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Protein

Pyruvate kinase PKLR

Gene

Pklr

Organism
Rattus norvegicus (Rat)
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, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (LOC108351137), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh-ps2), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (RGD1562758)
  2. Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Alpha-enolase (Eno1), Beta-enolase (Eno3), Gamma-enolase (Eno2)
  5. Pyruvate kinase PKLR (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (LOC100362738), Pyruvate kinase (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (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

  • ATP biosynthetic process Source: RGD
  • carbohydrate metabolic process Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • glycolytic process Source: RGD
  • pyruvate biosynthetic process Source: RGD
  • response to ATP Source: RGD
  • response to cAMP Source: RGD
  • response to glucose Source: RGD
  • response to heat Source: RGD
  • response to hypoxia Source: RGD
  • response to lithium ion Source: RGD
  • response to metal ion Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
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-RNO-70171. Glycolysis.
SABIO-RKP12928.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi3336. Pklr.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3089.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120961 – 574Pyruvate kinase PKLRAdd BLAST574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei43PhosphoserineBy 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

PaxDbiP12928.
PRIDEiP12928.

PTM databases

iPTMnetiP12928.
PhosphoSitePlusiP12928.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020420.
ExpressionAtlasiP12928. baseline and differential.
GenevisibleiP12928. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP12928. 1 interactor.
STRINGi10116.ENSRNOP00000027700.

Chemistry databases

BindingDBiP12928.

Structurei

3D structure databases

ProteinModelPortaliP12928.
SMRiP12928.
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.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP12928.
KOiK12406.
OMAiPFERSED.
OrthoDBiEOG091G0597.
PhylomeDBiP12928.
TreeFamiTF300390.

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: P12928-1) [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
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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Alternative sequenceiVSP_0028841 – 33MSVQE…SGAPG → ME in isoform L-type. CuratedAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41882.1.
M17091
, M17088, M17089, 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]
UniGeneiRn.48821.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17091
, M17088, M17089, M17090 Genomic DNA. Translation: AAA41882.1.
M17091
, M17088, M17089, 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]
UniGeneiRn.48821.

3D structure databases

ProteinModelPortaliP12928.
SMRiP12928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12928. 1 interactor.
STRINGi10116.ENSRNOP00000027700.

Chemistry databases

BindingDBiP12928.
ChEMBLiCHEMBL3089.

PTM databases

iPTMnetiP12928.
PhosphoSitePlusiP12928.

Proteomic databases

PaxDbiP12928.
PRIDEiP12928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5313.
RGDi3336. Pklr.

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP12928.
KOiK12406.
OMAiPFERSED.
OrthoDBiEOG091G0597.
PhylomeDBiP12928.
TreeFamiTF300390.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
ReactomeiR-RNO-70171. Glycolysis.
SABIO-RKP12928.

Miscellaneous databases

PROiP12928.

Gene expression databases

BgeeiENSRNOG00000020420.
ExpressionAtlasiP12928. baseline and differential.
GenevisibleiP12928. RN.

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_RAT
AccessioniPrimary (citable) accession number: P12928
Secondary accession number(s): P04763, Q64618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 161 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.