FBXO4
entrez
26272
canonical
uniprot
Q9UKT5
canonical
ensembl
ENSG00000151876
resolver
ensp
ENSP00000281623
resolver
ensp
ENSP00000296812
resolver
ensp
ENSP00000421749
resolver
enst
ENST00000509134
resolver
genesymbol
FBXO4
resolver
genesymbol_syn
FBX4
resolver
hgnc
HGNC:13583
resolver
uniprot
B3KNA0
resolver
uniprot
D6RAJ6
resolver
uniprot
Q68CU8
resolver
uniprot
Q86VT8
resolver
uniprot
Q9UK98
resolver
uniprot_entry
B3KNA0_HUMAN
resolver
uniprot_entry
D6RAJ6_HUMAN
resolver
uniprot_entry
FBX4_HUMAN
resolver
uniprot_sec
Q68CU8
resolver
uniprot_sec
Q86VT8
resolver
uniprot_sec
Q9UK98
resolver
amino_acid_sequence
MAGSEPRSGTNSPPPPFSDWGRLEAAILSGWKTFWQSVSKERVARTTSREEVDEAASTLTRLPIDVQLYILSFLSPHDLCQLGSTNHYWNETVRDPILWRYFLLRDLPSWSSVDWKSLPDLEILKKPISEVTDGAFFDYMAVYRMCCPYTRRASKSSRPMYGAVTSFLHSLIIQNEPRFAMFGPGLEELNTSLVLSLMSSEELCPTAGLPQRQIDGIGSGVNFQLNNQHKFNILILYSTTRKERDRAREEHTSAVNKMFSRHNEGDDQQGSRYSVIPQIQKVCEVVDGFIYVANAEAHKRHEWQDEFSHIMAMTDPAFGSSGRPLLVLSCISQGDVKRMPCFYLAHELHLNLLNHPWLVQDTEAETLTGFLNGIEWILEEVESKRAR
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:10531035, PubMed:18598945, PubMed:20181953, PubMed:29142209). Promotes ubiquitination of cyclin-D1 (CCND1) and its subsequent proteasomal degradation (PubMed:18598945). However, it does not act as a major regulator of CCND1 stability during the G1/S transition (By similarity). Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 (PubMed:16275645, PubMed:20159592). Promotes ubiquitination of FXR1 following phosphorylation of FXR1 by GSK3B, leading to FXR1 degradation by the proteasome (PubMed:29142209). {ECO:0000250|UniProtKB:Q8CHQ0, ECO:0000269|PubMed:10531035, ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:29142209}.
uniprot
proteins
mass_dalton
44136
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="S->A: Reduces homodimerization. Reduces ubiquitination of CCND1."; /evidence="ECO:0000269|PubMed:18598945"; MUTAGEN 12; /note="S->E: No effect on homodimerization."; /evidence="ECO:0000269|PubMed:18598945"; MUTAGEN 13; /note="P->A: Reduces homodimerization."; /evidence="ECO:0000269|PubMed:18598945"; MUTAGEN 23; /note="L->A: Abolishes homodimerization."; /evidence="ECO:0000269|PubMed:18598945"; MUTAGEN 341; /note="C->W: Abolishes interaction with TERF1."; /evidence="ECO:0000269|PubMed:20159592"; MUTAGEN 345; /note="A->R: Abolishes interaction with TERF1."; /evidence="ECO:0000269|PubMed:20159592
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:10531035, ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945, ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:29142209}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-12 varies during the cell cycle (By similarity). 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 (By similarity). Phosphorylation at Ser-12 promotes homodimerization and is necessary for optimal ubiquitin ligase activity towards CCND1 (PubMed:18598945). {ECO:0000250|UniProtKB:Q8CHQ0, ECO:0000269|PubMed:18598945}.
uniprot
proteins
pubmed
10531035
uniprot
proteins
pubmed
10531037
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16275645
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18598945
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20159592
uniprot
proteins
pubmed
20181953
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29142209
uniprot
proteins
sequence_length
387
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8CHQ0}.
uniprot
proteins