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UniProtKB - P52480 (KPYM_MOUSE)

Entry version 210 (07 Apr 2021)
Sequence version 4 (01 May 2007)
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Protein

Pyruvate kinase PKM

Gene

Pkm

Organism
Mus musculus (Mouse)
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 (By similarity). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (By similarity). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (By similarity). In addition to its role in glycolysis, also regulates transcription (By similarity). Stimulates POU5F1-mediated transcriptional activation (By similarity). Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages (PubMed:29996098). Also acts as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (PubMed:28575669). Plays a general role in caspase independent cell death of tumor cells (By similarity).By similarity2 Publications

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%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated by 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%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

This protein is involved in step 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 (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm10358), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs)
  2. Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase 2 (Pgk2)
  3. no protein annotated in this organism
  4. 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno4), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno4), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno1), 2-phospho-D-glycerate hydro-lyase (EG433182), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno4), Gamma-enolase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno3), Alpha-enolase (Eno1), Beta-enolase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno2), 2-phospho-D-glycerate hydro-lyase (Eno3), 2-phospho-D-glycerate hydro-lyase (Eno1), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pkm), Pyruvate kinase (Pkm), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei70SerineBy similarity1
Binding sitei73SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi75PotassiumBy similarity1
Metal bindingi77PotassiumBy similarity1
Binding sitei106SerineBy similarity1
Metal bindingi113PotassiumBy similarity1
Metal bindingi114Potassium; via carbonyl oxygenBy similarity1
Binding sitei120ATPBy similarity1
Binding sitei207ATPBy similarity1
Binding sitei270Substrate; via amide nitrogenBy 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
Sitei433Crucial for phosphotyrosine bindingBy 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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi75 – 78ATPBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis, Translation regulation
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P52480

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

More...UniPathwayi		UPA00109;UER00188

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Pyruvate kinase PKM (EC:2.7.1.40By similarity)
Alternative name(s):
Pyruvate kinase muscle isozyme
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Pkm
Synonyms:Pk3, Pkm2, Pykm
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:97591, 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

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Myeloid-cell-specific ARNTL/BMAL1 and PKM2 double knockout reduces the risk of sepsis lethality which is associated with reduced serum lactate levels and reduced CD274 expression in macrophages.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi367K → M: Abolishes pyruvate kinase activity without affecting interaction with the ribosome. 1 Publication1
Mutagenesisi464H → A: Abolishes amino-acid binding without affecting interaction with the translating ribosome. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001120891 – 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-acetyllysineCombined sources1
Modified residuei66N6-succinyllysineCombined sources1
Modified residuei89N6-acetyllysineBy similarity1
Modified residuei97PhosphoserineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei105PhosphotyrosineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 residuei148PhosphotyrosineCombined sources1
Modified residuei166N6-acetyllysine; alternateCombined sources1
Modified residuei166N6-succinyllysine; alternateCombined sources1
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; alternateCombined sources1
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei322N6-acetyllysine; alternateCombined sources1
Modified residuei322N6-succinyllysine; alternateCombined sources1
Modified residuei4034-hydroxyprolineBy similarity1
Modified residuei4084-hydroxyprolineBy similarity1
Modified residuei433N6-acetyllysineBy similarity1
Modified residuei475N6-acetyllysineCombined sources1
Modified residuei498N6-succinyllysineCombined sources1

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

ISGylated.1 Publication
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

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3588
non-CPTAC-3654

Encyclopedia of Proteome Dynamics

More...EPDi		P52480

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P52480

MaxQB - The MaxQuant DataBase

More...MaxQBi		P52480

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

More...PaxDbi		P52480

PeptideAtlas

More...PeptideAtlasi		P52480

PRoteomics IDEntifications database

More...PRIDEi		P52480

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		263452 [P52480-1]
263453 [P52480-2]

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00407130
P52480

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P52480

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P52480

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

More...PhosphoSitePlusi		P52480

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P52480

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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Embryonic stem cells and embryonal carcinoma cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000032294, Expressed in retinal neural layer and 116 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P52480, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P52480, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202191, 54 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3059, PKM2 pyruvate kinase complex (tetramer) [P52480-1]
CPX-3060, PKM2 pyruvate kinase complex (dimer) [P52480-1]
CPX-3096, PKM1 pyruvate kinase complex [P52480-2]

Database of interacting proteins

More...DIPi		DIP-40536N

Protein interaction database and analysis system

More...IntActi		P52480, 33 interactors

Molecular INTeraction database

More...MINTi		P52480

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000034834

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P52480, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...SMRi		P52480

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>Regioni307 – 531Interaction with POU5F1By similarityAdd BLAST225
Regioni389 – 433Intersubunit contactAdd BLAST45
Regioni432 – 437D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity6
Regioni516 – 521D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity6

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00390000008859

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_015439_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P52480

Identification of Orthologs from Complete Genome Data

More...OMAi		QVPIVQK

Database of Orthologous Groups

More...OrthoDBi		933620at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P52480

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
3.20.20.60, 1 hit
3.40.1380.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001697, Pyr_Knase
IPR015813, Pyrv/PenolPyrv_Kinase-like_dom
IPR040442, Pyrv_Kinase-like_dom_sf
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

More...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

More...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

More...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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 M2 (identifier: P52480-1) [UniParc]FASTAAdd to basket
Also known as: PKM21 Publication

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

« Hide
        10         20         30         40         50
MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT 
        60         70         80         90        100
IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS 
       110        120        130        140        150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 
       160        170        180        190        200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DFLVTEVENG 
       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 IAREAEAAIY HLQLFEELRR 
       410        420        430        440        450
LAPITSDPTE AAAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI 
       460        470        480        490        500
IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN AWAEDVDLRV NLAMDVGKAR 
       510        520        530 
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
Length:531
Mass (Da):57,845
Last modified:May 1, 2007 - v4
<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:i34CBBC01BC0C047D
GO
Isoform M1 (identifier: P52480-2) [UniParc]FASTAAdd to basket
Also known as: PKM11 Publication

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

Show »
Length:531
Mass (Da):57,985
Checksum:iD0D163786CC6D4A6
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
A0A1L1SQV8A0A1L1SQV8_MOUSE
Pyruvate kinase
Pkm
187Annotation 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>
A0A1L1SSN6A0A1L1SSN6_MOUSE
Pyruvate kinase
Pkm
176Annotation 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>
A0A1L1ST52A0A1L1ST52_MOUSE
Pyruvate kinase
Pkm
102Annotation 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>
A0A1L1STV8A0A1L1STV8_MOUSE
Pyruvate kinase
Pkm
184Annotation 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>
A0A1L1SU37A0A1L1SU37_MOUSE
Pyruvate kinase
Pkm
232Annotation 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>
A0A1L1SUV0A0A1L1SUV0_MOUSE
Pyruvate kinase
Pkm
155Annotation 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>
A0A1L1SVH2A0A1L1SVH2_MOUSE
Pyruvate kinase PKM
Pkm
51Annotation 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 conflicti8A → V in CAA65761 (PubMed:9545585).Curated1
Sequence conflicti121T → A in BAE30642 (PubMed:16141072).Curated1
Sequence conflicti121T → A in BAE32031 (PubMed:16141072).Curated1
Sequence conflicti158W → R in BAA07457 (PubMed:7612666).Curated1
Sequence conflicti166K → E in BAE42098 (PubMed:16141072).Curated1
Sequence conflicti170V → L in BAE30642 (PubMed:16141072).Curated1
Sequence conflicti170V → L in BAE32031 (PubMed:16141072).Curated1
Sequence conflicti177D → G in BAE42199 (PubMed:16141072).Curated1
Sequence conflicti230K → R in BAE30642 (PubMed:16141072).Curated1
Sequence conflicti230K → R in BAE32031 (PubMed:16141072).Curated1
Sequence conflicti299I → T in BAA07457 (PubMed:7612666).Curated1
Sequence conflicti309A → S in BAA07457 (PubMed:7612666).Curated1
Sequence conflicti327A → S in BAA07457 (PubMed:7612666).Curated1
Sequence conflicti327A → S in CAA65761 (PubMed:9545585).Curated1
Sequence conflicti333S → I in BAA07457 (PubMed:7612666).Curated1
Sequence conflicti333S → I in CAA65761 (PubMed:9545585).Curated1
Sequence conflicti485D → N in BAE33055 (PubMed:16141072).Curated1
Sequence conflicti485D → N in BAE42192 (PubMed:16141072).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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_025057389 – 433IYHLQ…IVLTK → MFHRLLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationAdd BLAST45

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D38379 mRNA Translation: BAA07457.1
X97047 mRNA Translation: CAA65761.1
AK002341 mRNA Translation: BAB22025.1
AK135397 mRNA Translation: BAE22519.1
AK151724 mRNA Translation: BAE30642.1
AK153483 mRNA Translation: BAE32031.1
AK155110 mRNA Translation: BAE33055.1
AK155655 mRNA Translation: BAE33370.1
AK170892 mRNA Translation: BAE42098.1
AK168943 mRNA Translation: BAE40751.1
AK171023 mRNA Translation: BAE42192.1
AK171033 mRNA Translation: BAE42199.1
AC160637 Genomic DNA No translation available.
BC016619 mRNA Translation: AAH16619.1
BC094663 mRNA Translation: AAH94663.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS40659.1 [P52480-1]
CCDS57681.1 [P52480-2]

Protein sequence database of the Protein Information Resource

More...PIRi		S55921

NCBI Reference Sequences

More...RefSeqi		NP_001240812.1, NM_001253883.1 [P52480-2]
NP_035229.2, NM_011099.3 [P52480-1]
XP_006510918.1, XM_006510855.1 [P52480-1]
XP_011240975.1, XM_011242673.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294 [P52480-1]
ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294 [P52480-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18746

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18746

UCSC genome browser

More...UCSCi		uc009pyf.2, mouse [P52480-1]
uc009pyh.2, mouse [P52480-2]

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
D38379 mRNA Translation: BAA07457.1
X97047 mRNA Translation: CAA65761.1
AK002341 mRNA Translation: BAB22025.1
AK135397 mRNA Translation: BAE22519.1
AK151724 mRNA Translation: BAE30642.1
AK153483 mRNA Translation: BAE32031.1
AK155110 mRNA Translation: BAE33055.1
AK155655 mRNA Translation: BAE33370.1
AK170892 mRNA Translation: BAE42098.1
AK168943 mRNA Translation: BAE40751.1
AK171023 mRNA Translation: BAE42192.1
AK171033 mRNA Translation: BAE42199.1
AC160637 Genomic DNA No translation available.
BC016619 mRNA Translation: AAH16619.1
BC094663 mRNA Translation: AAH94663.1
CCDSiCCDS40659.1 [P52480-1]
CCDS57681.1 [P52480-2]
PIRiS55921
RefSeqiNP_001240812.1, NM_001253883.1 [P52480-2]
NP_035229.2, NM_011099.3 [P52480-1]
XP_006510918.1, XM_006510855.1 [P52480-1]
XP_011240975.1, XM_011242673.1

3D structure databases

SMRiP52480
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202191, 54 interactors
ComplexPortaliCPX-3059, PKM2 pyruvate kinase complex (tetramer) [P52480-1]
CPX-3060, PKM2 pyruvate kinase complex (dimer) [P52480-1]
CPX-3096, PKM1 pyruvate kinase complex [P52480-2]
DIPiDIP-40536N
IntActiP52480, 33 interactors
MINTiP52480
STRINGi10090.ENSMUSP00000034834

PTM databases

iPTMnetiP52480
PhosphoSitePlusiP52480
SwissPalmiP52480

2D gel databases

REPRODUCTION-2DPAGEiIPI00407130
P52480
SWISS-2DPAGEiP52480

Proteomic databases

CPTACinon-CPTAC-3588
non-CPTAC-3654
EPDiP52480
jPOSTiP52480
MaxQBiP52480
PaxDbiP52480
PeptideAtlasiP52480
PRIDEiP52480
ProteomicsDBi263452 [P52480-1]
263453 [P52480-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		14162, 1177 antibodies

Genome annotation databases

EnsembliENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294 [P52480-1]
ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294 [P52480-2]
GeneIDi18746
KEGGimmu:18746
UCSCiuc009pyf.2, mouse [P52480-1]
uc009pyh.2, mouse [P52480-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5315
MGIiMGI:97591, Pkm

Phylogenomic databases

eggNOGiKOG2323, Eukaryota
GeneTreeiENSGT00390000008859
HOGENOMiCLU_015439_0_1_1
InParanoidiP52480
OMAiQVPIVQK
OrthoDBi933620at2759
PhylomeDBiP52480
TreeFamiTF300390

Enzyme and pathway databases

UniPathwayiUPA00109;UER00188
ReactomeiR-MMU-6798695, Neutrophil degranulation
R-MMU-70171, Glycolysis
SABIO-RKiP52480

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		18746, 23 hits in 52 CRISPR screens

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

More...ChiTaRSi		Pkm, mouse

Protein Ontology

More...PROi		PR:P52480
RNActiP52480, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000032294, Expressed in retinal neural layer and 116 other tissues
ExpressionAtlasiP52480, baseline and differential
GenevisibleiP52480, MM

Family and domain databases

CDDicd00288, Pyruvate_Kinase, 1 hit
Gene3Di2.40.33.10, 1 hit
3.20.20.60, 1 hit
3.40.1380.20, 1 hit
InterProiView protein in InterPro
IPR001697, Pyr_Knase
IPR015813, Pyrv/PenolPyrv_Kinase-like_dom
IPR040442, Pyrv_Kinase-like_dom_sf
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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKPYM_MOUSE
<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: P52480
Secondary accession number(s): Q3TBV8
, Q3TBW5, Q3TC59, Q3U1X3, Q3U5P6, Q4VC20, Q64484, Q91YI8, Q9CWB1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: April 7, 2021
This is version 210 of the entry and version 4 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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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