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Entry version 154 (03 Jul 2019)
Sequence version 3 (23 Jan 2007)
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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

Pfkm

Organism
Rattus norvegicus (Rat)
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.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<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

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. Hexokinase-3 (Hk3), Mutant type II hexokinase, Hexokinase-4 (Gck), Hexokinase-2 (Hk2), Hexokinase-3 (Hk3), Phosphotransferase (Gck), Hexokinase-1 (Hk1), Hexokinase 3, isoform CRA_a (Hk3), Phosphotransferase (Gck), Hexokinase-1 (Hk1), Uncharacterized protein
  2. Glucose-6-phosphate isomerase (Gpi)
  3. ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkl), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase (Aldoc), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (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 <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 sitei25ATP; via amide nitrogenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi119Magnesium; catalyticUniRule annotation1
<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 sitei166Proton acceptorUniRule annotation1
Binding sitei201Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Binding sitei292Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei471Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei566Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei629Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei655Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei735Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

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 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

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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-70171 Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P47858

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, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
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:Pfkm
Synonyms:Pfk-m
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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

Organism-specific databases

Rat genome database

More...
RGDi
68419 Pfkm

<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

Keywords - Cellular componenti

Cytoplasm

<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_00001120202 – 780ATP-dependent 6-phosphofructokinase, muscle 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-acetylthreonineBy similarity1
Modified residuei133PhosphoserineCombined sources1
Modified residuei377PhosphoserineCombined 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>Glycosylationi530O-linked (GlcNAc) serineBy similarity1
Modified residuei775PhosphoserineCombined 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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P47858

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

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PaxDbi
P47858

PRoteomics IDEntifications database

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PRIDEi
P47858

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P47858

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

More...
PhosphoSitePlusi
P47858

<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 (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable).

Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).

UniRule annotationBy similarityCurated

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
249268, 5 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2050 6-phosphofructokinase, M4 homotetramer
CPX-2058 6-phosphofructokinase, ML3 heterotetramer
CPX-2059 6-phosphofructokinase, M2L2 heterotetramer
CPX-2060 6-phosphofructokinase, M3L heterotetramer

Protein interaction database and analysis system

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IntActi
P47858, 2 interactors

Molecular INTeraction database

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MINTi
P47858

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000013374

<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

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SMRi
P47858

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 – 390N-terminal catalytic PFK domain 1Add BLAST389
Regioni164 – 166Substrate bindingUniRule annotation3
Regioni208 – 210Substrate bindingUniRule annotation3
Regioni298 – 301Substrate bindingUniRule annotation4
Regioni391 – 401Interdomain linkerAdd BLAST11
Regioni402 – 780C-terminal regulatory PFK domain 2Add BLAST379
Regioni528 – 532Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni573 – 575Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni661 – 664Allosteric 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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000200154

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P47858

KEGG Orthology (KO)

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KOi
K00850

Database of Orthologous Groups

More...
OrthoDBi
172878at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P47858

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00764 Eukaryotic_PFK, 1 hit

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

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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>. 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>Sequence (1+)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.

<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.

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

P47858-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTHEEHHEAK TLGIGKAIAV LTSGGDAQGM NATVRAVVRV GIFTGLRVFF
60 70 80 90 100
VHEGYQGLVD GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLNDLQ KDGKITAEER
160 170 180 190 200
TKSSYLNIVF LVGSIDNDFC GTDMTIGTDS ALHRIVEIVD AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET
260 270 280 290 300
RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NTAVRLPLME
360 370 380 390 400
CVQVTKDVTK AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL
410 420 430 440 450
HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE
460 470 480 490 500
AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ ISANITKYNI QGLVIIGGFE
510 520 530 540 550
AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI GADTALNTIC
560 570 580 590 600
TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
610 620 630 640 650
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG
660 670 680 690 700
IFDSRKNVLG HMQQGGNPTP FDRNFATKMG AKATNWMSGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVTELKDQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
Length:780
Mass (Da):85,560
Last modified:January 23, 2007 - v3
<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:iCECC3995C4F271FA
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2KBC7A0A0G2KBC7_RAT
ATP-dependent 6-phosphofructokinase
Pfkm
851Annotation score:

Annotation score:4 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>
Q52KS1Q52KS1_RAT
ATP-dependent 6-phosphofructokinase
Pfkm Pfk-M, rCG_50717
780Annotation score:

Annotation score:4 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 conflicti33T → A in BAA21013 (Ref. 3) Curated1
Sequence conflicti46L → A in BAA21013 (Ref. 3) Curated1
Sequence conflicti150R → A in BAA21013 (Ref. 3) Curated1
Sequence conflicti160F → G in BAA21013 (Ref. 3) Curated1
Sequence conflicti180S → F in BAA21013 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U25651 mRNA Translation: AAC52786.1
D21869 mRNA Translation: BAA21013.1

Protein sequence database of the Protein Information Resource

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PIRi
S71429

NCBI Reference Sequences

More...
RefSeqi
NP_113903.1, NM_031715.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
65152

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:65152

UCSC genome browser

More...
UCSCi
RGD:68419 rat

<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
U25651 mRNA Translation: AAC52786.1
D21869 mRNA Translation: BAA21013.1
PIRiS71429
RefSeqiNP_113903.1, NM_031715.1

3D structure databases

SMRiP47858
ModBaseiSearch...

Protein-protein interaction databases

BioGridi249268, 5 interactors
ComplexPortaliCPX-2050 6-phosphofructokinase, M4 homotetramer
CPX-2058 6-phosphofructokinase, ML3 heterotetramer
CPX-2059 6-phosphofructokinase, M2L2 heterotetramer
CPX-2060 6-phosphofructokinase, M3L heterotetramer
IntActiP47858, 2 interactors
MINTiP47858
STRINGi10116.ENSRNOP00000013374

PTM databases

iPTMnetiP47858
PhosphoSitePlusiP47858

Proteomic databases

jPOSTiP47858
PaxDbiP47858
PRIDEiP47858

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi65152
KEGGirno:65152
UCSCiRGD:68419 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5213
RGDi68419 Pfkm

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
HOGENOMiHOG000200154
InParanoidiP47858
KOiK00850
OrthoDBi172878at2759
PhylomeDBiP47858

Enzyme and pathway databases

UniPathwayiUPA00109;UER00182
ReactomeiR-RNO-70171 Glycolysis
SABIO-RKiP47858

Miscellaneous databases

Protein Ontology

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PROi
PR:P47858

Family and domain databases

CDDicd00764 Eukaryotic_PFK, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiPFKAM_RAT
<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: P47858
Secondary accession number(s): Q63736
<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: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 3, 2019
This is version 154 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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