FBXO31
entrez
79791
canonical
uniprot
Q5XUX0
canonical
ensembl
ENSG00000103264
resolver
ensp
ENSP00000310841
resolver
ensp
ENSP00000479703
resolver
enst
ENST00000618298
resolver
genesymbol
FBXO31
resolver
genesymbol_syn
FBX14
resolver
genesymbol_syn
FBX31
resolver
hgnc
HGNC:16510
resolver
uniprot
A0A0C4DGU8
resolver
uniprot
Q5K680
resolver
uniprot
Q8WYV1
resolver
uniprot
Q96D73
resolver
uniprot
Q9UFV4
resolver
uniprot_entry
A0A0C4DGU8_HUMAN
resolver
uniprot_entry
FBX31_HUMAN
resolver
uniprot_sec
Q5K680
resolver
uniprot_sec
Q8WYV1
resolver
uniprot_sec
Q96D73
resolver
uniprot_sec
Q9UFV4
resolver
amino_acid_sequence
MAVCARLCGVGPSRGCRRRQQRRGPAETAAADSEPDTDPEEERIEASAGVGGGLCAGPSPPPPRCSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVDDPMRFKPLFRIHLMERKAATVECMYGHKGPHHGHIQIVKKDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSRPDDLIKPGLFKGTYGSHGLEIVMLSFHGRRARGTKITGDPNIPAGQQTVEIDLRHRIQLPDLENQRNFNELSRIVLEVRERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQPFVLPVGVSSRNEDYPRTCRMCFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRVQATFRNADAPSPQAFDEMLKNIQSLTS
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal recessive 45 (MRT45) [MIM:615979]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT45 manifestations include mild to moderate intellectual disability and dysmorphic features, including coarse facies, broad nasal bridge, fleshy nares, and thick, prominent lips. {ECO:0000269|PubMed:24623383, ECO:0000269|PubMed:33675180, ECO:0000269|PubMed:39880951}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Substrate-recognition component of the SCF(FBXO31) protein ligase complex, which specifically mediates the ubiquitination of proteins amidated at their C-terminus in response to oxidative stress, leading to their degradation by the proteasome (PubMed:39880951). FBXO31 specifically recognizes and binds C-terminal peptides bearing an amide: C-terminal amidation in response to oxidative stress takes place following protein fragmentation (PubMed:39880951). The SCF(FBXO31) also plays a role in G1 arrest following DNA damage by mediating ubiquitination of phosphorylated cyclin-D1 (CCND1), promoting its degradation by the proteasome, resulting in G1 arrest (PubMed:19412162, PubMed:29279382). The SCF(FBXO31) complex is however not a major regulator of CCND1 stability during the G1/S transition (By similarity). In response to genotoxic stress, the SCF(FBXO31) complex directs ubiquitination and degradation of phosphorylated MDM2, thereby promoting p53/TP53-mediated DNA damage response (PubMed:26124108). SCF(FBXO31) complex is required for genomic integrity by catalyzing ubiquitination and degradation of cyclin-A (CCNA1 and/or CCNA2) during the G1 phase (PubMed:31413110). In response to genotoxic stress, the SCF(FBXO31) complex directs ubiquitination and degradation of phosphorylated FBXO46 and MAP2K6 (PubMed:24936062, PubMed:30171069). SCF(FBXO31) complex promotes ubiquitination and degradation of CDT1 during the G2 phase to prevent re-replication (PubMed:24828503). The SCF(FBXO31) complex also mediates ubiquitination and degradation of DUSP6, OGT and PARD6A (PubMed:23469015, PubMed:34686346, PubMed:39894887). {ECO:0000250|UniProtKB:Q3TQF0, ECO:0000269|PubMed:19412162, ECO:0000269|PubMed:23469015, ECO:0000269|PubMed:24828503, ECO:0000269|PubMed:24936062, ECO:0000269|PubMed:26124108, ECO:0000269|PubMed:29279382, ECO:0000269|PubMed:30171069, ECO:0000269|PubMed:31413110, ECO:0000269|PubMed:34686346, ECO:0000269|PubMed:39880951, ECO:0000269|PubMed:39894887}.
uniprot
proteins
mass_dalton
60664
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="S->A: Abolished phosphorylation by AKT1."; /evidence="ECO:0000269|PubMed:29343641"; MUTAGEN 64..67; /note="RCSL->ACSA: Abolished ubiquitination and degradation by the APC/C complex."; /evidence="ECO:0000269|PubMed:29343641"; MUTAGEN 206; /note="C->A,S: Impaired folding, inducing the formation of insoluble aggregates."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 214; /note="H->A,F,N: Impaired folding, inducing the formation of insoluble aggregates."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 230; /note="C->A: Impaired folding, inducing the formation of insoluble aggregates."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 236; /note="H->A: Impaired folding, inducing the formation of insoluble aggregates."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 278; /note="S->A: Fails to accumulate following gamma-irradiation."; /evidence="ECO:0000269|PubMed:19412162"; MUTAGEN 297..299; /note="DDL->AAA: Abolished interaction with cyclin-A."; /evidence="ECO:0000269|PubMed:31413110"; MUTAGEN 309; /note="Y->A: Abolished ability to promote ubiquitination of amidated proteins."; /evidence="ECO:0000269|PubMed:39880951"; MUTAGEN 311; /note="S->A: Does not affect ability to promote ubiquitination of CCND1."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 312; /note="H->A: Decreased ability to promote ubiquitination of CCND1."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 330; /note="K->A: Decreased ability to promote ubiquitination of CCND1."; /evidence="ECO:0000269|PubMed:29279382"; MUTAGEN 337; /note="I->D: Abolished ability to promote ubiquitination of amidated proteins."; /evidence="ECO:0000269|PubMed:39880951"; MUTAGEN 343; /note="T->V: Abolished ability to promote ubiquitination of amidated proteins."; /evidence="ECO:0000269|PubMed:39880951"; MUTAGEN 400; /note="S->A: No effect following gamma-irradiation."; /evidence="ECO:0000269|PubMed:19412162"; MUTAGEN 419; /note="T->A: Decreased phosphorylation, leading to impair ubiquitination by the SCF(FBXO46) complex."; /evidence="ECO:0000269|PubMed:30171069"; MUTAGEN 461..464; /note="RTCR->ATCA: Abolished interaction with FBXO46, preventing ubiquitination and degradation by the SCF(FBXO46) complex."; /evidence="ECO:0000269|PubMed:30171069"; MUTAGEN 480; /note="S->A: Decreased phosphorylation, leading to impair ubiquitination by the SCF(FBXO46) complex."; /evidence="ECO:0000269|PubMed:30171069
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19412162, ECO:0000269|PubMed:23469015, ECO:0000269|PubMed:24828503, ECO:0000269|PubMed:24936062, ECO:0000269|PubMed:29279382, ECO:0000269|PubMed:31413110, ECO:0000269|PubMed:34686346, ECO:0000269|PubMed:39880951, ECO:0000269|PubMed:39894887}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-278 by ATM following gamma-irradiation results in its stabilization (PubMed:19412162). Phosphorylation at Thr-419 and Ser-480 in absence of stress promotes its ubiquitination and degradation by the SCF(FBXO46) complex (PubMed:30171069). Phosphorylation at Ser-33 by AKT1 promotes association with CDC20 and ubiquitination by the APC/C complex (PubMed:29343641). {ECO:0000269|PubMed:19412162, ECO:0000269|PubMed:29343641, ECO:0000269|PubMed:30171069}.; PTM: Ubiquitinated by the SCF(FBXO46) complex in absence of stress, promoting its degradation (PubMed:30171069). Ubiquitinated by the APC/C complex following phosphorylation at Ser-33, leading to its degradation by the proteasome (PubMed:29343641). {ECO:0000269|PubMed:29343641, ECO:0000269|PubMed:30171069}.
uniprot
proteins
protein_family
FBXO31 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
15520277
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16357137
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19412162
uniprot
proteins
pubmed
23469015
uniprot
proteins
pubmed
24623383
uniprot
proteins
pubmed
24828503
uniprot
proteins
pubmed
24936062
uniprot
proteins
pubmed
26124108
uniprot
proteins
pubmed
29279382
uniprot
proteins
pubmed
29343641
uniprot
proteins
pubmed
30171069
uniprot
proteins
pubmed
31413110
uniprot
proteins
pubmed
32989326
uniprot
proteins
pubmed
33675180
uniprot
proteins
pubmed
34686346
uniprot
proteins
pubmed
39880951
uniprot
proteins
pubmed
39894887
uniprot
proteins
sequence_length
539
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24828503, ECO:0000269|PubMed:30171069}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:B2RYN2}.
uniprot
proteins