Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate kinase PKLR

Gene

PKLR

Organism
Homo sapiens (Human)
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:
  • Mg2+1 Publication
  • K+1 Publication

Enzyme regulationi

Allosterically activated by fructose 1,6-bisphosphate.1 Publication

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, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM2)
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 sitei116SubstrateCombined sources1 Publication1
Metal bindingi118PotassiumCombined sources1 Publication1
Metal bindingi120PotassiumCombined sources1 Publication1
Metal bindingi156PotassiumCombined sources1 Publication1
Metal bindingi157Potassium; via carbonyl oxygenCombined sources1 Publication1
Binding sitei313Substrate; via amide nitrogenCombined sources1 Publication1
Sitei313Transition state stabilizerBy similarity1
Metal bindingi315ManganeseCombined sources1 Publication1
Binding sitei338Substrate; via amide nitrogenCombined sources1 Publication1
Metal bindingi339ManganeseCombined sources1 Publication1
Binding sitei339Substrate; via amide nitrogenCombined sources1 Publication1
Binding sitei371SubstrateCombined sources1 Publication1
Binding sitei525Allosteric activatorCombined sources1 Publication1
Binding sitei532Allosteric activatorCombined sources1 Publication1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • potassium ion binding Source: InterPro
  • pyruvate kinase activity Source: UniProtKB

GO - Biological processi

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

BioCyciMetaCyc:HS07088-MONOMER.
ZFISH:HS07088-MONOMER.
BRENDAi2.7.1.40. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-210745. Regulation of gene expression in beta cells.
R-HSA-70171. Glycolysis.
SABIO-RKP30613.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKLR (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase 1
Pyruvate kinase isozymes L/R
R-type/L-type pyruvate kinase
Red cell/liver pyruvate kinase
Gene namesi
Name:PKLR
Synonyms:PK1, PKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9020. PKLR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Pyruvate kinase hyperactivity (PKHYP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant phenotype characterized by increase of red blood cell ATP.
See also OMIM:102900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01143537G → E in PKHYP. 1 PublicationCorresponds to variant rs118204087dbSNPEnsembl.1
Pyruvate kinase deficiency of red cells (PKRD)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia.
See also OMIM:266200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05846740R → W in PKRD. 1 Publication1
Natural variantiVAR_05846848 – 53Missing in PKRD. 1 Publication6
Natural variantiVAR_05846973L → P in PKRD. 1 Publication1
Natural variantiVAR_01143680S → P in PKRD. 1
Natural variantiVAR_01143786R → P in PKRD. 1
Natural variantiVAR_01143890I → N in PKRD. 1 Publication1
Natural variantiVAR_01143995G → R in PKRD. Corresponds to variant rs750857114dbSNPEnsembl.1
Natural variantiVAR_004028107M → T in PKRD. 1
Natural variantiVAR_011440111G → R in PKRD. 1 Publication1
Natural variantiVAR_011441115A → P in PKRD; Val de Marne. 1
Natural variantiVAR_011442120S → F in PKRD; Beaujon. 1
Natural variantiVAR_011443130S → Y in PKRD; Conakry. 1 PublicationCorresponds to variant rs118204089dbSNPEnsembl.1
Natural variantiVAR_004029131Missing in PKRD. 1
Natural variantiVAR_004030134V → D in PKRD. 1 PublicationCorresponds to variant rs574051756dbSNPEnsembl.1
Natural variantiVAR_011474153I → T in PKRD. 1
Natural variantiVAR_058470154A → T in PKRD. 1 PublicationCorresponds to variant rs780192373dbSNPEnsembl.1
Natural variantiVAR_004031155L → P in PKRD. 1 Publication1
Natural variantiVAR_011444159G → V in PKRD. 1
Natural variantiVAR_004033163R → C in PKRD; Linz. 1 PublicationCorresponds to variant rs118204083dbSNPEnsembl.1
Natural variantiVAR_058471163R → L in PKRD. 1 Publication1
Natural variantiVAR_058472165G → V in PKRD. 1 Publication1
Natural variantiVAR_004032172E → Q in PKRD; Sassari. 1 PublicationCorresponds to variant rs757359024dbSNPEnsembl.1
Natural variantiVAR_011475219I → T in PKRD. Corresponds to variant rs200572803dbSNPEnsembl.1
Natural variantiVAR_004034221D → DD in PKRD. 1
Natural variantiVAR_011445222G → A in PKRD; Katsushika. 1
Natural variantiVAR_011447263G → R in PKRD. 1
Natural variantiVAR_011448263G → W in PKRD. 1
Natural variantiVAR_058473272L → V in PKRD. 1 PublicationCorresponds to variant rs147659527dbSNPEnsembl.1
Natural variantiVAR_004035275G → R in PKRD. Corresponds to variant rs747549978dbSNPEnsembl.1
Natural variantiVAR_004036281D → N in PKRD. 1
Natural variantiVAR_004037287F → V in PKRD. 1
Natural variantiVAR_011449288V → L in PKRD; Moriguchi. 1
Natural variantiVAR_011446293D → N in PKRD. 1
Natural variantiVAR_011450295A → V in PKRD. Corresponds to variant rs766353400dbSNPEnsembl.1
Natural variantiVAR_011451310I → N in PKRD; Dordrecht. 1 Publication1
Natural variantiVAR_004038314I → T in PKRD; Hong Kong. 1
Natural variantiVAR_011452315E → K in PKRD. 1
Natural variantiVAR_058474320V → L in PKRD. 1 PublicationCorresponds to variant rs549295725dbSNPEnsembl.1
Natural variantiVAR_004039331D → E in PKRD; Parma. 1 PublicationCorresponds to variant rs138476691dbSNPEnsembl.1
Natural variantiVAR_011453331D → N in PKRD. Corresponds to variant rs773893686dbSNPEnsembl.1
Natural variantiVAR_004040332G → S in PKRD; loss of catalytical activity. 3 PublicationsCorresponds to variant rs773626254dbSNPEnsembl.1
Natural variantiVAR_011476335V → M in PKRD. 1 Publication1
Natural variantiVAR_004041336A → S in PKRD. 1 Publication1
Natural variantiVAR_004042337R → P in PKRD. 1 Publication1
Natural variantiVAR_004043337R → Q in PKRD. 1 Publication1
Natural variantiVAR_004044339D → H in PKRD. 1 Publication1
Natural variantiVAR_004045341G → A in PKRD. 2 Publications1
Natural variantiVAR_011454341G → D in PKRD. 1
Natural variantiVAR_011455342I → F in PKRD. 1
Natural variantiVAR_011456348K → N in PKRD; Kamata. 1
Natural variantiVAR_011457348Missing in PKRD; Brescia. 1 Publication1
Natural variantiVAR_011477352A → D in PKRD. 1
Natural variantiVAR_004046354Missing in PKRD. 1 Publication1
Natural variantiVAR_004047357I → T in PKRD. 1 PublicationCorresponds to variant rs779152555dbSNPEnsembl.1
Natural variantiVAR_058475358G → E in PKRD. 1 Publication1
Natural variantiVAR_004048359R → C in PKRD; Aomori. Corresponds to variant rs138871700dbSNPEnsembl.1
Natural variantiVAR_004049359R → H in PKRD. 1 Publication1
Natural variantiVAR_004050361N → D in PKRD. 1 PublicationCorresponds to variant rs765903674dbSNPEnsembl.1
Natural variantiVAR_011458364G → D in PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity. 1 Publication1
Natural variantiVAR_004051368V → F in PKRD; Osaka. 1 Publication1
Natural variantiVAR_058476374L → P in PKRD. 1 Publication1
Natural variantiVAR_011459376S → I in PKRD. 1
Natural variantiVAR_004052384T → M in PKRD; Tokyo/Beirut; most common mutation in Japanese population; no conformational change. 3 PublicationsCorresponds to variant rs74315362dbSNPEnsembl.1
Natural variantiVAR_011478385R → W in PKRD. 1
Natural variantiVAR_011460387E → G in PKRD. 1 Publication1
Natural variantiVAR_011461390D → N in PKRD; Mantova; almost complete inactivation. 1 PublicationCorresponds to variant rs147034239dbSNPEnsembl.1
Natural variantiVAR_004053392A → T in PKRD. 1 Publication1
Natural variantiVAR_004054393N → K in PKRD. 1 Publication1
Natural variantiVAR_004055393N → S in PKRD; Paris. 1 PublicationCorresponds to variant rs776594413dbSNPEnsembl.1
Natural variantiVAR_011462394A → D in PKRD. 1 Publication1
Natural variantiVAR_011463394A → V in PKRD. 1 Publication1
Natural variantiVAR_004056401C → CS in PKRD. 1
Natural variantiVAR_011464408T → A in PKRD; Hirosaki. 1
Natural variantiVAR_004057408T → I in PKRD. 1 Publication1
Natural variantiVAR_004058421Q → K in PKRD; Fukushima/Maebashi/Sendai. 1 PublicationCorresponds to variant rs118204084dbSNPEnsembl.1
Natural variantiVAR_004059426R → Q in PKRD; Sapporo. 1 PublicationCorresponds to variant rs768002493dbSNPEnsembl.1
Natural variantiVAR_004060426R → W in PKRD; Naniwa. 1
Natural variantiVAR_011465427E → A in PKRD. 1
Natural variantiVAR_011466427E → D in PKRD. 1
Natural variantiVAR_004061431A → T in PKRD. 1 PublicationCorresponds to variant rs762591322dbSNPEnsembl.1
Natural variantiVAR_004062458G → D in PKRD. 1 PublicationCorresponds to variant rs755522396dbSNPEnsembl.1
Natural variantiVAR_004063459A → V in PKRD. 1
Natural variantiVAR_004064460V → M in PKRD. 1 PublicationCorresponds to variant rs752034960dbSNPEnsembl.1
Natural variantiVAR_011479468A → G in PKRD. Corresponds to variant rs750540943dbSNPEnsembl.1
Natural variantiVAR_004065468A → V in PKRD; Hadano. 1
Natural variantiVAR_011467477T → A in PKRD. Corresponds to variant rs759466273dbSNPEnsembl.1
Natural variantiVAR_011480479R → H in PKRD; Amish; no conformational change. 2 PublicationsCorresponds to variant rs118204085dbSNPEnsembl.1
Natural variantiVAR_011468485S → F in PKRD. 1
Natural variantiVAR_004066486R → W in PKRD; frequent mutation; no conformational change. 4 PublicationsCorresponds to variant rs116100695dbSNPEnsembl.1
Natural variantiVAR_011469488R → Q in PKRD. Corresponds to variant rs369183199dbSNPEnsembl.1
Natural variantiVAR_004067490R → W in PKRD. Corresponds to variant rs200133000dbSNPEnsembl.1
Natural variantiVAR_011470495A → T in PKRD. 1
Natural variantiVAR_004068495A → V in PKRD. 1 PublicationCorresponds to variant rs141560532dbSNPEnsembl.1
Natural variantiVAR_004069498R → C in PKRD. 1 PublicationCorresponds to variant rs551883218dbSNPEnsembl.1
Natural variantiVAR_004070498R → H in PKRD. 2 PublicationsCorresponds to variant rs758327704dbSNPEnsembl.1
Natural variantiVAR_011471504R → L in PKRD; instability of the protein. 1 PublicationCorresponds to variant rs185753709dbSNPEnsembl.1
Natural variantiVAR_004071510R → Q in PKRD; the most common mutation in European population. 3 PublicationsCorresponds to variant rs113403872dbSNPEnsembl.1
Natural variantiVAR_011472511G → R in PKRD. 1
Natural variantiVAR_011473531R → C in PKRD. 1
Natural variantiVAR_004072532R → Q in PKRD. 1 PublicationCorresponds to variant rs758278200dbSNPEnsembl.1
Natural variantiVAR_004073532R → W in PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP. 2 PublicationsCorresponds to variant rs201255024dbSNPEnsembl.1
Natural variantiVAR_004074552V → M in PKRD. Corresponds to variant rs370316462dbSNPEnsembl.1
Natural variantiVAR_011481557G → A in PKRD. 1
Natural variantiVAR_004075559R → G in PKRD. 1
Natural variantiVAR_004076566N → K in PKRD. 1
Natural variantiVAR_011482569R → Q in PKRD. 1 PublicationCorresponds to variant rs61755431dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi5313.
MalaCardsiPKLR.
MIMi102900. phenotype.
266200. phenotype.
OpenTargetsiENSG00000143627.
ENSG00000262785.
Orphaneti766. Hemolytic anemia due to red cell pyruvate kinase deficiency.
PharmGKBiPA33352.

Chemistry databases

ChEMBLiCHEMBL1075126.
DrugBankiDB00119. Pyruvic acid.

Polymorphism and mutation databases

BioMutaiPKLR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120941 – 574Pyruvate kinase PKLRAdd BLAST574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineCombined sources1
Modified residuei19PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei109N6-succinyllysineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei148PhosphotyrosineBy similarity1
Modified residuei292PhosphoserineCombined sources1
Modified residuei313N6-acetyllysineBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP30613.
MaxQBiP30613.
PaxDbiP30613.
PeptideAtlasiP30613.
PRIDEiP30613.

2D gel databases

REPRODUCTION-2DPAGEP30613.
SWISS-2DPAGEP30613.

PTM databases

iPTMnetiP30613.
PhosphoSitePlusiP30613.
SwissPalmiP30613.

Miscellaneous databases

PMAP-CutDBP30613.

Expressioni

Gene expression databases

BgeeiENSG00000143627.
CleanExiHS_PKLR.
ExpressionAtlasiP30613. baseline and differential.
GenevisibleiP30613. HS.

Organism-specific databases

HPAiCAB034376.
CAB034378.
HPA006653.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi111330. 15 interactors.
IntActiP30613. 6 interactors.
STRINGi9606.ENSP00000339933.

Chemistry databases

BindingDBiP30613.

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni49 – 51Combined sources3
Helixi55 – 57Combined sources3
Helixi61 – 64Combined sources4
Helixi69 – 74Combined sources6
Beta strandi88 – 93Combined sources6
Turni96 – 98Combined sources3
Helixi101 – 110Combined sources10
Beta strandi112 – 118Combined sources7
Helixi124 – 139Combined sources16
Turni140 – 143Combined sources4
Helixi145 – 147Combined sources3
Beta strandi152 – 156Combined sources5
Beta strandi162 – 164Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi182 – 186Combined sources5
Helixi189 – 191Combined sources3
Beta strandi199 – 203Combined sources5
Helixi207 – 210Combined sources4
Beta strandi216 – 219Combined sources4
Turni220 – 223Combined sources4
Beta strandi224 – 232Combined sources9
Beta strandi235 – 242Combined sources8
Beta strandi244 – 246Combined sources3
Beta strandi251 – 253Combined sources3
Helixi266 – 277Combined sources12
Beta strandi281 – 285Combined sources5
Helixi291 – 301Combined sources11
Helixi303 – 305Combined sources3
Beta strandi309 – 314Combined sources6
Helixi317 – 321Combined sources5
Helixi323 – 329Combined sources7
Beta strandi330 – 336Combined sources7
Helixi337 – 343Combined sources7
Helixi346 – 348Combined sources3
Helixi349 – 363Combined sources15
Beta strandi367 – 372Combined sources6
Helixi375 – 378Combined sources4
Helixi385 – 397Combined sources13
Beta strandi400 – 405Combined sources6
Helixi406 – 409Combined sources4
Helixi414 – 430Combined sources17
Helixi434 – 442Combined sources9
Helixi451 – 466Combined sources16
Beta strandi469 – 474Combined sources6
Beta strandi476 – 478Combined sources3
Helixi479 – 485Combined sources7
Beta strandi490 – 498Combined sources9
Helixi500 – 505Combined sources6
Helixi506 – 508Combined sources3
Beta strandi512 – 516Combined sources5
Helixi525 – 542Combined sources18
Beta strandi551 – 561Combined sources11
Beta strandi565 – 572Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VGBX-ray2.73A/B/C/D47-574[»]
2VGFX-ray2.75A/B/C/D47-574[»]
2VGGX-ray2.74A/B/C/D47-574[»]
2VGIX-ray2.87A/B/C/D47-574[»]
4IMAX-ray1.95A/B/C/D34-574[»]
4IP7X-ray1.80A/B/C/D34-574[»]
ProteinModelPortaliP30613.
SMRiP30613.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30613.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni475 – 480Allosteric activator bindingCombined sources1 Publication6
Regioni559 – 564Allosteric activator bindingCombined sources1 Publication6

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP30613.
KOiK12406.
OMAiPFERSED.
OrthoDBiEOG091G0597.
PhylomeDBiP30613.
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: P30613-1) [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
MSIQENISSL QLRSWVSKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE
60 70 80 90 100
LGTAFFQQQQ LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS
110 120 130 140 150
VERLKEMIKA GMNIARLNFS HGSHEYHAES IANVREAVES FAGSPLSYRP
160 170 180 190 200
VAIALDTKGP EIRTGILQGG PESEVELVKG SQVLVTVDPA FRTRGNANTV
210 220 230 240 250
WVDYPNIVRV VPVGGRIYID DGLISLVVQK IGPEGLVTQV ENGGVLGSRK
260 270 280 290 300
GVNLPGAQVD LPGLSEQDVR DLRFGVEHGV DIVFASFVRK ASDVAAVRAA
310 320 330 340 350
LGPEGHGIKI ISKIENHEGV KRFDEILEVS DGIMVARGDL GIEIPAEKVF
360 370 380 390 400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD
410 420 430 440 450
CIMLSGETAK GNFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD
460 470 480 490 500
PTEVTAIGAV EAAFKCCAAA IIVLTTTGRS AQLLSRYRPR AAVIAVTRSA
510 520 530 540 550
QAARQVHLCR GVFPLLYREP PEAIWADDVD RRVQFGIESG KLRGFLRVGD
560 570
LVIVVTGWRP GSGYTNIMRV LSIS
Length:574
Mass (Da):61,830
Last modified:May 30, 2000 - v2
Checksum:i3B430896832032F5
GO
Isoform L-type (identifier: P30613-2) [UniParc]FASTAAdd to basket
Also known as: PKL

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

Show »
Length:543
Mass (Da):58,494
Checksum:iCA16D3984B868D9E
GO

Sequence cautioni

The sequence BAA02515 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti381P → A in BAA02515 (Ref. 3) Curated1
Sequence conflicti423A → R in AAA60104 (PubMed:3126495).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01143537G → E in PKHYP. 1 PublicationCorresponds to variant rs118204087dbSNPEnsembl.1
Natural variantiVAR_05846740R → W in PKRD. 1 Publication1
Natural variantiVAR_05846848 – 53Missing in PKRD. 1 Publication6
Natural variantiVAR_05846973L → P in PKRD. 1 Publication1
Natural variantiVAR_01143680S → P in PKRD. 1
Natural variantiVAR_01143786R → P in PKRD. 1
Natural variantiVAR_01143890I → N in PKRD. 1 Publication1
Natural variantiVAR_01143995G → R in PKRD. Corresponds to variant rs750857114dbSNPEnsembl.1
Natural variantiVAR_004028107M → T in PKRD. 1
Natural variantiVAR_011440111G → R in PKRD. 1 Publication1
Natural variantiVAR_011441115A → P in PKRD; Val de Marne. 1
Natural variantiVAR_011442120S → F in PKRD; Beaujon. 1
Natural variantiVAR_011443130S → Y in PKRD; Conakry. 1 PublicationCorresponds to variant rs118204089dbSNPEnsembl.1
Natural variantiVAR_004029131Missing in PKRD. 1
Natural variantiVAR_004030134V → D in PKRD. 1 PublicationCorresponds to variant rs574051756dbSNPEnsembl.1
Natural variantiVAR_011474153I → T in PKRD. 1
Natural variantiVAR_058470154A → T in PKRD. 1 PublicationCorresponds to variant rs780192373dbSNPEnsembl.1
Natural variantiVAR_004031155L → P in PKRD. 1 Publication1
Natural variantiVAR_011444159G → V in PKRD. 1
Natural variantiVAR_004033163R → C in PKRD; Linz. 1 PublicationCorresponds to variant rs118204083dbSNPEnsembl.1
Natural variantiVAR_058471163R → L in PKRD. 1 Publication1
Natural variantiVAR_058472165G → V in PKRD. 1 Publication1
Natural variantiVAR_004032172E → Q in PKRD; Sassari. 1 PublicationCorresponds to variant rs757359024dbSNPEnsembl.1
Natural variantiVAR_011475219I → T in PKRD. Corresponds to variant rs200572803dbSNPEnsembl.1
Natural variantiVAR_004034221D → DD in PKRD. 1
Natural variantiVAR_011445222G → A in PKRD; Katsushika. 1
Natural variantiVAR_011447263G → R in PKRD. 1
Natural variantiVAR_011448263G → W in PKRD. 1
Natural variantiVAR_058473272L → V in PKRD. 1 PublicationCorresponds to variant rs147659527dbSNPEnsembl.1
Natural variantiVAR_004035275G → R in PKRD. Corresponds to variant rs747549978dbSNPEnsembl.1
Natural variantiVAR_004036281D → N in PKRD. 1
Natural variantiVAR_004037287F → V in PKRD. 1
Natural variantiVAR_011449288V → L in PKRD; Moriguchi. 1
Natural variantiVAR_011446293D → N in PKRD. 1
Natural variantiVAR_011450295A → V in PKRD. Corresponds to variant rs766353400dbSNPEnsembl.1
Natural variantiVAR_011451310I → N in PKRD; Dordrecht. 1 Publication1
Natural variantiVAR_004038314I → T in PKRD; Hong Kong. 1
Natural variantiVAR_011452315E → K in PKRD. 1
Natural variantiVAR_058474320V → L in PKRD. 1 PublicationCorresponds to variant rs549295725dbSNPEnsembl.1
Natural variantiVAR_004039331D → E in PKRD; Parma. 1 PublicationCorresponds to variant rs138476691dbSNPEnsembl.1
Natural variantiVAR_011453331D → N in PKRD. Corresponds to variant rs773893686dbSNPEnsembl.1
Natural variantiVAR_004040332G → S in PKRD; loss of catalytical activity. 3 PublicationsCorresponds to variant rs773626254dbSNPEnsembl.1
Natural variantiVAR_011476335V → M in PKRD. 1 Publication1
Natural variantiVAR_004041336A → S in PKRD. 1 Publication1
Natural variantiVAR_004042337R → P in PKRD. 1 Publication1
Natural variantiVAR_004043337R → Q in PKRD. 1 Publication1
Natural variantiVAR_004044339D → H in PKRD. 1 Publication1
Natural variantiVAR_004045341G → A in PKRD. 2 Publications1
Natural variantiVAR_011454341G → D in PKRD. 1
Natural variantiVAR_011455342I → F in PKRD. 1
Natural variantiVAR_011456348K → N in PKRD; Kamata. 1
Natural variantiVAR_011457348Missing in PKRD; Brescia. 1 Publication1
Natural variantiVAR_011477352A → D in PKRD. 1
Natural variantiVAR_004046354Missing in PKRD. 1 Publication1
Natural variantiVAR_004047357I → T in PKRD. 1 PublicationCorresponds to variant rs779152555dbSNPEnsembl.1
Natural variantiVAR_058475358G → E in PKRD. 1 Publication1
Natural variantiVAR_004048359R → C in PKRD; Aomori. Corresponds to variant rs138871700dbSNPEnsembl.1
Natural variantiVAR_004049359R → H in PKRD. 1 Publication1
Natural variantiVAR_004050361N → D in PKRD. 1 PublicationCorresponds to variant rs765903674dbSNPEnsembl.1
Natural variantiVAR_011458364G → D in PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity. 1 Publication1
Natural variantiVAR_004051368V → F in PKRD; Osaka. 1 Publication1
Natural variantiVAR_058476374L → P in PKRD. 1 Publication1
Natural variantiVAR_011459376S → I in PKRD. 1
Natural variantiVAR_004052384T → M in PKRD; Tokyo/Beirut; most common mutation in Japanese population; no conformational change. 3 PublicationsCorresponds to variant rs74315362dbSNPEnsembl.1
Natural variantiVAR_011478385R → W in PKRD. 1
Natural variantiVAR_011460387E → G in PKRD. 1 Publication1
Natural variantiVAR_011461390D → N in PKRD; Mantova; almost complete inactivation. 1 PublicationCorresponds to variant rs147034239dbSNPEnsembl.1
Natural variantiVAR_004053392A → T in PKRD. 1 Publication1
Natural variantiVAR_004054393N → K in PKRD. 1 Publication1
Natural variantiVAR_004055393N → S in PKRD; Paris. 1 PublicationCorresponds to variant rs776594413dbSNPEnsembl.1
Natural variantiVAR_011462394A → D in PKRD. 1 Publication1
Natural variantiVAR_011463394A → V in PKRD. 1 Publication1
Natural variantiVAR_004056401C → CS in PKRD. 1
Natural variantiVAR_011464408T → A in PKRD; Hirosaki. 1
Natural variantiVAR_004057408T → I in PKRD. 1 Publication1
Natural variantiVAR_004058421Q → K in PKRD; Fukushima/Maebashi/Sendai. 1 PublicationCorresponds to variant rs118204084dbSNPEnsembl.1
Natural variantiVAR_004059426R → Q in PKRD; Sapporo. 1 PublicationCorresponds to variant rs768002493dbSNPEnsembl.1
Natural variantiVAR_004060426R → W in PKRD; Naniwa. 1
Natural variantiVAR_011465427E → A in PKRD. 1
Natural variantiVAR_011466427E → D in PKRD. 1
Natural variantiVAR_004061431A → T in PKRD. 1 PublicationCorresponds to variant rs762591322dbSNPEnsembl.1
Natural variantiVAR_004062458G → D in PKRD. 1 PublicationCorresponds to variant rs755522396dbSNPEnsembl.1
Natural variantiVAR_004063459A → V in PKRD. 1
Natural variantiVAR_004064460V → M in PKRD. 1 PublicationCorresponds to variant rs752034960dbSNPEnsembl.1
Natural variantiVAR_011479468A → G in PKRD. Corresponds to variant rs750540943dbSNPEnsembl.1
Natural variantiVAR_004065468A → V in PKRD; Hadano. 1
Natural variantiVAR_011467477T → A in PKRD. Corresponds to variant rs759466273dbSNPEnsembl.1
Natural variantiVAR_011480479R → H in PKRD; Amish; no conformational change. 2 PublicationsCorresponds to variant rs118204085dbSNPEnsembl.1
Natural variantiVAR_011468485S → F in PKRD. 1
Natural variantiVAR_004066486R → W in PKRD; frequent mutation; no conformational change. 4 PublicationsCorresponds to variant rs116100695dbSNPEnsembl.1
Natural variantiVAR_011469488R → Q in PKRD. Corresponds to variant rs369183199dbSNPEnsembl.1
Natural variantiVAR_004067490R → W in PKRD. Corresponds to variant rs200133000dbSNPEnsembl.1
Natural variantiVAR_011470495A → T in PKRD. 1
Natural variantiVAR_004068495A → V in PKRD. 1 PublicationCorresponds to variant rs141560532dbSNPEnsembl.1
Natural variantiVAR_004069498R → C in PKRD. 1 PublicationCorresponds to variant rs551883218dbSNPEnsembl.1
Natural variantiVAR_004070498R → H in PKRD. 2 PublicationsCorresponds to variant rs758327704dbSNPEnsembl.1
Natural variantiVAR_011471504R → L in PKRD; instability of the protein. 1 PublicationCorresponds to variant rs185753709dbSNPEnsembl.1
Natural variantiVAR_018848506V → I.1 PublicationCorresponds to variant rs8177988dbSNPEnsembl.1
Natural variantiVAR_004071510R → Q in PKRD; the most common mutation in European population. 3 PublicationsCorresponds to variant rs113403872dbSNPEnsembl.1
Natural variantiVAR_011472511G → R in PKRD. 1
Natural variantiVAR_011473531R → C in PKRD. 1
Natural variantiVAR_004072532R → Q in PKRD. 1 PublicationCorresponds to variant rs758278200dbSNPEnsembl.1
Natural variantiVAR_004073532R → W in PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP. 2 PublicationsCorresponds to variant rs201255024dbSNPEnsembl.1
Natural variantiVAR_004074552V → M in PKRD. Corresponds to variant rs370316462dbSNPEnsembl.1
Natural variantiVAR_011481557G → A in PKRD. 1
Natural variantiVAR_004075559R → G in PKRD. 1
Natural variantiVAR_004076566N → K in PKRD. 1
Natural variantiVAR_011482569R → Q in PKRD. 1 PublicationCorresponds to variant rs61755431dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0028831 – 33MSIQE…IGAPG → ME in isoform L-type. CuratedAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015983 mRNA. Translation: BAA31706.1.
M15465 mRNA. Translation: AAA60104.1.
D13243 Genomic DNA. Translation: BAA02515.1. Sequence problems.
AY316591 Genomic DNA. Translation: AAP69527.1.
BC025737 mRNA. Translation: AAH25737.1.
S60712 mRNA. Translation: AAB26262.1.
CCDSiCCDS1109.1. [P30613-1]
CCDS44240.1. [P30613-2]
PIRiI52269. KIHUPR.
RefSeqiNP_000289.1. NM_000298.5. [P30613-1]
NP_870986.1. NM_181871.3. [P30613-2]
UniGeneiHs.95990.

Genome annotation databases

EnsembliENST00000342741; ENSP00000339933; ENSG00000143627. [P30613-1]
ENST00000392414; ENSP00000376214; ENSG00000143627. [P30613-2]
ENST00000571194; ENSP00000461487; ENSG00000262785. [P30613-2]
ENST00000572740; ENSP00000459921; ENSG00000262785. [P30613-1]
GeneIDi5313.
KEGGihsa:5313.
UCSCiuc001fka.5. human. [P30613-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Pyruvate kinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015983 mRNA. Translation: BAA31706.1.
M15465 mRNA. Translation: AAA60104.1.
D13243 Genomic DNA. Translation: BAA02515.1. Sequence problems.
AY316591 Genomic DNA. Translation: AAP69527.1.
BC025737 mRNA. Translation: AAH25737.1.
S60712 mRNA. Translation: AAB26262.1.
CCDSiCCDS1109.1. [P30613-1]
CCDS44240.1. [P30613-2]
PIRiI52269. KIHUPR.
RefSeqiNP_000289.1. NM_000298.5. [P30613-1]
NP_870986.1. NM_181871.3. [P30613-2]
UniGeneiHs.95990.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VGBX-ray2.73A/B/C/D47-574[»]
2VGFX-ray2.75A/B/C/D47-574[»]
2VGGX-ray2.74A/B/C/D47-574[»]
2VGIX-ray2.87A/B/C/D47-574[»]
4IMAX-ray1.95A/B/C/D34-574[»]
4IP7X-ray1.80A/B/C/D34-574[»]
ProteinModelPortaliP30613.
SMRiP30613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111330. 15 interactors.
IntActiP30613. 6 interactors.
STRINGi9606.ENSP00000339933.

Chemistry databases

BindingDBiP30613.
ChEMBLiCHEMBL1075126.
DrugBankiDB00119. Pyruvic acid.

PTM databases

iPTMnetiP30613.
PhosphoSitePlusiP30613.
SwissPalmiP30613.

Polymorphism and mutation databases

BioMutaiPKLR.

2D gel databases

REPRODUCTION-2DPAGEP30613.
SWISS-2DPAGEP30613.

Proteomic databases

EPDiP30613.
MaxQBiP30613.
PaxDbiP30613.
PeptideAtlasiP30613.
PRIDEiP30613.

Protocols and materials databases

DNASUi5313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342741; ENSP00000339933; ENSG00000143627. [P30613-1]
ENST00000392414; ENSP00000376214; ENSG00000143627. [P30613-2]
ENST00000571194; ENSP00000461487; ENSG00000262785. [P30613-2]
ENST00000572740; ENSP00000459921; ENSG00000262785. [P30613-1]
GeneIDi5313.
KEGGihsa:5313.
UCSCiuc001fka.5. human. [P30613-1]

Organism-specific databases

CTDi5313.
DisGeNETi5313.
GeneCardsiPKLR.
HGNCiHGNC:9020. PKLR.
HPAiCAB034376.
CAB034378.
HPA006653.
MalaCardsiPKLR.
MIMi102900. phenotype.
266200. phenotype.
609712. gene.
neXtProtiNX_P30613.
OpenTargetsiENSG00000143627.
ENSG00000262785.
Orphaneti766. Hemolytic anemia due to red cell pyruvate kinase deficiency.
PharmGKBiPA33352.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiP30613.
KOiK12406.
OMAiPFERSED.
OrthoDBiEOG091G0597.
PhylomeDBiP30613.
TreeFamiTF300390.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciMetaCyc:HS07088-MONOMER.
ZFISH:HS07088-MONOMER.
BRENDAi2.7.1.40. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-210745. Regulation of gene expression in beta cells.
R-HSA-70171. Glycolysis.
SABIO-RKP30613.

Miscellaneous databases

EvolutionaryTraceiP30613.
GeneWikiiPKLR.
GenomeRNAii5313.
PMAP-CutDBP30613.
PROiP30613.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143627.
CleanExiHS_PKLR.
ExpressionAtlasiP30613. baseline and differential.
GenevisibleiP30613. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P30613
Secondary accession number(s): O75758, P11973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: November 30, 2016
This is version 199 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.