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    PKM pyruvate kinase M1/2 [ Homo sapiens (human) ]

    Gene ID: 5315, updated on 10-Dec-2024

    Summary

    Official Symbol
    PKMprovided by HGNC
    Official Full Name
    pyruvate kinase M1/2provided by HGNC
    Primary source
    HGNC:HGNC:9021
    See related
    Ensembl:ENSG00000067225 MIM:179050; AllianceGenome:HGNC:9021
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    PK3; TCB; p58; OIP3; PKM2; CTHBP; THBP1; HEL-S-30
    Summary
    This gene encodes a protein involved in glycolysis. The encoded protein is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. This protein has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Several alternatively spliced transcript variants encoding a few distinct isoforms have been reported. [provided by RefSeq, May 2011]
    Expression
    Ubiquitous expression in brain (RPKM 155.4), esophagus (RPKM 151.3) and 24 other tissues See more
    Orthologs
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    See PKM in Genome Data Viewer
    Location:
    15q23
    Exon count:
    17
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 15 NC_000015.10 (72199029..72231591, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 15 NC_060939.1 (70015755..70047883, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 15 NC_000015.9 (72491370..72523531, complement)

    Chromosome 15 - NC_000015.10Genomic Context describing neighboring genes Neighboring gene SUMO peptidase family member, NEDD8 specific Neighboring gene ribosomal protein L21 pseudogene 115 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9712 Neighboring gene uncharacterized LOC124903522 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9713 Neighboring gene Sharpr-MPRA regulatory region 4122 Neighboring gene GRAM domain containing 2A Neighboring gene NANOG-H3K4me1 hESC enhancer GRCh37_chr15:72485963-72486586 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9714 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6617 Neighboring gene Sharpr-MPRA regulatory region 1213 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9715 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6618 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6619 Neighboring gene MED14-independent group 3 enhancer GRCh37_chr15:72529434-72530633 Neighboring gene poly(ADP-ribose) polymerase family member 6 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 6620 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9717 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 9718 Neighboring gene uncharacterized LOC105370887

    Genomic regions, transcripts, and products

    Expression

    • Project title: Tissue-specific circular RNA induction during human fetal development
    • Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
    • BioProject: PRJNA270632
    • Publication: PMID 26076956
    • Analysis date: Mon Apr 2 22:54:59 2018

    Bibliography

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    HIV-1 interactions

    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 env Tandem affinity purification and mass spectrometry analysis identify pyruvate kinase of muscle (PKM), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
    Envelope surface glycoprotein gp160, precursor env HIV-1 gp160 is identified to have a physical interaction with pyruvate kinase, muscle (PKM2) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses PubMed
    Gag-Pol gag-pol Tandem affinity purification and mass spectrometry analysis identify pyruvate kinase of muscle (PKM), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
    Nef nef Tandem affinity purification and mass spectrometry analysis identify pyruvate kinase of muscle (PKM), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
    Pr55(Gag) gag Tandem affinity purification and mass spectrometry analysis identify pyruvate kinase of muscle (PKM), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
    Tat tat Expression of HIV-1 Tat upregulates the abundance of pyruvate kinase, muscle (PKM) in the nucleoli of Jurkat T-cells PubMed
    Vpr vpr A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies upregulation of pyruvate kinase, muscle (PKM) expression by HIV-1 Vpr in Vpr transduced macrophages PubMed
    retropepsin gag-pol Positional proteomics analysis identifies the cleavage of human pyruvate kinase, muscle (PKM) at amino acid residues 306-307 and 359-361 by the HIV-1 protease PubMed

    Go to the HIV-1, Human Interaction Database

    Pathways from PubChem

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Clone Names

    • MGC3932

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables MHC class II protein complex binding HDA PubMed 
    enables RNA binding HDA PubMed 
    enables cadherin binding HDA PubMed 
    enables histone H2AXY142 kinase activity IEA
    Inferred from Electronic Annotation
    more info
     
    NOT enables histone H3T11 kinase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables histone H3T11 kinase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables histone H3Y41 kinase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables mRNA binding ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables potassium ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables protein tyrosine kinase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables pyruvate kinase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables pyruvate kinase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables pyruvate kinase activity TAS
    Traceable Author Statement
    more info
    PubMed 
    enables transcription coactivator activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in canonical glycolysis IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in cellular response to insulin stimulus IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in chromatin remodeling IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in glycolytic process IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in glycolytic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    involved_in glycolytic process IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in positive regulation of cytoplasmic translation ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    involved_in positive regulation of sprouting angiogenesis IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in positive regulation of transcription by RNA polymerase II IDA
    Inferred from Direct Assay
    more info
    PubMed 
    involved_in programmed cell death IDA
    Inferred from Direct Assay
    more info
    PubMed 

    General protein information

    Preferred Names
    pyruvate kinase PKM
    Names
    OPA-interacting protein 3
    PK, muscle type
    cytosolic thyroid hormone-binding protein
    epididymis secretory protein Li 30
    pyruvate kinase 2/3
    pyruvate kinase isozymes M1/M2
    pyruvate kinase muscle isozyme
    pyruvate kinase, muscle
    threonine-protein kinase PKM2
    thyroid hormone-binding protein 1
    thyroid hormone-binding protein, cytosolic
    tumor M2-PK
    tyrosine-protein kinase PKM2
    NP_001193725.1
    NP_001193726.1
    NP_001193727.1
    NP_001193728.1
    NP_001303247.1
    NP_001398010.1
    NP_002645.3
    NP_872270.1
    NP_872271.1
    XP_005254500.1
    XP_005254502.1
    XP_011519972.1
    XP_047288618.1
    XP_047288619.1
    XP_047288620.1
    XP_047288621.1
    XP_047288622.1
    XP_054234160.1
    XP_054234161.1
    XP_054234162.1
    XP_054234163.1

    NCBI Reference Sequences (RefSeq)

    NEW Try the new Transcript table

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_052978.2 RefSeqGene

      Range
      5401..37562
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001206796.3NP_001193725.1  pyruvate kinase PKM isoform c

      See identical proteins and their annotated locations for NP_001193725.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) represents the longest transcript and encodes the longest isoform (c).
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS92037.1
      UniProtKB/TrEMBL
      A0A804F729, B4DRT3
      Related
      ENSP00000455901.2, ENST00000565154.6
      Conserved Domains (2) summary
      cd00288
      Location:116604
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
      TIGR01064
      Location:117601
      pyruv_kin; pyruvate kinase
    2. NM_001206797.3NP_001193726.1  pyruvate kinase PKM isoform d

      See identical proteins and their annotated locations for NP_001193726.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (5) differs in the 5' UTR and coding sequence, lacks an alternate in-frame segment, and has an alternate in-frame coding exon compared to variant 4. The resulting isoform (d) is shorter at the N-terminus, lacks an alternate internal segment, and has a different internal segment compared to isoform c.
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS73752.1
      UniProtKB/TrEMBL
      B4DNK4, B4DRT3
      Related
      ENSP00000373745.4, ENST00000389093.7
      Conserved Domains (1) summary
      cd00288
      Location:42456
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
    3. NM_001206798.3NP_001193727.1  pyruvate kinase PKM isoform e

      See identical proteins and their annotated locations for NP_001193727.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (6) differs in the 5' UTR and coding sequence, lacks an alternate exon, and has an alternate in-frame coding exon compared to variant 4. The resulting isoform (e) has a shorter and distinct N-terminus, lacks an alternate internal segment, and has a different internal segment compared to isoform c.
      Source sequence(s)
      AC020779
      UniProtKB/TrEMBL
      B4DRT3
      Conserved Domains (2) summary
      cd00288
      Location:68515
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
      TIGR01064
      Location:68512
      pyruv_kin; pyruvate kinase
    4. NM_001206799.2NP_001193728.1  pyruvate kinase PKM isoform f

      See identical proteins and their annotated locations for NP_001193728.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (7) differs in the 5' UTR and coding sequence compared to variant 4. The resulting isoform (f) has a shorter and distinct N-terminus compared to isoform c.
      Source sequence(s)
      AC020779, AK294315, AK309781, BC000481, BC035198
      UniProtKB/TrEMBL
      B4DRT3
      Conserved Domains (2) summary
      cd00288
      Location:47535
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
      TIGR01064
      Location:48532
      pyruv_kin; pyruvate kinase
    5. NM_001316318.2NP_001303247.1  pyruvate kinase PKM isoform g

      Status: REVIEWED

      Description
      Transcript Variant: This variant (8) lacks an alternate in-frame exon in the 5' end of the coding sequence compared to variant 4. The resulting isoform (g) has the same N- and C-termini but is shorter compared to isoform c.
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS92035.1
      UniProtKB/TrEMBL
      A0A804F6T5, B4DRT3
      Related
      ENSP00000455736.2, ENST00000565184.6
      Conserved Domains (2) summary
      cd00288
      Location:77565
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
      TIGR01064
      Location:78562
      pyruv_kin; pyruvate kinase
    6. NM_001411081.1NP_001398010.1  pyruvate kinase PKM isoform h

      Status: REVIEWED

      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS92036.1
      UniProtKB/TrEMBL
      A0A8V8TNX9, B4DRT3
      Related
      ENSP00000513903.1, ENST00000698741.1
    7. NM_002654.6NP_002645.3  pyruvate kinase PKM isoform a

      See identical proteins and their annotated locations for NP_002645.3

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) differs in the 5' UTR and coding sequence and has an alternate in-frame coding exon compared to variant 4. The resulting isoform (a, also called M2) is shorter at the N-terminus and has a different internal segment compared to isoform c.
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS32284.1
      UniProtKB/Swiss-Prot
      A6NFK3, B2R5N8, B3KRY0, B4DFX8, B4DUU6, P14618, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2
      UniProtKB/TrEMBL
      B4DRT3, V9HWB8
      Related
      ENSP00000334983.5, ENST00000335181.10
      Conserved Domains (1) summary
      cd00288
      Location:42530
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
    8. NM_182470.4NP_872270.1  pyruvate kinase PKM isoform b

      See identical proteins and their annotated locations for NP_872270.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 4. The resulting isoform (b, also called M1) is shorter at the N-terminus compared to isoform c.
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS32285.1
      UniProtKB/TrEMBL
      B4DRT3
      Related
      ENSP00000320171.6, ENST00000319622.10
      Conserved Domains (1) summary
      cd00288
      Location:42530
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
    9. NM_182471.4NP_872271.1  pyruvate kinase PKM isoform b

      See identical proteins and their annotated locations for NP_872271.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR and coding sequence compared to variant 4. The resulting isoform (b, also called M1) is shorter at the N-terminus compared to isoform c.
      Source sequence(s)
      AC020779
      Consensus CDS
      CCDS32285.1
      UniProtKB/TrEMBL
      B4DRT3
      Related
      ENSP00000456970.1, ENST00000568459.5
      Conserved Domains (1) summary
      cd00288
      Location:42530
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000015.10 Reference GRCh38.p14 Primary Assembly

      Range
      72199029..72231591 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_005254445.6XP_005254502.1  pyruvate kinase PKM isoform X7

      See identical proteins and their annotated locations for XP_005254502.1

      UniProtKB/Swiss-Prot
      A6NFK3, B2R5N8, B3KRY0, B4DFX8, B4DUU6, P14618, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2
      UniProtKB/TrEMBL
      B4DRT3, V9HWB8
      Conserved Domains (1) summary
      cd00288
      Location:42530
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
    2. XM_011521670.2XP_011519972.1  pyruvate kinase PKM isoform X4

      See identical proteins and their annotated locations for XP_011519972.1

      UniProtKB/TrEMBL
      B4DRT3
      Conserved Domains (1) summary
      cd00288
      Location:77565
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
    3. XM_047432666.1XP_047288622.1  pyruvate kinase PKM isoform X7

      UniProtKB/Swiss-Prot
      A6NFK3, B2R5N8, B3KRY0, B4DFX8, B4DUU6, P14618, P14786, Q53GK4, Q96E76, Q9BWB5, Q9UCV6, Q9UPF2
      UniProtKB/TrEMBL
      B4DRT3, V9HWB8
    4. XM_047432664.1XP_047288620.1  pyruvate kinase PKM isoform X5

      UniProtKB/TrEMBL
      B4DRT3
    5. XM_047432665.1XP_047288621.1  pyruvate kinase PKM isoform X6

      UniProtKB/TrEMBL
      B4DRT3
    6. XM_005254443.2XP_005254500.1  pyruvate kinase PKM isoform X3

      UniProtKB/TrEMBL
      B4DRT3
      Conserved Domains (2) summary
      cd00288
      Location:102590
      Pyruvate_Kinase; Pyruvate kinase (PK): Large allosteric enzyme that regulates glycolysis through binding of the substrate, phosphoenolpyruvate, and one or more allosteric effectors. Like other allosteric enzymes, PK has a high substrate affinity R state and a low ...
      TIGR01064
      Location:103587
      pyruv_kin; pyruvate kinase
    7. XM_047432662.1XP_047288618.1  pyruvate kinase PKM isoform X1

      UniProtKB/TrEMBL
      B4DRT3
    8. XM_047432663.1XP_047288619.1  pyruvate kinase PKM isoform X2

      UniProtKB/TrEMBL
      B4DRT3

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060939.1 Alternate T2T-CHM13v2.0

      Range
      70015755..70047883 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054378186.1XP_054234161.1  pyruvate kinase PKM isoform X4

      UniProtKB/TrEMBL
      B4DRT3
    2. XM_054378187.1XP_054234162.1  pyruvate kinase PKM isoform X5

      UniProtKB/TrEMBL
      B4DRT3
    3. XM_054378188.1XP_054234163.1  pyruvate kinase PKM isoform X6

      UniProtKB/TrEMBL
      B4DRT3
    4. XM_054378185.1XP_054234160.1  pyruvate kinase PKM isoform X3

      UniProtKB/TrEMBL
      B4DRT3