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Protein

Pyruvate kinase PKLR

Gene

Pklr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in glycolysis.By similarity

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate.By similarity

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, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (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
Binding sitei116SubstrateBy similarity1
Metal bindingi118PotassiumBy similarity1
Metal bindingi120PotassiumBy similarity1
Metal bindingi156PotassiumBy similarity1
Metal bindingi157Potassium; via carbonyl oxygenBy similarity1
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 sitei525Allosteric activatorBy similarity1
Binding sitei532Allosteric activatorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • endocrine pancreas development Source: Reactome
  • positive regulation of cellular metabolic process Source: Reactome
  • response to other organism Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-210745. Regulation of gene expression in beta cells.
SABIO-RKP53657.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKLR (EC:2.7.1.40)
Alternative name(s):
L-PK
Pyruvate kinase isozymes L/R
Gene namesi
Name:Pklr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97604. Pklr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120951 – 574Pyruvate kinase PKLRAdd BLAST574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei43Phosphoserine; by PKABy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei109N6-succinyllysineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei148PhosphotyrosineBy similarity1
Modified residuei292PhosphoserineBy similarity1
Modified residuei313N6-acetyllysineBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP53657.
PeptideAtlasiP53657.
PRIDEiP53657.

PTM databases

iPTMnetiP53657.
PhosphoSitePlusiP53657.

Expressioni

Gene expression databases

CleanExiMM_PKLR.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiP53657. 5 interactors.
MINTiMINT-1854544.
STRINGi10090.ENSMUSP00000035417.

Structurei

3D structure databases

ProteinModelPortaliP53657.
SMRiP53657.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni475 – 480Allosteric activator bindingBy similarity6
Regioni559 – 564Allosteric activator bindingBy similarity6

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP53657.
PhylomeDBiP53657.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform R-type (identifier: P53657-1) [UniParc]FASTAAdd to basket
Also known as: PKR

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
MSVQENELPQ QLWPWIFKSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE
60 70 80 90 100
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS
110 120 130 140 150
VDRLKEMIKA GMNIARLNFS HGSHEYHAES IANIREAAES FATSPLSYRP
160 170 180 190 200
VAIALDTKGP EIRTGVLQGG PESEVEIVKG SQVLVTVDPK FRTRGDAKTV
210 220 230 240 250
WVDYHNITQV VAVGGRIYID DGLISLVVRK IGPEGLVTEV EHGGFLGNRK
260 270 280 290 300
GVNLPNAEVD LPGLSEQDLL DLRFGVEHYV DIIFASFVRK ASDVVAVRDA
310 320 330 340 350
LGPEGRGIKI ISKIENHEGV KKFDEILEVS DGIMMARGDL GIEIPAEKVF
360 370 380 390 400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD
410 420 430 440 450
CIMLSGETAK GSFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD
460 470 480 490 500
PTEVTAIGAV EASFKCCAAA IIVLTKTGRS AQLLSRYRPR AAVIAVTRSA
510 520 530 540 550
QAARQVHLSR GVFPLLYREP PEAVWADDVD RRVQFGIESG KLRGFLRVGD
560 570
LVIVVTGWRP GSGYTNIMRV LTIS
Length:574
Mass (Da):62,309
Last modified:October 1, 1996 - v1
Checksum:i6C4689DE954E6166
GO
Isoform L-type (identifier: P53657-2)
Also known as: PKL
Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79731 mRNA. Translation: AAB35435.1.
D63764 mRNA. Translation: BAA23642.1.
CCDSiCCDS17489.1. [P53657-1]
UniGeneiMm.383180.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79731 mRNA. Translation: AAB35435.1.
D63764 mRNA. Translation: BAA23642.1.
CCDSiCCDS17489.1. [P53657-1]
UniGeneiMm.383180.

3D structure databases

ProteinModelPortaliP53657.
SMRiP53657.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53657. 5 interactors.
MINTiMINT-1854544.
STRINGi10090.ENSMUSP00000035417.

PTM databases

iPTMnetiP53657.
PhosphoSitePlusiP53657.

Proteomic databases

PaxDbiP53657.
PeptideAtlasiP53657.
PRIDEiP53657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:97604. Pklr.

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP53657.
PhylomeDBiP53657.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-210745. Regulation of gene expression in beta cells.
SABIO-RKP53657.

Miscellaneous databases

ChiTaRSiPklr. mouse.
PROiP53657.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PKLR.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPYR_MOUSE
AccessioniPrimary (citable) accession number: P53657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.