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Protein

Pyruvate kinase PKM

Gene

PKM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.3 Publications

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.2 Publications

Cofactori

Protein has several cofactor binding sites:

Activity regulationi

Isoform M2 is allosterically activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator of isoform M2.6 Publications

Kineticsi

  1. KM=2.7 mM for phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)2 Publications
  2. KM=0.17 mM for phosphoenolpyruvate (in the presence of 2 mM D-fructose 1,6-bisphosphate (FBP), at 32 degrees Celsius, pH 8.0)2 Publications
  3. KM=0.34 mM for ADP (at 32 degrees Celsius, pH 8.0)2 Publications
  4. KM=0.24 mM for ADP (in the presence of 2 mM FBP, at 32 degrees Celsius, pH 8.0)2 Publications
  5. KM=0.13 mM for phosphoenolpyruvate (in the presence of 2 mM FBP, at 25 degrees Celsius)2 Publications
  6. KM=0.63 mM for ADP (in the presence of 2 mM FBP, at 25 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH for T3 binding is 6.0-6.5. Increase in pH causes T3 binding to drop, does not bind T3 above pH 9.0 or below pH 5.0.2 Publications

    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, testis-specific (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (epd), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP)
    2. Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (pgk), Phosphoglycerate kinase, Phosphoglycerate kinase (HEL-S-68p), Phosphoglycerate kinase (HEL-S-272), Phosphoglycerate kinase
    3. no protein annotated in this organism
    4. Gamma-enolase (ENO2), Alpha-enolase (ENO1), Enolase 4 (ENO4), Beta-enolase (ENO3)
    5. Pyruvate kinase PKM (PKM), Pyruvate kinase PKLR (PKLR), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase, Pyruvate kinase (pyk), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (HEL-S-30), Pyruvate kinase, 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 sitei70Serine1
    Binding sitei73SubstrateBy similarity1
    Metal bindingi75PotassiumCombined sources1 Publication1
    Metal bindingi77PotassiumCombined sources1 Publication1
    Binding sitei106Serine1
    Metal bindingi113PotassiumCombined sources1 Publication1
    Metal bindingi114Potassium; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei120ATPCombined sources1 Publication1
    Binding sitei207ATPCombined sources1 Publication1
    Binding sitei270Substrate; via amide nitrogenBy similarity1
    Sitei270Transition state stabilizerBy similarity1
    Metal bindingi272MagnesiumCombined sources1 Publication1
    Binding sitei295Substrate; via amide nitrogenBy similarity1
    Metal bindingi296MagnesiumCombined sources1 Publication1
    Binding sitei296Substrate; via amide nitrogenBy similarity1
    Binding sitei328SubstrateBy similarity1
    Sitei433Crucial for phosphotyrosine binding1
    Binding sitei464Serine1
    Binding sitei482D-fructose 1,6-bisphosphate; part of allosteric siteCombined sources2 Publications1
    Binding sitei489D-fructose 1,6-bisphosphate; part of allosteric siteCombined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi75 – 78ATPCombined sources1 Publication4

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00906-MONOMER
    BRENDAi2.7.1.40 2681
    ReactomeiR-HSA-6798695 Neutrophil degranulation
    R-HSA-70171 Glycolysis
    SABIO-RKiP14618
    SIGNORiP14618
    UniPathwayi
    UPA00109;UER00188

    Protein family/group databases

    MoonDBiP14618 Curated
    MoonProtiP14618

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase PKM (EC:2.7.1.40)
    Alternative name(s):
    Cytosolic thyroid hormone-binding protein
    Short name:
    CTHBP
    Opa-interacting protein 3
    Short name:
    OIP-3
    Pyruvate kinase 2/3
    Pyruvate kinase muscle isozyme
    Thyroid hormone-binding protein 1
    Short name:
    THBP1
    Tumor M2-PK
    p58
    Gene namesi
    Name:PKM
    Synonyms:OIP3, PK2, PK3, PKM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 15

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000067225.17
    HGNCiHGNC:9021 PKM
    MIMi179050 gene
    neXtProtiNX_P14618

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi403P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-408. 1 Publication1
    Mutagenesisi408P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-403. 1 Publication1
    Mutagenesisi437S → Y: Unable to bind FBP but still activated by serine. 1 Publication1
    Mutagenesisi464H → A: Abolishes serine binding and allosteric activation. 1 Publication1

    Organism-specific databases

    DisGeNETi5315
    OpenTargetsiENSG00000067225
    PharmGKBiPA33353

    Chemistry databases

    ChEMBLiCHEMBL1075189
    DrugBankiDB02726 2-Phosphoglycolic Acid
    DB01733 L-Phospholactate
    DB00119 Pyruvic acid

    Polymorphism and mutation databases

    BioMutaiPKM
    DMDMi20178296

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources3 Publications
    ChainiPRO_00001120882 – 531Pyruvate kinase PKMAdd BLAST530

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1 Publication1
    Modified residuei3N6,N6,N6-trimethyllysineCombined sources1
    Modified residuei37PhosphoserineCombined sources1
    Modified residuei41PhosphothreonineCombined sources1
    Modified residuei62N6-acetyllysineCombined sources1
    Modified residuei66N6-succinyllysineBy similarity1
    Modified residuei89N6-acetyllysineCombined sources1
    Modified residuei97PhosphoserineBy similarity1
    Modified residuei100PhosphoserineBy similarity1
    Modified residuei105PhosphotyrosineCombined sources1
    Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei127PhosphoserineCombined sources1
    Modified residuei148PhosphotyrosineBy similarity1
    Modified residuei166N6-acetyllysine; alternateCombined sources1
    Modified residuei166N6-succinyllysine; alternateBy similarity1
    Cross-linki166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
    Modified residuei175PhosphotyrosineCombined sources1
    Modified residuei195PhosphothreonineCombined sources1
    Modified residuei266N6-acetyllysine; alternateCombined sources1
    Cross-linki266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Modified residuei270N6-acetyllysine; alternateBy similarity1
    Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Modified residuei305N6-acetyllysine1 Publication1
    Modified residuei322N6-acetyllysine; alternateBy similarity1
    Modified residuei322N6-succinyllysine; alternateBy similarity1
    Modified residuei4034-hydroxyproline1 Publication1
    Modified residuei4084-hydroxyproline1 Publication1
    Modified residuei433N6-acetyllysineCombined sources1
    Modified residuei475N6-acetyllysineBy similarity1
    Modified residuei498N6-succinyllysineBy similarity1

    Post-translational modificationi

    ISGylated.1 Publication
    Under hypoxia, hydroxylated by EGLN3.1 Publication
    Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.2 Publications
    FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35.1 Publication

    Keywords - PTMi

    Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP14618
    PaxDbiP14618
    PeptideAtlasiP14618
    PRIDEiP14618
    ProteomicsDBi53063
    53064 [P14618-2]
    53065 [P14618-3]
    TopDownProteomicsiP14618-1 [P14618-1]
    P14618-2 [P14618-2]

    2D gel databases

    DOSAC-COBS-2DPAGEiP14618
    OGPiP14618
    REPRODUCTION-2DPAGEiIPI00220644
    IPI00479186
    UCD-2DPAGEiP14618

    PTM databases

    iPTMnetiP14618
    PhosphoSitePlusiP14618
    SwissPalmiP14618

    Expressioni

    Tissue specificityi

    Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.1 Publication

    Gene expression databases

    BgeeiENSG00000067225 Expressed in 234 organ(s), highest expression level in anterior cingulate cortex
    CleanExiHS_PKM2
    ExpressionAtlasiP14618 baseline and differential
    GenevisibleiP14618 HS

    Organism-specific databases

    HPAiCAB019421
    HPA029501

    Interactioni

    Subunit structurei

    Monomer and homotetramer. Exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex. Exists in a nearly inactive dimeric form in tumor cells and the dimeric form has less affinity for the substrate. Binding to certain oncoproteins such as HPV-16 E7 oncoprotein can trigger dimerization. FBP stimulates the formation of tetramers from dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia. Interacts (isoform M2, but not isoform M1) with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (PubMed:25263439). Interacts with JMJD8 (PubMed:27199445).12 Publications

    Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi111332, 203 interactors
    ComplexPortaliCPX-3057 PKM2 pyruvate kinase complex (dimer) [P14618-1]
    CPX-3058 PKM2 pyruvate kinase complex (tetramer) [P14618-1]
    CPX-3093 PKM1 pyruvate kinase complex [P14618-2]
    DIPiDIP-31273N
    IntActiP14618, 246 interactors
    MINTiP14618
    STRINGi9606.ENSP00000320171

    Chemistry databases

    BindingDBiP14618

    Structurei

    Secondary structure

    1531
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP14618
    SMRiP14618
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14618

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni307 – 531Interaction with POU5F11 PublicationAdd BLAST225
    Regioni389 – 433Intersubunit contactAdd BLAST45
    Regioni432 – 437D-fructose 1,6-bisphosphate binding; part of allosteric siteCombined sources2 Publications6
    Regioni516 – 521D-fructose 1,6-bisphosphate binding; part of allosteric siteCombined sources2 Publications6

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    eggNOGiKOG2323 Eukaryota
    COG0469 LUCA
    GeneTreeiENSGT00390000008859
    HOGENOMiHOG000021559
    HOVERGENiHBG000941
    InParanoidiP14618
    KOiK00873
    OMAiKHEAIEQ
    PhylomeDBiP14618
    TreeFamiTF300390

    Family and domain databases

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

    Sequences (3+)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

    Isoform M2 (identifier: P14618-1) [UniParc]FASTAAdd to basket
    Also known as: M2-PK, PKM2

    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
    MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT
    60 70 80 90 100
    IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS
    110 120 130 140 150
    DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME
    160 170 180 190 200
    KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG
    210 220 230 240 250
    GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD
    260 270 280 290 300
    VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
    310 320 330 340 350
    IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN
    360 370 380 390 400
    AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR
    410 420 430 440 450
    LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI
    460 470 480 490 500
    IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR
    510 520 530
    GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
    Length:531
    Mass (Da):57,937
    Last modified:January 23, 2007 - v4
    Checksum:iAA94D7818ED6BBAD
    GO
    Isoform M1 (identifier: P14618-2) [UniParc] [UniParc]FASTAAdd to basket
    Also known as: M1-PK, PKM1

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

    Show »
    Length:531
    Mass (Da):58,062
    Checksum:iAB9B5B2308D26B79
    GO
    Isoform 3 (identifier: P14618-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-82: MSKPHSEAGT...RLNFSHGTHE → MSPEAQPQRT...PGTLASSVPL

    Note: No experimental confirmation available.
    Show »
    Length:516
    Mass (Da):56,273
    Checksum:i23200C40C7C42045
    GO

    Computationally mapped potential isoform sequencesi

    There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H3BTN5H3BTN5_HUMAN
    Pyruvate kinase
    PKM
    485Annotation score:
    B4DNK4B4DNK4_HUMAN
    Pyruvate kinase
    PKM
    457Annotation score:
    H3BR70H3BR70_HUMAN
    Pyruvate kinase
    PKM
    366Annotation score:
    H3BQ34H3BQ34_HUMAN
    Pyruvate kinase
    PKM
    281Annotation score:
    H3BUW1H3BUW1_HUMAN
    Pyruvate kinase PKM
    PKM
    162Annotation score:
    H3BT25H3BT25_HUMAN
    Pyruvate kinase PKM
    PKM
    151Annotation score:
    H3BU13H3BU13_HUMAN
    Pyruvate kinase PKM
    PKM
    82Annotation score:
    H3BTJ2H3BTJ2_HUMAN
    Pyruvate kinase PKM
    PKM
    168Annotation score:
    H3BQZ3H3BQZ3_HUMAN
    Pyruvate kinase PKM
    PKM
    69Annotation score:
    H3BN34H3BN34_HUMAN
    Pyruvate kinase PKM
    PKM
    51Annotation score:

    Sequence cautioni

    The sequence BAG57589 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti7E → Q in AAH12811 (PubMed:15489334).Curated1
    Sequence conflicti54A → T in BAG52542 (PubMed:14702039).Curated1
    Sequence conflicti103I → Y in AAA36672 (PubMed:2813362).Curated1
    Sequence conflicti132V → L in AAA36672 (PubMed:2813362).Curated1
    Sequence conflicti187Q → R in BAD96647 (Ref. 5) Curated1
    Sequence conflicti252H → R in BAD96647 (Ref. 5) Curated1
    Sequence conflicti339R → P in CAA39849 (PubMed:2040271).Curated1
    Sequence conflicti349A → V in BAG52542 (PubMed:14702039).Curated1
    Sequence conflicti379H → N in AAA36449 (PubMed:2854097).Curated1
    Sequence conflicti507D → H in AAH12811 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_033067204G → V1 PublicationCorresponds to variant dbSNP:rs17853396Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0433701 – 82MSKPH…HGTHE → MSPEAQPQRTKGPQQPCRSP IVKPGLPSFRPSSCTQPWLT HSWSTCAAWTLIHHPSQPGT LASSVPL in isoform 3. 1 PublicationAdd BLAST82
    Alternative sequenceiVSP_011101389 – 433IYHLQ…IVLTK → MFHRKLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationAdd BLAST45

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23725 mRNA Translation: AAA36449.1
    M26252 mRNA Translation: AAA36672.1
    X56494 Genomic DNA Translation: CAA39849.1
    AK092369 mRNA Translation: BAG52542.1
    AK222927 mRNA Translation: BAD96647.1
    AK294315 mRNA Translation: BAG57589.1 Different initiation.
    AK300800 mRNA Translation: BAG62458.1
    AK312253 mRNA Translation: BAG35185.1
    AY352517 Genomic DNA Translation: AAQ15274.1
    AC020779 Genomic DNA No translation available.
    CH471082 Genomic DNA Translation: EAW77884.1
    CH471082 Genomic DNA Translation: EAW77888.1
    BC000481 mRNA Translation: AAH00481.3
    BC007640 mRNA Translation: AAH07640.1
    BC007952 mRNA Translation: AAH07952.3
    BC012811 mRNA Translation: AAH12811.3
    BC035198 mRNA Translation: AAH35198.1
    AF025439 mRNA Translation: AAC39559.1
    CCDSiCCDS32284.1 [P14618-1]
    CCDS32285.1 [P14618-2]
    CCDS55972.1 [P14618-3]
    PIRiS30038
    S64635
    RefSeqiNP_001193725.1, NM_001206796.2
    NP_001193726.1, NM_001206797.2
    NP_001193727.1, NM_001206798.2 [P14618-3]
    NP_001193728.1, NM_001206799.1
    NP_001303247.1, NM_001316318.1
    NP_002645.3, NM_002654.5 [P14618-1]
    NP_872270.1, NM_182470.3 [P14618-2]
    NP_872271.1, NM_182471.3 [P14618-2]
    XP_005254502.1, XM_005254445.4 [P14618-1]
    XP_016877802.1, XM_017022313.1 [P14618-2]
    UniGeneiHs.534770
    Hs.704299

    Genome annotation databases

    EnsembliENST00000319622; ENSP00000320171; ENSG00000067225 [P14618-2]
    ENST00000335181; ENSP00000334983; ENSG00000067225 [P14618-1]
    ENST00000449901; ENSP00000403365; ENSG00000067225 [P14618-3]
    ENST00000565154; ENSP00000455901; ENSG00000067225 [P14618-2]
    ENST00000565184; ENSP00000455736; ENSG00000067225 [P14618-2]
    ENST00000568459; ENSP00000456970; ENSG00000067225 [P14618-2]
    GeneIDi5315
    KEGGihsa:5315
    UCSCiuc002atw.2 human [P14618-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Pyruvate kinase entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23725 mRNA Translation: AAA36449.1
    M26252 mRNA Translation: AAA36672.1
    X56494 Genomic DNA Translation: CAA39849.1
    AK092369 mRNA Translation: BAG52542.1
    AK222927 mRNA Translation: BAD96647.1
    AK294315 mRNA Translation: BAG57589.1 Different initiation.
    AK300800 mRNA Translation: BAG62458.1
    AK312253 mRNA Translation: BAG35185.1
    AY352517 Genomic DNA Translation: AAQ15274.1
    AC020779 Genomic DNA No translation available.
    CH471082 Genomic DNA Translation: EAW77884.1
    CH471082 Genomic DNA Translation: EAW77888.1
    BC000481 mRNA Translation: AAH00481.3
    BC007640 mRNA Translation: AAH07640.1
    BC007952 mRNA Translation: AAH07952.3
    BC012811 mRNA Translation: AAH12811.3
    BC035198 mRNA Translation: AAH35198.1
    AF025439 mRNA Translation: AAC39559.1
    CCDSiCCDS32284.1 [P14618-1]
    CCDS32285.1 [P14618-2]
    CCDS55972.1 [P14618-3]
    PIRiS30038
    S64635
    RefSeqiNP_001193725.1, NM_001206796.2
    NP_001193726.1, NM_001206797.2
    NP_001193727.1, NM_001206798.2 [P14618-3]
    NP_001193728.1, NM_001206799.1
    NP_001303247.1, NM_001316318.1
    NP_002645.3, NM_002654.5 [P14618-1]
    NP_872270.1, NM_182470.3 [P14618-2]
    NP_872271.1, NM_182471.3 [P14618-2]
    XP_005254502.1, XM_005254445.4 [P14618-1]
    XP_016877802.1, XM_017022313.1 [P14618-2]
    UniGeneiHs.534770
    Hs.704299

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1T5AX-ray2.80A/B/C/D1-531[»]
    1ZJHX-ray2.20A3-531[»]
    3BJFX-ray2.03A/B/C/D14-531[»]
    3BJTX-ray2.50A/B/C/D2-531[»]
    3G2GX-ray2.00A/B/C/D1-531[»]
    3GQYX-ray1.85A/B/C/D1-531[»]
    3GR4X-ray1.60A/B/C/D1-531[»]
    3H6OX-ray2.00A/B/C/D1-531[»]
    3ME3X-ray1.95A/B/C/D1-531[»]
    3SRDX-ray2.90A/B/C/D1-531[»]
    3SRFX-ray2.84A/B/C/D/E/F/G/H1-531[»]
    3SRHX-ray2.60A/B/C/D1-531[»]
    3U2ZX-ray2.10A/B/C/D1-531[»]
    4B2DX-ray2.30A/B/C/D2-531[»]
    4FXFX-ray2.55A/B/C/D1-531[»]
    4FXJX-ray2.90A/B/C/D1-531[»]
    4G1NX-ray2.30A/B/C/D14-531[»]
    4JPGX-ray2.33A/B/C/D1-531[»]
    4QG6X-ray3.21A/B/C/D1-531[»]
    4QG8X-ray2.30A/B/C/D1-531[»]
    4QG9X-ray2.38A/B/C/D1-531[»]
    4QGCX-ray2.30A/B/C/D1-531[»]
    4RPPX-ray2.58A/B/C/D1-531[»]
    4WJ8X-ray2.87A/B/C/D1-531[»]
    4YJ5X-ray2.41A/B/C/D14-531[»]
    5X0IX-ray2.64A/B/C/D1-531[»]
    5X1VX-ray2.10A/B/C/D1-531[»]
    5X1WX-ray3.00A/B/C/D1-531[»]
    6B6UX-ray1.35A/B7-531[»]
    6GG4X-ray2.46A/B/C/D1-531[»]
    6GG5X-ray3.20A/B/C/D1-531[»]
    6GG6X-ray2.96A/B/C/D/E/F/G/H1-531[»]
    ProteinModelPortaliP14618
    SMRiP14618
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111332, 203 interactors
    ComplexPortaliCPX-3057 PKM2 pyruvate kinase complex (dimer) [P14618-1]
    CPX-3058 PKM2 pyruvate kinase complex (tetramer) [P14618-1]
    CPX-3093 PKM1 pyruvate kinase complex [P14618-2]
    DIPiDIP-31273N
    IntActiP14618, 246 interactors
    MINTiP14618
    STRINGi9606.ENSP00000320171

    Chemistry databases

    BindingDBiP14618
    ChEMBLiCHEMBL1075189
    DrugBankiDB02726 2-Phosphoglycolic Acid
    DB01733 L-Phospholactate
    DB00119 Pyruvic acid

    Protein family/group databases

    MoonDBiP14618 Curated
    MoonProtiP14618

    PTM databases

    iPTMnetiP14618
    PhosphoSitePlusiP14618
    SwissPalmiP14618

    Polymorphism and mutation databases

    BioMutaiPKM
    DMDMi20178296

    2D gel databases

    DOSAC-COBS-2DPAGEiP14618
    OGPiP14618
    REPRODUCTION-2DPAGEiIPI00220644
    IPI00479186
    UCD-2DPAGEiP14618

    Proteomic databases

    EPDiP14618
    PaxDbiP14618
    PeptideAtlasiP14618
    PRIDEiP14618
    ProteomicsDBi53063
    53064 [P14618-2]
    53065 [P14618-3]
    TopDownProteomicsiP14618-1 [P14618-1]
    P14618-2 [P14618-2]

    Protocols and materials databases

    DNASUi5315
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000319622; ENSP00000320171; ENSG00000067225 [P14618-2]
    ENST00000335181; ENSP00000334983; ENSG00000067225 [P14618-1]
    ENST00000449901; ENSP00000403365; ENSG00000067225 [P14618-3]
    ENST00000565154; ENSP00000455901; ENSG00000067225 [P14618-2]
    ENST00000565184; ENSP00000455736; ENSG00000067225 [P14618-2]
    ENST00000568459; ENSP00000456970; ENSG00000067225 [P14618-2]
    GeneIDi5315
    KEGGihsa:5315
    UCSCiuc002atw.2 human [P14618-1]

    Organism-specific databases

    CTDi5315
    DisGeNETi5315
    EuPathDBiHostDB:ENSG00000067225.17
    GeneCardsiPKM
    HGNCiHGNC:9021 PKM
    HPAiCAB019421
    HPA029501
    MIMi179050 gene
    neXtProtiNX_P14618
    OpenTargetsiENSG00000067225
    PharmGKBiPA33353
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2323 Eukaryota
    COG0469 LUCA
    GeneTreeiENSGT00390000008859
    HOGENOMiHOG000021559
    HOVERGENiHBG000941
    InParanoidiP14618
    KOiK00873
    OMAiKHEAIEQ
    PhylomeDBiP14618
    TreeFamiTF300390

    Enzyme and pathway databases

    UniPathwayi
    UPA00109;UER00188

    BioCyciMetaCyc:HS00906-MONOMER
    BRENDAi2.7.1.40 2681
    ReactomeiR-HSA-6798695 Neutrophil degranulation
    R-HSA-70171 Glycolysis
    SABIO-RKiP14618
    SIGNORiP14618

    Miscellaneous databases

    ChiTaRSiPKM human
    EvolutionaryTraceiP14618
    GeneWikiiPKM2
    GenomeRNAii5315
    PROiPR:P14618
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000067225 Expressed in 234 organ(s), highest expression level in anterior cingulate cortex
    CleanExiHS_PKM2
    ExpressionAtlasiP14618 baseline and differential
    GenevisibleiP14618 HS

    Family and domain databases

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

    Entry informationi

    Entry nameiKPYM_HUMAN
    AccessioniPrimary (citable) accession number: P14618
    Secondary accession number(s): A6NFK3
    , B2R5N8, B3KRY0, B4DFX8, B4DUU6, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: November 7, 2018
    This is version 241 of the entry and version 4 of the sequence. See 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    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. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
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