Fbxo4
entrez
106052
canonical
uniprot
Q8CHQ0
canonical
ensembl
ENSMUSG00000022184
resolver
ensp
ENSMUSP00000022791
resolver
enst
ENSMUST00000022791
resolver
genesymbol
Fbxo4
resolver
genesymbol_syn
Fbx4
resolver
uniprot
E9QPM9
resolver
uniprot
Q99JG8
resolver
uniprot_entry
FBX4_MOUSE
resolver
uniprot_sec
E9QPM9
resolver
uniprot_sec
Q99JG8
resolver
amino_acid_sequence
MAGSEPRGAGSPPPASDWGRLEAAILSGWRTFWYSVAKERATPTASRKEAAEETSALTRLPVDVQLYILSFLSPHDLCQLGSTDHYWNKTIRDPILWRYFLLRDLPSWSSVDWKSLPDLEILKKPISEVTDSTCLDYMEVYKMCCPYTRRALKASRPMYGVVTSFLHSLIIQNEPRFAMFGPGLEELNTSLVLSLMSSEDLCPTAGLPHRQIDGIGSGVNFQLNNQQKFNILILYSTTRKERDRAREEHTSTVNKMFSLQSEGDEQQGSRYSVIPQIQKVCEVVDGFIYVANAEAHRRHEWQDEFSRIMAMTDPAFGSSGRPMLVLSCISQADVKRMPCFYLAHELHLSLLNHPWMVQDTEAETLTGFLNGIEWILEEVESKRAK
uniprot
proteins
function
FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:17081987, PubMed:18598945, PubMed:19767775, PubMed:29142209). Promotes ubiquitination of cyclin-D1 (CCND1) and its subsequent proteasomal degradation (PubMed:17081987, PubMed:18598945, PubMed:19767775). However, it does not act as a major regulator of CCND1 stability during the G1/S transition (PubMed:22124152). Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 (By similarity). Promotes ubiquitination of FXR1 following phosphorylation of FXR1 by GSK3B, leading to FXR1 degradation by the proteasome (PubMed:29142209). {ECO:0000250|UniProtKB:Q9UKT5, ECO:0000269|PubMed:17081987, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:19767775, ECO:0000269|PubMed:29142209}.
uniprot
proteins
mass_dalton
43777
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17081987, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:19767775, ECO:0000269|PubMed:29142209}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-11 varies during the cell cycle. It is low in resting cells and high in the S phase and the G2/M phase of the cell cycle. Phosphorylation is decreased during late G1 phase. Phosphorylation at Ser-11 is important for homodimerization and for optimal ubiquitin ligase activity towards CCND1. {ECO:0000269|PubMed:18598945}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081987
uniprot
proteins
pubmed
18598945
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19487455
uniprot
proteins
pubmed
19767775
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22124152
uniprot
proteins
pubmed
29142209
uniprot
proteins
sequence_length
385
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081987}.
uniprot
proteins