FBXO6
entrez
26270
canonical
uniprot
Q9NRD1
canonical
ensembl
ENSG00000116663
resolver
ensp
ENSP00000365944
resolver
ensp
ENSP00000388781
resolver
ensp
ENSP00000577539
resolver
ensp
ENSP00000577540
resolver
ensp
ENSP00000577541
resolver
ensp
ENSP00000577542
resolver
ensp
ENSP00000577543
resolver
ensp
ENSP00000631725
resolver
ensp
ENSP00000631726
resolver
enst
ENST00000376753
resolver
enst
ENST00000907480
resolver
enst
ENST00000907481
resolver
enst
ENST00000907482
resolver
enst
ENST00000907483
resolver
enst
ENST00000907484
resolver
enst
ENST00000961666
resolver
enst
ENST00000961667
resolver
genesymbol
FBXO6
resolver
genesymbol_syn
FBG2
resolver
genesymbol_syn
FBS2
resolver
genesymbol_syn
FBX6
resolver
hgnc
HGNC:13585
resolver
uniprot
B1AK42
resolver
uniprot
B2RC88
resolver
uniprot
Q9UKT3
resolver
uniprot_entry
FBX6_HUMAN
resolver
uniprot_sec
B1AK42
resolver
uniprot_sec
B2RC88
resolver
uniprot_sec
Q9UKT3
resolver
amino_acid_sequence
MDAPHSKAALDSINELPENILLELFTHVPARQLLLNCRLVCSLWRDLIDLMTLWKRKCLREGFITKDWDQPVADWKIFYFLRSLHRNLLRNPCAEEDMFAWQIDFNGGDRWKVESLPGAHGTDFPDPKVKKYFVTSYEMCLKSQLVDLVAEGYWEELLDTFRPDIVVKDWFAARADCGCTYQLKVQLASADYFVLASFEPPPVTIQQWNNATWTEVSYTFSDYPRGVRYILFQHGGRDTQYWAGWYGPRVTNSSIVVSPKMTRNQASSEAQPGQKHGQEEAAQSPYRAVVQIF
uniprot
proteins
function
FUNCTION: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to ensure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication. {ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:19716789}.
uniprot
proteins
mass_dalton
33933
uniprot
proteins
mutagenesis
MUTAGEN 241..242; /note="YW->AA: Abolishes interaction with glycosylated concanavalin-A in vitro."; /evidence="ECO:0000269|PubMed:18203720
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
pubmed
10531035
uniprot
proteins
pubmed
10945468
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
18203720
uniprot
proteins
pubmed
19716789
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
sequence_length
293
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19716789}.
uniprot
proteins