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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

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.

Miscellaneous

In human PFK exists as a system of 3 types of subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

<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: 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
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM)
  4. Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (BQ8482_350140), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase B (ALDOB)
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 ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei34ATP; via amide nitrogenUniRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi128Magnesium; catalyticUniRule annotation1
<p>This subsection of the ‘Function’ 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 sitei175Proton acceptorUniRule annotation1
Binding sitei210Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei273SubstrateUniRule annotation1
Binding sitei301Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei481Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei576Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei639Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei665Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei744Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi97 – 98ATPUniRule annotation2
Nucleotide bindingi127 – 130ATPUniRule 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

  • 6-phosphofructokinase activity Source: Reactome
  • AMP binding Source: GO_Central
  • ATP binding Source: GO_Central
  • cadherin binding Source: BHF-UCL
  • fructose-6-phosphate binding Source: GO_Central
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • monosaccharide binding Source: GO_Central
  • protein-containing complex binding Source: MGI

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS00894-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-70171 Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q01813

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_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:
ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
PhosphohexokinaseUniRule annotation
<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:PFKP
Synonyms:PFKF
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000067057.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8878 PFKP

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
171840 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q01813

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

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

Keywords - Cellular componenti

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

Organism-specific databases

DisGeNET

More...
DisGeNETi
5214

Open Targets

More...
OpenTargetsi
ENSG00000067057

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33217

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PFKP

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1346355

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001120241 – 784ATP-dependent 6-phosphofructokinase, platelet typeAdd BLAST784

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 residuei1N-acetylmethionineCombined sources1
Modified residuei6PhosphoserineCombined sources1
Modified residuei12PhosphoserineBy similarity1
Modified residuei21PhosphoserineCombined sources1
Modified residuei142PhosphoserineBy similarity1
Modified residuei386PhosphoserineCombined sources1
Modified residuei395N6-acetyllysineCombined sources1
Modified residuei486N6-acetyllysineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi540O-linked (GlcNAc) serineBy similarity1
Modified residuei651PhosphotyrosineCombined sources1
Modified residuei688N6-acetyllysineCombined sources1
Modified residuei783PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q01813

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01813

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

More...
PaxDbi
Q01813

PeptideAtlas

More...
PeptideAtlasi
Q01813

PRoteomics IDEntifications database

More...
PRIDEi
Q01813

ProteomicsDB human proteome resource

More...
ProteomicsDBi
57992

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01813

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

More...
PhosphoSitePlusi
Q01813

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q01813

<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
ENSG00000067057 Expressed in 232 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

More...
CleanExi
HS_PFKP

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q01813 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01813 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA018257
HPA056484

<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

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). In platelets, brain and fibroblasts, PFK contains a higher proportion of PFKP subunits. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable).UniRule annotationCurated

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111235, 83 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1999 6-phosphofructokinase, P4 homotetramer

Database of interacting proteins

More...
DIPi
DIP-45850N

Protein interaction database and analysis system

More...
IntActi
Q01813, 39 interactors

Molecular INTeraction database

More...
MINTi
Q01813

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000370517

<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

1784
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q01813

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

More...
SMRi
Q01813

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni1 – 399N-terminal catalytic PFK domain 1Add BLAST399
Regioni173 – 175Substrate bindingUniRule annotation3
Regioni217 – 219Substrate bindingUniRule annotation3
Regioni307 – 310Substrate bindingUniRule annotation4
Regioni400 – 411Interdomain linkerAdd BLAST12
Regioni412 – 784C-terminal regulatory PFK domain 2Add BLAST373
Regioni538 – 542Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni583 – 585Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni671 – 674Allosteric activator fructose 2,6-bisphosphate bindingUniRule 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2440 Eukaryota
COG0205 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155002

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000200154

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000976

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01813

KEGG Orthology (KO)

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KOi
K00850

Identification of Orthologs from Complete Genome Data

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OMAi
PLVECVQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G01YN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q01813

TreeFam database of animal gene trees

More...
TreeFami
TF300411

Family and domain databases

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
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q01813-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG
60 70 80 90 100
IYVGAKVYFI YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA
110 120 130 140 150
FRTREGRLKA ACNLLQRGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAR
160 170 180 190 200
NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA
210 220 230 240 250
IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE
260 270 280 290 300
QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT
310 320 330 340 350
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN
360 370 380 390 400
HAVRLPLMEC VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK
410 420 430 440 450
LPDDQIPKTN CNVAVINVGA PAAGMNAAVR SAVRVGIADG HRMLAIYDGF
460 470 480 490 500
DGFAKGQIKE IGWTDVGGWT GQGGSILGTK RVLPGKYLEE IATQMRTHSI
510 520 530 540 550
NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS NNVPGSDFSI
560 570 580 590 600
GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
610 620 630 640 650
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI
660 670 680 690 700
YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK
710 720 730 740 750
LKEARGRGKK FTTDDSICVL GISKRNVIFQ PVAELKKQTD FEHRIPKEQW
760 770 780
WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ PWSV
Length:784
Mass (Da):85,596
Last modified:February 1, 1996 - 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:i22522E77E9AF80F6
GO
Isoform 2 (identifier: Q01813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: MDADDSRAPK...DWESVSSILQ → MCGYERCRPC...RFPCPGRHAL

Note: No experimental confirmation available.
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Length:776
Mass (Da):85,316
Checksum:i649595FEDE1A9187
GO

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

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1APP6B1APP6_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
240Annotation 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>
V9GY25V9GY25_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
118Annotation 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>
B1APP8B1APP8_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
202Annotation 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>
Q5VSR5Q5VSR5_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
210Annotation 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>
V9GYV7V9GYV7_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
113Annotation 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>
H0Y3Y3H0Y3Y3_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
166Annotation 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>
H0Y757H0Y757_HUMAN
ATP-dependent 6-phosphofructokinase...
PFKP
103Annotation 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 conflicti484 – 485PG → IP (PubMed:1834056).Curated2
Sequence conflicti498Missing in AAA36435 (PubMed:1834056).Curated1
Sequence conflicti655S → P in BAG52577 (PubMed:14702039).Curated1
Sequence conflicti699A → E in AAA36435 (PubMed:1834056).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0464161 – 87MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2. 1 PublicationAdd BLAST87

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D25328 mRNA Translation: BAA04998.1
AK092597 mRNA Translation: BAG52577.1
AK291841 mRNA Translation: BAF84530.1
AL731533 Genomic DNA No translation available.
AL451164 Genomic DNA No translation available.
BC002536 mRNA Translation: AAH02536.1
BC029138 mRNA Translation: AAH29138.1
M64784 mRNA Translation: AAA36435.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS55698.1 [Q01813-2]
CCDS7059.1 [Q01813-1]

Protein sequence database of the Protein Information Resource

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PIRi
JC2055

NCBI Reference Sequences

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RefSeqi
NP_001229268.1, NM_001242339.1 [Q01813-2]
NP_002618.1, NM_002627.4 [Q01813-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.26010

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000381075; ENSP00000370465; ENSG00000067057 [Q01813-2]
ENST00000381125; ENSP00000370517; ENSG00000067057 [Q01813-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5214

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5214

UCSC genome browser

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UCSCi
uc001igp.4 human [Q01813-1]

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
D25328 mRNA Translation: BAA04998.1
AK092597 mRNA Translation: BAG52577.1
AK291841 mRNA Translation: BAF84530.1
AL731533 Genomic DNA No translation available.
AL451164 Genomic DNA No translation available.
BC002536 mRNA Translation: AAH02536.1
BC029138 mRNA Translation: AAH29138.1
M64784 mRNA Translation: AAA36435.1
CCDSiCCDS55698.1 [Q01813-2]
CCDS7059.1 [Q01813-1]
PIRiJC2055
RefSeqiNP_001229268.1, NM_001242339.1 [Q01813-2]
NP_002618.1, NM_002627.4 [Q01813-1]
UniGeneiHs.26010

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RH3X-ray3.02A/B/C/D26-762[»]
4U1RX-ray2.80A/B/C/D26-762[»]
4WL0X-ray2.89A/B/C/D26-762[»]
4XYJX-ray3.10A/B/C/D/E/F/G/H1-784[»]
4XYKX-ray3.40A/B/C/D1-784[»]
4XZ2X-ray2.67A/B/C/D26-762[»]
ProteinModelPortaliQ01813
SMRiQ01813
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111235, 83 interactors
ComplexPortaliCPX-1999 6-phosphofructokinase, P4 homotetramer
DIPiDIP-45850N
IntActiQ01813, 39 interactors
MINTiQ01813
STRINGi9606.ENSP00000370517

PTM databases

iPTMnetiQ01813
PhosphoSitePlusiQ01813
SwissPalmiQ01813

Polymorphism and mutation databases

BioMutaiPFKP
DMDMi1346355

Proteomic databases

EPDiQ01813
MaxQBiQ01813
PaxDbiQ01813
PeptideAtlasiQ01813
PRIDEiQ01813
ProteomicsDBi57992

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5214
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381075; ENSP00000370465; ENSG00000067057 [Q01813-2]
ENST00000381125; ENSP00000370517; ENSG00000067057 [Q01813-1]
GeneIDi5214
KEGGihsa:5214
UCSCiuc001igp.4 human [Q01813-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5214
DisGeNETi5214
EuPathDBiHostDB:ENSG00000067057.16

GeneCards: human genes, protein and diseases

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GeneCardsi
PFKP
HGNCiHGNC:8878 PFKP
HPAiHPA018257
HPA056484
MIMi171840 gene
neXtProtiNX_Q01813
OpenTargetsiENSG00000067057
PharmGKBiPA33217

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
GeneTreeiENSGT00940000155002
HOGENOMiHOG000200154
HOVERGENiHBG000976
InParanoidiQ01813
KOiK00850
OMAiPLVECVQ
OrthoDBiEOG091G01YN
PhylomeDBiQ01813
TreeFamiTF300411

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

BioCyciMetaCyc:HS00894-MONOMER
ReactomeiR-HSA-70171 Glycolysis
SABIO-RKiQ01813

Miscellaneous databases

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

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ChiTaRSi
PFKP human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PFKP

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

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GenomeRNAii
5214

Protein Ontology

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PROi
PR:Q01813

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000067057 Expressed in 232 organ(s), highest expression level in testis
CleanExiHS_PFKP
ExpressionAtlasiQ01813 baseline and differential
GenevisibleiQ01813 HS

Family and domain databases

HAMAPiMF_03184 Phosphofructokinase_I_E, 1 hit
InterProiView protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPFKAP_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: Q01813
Secondary accession number(s): B3KS15, Q5VSR7, Q5VSR8
<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 1, 1993
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 199 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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