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Q5NVN0

- KPYM_PONAB

UniProt

Q5NVN0 - KPYM_PONAB

Protein

Pyruvate kinase PKM

Gene

PKM

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 3 (23 Jan 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.By similarity
    Potassium.By similarity

    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
    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. pyruvate kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    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:PKM2
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 531530Pyruvate kinase PKMPRO_0000112090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei62 – 621N6-acetyllysineBy similarity
    Modified residuei66 – 661N6-succinyllysineBy similarity
    Modified residuei89 – 891N6-acetyllysineBy similarity
    Modified residuei105 – 1051PhosphotyrosineBy similarity
    Modified residuei148 – 1481PhosphotyrosineBy similarity
    Modified residuei166 – 1661N6-acetyllysine; alternateBy similarity
    Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
    Modified residuei175 – 1751PhosphotyrosineBy similarity
    Modified residuei195 – 1951PhosphothreonineBy similarity
    Modified residuei266 – 2661N6-acetyllysineBy similarity
    Modified residuei270 – 2701N6-acetyllysineBy similarity
    Modified residuei305 – 3051N6-acetyllysineBy similarity
    Modified residuei322 – 3221N6-acetyllysine; alternateBy similarity
    Modified residuei322 – 3221N6-succinyllysine; alternateBy similarity
    Modified residuei475 – 4751N6-acetyllysineBy similarity
    Modified residuei498 – 4981N6-succinyllysineBy similarity

    Post-translational modificationi

    ISGylated.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, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ5NVN0.

    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. Interacts with HERC1 POU5F1 and PML By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5NVN0.
    SMRiQ5NVN0. 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

    HOVERGENiHBG000941.
    KOiK00873.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q5NVN0-1 [UniParc]FASTAAdd to Basket

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    MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT    50
    IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS 100
    DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 150
    KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLLTEVENG 200
    GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD 250
    VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
    IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSGVAN 350
    AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR 400
    ASSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI 450
    IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR 500
    GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P 531
    Length:531
    Mass (Da):58,018
    Last modified:January 23, 2007 - v3
    Checksum:i86BDD4AEF68B5510
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531D → G in CAH93166. 1 PublicationCurated
    Sequence conflicti329 – 3291Q → R in CAH93166. 1 PublicationCurated
    Sequence conflicti347 – 3471G → D in CAH93166. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR861086 mRNA. Translation: CAH93166.1.
    CR925988 mRNA. Translation: CAI29633.1.
    RefSeqiNP_001127083.1. NM_001133611.1.

    Genome annotation databases

    GeneIDi100174114.
    KEGGipon:100174114.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR861086 mRNA. Translation: CAH93166.1 .
    CR925988 mRNA. Translation: CAI29633.1 .
    RefSeqi NP_001127083.1. NM_001133611.1.

    3D structure databases

    ProteinModelPortali Q5NVN0.
    SMRi Q5NVN0. Positions 13-531.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5NVN0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174114.
    KEGGi pon:100174114.

    Organism-specific databases

    CTDi 396456.

    Phylogenomic databases

    HOVERGENi HBG000941.
    KOi K00873.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00188 .

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiKPYM_PONAB
    AccessioniPrimary (citable) accession number: Q5NVN0
    Secondary accession number(s): Q5R500
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 74 of the entry and version 3 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3