{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P14618","secondaryAccessions":["A6NFK3","B2R5N8","B3KRY0","B4DFX8","B4DUU6","P14786","Q53GK4","Q96E76","Q9BWB5","Q9UCV6","Q9UPF2"],"uniProtkbId":"KPYM_HUMAN","entryAudit":{"firstPublicDate":"1990-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":283,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Pyruvate kinase PKM"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}],"value":"2.7.1.40"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2813362"}],"value":"Cytosolic thyroid hormone-binding protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2813362"}],"value":"CTHBP"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9466265"}],"value":"Opa-interacting protein 3"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9466265"}],"value":"OIP-3"}]},{"fullName":{"value":"Pyruvate kinase 2/3"}},{"fullName":{"value":"Pyruvate kinase muscle isozyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Threonine-protein kinase PKM2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22901803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}],"value":"2.7.11.1"}]},{"fullName":{"value":"Thyroid hormone-binding protein 1"},"shortNames":[{"value":"THBP1"}]},{"fullName":{"value":"Tumor M2-PK"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Tyrosine-protein kinase PKM2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22306293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}],"value":"2.7.10.2"}]},{"fullName":{"value":"p58"}}]},"genes":[{"geneName":{"value":"PKM"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9466265"}],"value":"OIP3"},{"value":"PK2"},{"value":"PK3"},{"value":"PKM2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}],"value":"Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P52480"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17308100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18191611"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337823"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21620138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22306293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22901803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26787900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33314660"}],"value":"Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Promotes transcription of VEGFA following translocation to the nucleus along with the NFKB1/p50 and RELA/p65 subunits of the NF-kappa-B transcription factor complex which is triggered by interaction with FOXM1 isoform 5 (FOXM1D) and leads to increased angiogenesis (PubMed:33314660). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100)"}],"commentType":"FUNCTION","molecule":"Isoform M2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337823"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}],"value":"Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed:18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed:20847263)"}],"commentType":"FUNCTION","molecule":"Isoform M1"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Isoform M2","reaction":{"name":"pyruvate + ATP = phosphoenolpyruvate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18157"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.40","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:18159"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Isoform M2","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.10.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22306293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:10597"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22306293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Isoform M2","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22901803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22901803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Isoform M1","reaction":{"name":"pyruvate + ATP = phosphoenolpyruvate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18157"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.40","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23530218"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23530218"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18298799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337815"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23064226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2813362"}],"value":"Isoform M2 is allosterically activated by D-fructose 1,6-bisphosphate (FBP) (PubMed:15996096, PubMed:18337815, PubMed:1854723, PubMed:2813362). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3) (PubMed:15996096). The activity of the tetrameric form is inhibited by PML (PubMed:18298799). 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 (PubMed:18337815). 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 (PubMed:23064226). Acetylation at Lys-433 promotes its translocation into the nucleus and homodimerization, promoting the protein kinase activity (PubMed:24120661)"}],"commentType":"ACTIVITY REGULATION","molecule":"Isoform M2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20847263"}],"value":"Has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity"}],"commentType":"ACTIVITY REGULATION","molecule":"Isoform M1"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":2.7,"unit":"mM","substrate":"phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]},{"constant":0.17,"unit":"mM","substrate":"phosphoenolpyruvate (in the presence of 2 mM D-fructose 1,6-bisphosphate (FBP), at 32 degrees Celsius, pH 8.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]},{"constant":0.34,"unit":"mM","substrate":"ADP (at 32 degrees Celsius, pH 8.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]},{"constant":0.24,"unit":"mM","substrate":"ADP (in the presence of 2 mM FBP, at 32 degrees Celsius, pH 8.0)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]},{"constant":0.13,"unit":"mM","substrate":"phosphoenolpyruvate (in the presence of 2 mM FBP, at 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]},{"constant":0.63,"unit":"mM","substrate":"ADP (in the presence of 2 mM FBP, at 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}],"value":"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."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12650930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15996096"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18191611"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18298799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337815"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1854723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21483450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21620138"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22306293"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23064226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25263439"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27199445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27573352"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2813362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32268273"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33314660"}],"value":"Monomer and homotetramer; exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). The monomeric form binds 3,3',5-triiodo-L-thyronine (T3) (PubMed:15996096). Tetramer formation induces pyruvate kinase activity (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). FBP stimulates the formation of tetramers from dimers (PubMed:15996096, PubMed:18298799, PubMed:18337815, PubMed:1854723, PubMed:23064226, PubMed:2813362). Homodimer; exists in a dimeric form in tumor cells and the dimeric form has less affinity for the phosphoenolpyruvate substrate (PubMed:22306293, PubMed:24120661). The homodimer converts into a protein kinase (PubMed:22306293, PubMed:24120661). Interacts with HERC1, POU5F1 and PML (PubMed:12650930, PubMed:18191611). Interacts with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A (PubMed:21483450, PubMed:21620138). Interacts with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia (PubMed:21620138). Interacts with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation (PubMed:25263439). Interacts with JMJD8 (PubMed:27199445). Interacts with TRAF4 (PubMed:32268273). Interacts with (phosphorylated) CTNNB1; leading to activate transcription (PubMed:22056988). Interacts with TSC22D2; the interaction results in reduced nuclear levels of PKM isoform M2, leading to repression of cyclin CCND1 transcription and reduced cell growth (PubMed:27573352). Interacts with FOXM1 isoform 5 (FOXM1D); FOXM1D binds to the PKM2 homotetramer to form a heterooctamer, consisting of the PKM2 homotetramer with 4 copies of FOXM1, which reduces PKM2 activity, leading to promotion of glycolysis (PubMed:33314660). Interaction with FOXM1D also promotes nuclear translocation of PKM2 along with the NFKB1/p50 and RELA/p65 subunits of the NF-kappa-B transcription factor complex, leading to increased VEGFA transcription and angiogenesis (PubMed:33314660)"}],"commentType":"SUBUNIT","molecule":"Isoform M2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24120661"}],"value":"(Microbial infection) Binding to certain oncoproteins such as HPV-16 E7 oncoprotein promotes homodimerization"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P49407","geneName":"ARRB1","intActId":"EBI-743313"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P32121","geneName":"ARRB2","intActId":"EBI-714559"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q96IK1-2","geneName":"BOD1","intActId":"EBI-18924329"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P35222","geneName":"CTNNB1","intActId":"EBI-491549"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P53355","geneName":"DAPK1","intActId":"EBI-358616"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P22607","geneName":"FGFR3","intActId":"EBI-348399"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"P04049","geneName":"RAF1","intActId":"EBI-365996"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q8N488","geneName":"RYBP","intActId":"EBI-752324"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q7Z699","geneName":"SPRED1","intActId":"EBI-5235340"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q9BSI4","geneName":"TINF2","intActId":"EBI-717399"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q9UMX0","geneName":"UBQLN1","intActId":"EBI-741480"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q9Y649","intActId":"EBI-25900580"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618","intActId":"EBI-353408"},"interactantTwo":{"uniProtKBAccession":"Q9WMX2","intActId":"EBI-710918"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"P35222","geneName":"CTNNB1","intActId":"EBI-491549"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"P53355","geneName":"DAPK1","intActId":"EBI-358616"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"Q9H6Z9","geneName":"EGLN3","intActId":"EBI-1175354"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"P68431","geneName":"H3C12","intActId":"EBI-79722"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"Q16665","geneName":"HIF1A","intActId":"EBI-447269"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P14618-1","intActId":"EBI-4304679"},"interactantTwo":{"uniProtKBAccession":"P27361","geneName":"MAPK3","intActId":"EBI-73995"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR 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Nuclear translocation is promoted by acetylation by EP300 (PubMed:24120661). 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