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Protein

Pyruvate kinase PKM

Gene

PKM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 betwween 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

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.2 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme 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 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

    Pathway:iglycolysis

    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, 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, Enolase, Enolase (ENO3), Enolase (ENO2), Enolase (ENO3), Enolase (ENO2), Enolase (ENO1), Enolase (ENO3), Enolase (ENO1), Enolase, Enolase, Enolase (ENO3), 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 (HEL-S-30), Pyruvate kinase (PKM), 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701Serine
    Binding sitei73 – 731SubstrateBy similarity
    Metal bindingi75 – 751PotassiumBy similarity
    Metal bindingi77 – 771PotassiumBy similarity
    Binding sitei106 – 1061Serine
    Metal bindingi113 – 1131Potassium
    Metal bindingi114 – 1141Potassium; via carbonyl oxygenBy similarity
    Sitei270 – 2701Transition state stabilizer
    Metal bindingi272 – 2721Magnesium
    Binding sitei295 – 2951Substrate; via amide nitrogenBy similarity
    Metal bindingi296 – 2961Magnesium
    Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
    Binding sitei328 – 3281SubstrateBy similarity
    Sitei433 – 4331Crucial for phosphotyrosine binding
    Binding sitei464 – 4641Serine
    Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric site
    Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric site

    GO - Molecular functioni

    • ADP binding Source: Ensembl
    • ATP binding Source: UniProtKB-KW
    • magnesium ion binding Source: InterPro
    • MHC class II protein complex binding Source: UniProtKB
    • poly(A) RNA binding Source: UniProtKB
    • 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:HS00906-MONOMER.
    BRENDAi2.7.1.40. 2681.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKP14618.
    UniPathwayiUPA00109; UER00188.

    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
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9021. PKM.

    Subcellular locationi

    • Cytoplasm
    • Nucleus

    • Note: Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.

    GO - Cellular componenti

    • cilium Source: Ensembl
    • cytoplasm Source: UniProtKB
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • extracellular matrix Source: UniProtKB
    • extracellular vesicle Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • myelin sheath Source: Ensembl
    • nucleus Source: UniProtKB
    • plasma membrane Source: HPA
    • vesicle Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi403 – 4031P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-408. 1 Publication
    Mutagenesisi408 – 4081P → A: Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-403. 1 Publication
    Mutagenesisi437 – 4371S → Y: Unable to bind FBP but still activated by serine. 1 Publication
    Mutagenesisi464 – 4641H → A: Abolishes serine binding and allosteric activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA33353.

    Chemistry

    DrugBankiDB00119. Pyruvic acid.

    Polymorphism and mutation databases

    BioMutaiPKM.
    DMDMi20178296.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 531530Pyruvate kinase PKMPRO_0000112088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei37 – 371Phosphoserine9 Publications
    Modified residuei62 – 621N6-acetyllysine1 Publication
    Modified residuei66 – 661N6-succinyllysineBy similarity
    Modified residuei89 – 891N6-acetyllysine1 Publication
    Modified residuei105 – 1051Phosphotyrosine1 Publication
    Modified residuei148 – 1481PhosphotyrosineBy similarity
    Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
    Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
    Modified residuei175 – 1751Phosphotyrosine1 Publication
    Modified residuei195 – 1951Phosphothreonine1 Publication
    Modified residuei249 – 2491PhosphoserineBy similarity
    Modified residuei266 – 2661N6-acetyllysine1 Publication
    Modified residuei270 – 2701N6-acetyllysineBy similarity
    Modified residuei305 – 3051N6-acetyllysine1 Publication
    Modified residuei322 – 3221N6-acetyllysine; alternateBy similarity
    Modified residuei322 – 3221N6-succinyllysine; alternateBy similarity
    Modified residuei403 – 40314-hydroxyproline1 Publication
    Modified residuei408 – 40814-hydroxyproline1 Publication
    Modified residuei433 – 4331N6-acetyllysine1 Publication
    Modified residuei475 – 4751N6-acetyllysineBy similarity
    Modified residuei498 – 4981N6-succinyllysineBy similarity

    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

    Keywords - PTMi

    Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP14618.
    PaxDbiP14618.
    PRIDEiP14618.

    2D gel databases

    DOSAC-COBS-2DPAGEP14618.
    OGPiP14618.
    REPRODUCTION-2DPAGEIPI00220644.
    IPI00479186.
    UCD-2DPAGEP14618.

    PTM databases

    PhosphoSiteiP14618.

    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

    BgeeiP14618.
    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 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.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX24EBI-353408,EBI-710918From a different organism.
    ARAFP103982EBI-353408,EBI-365961
    ARRB1P494073EBI-353408,EBI-743313
    ARRB2P321214EBI-353408,EBI-714559
    DAPK1P533553EBI-353408,EBI-358616
    EGLN3Q9H6Z92EBI-4304679,EBI-1175354
    HIF1AQ166657EBI-4304679,EBI-447269
    HIST1H3DP684313EBI-4304679,EBI-79722
    HTTP428583EBI-353408,EBI-466029
    MAPK3P273613EBI-4304679,EBI-73995
    RAF1P040493EBI-353408,EBI-365996

    Protein-protein interaction databases

    BioGridi111332. 115 interactions.
    DIPiDIP-31273N.
    IntActiP14618. 231 interactions.
    MINTiMINT-4998892.
    STRINGi9606.ENSP00000320171.

    Structurei

    Secondary structure

    1
    531
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 173Combined sources
    Helixi18 – 214Combined sources
    Helixi26 – 316Combined sources
    Beta strandi35 – 373Combined sources
    Beta strandi45 – 506Combined sources
    Turni53 – 553Combined sources
    Helixi58 – 6710Combined sources
    Beta strandi71 – 755Combined sources
    Helixi76 – 783Combined sources
    Helixi81 – 9616Combined sources
    Turni97 – 1004Combined sources
    Turni102 – 1043Combined sources
    Beta strandi109 – 1135Combined sources
    Beta strandi119 – 1213Combined sources
    Beta strandi127 – 1293Combined sources
    Beta strandi132 – 1343Combined sources
    Beta strandi139 – 1435Combined sources
    Helixi146 – 1483Combined sources
    Beta strandi154 – 1607Combined sources
    Helixi164 – 1674Combined sources
    Beta strandi173 – 1764Combined sources
    Turni177 – 1804Combined sources
    Beta strandi181 – 1888Combined sources
    Beta strandi190 – 19910Combined sources
    Beta strandi201 – 2033Combined sources
    Beta strandi204 – 2063Combined sources
    Beta strandi208 – 2103Combined sources
    Beta strandi212 – 2143Combined sources
    Helixi223 – 23412Combined sources
    Beta strandi238 – 2425Combined sources
    Helixi248 – 25811Combined sources
    Turni259 – 2646Combined sources
    Beta strandi265 – 2717Combined sources
    Helixi274 – 2785Combined sources
    Helixi280 – 2867Combined sources
    Beta strandi287 – 2937Combined sources
    Helixi294 – 3007Combined sources
    Helixi303 – 3053Combined sources
    Helixi306 – 32015Combined sources
    Beta strandi324 – 3296Combined sources
    Helixi332 – 3354Combined sources
    Beta strandi337 – 3393Combined sources
    Helixi342 – 35413Combined sources
    Beta strandi357 – 3626Combined sources
    Helixi363 – 3664Combined sources
    Beta strandi367 – 3693Combined sources
    Helixi371 – 38717Combined sources
    Helixi391 – 40111Combined sources
    Turni402 – 4043Combined sources
    Helixi408 – 42215Combined sources
    Beta strandi428 – 4314Combined sources
    Beta strandi433 – 4353Combined sources
    Helixi436 – 4427Combined sources
    Beta strandi450 – 4556Combined sources
    Helixi457 – 4626Combined sources
    Helixi463 – 4653Combined sources
    Beta strandi469 – 4735Combined sources
    Helixi482 – 49918Combined sources
    Beta strandi508 – 51811Combined sources
    Beta strandi522 – 5298Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP14618.
    SMRiP14618. Positions 13-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14618.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni307 – 531225Interaction with POU5F1Add
    BLAST
    Regioni389 – 43345Intersubunit contactAdd
    BLAST
    Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric site
    Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric site

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0469.
    GeneTreeiENSGT00390000008859.
    HOGENOMiHOG000021559.
    HOVERGENiHBG000941.
    InParanoidiP14618.
    KOiK00873.
    OMAiCRIAYET.
    OrthoDBiEOG78M01Q.
    PhylomeDBiP14618.
    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 (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

    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

    Sequence cautioni

    The sequence BAG57589.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71E → Q in AAH12811 (PubMed:15489334).Curated
    Sequence conflicti54 – 541A → T in BAG52542 (PubMed:14702039).Curated
    Sequence conflicti103 – 1031I → Y in AAA36672 (PubMed:2813362).Curated
    Sequence conflicti132 – 1321V → L in AAA36672 (PubMed:2813362).Curated
    Sequence conflicti187 – 1871Q → R in BAD96647 (Ref. 5) Curated
    Sequence conflicti252 – 2521H → R in BAD96647 (Ref. 5) Curated
    Sequence conflicti339 – 3391R → P in CAA39849 (PubMed:2040271).Curated
    Sequence conflicti349 – 3491A → V in BAG52542 (PubMed:14702039).Curated
    Sequence conflicti379 – 3791H → N in AAA36449 (PubMed:2854097).Curated
    Sequence conflicti507 – 5071D → H in AAH12811 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti204 – 2041G → V.1 Publication
    Corresponds to variant rs17853396 [ dbSNP | Ensembl ].
    VAR_033067

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8282MSKPH…HGTHE → MSPEAQPQRTKGPQQPCRSP IVKPGLPSFRPSSCTQPWLT HSWSTCAAWTLIHHPSQPGT LASSVPL in isoform 3. 1 PublicationVSP_043370Add
    BLAST
    Alternative sequencei389 – 43345IYHLQ…IVLTK → MFHRKLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationVSP_011101Add
    BLAST

    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_001206796.1.
    NP_001193726.1. NM_001206797.1.
    NP_001193727.1. NM_001206798.1. [P14618-3]
    NP_001193728.1. NM_001206799.1.
    NP_002645.3. NM_002654.4. [P14618-1]
    NP_872270.1. NM_182470.2. [P14618-2]
    NP_872271.1. NM_182471.2. [P14618-2]
    XP_005254502.1. XM_005254445.3. [P14618-1]
    UniGeneiHs.534770.

    Genome annotation databases

    EnsembliENST00000335181; ENSP00000334983; ENSG00000067225.
    ENST00000449901; ENSP00000403365; ENSG00000067225. [P14618-3]
    GeneIDi5315.
    KEGGihsa:5315.
    UCSCiuc002atv.2. human. [P14618-2]
    uc002aty.2. human. [P14618-1]
    uc010ukj.2. human. [P14618-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    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_001206796.1.
    NP_001193726.1. NM_001206797.1.
    NP_001193727.1. NM_001206798.1. [P14618-3]
    NP_001193728.1. NM_001206799.1.
    NP_002645.3. NM_002654.4. [P14618-1]
    NP_872270.1. NM_182470.2. [P14618-2]
    NP_872271.1. NM_182471.2. [P14618-2]
    XP_005254502.1. XM_005254445.3. [P14618-1]
    UniGeneiHs.534770.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP14618.
    SMRiP14618. Positions 13-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111332. 115 interactions.
    DIPiDIP-31273N.
    IntActiP14618. 231 interactions.
    MINTiMINT-4998892.
    STRINGi9606.ENSP00000320171.

    Chemistry

    ChEMBLiCHEMBL1075189.
    DrugBankiDB00119. Pyruvic acid.

    PTM databases

    PhosphoSiteiP14618.

    Polymorphism and mutation databases

    BioMutaiPKM.
    DMDMi20178296.

    2D gel databases

    DOSAC-COBS-2DPAGEP14618.
    OGPiP14618.
    REPRODUCTION-2DPAGEIPI00220644.
    IPI00479186.
    UCD-2DPAGEP14618.

    Proteomic databases

    MaxQBiP14618.
    PaxDbiP14618.
    PRIDEiP14618.

    Protocols and materials databases

    DNASUi5315.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000335181; ENSP00000334983; ENSG00000067225.
    ENST00000449901; ENSP00000403365; ENSG00000067225. [P14618-3]
    GeneIDi5315.
    KEGGihsa:5315.
    UCSCiuc002atv.2. human. [P14618-2]
    uc002aty.2. human. [P14618-1]
    uc010ukj.2. human. [P14618-3]

    Organism-specific databases

    CTDi5315.
    GeneCardsiGC15M072492.
    HGNCiHGNC:9021. PKM.
    HPAiCAB019421.
    HPA029501.
    MIMi179050. gene.
    neXtProtiNX_P14618.
    PharmGKBiPA33353.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0469.
    GeneTreeiENSGT00390000008859.
    HOGENOMiHOG000021559.
    HOVERGENiHBG000941.
    InParanoidiP14618.
    KOiK00873.
    OMAiCRIAYET.
    OrthoDBiEOG78M01Q.
    PhylomeDBiP14618.
    TreeFamiTF300390.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00188.
    BioCyciMetaCyc:HS00906-MONOMER.
    BRENDAi2.7.1.40. 2681.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKP14618.

    Miscellaneous databases

    EvolutionaryTraceiP14618.
    GeneWikiiPKM2.
    GenomeRNAii5315.
    NextBioi20554.
    PROiP14618.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP14618.
    CleanExiHS_PKM2.
    ExpressionAtlasiP14618. baseline and differential.
    GenevisibleiP14618. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma."
      Tani K., Yoshida M.C., Satoh H., Mitamura K., Noguchi T., Tanaka T., Fujii H., Miwa S.
      Gene 73:509-516(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
      Tissue: Liver.
    2. "Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase."
      Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.
      Proc. Natl. Acad. Sci. U.S.A. 86:7861-7865(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2), PROTEIN SEQUENCE OF 70-98, SUBUNIT, ENZYME REGULATION.
    3. Erratum
      Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.
      Proc. Natl. Acad. Sci. U.S.A. 87:1625-1625(1990)
    4. "Isolation and characterization of the human pyruvate kinase M gene."
      Takenaka M., Noguchi T., Sadahiro S., Hirai H., Yamada K., Matsuda T., Imai E., Tanaka T.
      Eur. J. Biochem. 198:101-106(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS M1 AND 3).
      Tissue: Astrocyte and Fetal brain.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2).
      Tissue: Kidney.
    7. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), VARIANT VAL-204.
      Tissue: Kidney, Lung carcinoma, Ovary, Retina and Rhabdomyosarcoma.
    11. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-43; 57-73; 93-115; 126-135; 167-186; 231-246; 271-311; 401-422; 448-455 AND 490-498, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    12. "An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate."
      Ashizawa K., McPhie P., Lin K.-H., Cheng S.-Y.
      Biochemistry 30:7105-7111(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH THYROID HORMONE.
    13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-32.
      Tissue: Platelet.
    14. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 74-89, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    15. "Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth."
      Williams J.M., Chen G.-C., Zhu L., Rest R.F.
      Mol. Microbiol. 27:171-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-531 (ISOFORM M2).
    16. Cited for: INTERACTION WITH HERC1.
    17. Cited for: ISGYLATION.
    18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death."
      Stetak A., Veress R., Ovadi J., Csermely P., Keri G., Ullrich A.
      Cancer Res. 67:1602-1608(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    22. "Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein."
      Shimada N., Shinagawa T., Ishii S.
      Genes Cells 13:245-254(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION.
    23. "Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription."
      Lee J., Kim H.K., Han Y.-M., Kim J.
      Int. J. Biochem. Cell Biol. 40:1043-1054(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POU5F1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    25. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; TYR-175 AND THR-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-89; LYS-166; LYS-266 AND LYS-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1."
      Luo W., Hu H., Chang R., Zhong J., Knabel M., O'Meally R., Cole R.N., Pandey A., Semenza G.L.
      Cell 145:732-744(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGLN3 AND HIF1A, SUBCELLULAR LOCATION, INDUCTION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT PRO-403 AND PRO-408, MUTAGENESIS OF PRO-403 AND PRO-408.
    33. "The oxygen sensor PHD3 limits glycolysis under hypoxia via direct binding to pyruvate kinase."
      Chen N., Rinner O., Czernik D., Nytko K.J., Zheng D., Stiehl D.P., Zamboni N., Gstaiger M., Frei C.
      Cell Res. 21:983-986(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGLN3.
    34. "Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth."
      Lv L., Li D., Zhao D., Lin R., Chu Y., Zhang H., Zha Z., Liu Y., Li Z., Xu Y., Wang G., Huang Y., Xiong Y., Guan K.L., Lei Q.Y.
      Mol. Cell 42:719-730(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-305.
    35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    37. "Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis."
      Dombrauckas J.D., Santarsiero B.D., Mesecar A.D.
      Biochemistry 44:9417-9429(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF ISOFORM M2 IN COMPLEX WITH OXALATE AND FBP, CATALYTIC ACTIVITY, SUBUNIT, ENZYME MECHANISM, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    38. "Structure of human muscle pyruvate kinase (PKM2)."
      Structural genomics consortium (SGC)
      Submitted (MAY-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    39. "Pyruvate kinase M2 is a phosphotyrosine-binding protein."
      Christofk H.R., Vander Heiden M.G., Wu N., Asara J.M., Cantley L.C.
      Nature 452:181-186(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 14-531 ALONE AND IN COMPLEX WITH FBP, ENZYME REGULATION.
    40. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-531, ENZYME REGULATION BY SERINE, MAGNESIUM-BINDING SITES, SUBUNIT, MUTAGENESIS OF SER-437 AND HIS-464.

    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 historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 205 of the entry and version 4 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, 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.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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

    External Data

    Dasty 3

    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 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.