FOXK2
entrez
3607
canonical
uniprot
Q01167
canonical
ensembl
ENSG00000141568
resolver
ensp
ENSP00000335677
resolver
ensp
ENSP00000436108
resolver
ensp
ENSP00000793533
resolver
genesymbol
FOXK2
resolver
genesymbol_syn
ILF
resolver
genesymbol_syn
ILF1
resolver
hgnc
HGNC:6036
resolver
uniprot
A6NEP5
resolver
uniprot
Q13622
resolver
uniprot
Q13623
resolver
uniprot
Q13624
resolver
uniprot_entry
FOXK2_HUMAN
resolver
uniprot_sec
A6NEP5
resolver
uniprot_sec
Q13622
resolver
uniprot_sec
Q13623
resolver
uniprot_sec
Q13624
resolver
amino_acid_sequence
MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALSSEKREKQEASESPVKAVQPHISPLTINIPDTMAHLISPLPSPTGTISAANSCPSSPRGAGSSGYKVGRVMPSDLNLMADNSQPENEKEASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASESKLIEQAFRKRRPRGVPCFRTPLGPLSSRSAPASPNHAGVLSAHSSGAQTPESLSREGSPAPLEPEPGAAQPKLAVIQEARFAQSAPGSPLSSQPVLITVQRQLPQAIKPVTYTVATPVTTSTSQPPVVQTVHVVHQIPAVSVTSVAGLAPANTYTVSGQAVVTPAAVLAPPKAEAQENGDHREVKVKVEPIPAIGHATLGTASRIIQTAQTTPVQTVTIVQQAPLGQHQLPIKTVTQNGTHVASVPTAVHGQVNNAAASPLHMLATHASASASLPTKRHNGDQPEQPELKRIKTEDGEGIVIALSVDTPPAAVREKGVQN
uniprot
proteins
function
FUNCTION: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (PubMed:38735474). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context (PubMed:22083952, PubMed:25451922). Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity). Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity). Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity). Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription (PubMed:22083952). Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence (PubMed:20097901). Binds to NFAT-like motifs (purine-rich) in the IL2 promoter (PubMed:1339390). Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus (PubMed:25805136). Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements (PubMed:1909027). Accessory component of the polycomb repressive deubiquitinase (PR-DUB) complex; recruits the PR-DUB complex to specific FOXK2-bound genes (PubMed:24634419, PubMed:30664650). {ECO:0000250|UniProtKB:Q3UCQ1, ECO:0000269|PubMed:1339390, ECO:0000269|PubMed:1909027, ECO:0000269|PubMed:20097901, ECO:0000269|PubMed:22083952, ECO:0000269|PubMed:24634419, ECO:0000269|PubMed:25451922, ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:30664650, ECO:0000269|PubMed:38735474}.
uniprot
proteins
mass_dalton
69062
uniprot
proteins
mutagenesis
MUTAGEN 58; /note="R->A: Reduced interaction with BAP1."; /evidence="ECO:0000269|PubMed:24748658"; MUTAGEN 129; /note="R->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 130; /note="R->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 131; /note="G->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 133; /note="P->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 136; /note="Q->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 137; /note="L->A: Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 138; /note="P->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 141; /note="C->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 142; /note="T->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 145; /note="F->A: Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 146; /note="P->A: Highly reduces interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 147; /note="S->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 148; /note="T->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 150; /note="I->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 151; /note="K->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 152; /note="I->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 154; /note="F->A: Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 155; /note="T->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 157; /note="L->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 258; /note="K->A: Decreases DNA-binding to 40%."; /evidence="ECO:0000269|PubMed:16624804"; MUTAGEN 300; /note="K->A: Decreases DNA-binding to 20%."; /evidence="ECO:0000269|PubMed:16624804"; MUTAGEN 305; /note="S->A: Decreases DNA-binding to 70%."; /evidence="ECO:0000269|PubMed:16624804"; MUTAGEN 307; /note="R->A: Abolishes DNA-binding."; /evidence="ECO:0000269|PubMed:16624804"; MUTAGEN 308; /note="H->A: No effect on interaction with DVL2."; /evidence="ECO:0000269|PubMed:25805136"; MUTAGEN 328; /note="K->A: Decreases DNA-binding to 25%."; /evidence="ECO:0000269|PubMed:16624804"; MUTAGEN 373; /note="S->A: Decreased phosphorylation leading to increased stability of the protein; when associated with A-428."; /evidence="ECO:0000269|PubMed:20810654"; MUTAGEN 373; /note="S->D: Phosphomimetic mutant; decreased phosphorylation leading to decreased stability of the protein; when associated with D-428."; /evidence="ECO:0000269|PubMed:20810654"; MUTAGEN 428; /note="S->A: Decreased phosphorylation leading to increased stability of the protein; when associated with A-373."; /evidence="ECO:0000269|PubMed:20810654"; MUTAGEN 428; /note="S->D: Phosphomimetic mutant; decreased phosphorylation leading to decreased stability of the protein; when associated with D-373."; /evidence="ECO:0000269|PubMed:20810654"; MUTAGEN 527; /note="K->R: Abolished SUMOylation; when associated with R-633."; /evidence="ECO:0000269|PubMed:29540677"; MUTAGEN 633; /note="K->R: Abolished SUMOylation; when associated with R-527."; /evidence="ECO:0000269|PubMed:29540677
uniprot
proteins
post_translational_modification
PTM: Hyperphosphorylated during mitosis by CDK1 and, to a lower extent, CDK2 (PubMed:20810654). Phosphorylation at Ser-373 and Ser-428 affects stability by promoting degradation (PubMed:20810654). {ECO:0000269|PubMed:20810654}.; PTM: Ubiquitinated by the SCF-FBXO24 E3 ubiquitin ligase, leading to proteasomal degradation. {ECO:0000269|PubMed:38735474}.
uniprot
proteins
pubmed
12402362
uniprot
proteins
pubmed
1339390
uniprot
proteins
pubmed
16624804
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1909027
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20097901
uniprot
proteins
pubmed
20810654
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22083952
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24634419
uniprot
proteins
pubmed
24748658
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25451922
uniprot
proteins
pubmed
25805136
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29540677
uniprot
proteins
pubmed
30664650
uniprot
proteins
pubmed
38735474
uniprot
proteins
sequence_length
660
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20810654, ECO:0000269|PubMed:24748658, ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:38735474}. Cytoplasm {ECO:0000250|UniProtKB:Q3UCQ1}.
uniprot
proteins