Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Due to a server migration, the UniProt 'ID mapping', 'Peptide search' and 'community bibliography submission' tools will not be available on the 19th April 2021 during the morning (EST).

UniProtKB - P12928 (KPYR_RAT)

Entry version 187 (07 Apr 2021)
Sequence version 2 (01 Feb 1995)
Previous versions | rss
Add a publicationFeedback
Protein

Pyruvate kinase PKLR

Gene

Pklr

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

Plays a key role in glycolysis.By similarity

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. 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.

<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 fructose 1,6-bisphosphate.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 (LOC108351137), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase
  2. Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase (RGD1560402), Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase (Pgk2)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), 2-phospho-D-glycerate hydro-lyase (Eno1), 2-phospho-D-glycerate hydro-lyase (Eno1), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase (Eno4), Beta-enolase (Eno3), Gamma-enolase (Eno2), 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydro-lyase
  5. Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (LOC100362738), Pyruvate kinase (Pkm), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase
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 sitei116SubstrateBy 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 bindingi118PotassiumBy similarity1
Metal bindingi120PotassiumBy similarity1
Metal bindingi156PotassiumBy similarity1
Metal bindingi157Potassium; via carbonyl oxygenBy similarity1
Binding sitei163ATPBy similarity1
Binding sitei250ATPBy 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>Sitei313Transition state stabilizerBy similarity1
Metal bindingi315MagnesiumBy similarity1
Binding sitei338Substrate; via amide nitrogenBy similarity1
Metal bindingi339MagnesiumBy similarity1
Binding sitei339Substrate; via amide nitrogenBy similarity1
Binding sitei371SubstrateBy similarity1
Binding sitei525Fructose-1,6-bisphosphate; allosteric activatorBy similarity1
Binding sitei532Fructose-1,6-bisphosphate; allosteric activatorBy 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 bindingi118 – 121ATPBy 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
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-70171, Glycolysis

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P12928

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 PKLR (EC:2.7.1.40)
Alternative name(s):
L-PK
Pyruvate kinase isozymes L/R
<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:Pklr
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Rattus
<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
  • UP000002494 <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 2

Organism-specific databases

Rat genome database

More...RGDi		3336, Pklr

<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

<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		CHEMBL3089

<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_00001120961 – 574Pyruvate kinase PKLRAdd BLAST574

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 residuei2PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei43PhosphoserineBy similarity1
Modified residuei292PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P12928

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

More...PaxDbi		P12928

PRoteomics IDEntifications database

More...PRIDEi		P12928

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12928

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

More...PhosphoSitePlusi		P12928

<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		ENSRNOG00000020420, Expressed in duodenum and 18 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P12928, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P12928, 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%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

Homotetramer.

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P12928, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000027700

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P12928

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

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P12928

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni475 – 480Fructose-1,6-bisphosphate binding; allosteric activatorBy similarity6
Regioni559 – 564Fructose-1,6-bisphosphate binding; allosteric activatorBy 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		P12928

Identification of Orthologs from Complete Genome Data

More...OMAi		MVRVHHL

Database of Orthologous Groups

More...OrthoDBi		933620at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12928

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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform R-type (identifier: P12928-1) [UniParc]FASTAAdd to basket
Also known as: PKR

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
MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE 
        60         70         80         90        100
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS 
       110        120        130        140        150
VDRLKEMIKA GMNIARLNFS HGSHEYHAES IANIREATES FATSPLSYRP 
       160        170        180        190        200
VAIALDTKGP EIRTGVLQGG PESEVEIVKG SQVLVTVDPK FQTRGDAKTV 
       210        220        230        240        250
WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV EHGGILGSRK 
       260        270        280        290        300
GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA 
       310        320        330        340        350
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF 
       360        370        380        390        400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD 
       410        420        430        440        450
CIMLSGETAK GSFPVEAVMM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD 
       460        470        480        490        500
PTEVTAIGAV EASFKCCAAA IIVLTKTGRS AQLLSQYRPR AAVIAVTRSA 
       510        520        530        540        550
QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG KLRGFLRVGD 
       560        570 
LVIVVTGWRP GSGYTNIMRV LSVS
Length:574
Mass (Da):62,200
Last modified:February 1, 1995 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6BBC544653C51380
GO
Isoform L-type (identifier: P12928-2) [UniParc]FASTAAdd to basket
Also known as: PKL

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSVQENTLPQQLWPWIFRSQKDLAKSALSGAPG → ME

Show »
Length:543
Mass (Da):58,794
Checksum:iE5472B97649E2A47
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
A0A0H2UI07A0A0H2UI07_RAT
Pyruvate kinase
Pklr
558Annotation 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>

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 conflicti130S → Y in AAA41882 (PubMed:3654663).Curated1
Sequence conflicti130S → Y in AAA41883 (PubMed:3654663).Curated1
Sequence conflicti322K → R in AAA41882 (PubMed:3654663).Curated1
Sequence conflicti322K → R in AAA41883 (PubMed:3654663).Curated1
Sequence conflicti498R → G in AAA41880 (PubMed:3080337).Curated1
Sequence conflicti501Q → K in AAA41880 (PubMed:3080337).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_0028841 – 33MSVQE…SGAPG → ME in isoform L-type. CuratedAdd BLAST33

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
M17091 M17090 Genomic DNA Translation: AAA41882.1
M17091 M17090 Genomic DNA Translation: AAA41883.1
M17685 mRNA Translation: AAA41881.1
X05684 Genomic DNA Translation: CAA29169.1
M11709 mRNA Translation: AAA41880.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27427, KIRTPR
A92940, KIRTPL

NCBI Reference Sequences

More...RefSeqi		NP_036756.3, NM_012624.3 [P12928-2]
XP_006232655.1, XM_006232593.3 [P12928-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420 [P12928-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24651

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24651

UCSC genome browser

More...UCSCi		RGD:3336, rat [P12928-1]

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
M17091 M17090 Genomic DNA Translation: AAA41882.1
M17091 M17090 Genomic DNA Translation: AAA41883.1
M17685 mRNA Translation: AAA41881.1
X05684 Genomic DNA Translation: CAA29169.1
M11709 mRNA Translation: AAA41880.1
PIRiA27427, KIRTPR
A92940, KIRTPL
RefSeqiNP_036756.3, NM_012624.3 [P12928-2]
XP_006232655.1, XM_006232593.3 [P12928-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6ECHX-ray2.19A/B/C/D34-574[»]
6ECKX-ray2.36A/B34-574[»]
SMRiP12928
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP12928, 1 interactor
STRINGi10116.ENSRNOP00000027700

Chemistry databases

BindingDBiP12928
ChEMBLiCHEMBL3089

PTM databases

iPTMnetiP12928
PhosphoSitePlusiP12928

Proteomic databases

jPOSTiP12928
PaxDbiP12928
PRIDEiP12928

Genome annotation databases

EnsembliENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420 [P12928-1]
GeneIDi24651
KEGGirno:24651
UCSCiRGD:3336, rat [P12928-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5313
RGDi3336, Pklr

Phylogenomic databases

eggNOGiKOG2323, Eukaryota
GeneTreeiENSGT00390000008859
HOGENOMiCLU_015439_0_1_1
InParanoidiP12928
OMAiMVRVHHL
OrthoDBi933620at2759
PhylomeDBiP12928
TreeFamiTF300390

Enzyme and pathway databases

UniPathwayiUPA00109;UER00188
ReactomeiR-RNO-70171, Glycolysis
SABIO-RKiP12928

Miscellaneous databases

Protein Ontology

More...PROi		PR:P12928

Gene expression databases

BgeeiENSRNOG00000020420, Expressed in duodenum and 18 other tissues
ExpressionAtlasiP12928, baseline and differential
GenevisibleiP12928, RN

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 nameiKPYR_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: P12928
Secondary accession number(s): P04763, Q64618
<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, 1989
Last sequence update: February 1, 1995
Last modified: April 7, 2021
This is version 187 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again