FBXO22
entrez
26263
canonical
uniprot
Q8NEZ5
canonical
ensembl
ENSG00000167196
resolver
ensp
ENSP00000307833
resolver
ensp
ENSP00000396442
resolver
ensp
ENSP00000736065
resolver
genesymbol
FBXO22
resolver
genesymbol_syn
FBX22
resolver
hgnc
HGNC:13593
resolver
uniprot
Q0D2P8
resolver
uniprot
Q6PIL5
resolver
uniprot
Q8IXW3
resolver
uniprot
Q9H824
resolver
uniprot
Q9UKC0
resolver
uniprot_entry
FBX22_HUMAN
resolver
uniprot_sec
Q0D2P8
resolver
uniprot_sec
Q6PIL5
resolver
uniprot_sec
Q8IXW3
resolver
uniprot_sec
Q9H824
resolver
uniprot_sec
Q9UKC0
resolver
amino_acid_sequence
MEPVGCCGECRGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVLRTHRSVTWISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGHKRARKRTSMETALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQPFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVVSTFSDMNIILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEKTAEAAMQRLKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRIVTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK
uniprot
proteins
disease_involvement
DISEASE: Tayoun-Maawali syndrome (TYMAS) [MIM:621184]: An autosomal recessive pleiotropic syndrome characterized by multiple abnormalities encompassing early growth restriction, neurodevelopmental delay, and craniofacial, cardiovascular, gastrointestinal, urinary and endocrine anomalies. {ECO:0000269|PubMed:40215970}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that is implicated in the control of various cellular processes such as cell cycle control, transcriptional regulation, DNA damage repair, and apoptosis. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. Acts as a key regulator of histone methylation marks namely H3K9 and H3K36 methylation through the regulation of histone demethylase KDM4A protein levels (PubMed:21768309). In complex with KDM4A, also regulates the abundance of TP53 by targeting methylated TP53 for degradation at the late senescent stage (PubMed:26868148). Under oxidative stress, promotes the ubiquitination and degradation of BACH1. Mechanistically, reactive oxygen species (ROS) covalently modify cysteine residues on the bZIP domain of BACH1, leading to its release from chromatin and making it accessible to FBXO22 (PubMed:39504958). Upon amino acid depletion, mediates 'Lys-27'-linked ubiquitination of MTOR and thereby inhibits substrate recruitment to mTORC1 (PubMed:37979583). Also inhibits SARS-CoV-2 replication by inducing NSP5 degradation (PubMed:39223933). {ECO:0000269|PubMed:21768309, ECO:0000269|PubMed:22972877, ECO:0000269|PubMed:26868148, ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933, ECO:0000269|PubMed:39504958}.
uniprot
proteins
mass_dalton
44508
uniprot
proteins
mutagenesis
MUTAGEN 127; /note="T->A: Loss of EIF2AK4-induced cytoplasmic retention of FBXO22."; /evidence="ECO:0000269|PubMed:37979583
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by EIF2AK4 at Thr-127 causes cytoplasmic retention of FBXO22. {ECO:0000269|PubMed:37979583}.
uniprot
proteins
pubmed
10531035
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21768309
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22972877
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26868148
uniprot
proteins
pubmed
37979583
uniprot
proteins
pubmed
39223933
uniprot
proteins
pubmed
39504958
uniprot
proteins
pubmed
40215970
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933}. Nucleus {ECO:0000269|PubMed:37979583, ECO:0000269|PubMed:39223933}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Amino acid depletion lead to a time-dependent increase of FBXO22 in the cytoplasm. {ECO:0000269|PubMed:37979583}.
uniprot
proteins