Fbxo22
entrez
71999
canonical
uniprot
Q78JE5
canonical
ensembl
ENSMUSG00000032309
resolver
ensp
ENSMUSP00000034859
resolver
ensp
ENSMUSP00000117106
resolver
enst
ENSMUST00000034859
resolver
enst
ENSMUST00000146201
resolver
genesymbol
Fbxo22
resolver
genesymbol_syn
Fbx22
resolver
uniprot
F6YYL4
resolver
uniprot
Q3V492
resolver
uniprot_entry
F6YYL4_MOUSE
resolver
uniprot_entry
FBX22_MOUSE
resolver
uniprot_entry
Q3V492_MOUSE
resolver
amino_acid_sequence
MEPAGGGGGVSSSTDPRSTYVLSNLAEVVERVFTFLPAKALLRVAGVCRLWRECVRRVLRTHRSVTWISAGVAEAGHLEGHCLVRVVAEALENVRILPQTVLYMADSETFISLEECRGHKRARKRTTMETACALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQPFHFIKDSKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLHRVVSTFSDMNIILAGGQVDNLSSLTCEKNPLDIDATGVVGLSFSGHRIQSATVLLTEDVNDAKTVEAAMQRLKAANIPEQNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRIVTGNFILRRCNEVKEEDLFHSYTTIMALVHLGTSK
uniprot
proteins
function
FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. 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. {ECO:0000269|PubMed:22972877}.; 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 (PubMed:22972877). Acts as a key regulator of histone methylation marks namely H3K9 and H3K36 methylation through the regulation of histone demethylase KDM4A protein levels (By similarity). 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 (By similarity). Upon amino acid depletion, mediates 'Lys-27'-linked ubiquitination of MTOR and thereby inhibits substrate recruitment to mTORC1 (By similarity). {ECO:0000250|UniProtKB:Q8NEZ5, ECO:0000269|PubMed:22972877, ECO:0000269|PubMed:26868148}.
uniprot
proteins
mass_dalton
44203
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22972877
uniprot
proteins
pubmed
26868148
uniprot
proteins
sequence_length
402
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22972877}.
uniprot
proteins