pfructokinase_euk
IPR022953, ATP_PFK
IPR041914, PFK_vert-type
IPR015912, Phosphofructokinase_CS
IPR000023, Phosphofructokinase_dom
IPR035966, PKF_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00365, PFK, 2 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000533, ATP_PFK_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00476, PHFRCTKINASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53784, SSF53784, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02478, 6PF1K_euk, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00433, PHOSPHOFRUCTOKINASE, 2 hits

<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%5Flength">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: P17858-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL 
        60         70         80         90        100
IYEGYEGLVE GGENIKQANW LSVSNIIQLG GTIIGSARCK AFTTREGRRA 
       110        120        130        140        150
AAYNLVQHGI TNLCVIGGDG SLTGANIFRS EWGSLLEELV AEGKISETTA 
       160        170        180        190        200
RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ 
       210        220        230        240        250
RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET 
       260        270        280        290        300
RSRGSRLNII IIAEGAIDRN GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 
       310        320        330        340        350
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVTLSG NQSVRLPLME 
       360        370        380        390        400
CVQMTKEVQK AMDDKRFDEA TQLRGGSFEN NWNIYKLLAH QKPPKEKSNF 
       410        420        430        440        450
SLAILNVGAP AAGMNAAVRS AVRTGISHGH TVYVVHDGFE GLAKGQVQEV 
       460        470        480        490        500
GWHDVAGWLG RGGSMLGTKR TLPKGQLESI VENIRIYGIH ALLVVGGFEA 
       510        520        530        540        550
YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME 
       560        570        580        590        600
SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 
       610        620        630        640        650
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV 
       660        670        680        690        700
FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL REVYRKGRVF 
       710        720        730        740        750
ANAPDSACVI GLKKKAVAFS PVTELKKDTD FEHRMPREQW WLSLRLMLKM 
       760        770        780
LAQYRISMAA YVSGELEHVT RRTLSMDKGF
Length:780
Mass (Da):85,018
Last modified:March 6, 2007 - v6
<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:i0D686CE074E9626D
GO
Isoform 2 (identifier: P17858-2) [UniParc]FASTAAdd to basket
Also known as: a

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MAAVDLEKLRASGAGKAIGVLTSGGDAQ → MCNQGRGRES...GGTSIMSRLG

Show »
Length:827
Mass (Da):90,203
Checksum:iADBECCB9B1FB234C
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WEU2F8WEU2_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKL
42Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti27A → R in CAA33597 (PubMed:2533063).Curated1
Sequence conflicti27A → R in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti86S → T in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti89C → S in CAA33597 (PubMed:2533063).Curated1
Sequence conflicti89C → S in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti103Y → N in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti236E → EAPPE in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti386K → R in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti389A → T in CAA33597 (PubMed:2533063).Curated1
Sequence conflicti389A → T in CAB46744 (PubMed:2139864).Curated1
Sequence conflicti648K → N in AAH08964 (PubMed:15489334).Curated1
Sequence conflicti648K → N in AAH09919 (PubMed:15489334).Curated1
Sequence conflicti717V → A in AAH08964 (PubMed:15489334).Curated1
Sequence conflicti717V → A in AAH09919 (PubMed:15489334).Curated1

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_00607081G → A1 Publication1
Natural variantiVAR_006071151R → W1 PublicationCorresponds to variant dbSNP:rs755851304Ensembl.1
Natural variantiVAR_030872237D → V. Corresponds to variant dbSNP:rs1057037EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0118541 – 28MAAVD…GGDAQ → MCNQGRGRESSRGGLHVQGS CRGLSRSPQQETGFAKAPAG TDCFFHCSPGSRGQGDRKEE VTSEPGGTSIMSRLG in isoform 2. 1 PublicationAdd BLAST28

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
X15573 mRNA Translation: CAA33597.1
X16911 X16930 Genomic DNA Translation: CAB46744.1
AP001754 Genomic DNA Translation: BAA95561.1
BC006422 mRNA Translation: AAH06422.1
BC007536 mRNA Translation: AAH07536.1
BC008964 mRNA Translation: AAH08964.1
BC009919 mRNA Translation: AAH09919.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33582.1 [P17858-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A33639

NCBI Reference Sequences

More...RefSeqi		NP_001002021.2, NM_001002021.2
NP_002617.3, NM_002626.5 [P17858-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000349048.9; ENSP00000269848.6; ENSG00000141959.17

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5211

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5211

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000349048.9; ENSP00000269848.6; NM_002626.6; NP_002617.3

UCSC genome browser

More...UCSCi		uc002zel.4, human [P17858-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
X15573 mRNA Translation: CAA33597.1
X16911 X16930 Genomic DNA Translation: CAB46744.1
AP001754 Genomic DNA Translation: BAA95561.1
BC006422 mRNA Translation: AAH06422.1
BC007536 mRNA Translation: AAH07536.1
BC008964 mRNA Translation: AAH08964.1
BC009919 mRNA Translation: AAH09919.1
CCDSiCCDS33582.1 [P17858-1]
PIRiA33639
RefSeqiNP_001002021.2, NM_001002021.2
NP_002617.3, NM_002626.5 [P17858-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
7LW1electron microscopy2.90A/D/E/F1-780[»]
AlphaFoldDBiP17858
SMRiP17858
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111232, 135 interactors
ComplexPortaliCPX-1998, 6-phosphofructokinase, L4 homotetramer
CPX-2000, 6-phosphofructokinase, ML3 heterotetramer
CPX-2001, 6-phosphofructokinase, M2L2 heterotetramer
CPX-2002, 6-phosphofructokinase, M3L heterotetramer
CORUMiP17858
IntActiP17858, 46 interactors
MINTiP17858
STRINGi9606.ENSP00000269848

Chemistry databases

ChEMBLiCHEMBL2191

PTM databases

GlyConnecti2022, 1 N-Linked glycan (1 site)
GlyGeniP17858, 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site)
iPTMnetiP17858
MetOSiteiP17858
PhosphoSitePlusiP17858
SwissPalmiP17858

Genetic variation databases

BioMutaiPFKL
DMDMi134048493

Proteomic databases

CPTACiCPTAC-425
CPTAC-426
EPDiP17858
jPOSTiP17858
MassIVEiP17858
MaxQBiP17858
PaxDbiP17858
PeptideAtlasiP17858
PRIDEiP17858
ProteomicsDBi53520 [P17858-1]
53521 [P17858-2]
TopDownProteomicsiP17858-1 [P17858-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		24185, 323 antibodies from 34 providers

The DNASU plasmid repository

More...DNASUi		5211

Genome annotation databases

EnsembliENST00000349048.9; ENSP00000269848.6; ENSG00000141959.17
GeneIDi5211
KEGGihsa:5211
MANE-SelectiENST00000349048.9; ENSP00000269848.6; NM_002626.6; NP_002617.3
UCSCiuc002zel.4, human [P17858-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5211
DisGeNETi5211

GeneCards: human genes, protein and diseases

More...GeneCardsi		PFKL
HGNCiHGNC:8876, PFKL
HPAiENSG00000141959, Low tissue specificity
MIMi171860, gene
neXtProtiNX_P17858
OpenTargetsiENSG00000141959
PharmGKBiPA33215
VEuPathDBiHostDB:ENSG00000141959

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2440, Eukaryota
GeneTreeiENSGT00940000159292
HOGENOMiCLU_011053_0_0_1
InParanoidiP17858
OMAiWFNLRPM
OrthoDBi172878at2759
PhylomeDBiP17858
TreeFamiTF300411

Enzyme and pathway databases

UniPathwayiUPA00109;UER00182
PathwayCommonsiP17858
ReactomeiR-HSA-6798695, Neutrophil degranulation
R-HSA-70171, Glycolysis
SABIO-RKiP17858
SignaLinkiP17858
SIGNORiP17858

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5211, 16 hits in 1076 CRISPR screens

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

More...ChiTaRSi		PFKL, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PFKL

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

More...GenomeRNAii		5211
PharosiP17858, Tbio

Protein Ontology

More...PROi		PR:P17858
RNActiP17858, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000141959, Expressed in adult mammalian kidney and 240 other tissues
ExpressionAtlasiP17858, baseline and differential
GenevisibleiP17858, HS

Family and domain databases

CDDicd00764, Eukaryotic_PFK, 1 hit
Gene3Di3.40.50.460, 2 hits
HAMAPiMF_03184, Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161, 6-Pfructokinase_euk
IPR022953, ATP_PFK
IPR041914, PFK_vert-type
IPR015912, Phosphofructokinase_CS
IPR000023, Phosphofructokinase_dom
IPR035966, PKF_sf
PfamiView protein in Pfam
PF00365, PFK, 2 hits
PIRSFiPIRSF000533, ATP_PFK_euk, 1 hit
PRINTSiPR00476, PHFRCTKINASE
SUPFAMiSSF53784, SSF53784, 2 hits
TIGRFAMsiTIGR02478, 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433, PHOSPHOFRUCTOKINASE, 2 hits

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 nameiPFKAL_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: P17858
Secondary accession number(s): Q96A64, Q96IH4, Q9BR91
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: March 6, 2007
Last modified: May 25, 2022
This is version 240 of the entry and version 6 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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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