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P52480

- KPYM_MOUSE

UniProt

P52480 - KPYM_MOUSE

Protein

Pyruvate kinase PKM

Gene

Pkm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    Functioni

    Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation By similarity.By similarity

    Catalytic activityi

    ATP + pyruvate = ADP + phosphoenolpyruvate.

    Cofactori

    Magnesium.
    Potassium.

    Enzyme regulationi

    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 By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701SerineBy similarity
    Binding sitei73 – 731SubstrateBy similarity
    Metal bindingi75 – 751PotassiumBy similarity
    Metal bindingi77 – 771PotassiumBy similarity
    Binding sitei106 – 1061SerineBy similarity
    Metal bindingi113 – 1131PotassiumBy similarity
    Metal bindingi114 – 1141Potassium; via carbonyl oxygenBy similarity
    Sitei270 – 2701Transition state stabilizerBy similarity
    Metal bindingi272 – 2721MagnesiumBy similarity
    Binding sitei295 – 2951Substrate; via amide nitrogenBy similarity
    Metal bindingi296 – 2961MagnesiumBy similarity
    Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
    Binding sitei328 – 3281SubstrateBy similarity
    Sitei433 – 4331Crucial for phosphotyrosine bindingBy similarity
    Binding sitei464 – 4641SerineBy similarity
    Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity
    Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. potassium ion binding Source: InterPro
    4. protein binding Source: IntAct
    5. pyruvate kinase activity Source: MGI

    GO - Biological processi

    1. glycolytic process Source: MGI
    2. programmed cell death Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP52480.
    UniPathwayiUPA00109; UER00188.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase PKM (EC:2.7.1.40)
    Alternative name(s):
    Pyruvate kinase muscle isozyme
    Gene namesi
    Name:Pkm
    Synonyms:Pk3, Pkm2, Pykm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:97591. Pkm.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cilium Source: MGI
    2. extracellular vesicular exosome Source: Ensembl
    3. mitochondrion Source: MGI
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 531530Pyruvate kinase PKMPRO_0000112089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei62 – 621N6-acetyllysine1 Publication
    Modified residuei66 – 661N6-succinyllysine1 Publication
    Modified residuei89 – 891N6-acetyllysineBy similarity
    Modified residuei105 – 1051Phosphotyrosine1 Publication
    Modified residuei148 – 1481Phosphotyrosine1 Publication
    Modified residuei166 – 1661N6-acetyllysine; alternate1 Publication
    Modified residuei166 – 1661N6-succinyllysine; alternate1 Publication
    Modified residuei175 – 1751PhosphotyrosineBy similarity
    Modified residuei195 – 1951PhosphothreonineBy similarity
    Modified residuei266 – 2661N6-acetyllysineBy similarity
    Modified residuei270 – 2701N6-acetyllysine1 Publication
    Modified residuei305 – 3051N6-acetyllysineBy similarity
    Modified residuei322 – 3221N6-acetyllysine; alternate1 Publication
    Modified residuei322 – 3221N6-succinyllysine; alternate1 Publication
    Modified residuei403 – 40314-hydroxyprolineBy similarity
    Modified residuei408 – 40814-hydroxyprolineBy similarity
    Modified residuei433 – 4331N6-acetyllysineBy similarity
    Modified residuei475 – 4751N6-acetyllysine1 Publication
    Modified residuei498 – 4981N6-succinyllysine1 Publication

    Post-translational modificationi

    ISGylated.1 Publication
    Under hypoxia, hydroxylated by EGLN3.By similarity
    Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.By similarity

    Keywords - PTMi

    Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP52480.
    PaxDbiP52480.
    PRIDEiP52480.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00407130.
    P52480.
    SWISS-2DPAGEP52480.

    PTM databases

    PhosphoSiteiP52480.

    Expressioni

    Tissue specificityi

    Embryonic stem cells and embryonal carcinoma cells.1 Publication

    Gene expression databases

    BgeeiP52480.
    CleanExiMM_PKM2.
    GenevestigatoriP52480.

    Interactioni

    Subunit structurei

    Monomer and homotetramer. Exists as a monomer in the absence of fructose 1,6 bi-phosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. 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 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P266633EBI-647785,EBI-6857429From a different organism.
    Pou5f1P202636EBI-647785,EBI-1606219

    Protein-protein interaction databases

    BioGridi202191. 15 interactions.
    IntActiP52480. 16 interactions.
    MINTiMINT-1850796.

    Structurei

    3D structure databases

    ProteinModelPortaliP52480.
    SMRiP52480. Positions 13-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni307 – 531225Interaction with POU5F1By similarityAdd
    BLAST
    Regioni389 – 43345Intersubunit contactAdd
    BLAST
    Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity
    Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0469.
    GeneTreeiENSGT00390000008859.
    HOVERGENiHBG000941.
    InParanoidiP52480.
    KOiK00873.
    OMAiCIVENAG.
    OrthoDBiEOG78M01Q.
    PhylomeDBiP52480.
    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.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform M2 (identifier: P52480-1) [UniParc]FASTAAdd to Basket

    Also known as: PKM1

    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

    MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT    50
    IGPASRSVEM LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS 100
    DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 150
    KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKEKGA DFLVTEVENG 200
    GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKAAD 250
    VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
    IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN 350
    AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR 400
    LAPITSDPTE AAAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI 450
    IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN AWAEDVDLRV NLAMDVGKAR 500
    GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P 531
    Length:531
    Mass (Da):57,845
    Last modified:May 1, 2007 - v4
    Checksum:i34CBBC01BC0C047D
    GO
    Isoform M1 (identifier: P52480-2) [UniParc]FASTAAdd to Basket

    Also known as: PKM2

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

    Show »
    Length:531
    Mass (Da):57,985
    Checksum:iD0D163786CC6D4A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81A → V in CAA65761. (PubMed:9545585)Curated
    Sequence conflicti121 – 1211T → A in BAE30642. (PubMed:16141072)Curated
    Sequence conflicti121 – 1211T → A in BAE32031. (PubMed:16141072)Curated
    Sequence conflicti158 – 1581W → R in BAA07457. (PubMed:7612666)Curated
    Sequence conflicti166 – 1661K → E in BAE42098. (PubMed:16141072)Curated
    Sequence conflicti170 – 1701V → L in BAE30642. (PubMed:16141072)Curated
    Sequence conflicti170 – 1701V → L in BAE32031. (PubMed:16141072)Curated
    Sequence conflicti177 – 1771D → G in BAE42199. (PubMed:16141072)Curated
    Sequence conflicti230 – 2301K → R in BAE30642. (PubMed:16141072)Curated
    Sequence conflicti230 – 2301K → R in BAE32031. (PubMed:16141072)Curated
    Sequence conflicti299 – 2991I → T in BAA07457. (PubMed:7612666)Curated
    Sequence conflicti309 – 3091A → S in BAA07457. (PubMed:7612666)Curated
    Sequence conflicti327 – 3271A → S in BAA07457. (PubMed:7612666)Curated
    Sequence conflicti327 – 3271A → S in CAA65761. (PubMed:9545585)Curated
    Sequence conflicti333 – 3331S → I in BAA07457. (PubMed:7612666)Curated
    Sequence conflicti333 – 3331S → I in CAA65761. (PubMed:9545585)Curated
    Sequence conflicti485 – 4851D → N in BAE33055. (PubMed:16141072)Curated
    Sequence conflicti485 – 4851D → N in BAE42192. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei389 – 43345IYHLQ…IVLTK → MFHRLLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1. 1 PublicationVSP_025057Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38379 mRNA. Translation: BAA07457.1.
    X97047 mRNA. Translation: CAA65761.1.
    AK002341 mRNA. Translation: BAB22025.1.
    AK135397 mRNA. Translation: BAE22519.1.
    AK151724 mRNA. Translation: BAE30642.1.
    AK153483 mRNA. Translation: BAE32031.1.
    AK155110 mRNA. Translation: BAE33055.1.
    AK155655 mRNA. Translation: BAE33370.1.
    AK170892 mRNA. Translation: BAE42098.1.
    AK168943 mRNA. Translation: BAE40751.1.
    AK171023 mRNA. Translation: BAE42192.1.
    AK171033 mRNA. Translation: BAE42199.1.
    AC160637 Genomic DNA. No translation available.
    BC016619 mRNA. Translation: AAH16619.1.
    BC094663 mRNA. Translation: AAH94663.1.
    CCDSiCCDS40659.1. [P52480-1]
    CCDS57681.1. [P52480-2]
    PIRiS55921.
    RefSeqiNP_001240812.1. NM_001253883.1. [P52480-2]
    NP_035229.2. NM_011099.3. [P52480-1]
    XP_006510918.1. XM_006510855.1. [P52480-1]
    UniGeneiMm.326167.
    Mm.488724.

    Genome annotation databases

    EnsembliENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294. [P52480-1]
    ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294. [P52480-2]
    GeneIDi18746.
    KEGGimmu:18746.
    UCSCiuc009pyf.2. mouse. [P52480-1]
    uc009pyh.2. mouse. [P52480-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38379 mRNA. Translation: BAA07457.1 .
    X97047 mRNA. Translation: CAA65761.1 .
    AK002341 mRNA. Translation: BAB22025.1 .
    AK135397 mRNA. Translation: BAE22519.1 .
    AK151724 mRNA. Translation: BAE30642.1 .
    AK153483 mRNA. Translation: BAE32031.1 .
    AK155110 mRNA. Translation: BAE33055.1 .
    AK155655 mRNA. Translation: BAE33370.1 .
    AK170892 mRNA. Translation: BAE42098.1 .
    AK168943 mRNA. Translation: BAE40751.1 .
    AK171023 mRNA. Translation: BAE42192.1 .
    AK171033 mRNA. Translation: BAE42199.1 .
    AC160637 Genomic DNA. No translation available.
    BC016619 mRNA. Translation: AAH16619.1 .
    BC094663 mRNA. Translation: AAH94663.1 .
    CCDSi CCDS40659.1. [P52480-1 ]
    CCDS57681.1. [P52480-2 ]
    PIRi S55921.
    RefSeqi NP_001240812.1. NM_001253883.1. [P52480-2 ]
    NP_035229.2. NM_011099.3. [P52480-1 ]
    XP_006510918.1. XM_006510855.1. [P52480-1 ]
    UniGenei Mm.326167.
    Mm.488724.

    3D structure databases

    ProteinModelPortali P52480.
    SMRi P52480. Positions 13-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202191. 15 interactions.
    IntActi P52480. 16 interactions.
    MINTi MINT-1850796.

    PTM databases

    PhosphoSitei P52480.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00407130.
    P52480.
    SWISS-2DPAGE P52480.

    Proteomic databases

    MaxQBi P52480.
    PaxDbi P52480.
    PRIDEi P52480.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034834 ; ENSMUSP00000034834 ; ENSMUSG00000032294 . [P52480-1 ]
    ENSMUST00000163694 ; ENSMUSP00000128770 ; ENSMUSG00000032294 . [P52480-2 ]
    GeneIDi 18746.
    KEGGi mmu:18746.
    UCSCi uc009pyf.2. mouse. [P52480-1 ]
    uc009pyh.2. mouse. [P52480-2 ]

    Organism-specific databases

    CTDi 5315.
    MGIi MGI:97591. Pkm.

    Phylogenomic databases

    eggNOGi COG0469.
    GeneTreei ENSGT00390000008859.
    HOVERGENi HBG000941.
    InParanoidi P52480.
    KOi K00873.
    OMAi CIVENAG.
    OrthoDBi EOG78M01Q.
    PhylomeDBi P52480.
    TreeFami TF300390.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00188 .
    SABIO-RK P52480.

    Miscellaneous databases

    ChiTaRSi PKM2. mouse.
    NextBioi 294905.
    PROi P52480.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52480.
    CleanExi MM_PKM2.
    Genevestigatori P52480.

    Family and domain databases

    Gene3Di 2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    InterProi IPR001697. 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 ]
    PANTHERi PTHR11817. PTHR11817. 1 hit.
    Pfami PF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01050. PYRUVTKNASE.
    SUPFAMi SSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
    PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the complementary DNA for the mouse pyruvate kinase M-2 gene whose expression is dependent upon cell differentiation."
      Izumi S., Manabe A., Tomoyasu A., Kihara-Negishi F., Ariga H.
      Biochim. Biophys. Acta 1267:135-138(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
    2. "Gene expression of mouse M1 and M2 pyruvate kinase isoenzymes correlates with differential poly(A) tract extension of their mRNAs during the development of spermatogenesis."
      de Luis O., del Mazo J.
      Biochim. Biophys. Acta 1396:294-305(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
      Strain: Swiss.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395 (ISOFORM M1).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Kidney and Muellerian duct.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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).
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Mammary tumor.
    6. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-56; 67-89; 93-115; 126-136; 142-162; 167-224; 231-246; 248-255; 279-305; 320-336; 343-399; 401-433; 468-498 AND 506-526, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. Cited for: ISGYLATION.
    8. "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: TISSUE SPECIFICITY.
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105 AND TYR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-166; LYS-270; LYS-322 AND LYS-475, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-166; LYS-322 AND LYS-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKPYM_MOUSE
    AccessioniPrimary (citable) accession number: P52480
    Secondary accession number(s): Q3TBV8
    , Q3TBW5, Q3TC59, Q3U1X3, Q3U5P6, Q4VC20, Q64484, Q91YI8, Q9CWB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, 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

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3