FOXO4
entrez
4303
canonical
uniprot
P98177
canonical
ensembl
ENSG00000184481
resolver
ensp
ENSP00000342209
resolver
ensp
ENSP00000363377
resolver
genesymbol
FOXO4
resolver
genesymbol_syn
AFX
resolver
genesymbol_syn
AFX1
resolver
genesymbol_syn
MLLT7
resolver
hgnc
HGNC:7139
resolver
uniprot
B7WPJ7
resolver
uniprot
O43821
resolver
uniprot
Q13720
resolver
uniprot
Q3KPF1
resolver
uniprot
Q8TDK9
resolver
uniprot_entry
FOXO4_HUMAN
resolver
uniprot_sec
B7WPJ7
resolver
uniprot_sec
O43821
resolver
uniprot_sec
Q13720
resolver
uniprot_sec
Q3KPF1
resolver
uniprot_sec
Q8TDK9
resolver
amino_acid_sequence
MDPGNENSATEAAAIIDLDPDFEPQSRPRSCTWPLPRPEIANQPSEPPEVEPDLGEKVHTEGRSEPILLPSRLPEPAGGPQPGILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPEGGKSGKAPRRRAASMDSSSKLLRGRSKAPKKKPSVLPAPPEGATPTSPVGHFAKWSGSPCSRNREEADMWTTFRPRSSSNASSVSTRLSPLRPESEVLAEEIPASVSSYAGGVPPTLNEGLELLDGLNLTSSHSLLSRSGLSGFSLQHPGVTGPLHTYSSSLFSPAEGPLSAGEGCFSSSQALEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGLPSSSKLATGVGLCPKPLEAPGPSSLVPTLSMIAPPPVMASAPIPKALGTPVLTPPTEAASQDRMPQDLDLDMYMENLECDMDNIISDLMDEGEGLDFNFEPDP
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving FOXO4 is found in acute leukemias. Translocation t(X;11)(q13;q23) with KMT2A/MLL1. The result is a rogue activator protein.
uniprot
proteins
function
FUNCTION: Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269|PubMed:10217147, ECO:0000269|PubMed:10783894, ECO:0000269|PubMed:12761217, ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:16054032, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:20874444, ECO:0000269|PubMed:22972301}.
uniprot
proteins
mass_dalton
53684
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="T->A: Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-197 and A-262."; /evidence="ECO:0000269|PubMed:10518537, ECO:0000269|PubMed:16272144, ECO:0000269|PubMed:22972301"; MUTAGEN 197; /note="S->A: Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-262."; /evidence="ECO:0000269|PubMed:10217147, ECO:0000269|PubMed:10518537, ECO:0000269|PubMed:16272144, ECO:0000269|PubMed:22972301"; MUTAGEN 262; /note="S->A: Abolishes phosphorylation. No effect on cellular location or transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-197."; /evidence="ECO:0000269|PubMed:10217147, ECO:0000269|PubMed:10518537, ECO:0000269|PubMed:16272144, ECO:0000269|PubMed:22972301
uniprot
proteins
post_translational_modification
PTM: Acetylation by CREBBP/CBP, which is induced by peroxidase stress, inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-dependent and stimulates transcriptional activity. {ECO:0000269|PubMed:15126506}.; PTM: Phosphorylation by PKB/AKT1 inhibits transcriptional activity and is responsible for cytoplasmic localization. May be phosphorylated at multiple sites by NLK. {ECO:0000269|PubMed:10217147, ECO:0000269|PubMed:10518537, ECO:0000269|PubMed:16272144}.; PTM: Monoubiquitinated; monoubiquitination is induced by oxidative stress and reduced by deacetylase inhibitors; results in its relocalization to the nucleus and its increased transcriptional activity. Deubiquitinated by USP7; deubiquitination is induced by oxidative stress; enhances its interaction with USP7 and consequently, deubiquitination; increases its translocation to the cytoplasm and inhibits its transcriptional activity. Hydrogen-peroxide-induced ubiquitination and USP7-mediated deubiquitination have no major effect on its protein stability. {ECO:0000269|PubMed:16964248}.
uniprot
proteins
pubmed
10217147
uniprot
proteins
pubmed
10518537
uniprot
proteins
pubmed
10783894
uniprot
proteins
pubmed
10921784
uniprot
proteins
pubmed
11352721
uniprot
proteins
pubmed
11779849
uniprot
proteins
pubmed
12761217
uniprot
proteins
pubmed
15126506
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15688030
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16054032
uniprot
proteins
pubmed
16114898
uniprot
proteins
pubmed
16272144
uniprot
proteins
pubmed
16964248
uniprot
proteins
pubmed
20874444
uniprot
proteins
pubmed
22972301
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7529552
uniprot
proteins
pubmed
9010221
uniprot
proteins
pubmed
9341872
uniprot
proteins
sequence_length
505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm.
uniprot
proteins