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Protein

Pyruvate kinase PKM

Gene

Pkm

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

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity).By similarity

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.

<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

Protein has several cofactor binding sites:

<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 D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator (By similarity).By similarity

<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 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (LOC108351137), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh)
  2. Phosphoglycerate kinase (Pgk2), Phosphoglycerate kinase, Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), Gamma-enolase (Eno2), Beta-enolase (Eno3)
  5. Pyruvate kinase (Pkm), Pyruvate kinase, Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase, Pyruvate kinase PKLR (Pklr), Pyruvate kinase PKM (Pkm)
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 pyruvate from D-glyceraldehyde 3-phosphate, 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 sitei70SerineBy similarity1
Binding sitei73SubstrateBy similarity1
<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 bindingi75PotassiumBy similarity1
Metal bindingi77PotassiumBy similarity1
Binding sitei106SerineBy similarity1
Metal bindingi113PotassiumBy similarity1
Metal bindingi114Potassium; via carbonyl oxygenBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei270Transition state stabilizerBy similarity1
Metal bindingi272MagnesiumBy similarity1
Binding sitei295Substrate; via amide nitrogenBy similarity1
Metal bindingi296MagnesiumBy similarity1
Binding sitei296Substrate; via amide nitrogenBy similarity1
Binding sitei328SubstrateBy similarity1
Binding sitei464SerineBy similarity1
Binding sitei482D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity1
Binding sitei489D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity1

<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, Potassium, Pyruvate

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-6798695 Neutrophil degranulation
R-RNO-70171 Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P11980

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

More...
UniPathwayi
UPA00109;UER00188

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P11980

<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:
Pyruvate kinase PKM (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase muscle isozyme
<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:Pkm
Synonyms:Pkm2, Pykm
<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: Chromosome 8

Organism-specific databases

Rat genome database

More...
RGDi
3337 Pkm

<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, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4994

<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_00001120921 – 531Pyruvate kinase PKMAdd BLAST531

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 residuei3N6,N6,N6-trimethyllysineBy similarity1
Modified residuei37PhosphoserineBy similarity1
Modified residuei41PhosphothreonineBy similarity1
Modified residuei62N6-acetyllysineBy similarity1
Modified residuei66N6-succinyllysineBy similarity1
Modified residuei89N6-acetyllysineBy similarity1
Modified residuei97PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei105PhosphotyrosineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei127PhosphoserineBy similarity1
Modified residuei148PhosphotyrosineBy similarity1
Modified residuei166N6-acetyllysine; alternateBy similarity1
Modified residuei166N6-succinyllysine; alternateBy similarity1
Cross-linki166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei175PhosphotyrosineBy similarity1
Modified residuei195PhosphothreonineBy similarity1
Modified residuei266N6-acetyllysine; alternateBy similarity1
Cross-linki266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei270N6-acetyllysine; alternateBy similarity1
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei322N6-acetyllysine; alternateBy similarity1
Modified residuei322N6-succinyllysine; alternateBy similarity1
Modified residuei4084-hydroxyprolineBy similarity1
Modified residuei475N6-acetyllysineBy similarity1
Modified residuei498N6-succinyllysineBy similarity1

<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

ISGylated.By similarity
Under hypoxia, hydroxylated by EGLN3.By similarity
Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P11980

PRoteomics IDEntifications database

More...
PRIDEi
P11980

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P11980

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11980

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

More...
PhosphoSitePlusi
P11980

<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
ENSRNOG00000011329 Expressed in 9 organ(s), highest expression level in skeletal muscle tissue

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P11980 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P11980 RN

<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

Monomer and homotetramer. Exists as a monomer in the absence of fructose 1,6 bi-phosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. FBP stimulates the formation of tetramers from dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (By similarity). Interacts (isoform M2, but not isoform M1) with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (By similarity). Interacts with JMJD8 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247659, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P11980

Protein interaction database and analysis system

More...
IntActi
P11980, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000015331

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P11980

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P11980

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

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SMRi
P11980

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>Regioni307 – 531Interaction with POU5F1By similarityAdd BLAST225
Regioni389 – 433Intersubunit contactAdd BLAST45
Regioni432 – 437D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity6
Regioni514 – 521D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity8

<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 pyruvate kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2323 Eukaryota
COG0469 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008859

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000021559

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000941

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11980

KEGG Orthology (KO)

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KOi
K00873

Identification of Orthologs from Complete Genome Data

More...
OMAi
KHEAIEQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0597

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P11980

TreeFam database of animal gene trees

More...
TreeFami
TF300390

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00288 Pyruvate_Kinase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.33.10, 1 hit
3.40.1380.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001697 Pyr_Knase
IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
IPR011037 Pyrv_Knase-like_insert_dom_sf
IPR018209 Pyrv_Knase_AS
IPR015793 Pyrv_Knase_brl
IPR015795 Pyrv_Knase_C
IPR036918 Pyrv_Knase_C_sf
IPR015806 Pyrv_Knase_insert_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR11817 PTHR11817, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00224 PK, 1 hit
PF02887 PK_C, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01050 PYRUVTKNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50800 SSF50800, 1 hit
SSF51621 SSF51621, 1 hit
SSF52935 SSF52935, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01064 pyruv_kin, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00110 PYRUVATE_KINASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform M1 (identifier: P11980-1) [UniParc]FASTAAdd to basket
Also known as: PKM1

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
MPKPDSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT
60 70 80 90 100
IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS
110 120 130 140 150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME
160 170 180 190 200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DYLVTEVENG
210 220 230 240 250
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKAAD
260 270 280 290 300
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
310 320 330 340 350
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN
360 370 380 390 400
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAVF HRLLFEELAR
410 420 430 440 450
ASSQSTDPLE AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI
460 470 480 490 500
IAVTRNPQTA RQAHLYRGIF PVLCKDAVLD AWAEDVDLRV NLAMNVGKAR
510 520 530
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
Length:531
Mass (Da):57,818
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:iF0B133FDDD5991A9
GO
Isoform M2 (identifier: P11980-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: PKM2

The sequence of this isoform differs from the canonical sequence as follows:
     389-433: VFHRLLFEEL...LAAALIVLTE → IYHLQLFEEL...CSGAIIVLTK

Show »
Length:531
Mass (Da):57,781
Checksum:i321D9EB3500272DA
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
A0A0G2JVG3A0A0G2JVG3_RAT
Pyruvate kinase
Pkm
489Annotation score:

Annotation score:2 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>

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_011107389 – 433VFHRL…IVLTE → IYHLQLFEELRRLAPITSDP TEAAAVGAVEASFKCCSGAI IVLTK in isoform M2. CuratedAdd BLAST45

Sequence databases

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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

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DDBJi
Links Updated
M24359 Genomic DNA Translation: AAB93666.1
M24359 Genomic DNA Translation: AAB93667.1
M14377 Genomic DNA No translation available.
X15800 mRNA Translation: CAA33799.1

Protein sequence database of the Protein Information Resource

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PIRi
A26186
B26186

NCBI Reference Sequences

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RefSeqi
NP_445749.1, NM_053297.2 [P11980-1]
XP_006243250.2, XM_006243188.3 [P11980-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Rn.1556

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000015332; ENSRNOP00000015331; ENSRNOG00000011329 [P11980-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
25630

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25630

UCSC genome browser

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UCSCi
RGD:3337 rat [P11980-1]

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
M24359 Genomic DNA Translation: AAB93666.1
M24359 Genomic DNA Translation: AAB93667.1
M14377 Genomic DNA No translation available.
X15800 mRNA Translation: CAA33799.1
PIRiA26186
B26186
RefSeqiNP_445749.1, NM_053297.2 [P11980-1]
XP_006243250.2, XM_006243188.3 [P11980-2]
UniGeneiRn.1556

3D structure databases

ProteinModelPortaliP11980
SMRiP11980
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247659, 3 interactors
CORUMiP11980
IntActiP11980, 4 interactors
STRINGi10116.ENSRNOP00000015331

Chemistry databases

BindingDBiP11980
ChEMBLiCHEMBL4994

Protein family/group databases

MoonProtiP11980

PTM databases

iPTMnetiP11980
PhosphoSitePlusiP11980

2D gel databases

World-2DPAGEi0004:P11980

Proteomic databases

PaxDbiP11980
PRIDEiP11980

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015332; ENSRNOP00000015331; ENSRNOG00000011329 [P11980-1]
GeneIDi25630
KEGGirno:25630
UCSCiRGD:3337 rat [P11980-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5315
RGDi3337 Pkm

Phylogenomic databases

eggNOGiKOG2323 Eukaryota
COG0469 LUCA
GeneTreeiENSGT00390000008859
HOGENOMiHOG000021559
HOVERGENiHBG000941
InParanoidiP11980
KOiK00873
OMAiKHEAIEQ
OrthoDBiEOG091G0597
PhylomeDBiP11980
TreeFamiTF300390

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00188

ReactomeiR-RNO-6798695 Neutrophil degranulation
R-RNO-70171 Glycolysis
SABIO-RKiP11980

Miscellaneous databases

Protein Ontology

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PROi
PR:P11980

Gene expression databases

BgeeiENSRNOG00000011329 Expressed in 9 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasiP11980 baseline and differential
GenevisibleiP11980 RN

Family and domain databases

CDDicd00288 Pyruvate_Kinase, 1 hit
Gene3Di2.40.33.10, 1 hit
3.40.1380.20, 1 hit
InterProiView protein in InterPro
IPR001697 Pyr_Knase
IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
IPR011037 Pyrv_Knase-like_insert_dom_sf
IPR018209 Pyrv_Knase_AS
IPR015793 Pyrv_Knase_brl
IPR015795 Pyrv_Knase_C
IPR036918 Pyrv_Knase_C_sf
IPR015806 Pyrv_Knase_insert_dom_sf
PANTHERiPTHR11817 PTHR11817, 1 hit
PfamiView protein in Pfam
PF00224 PK, 1 hit
PF02887 PK_C, 1 hit
PRINTSiPR01050 PYRUVTKNASE
SUPFAMiSSF50800 SSF50800, 1 hit
SSF51621 SSF51621, 1 hit
SSF52935 SSF52935, 1 hit
TIGRFAMsiTIGR01064 pyruv_kin, 1 hit
PROSITEiView protein in PROSITE
PS00110 PYRUVATE_KINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiKPYM_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: P11980
Secondary accession number(s): P11981
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 177 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, Direct protein sequencing, 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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