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Details on Person UniProt:Q9UKB1 FBXW11

Class:IdReferenceGeneProduct:55058
_chainChangeLogchain:1-542 added on Sat February 7 2015
_displayNameUniProt:Q9UKB1 FBXW11
_timestamp2024-11-03 20:09:55
chainchain:1-542
checksum7CD40087EFAA5C8A
commentFUNCTION Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10437795, PubMed:10648623, PubMed:11158290, PubMed:19966869, PubMed:20347421, PubMed:22017875, PubMed:22017876, PubMed:36608670). Probably recognizes and binds to phosphorylated target proteins: the interaction with substrates requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S (PubMed:10437795, PubMed:10648623, PubMed:19966869, PubMed:20347421, PubMed:22017875, PubMed:22017876, PubMed:36608670). SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling regulation (PubMed:10321728). SCF(FBXW11) plays a key role in NF-kappa-B activation by mediating ubiquitination of phosphorylated NFKBIA, leading to its degradation by the proteasome, thereby allowing the associated NF-kappa-B complex to translocate into the nucleus and to activate transcription (PubMed:10321728, PubMed:10437795, PubMed:10644755, PubMed:20347421). The SCF(FBXW11) complex also regulates NF-kappa-B by mediating ubiquitination of phosphorylated NFKB1: specifically ubiquitinates the p105 form of NFKB1, leading to its degradation (PubMed:11158290). SCF(FBXW11) mediates the ubiquitination of IFNAR1 (PubMed:14532120, PubMed:15337770). SCF(FBXW11) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25503564). Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1 (PubMed:18575781). Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint (PubMed:14603323). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2 (PubMed:15917222). SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2 (PubMed:29420262). SCF(FBXW11) acts as a regulator of mTORC1 signaling pathway by catalyzing ubiquitination and subsequent proteasomal degradation of phosphorylated DEPTOR, TFE3 and MITF (PubMed:22017875, PubMed:22017876, PubMed:36608670).FUNCTION (Microbial infection) Target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action.PATHWAY Protein modification; protein ubiquitination.SUBUNIT Self-associates (PubMed:10644755). Component of the SCF(FBXW11) complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer (PubMed:10066435, PubMed:10437795, PubMed:20347421, PubMed:22017875, PubMed:22017876, PubMed:36608670). Interacts with BST2 and USP47 (PubMed:19730691, PubMed:19966869). Interacts with TRIM21 (PubMed:16880511). Interacts with PER3 (PubMed:15917222). Interacts with INAVA (PubMed:29420262). Interacts with REST (PubMed:18354482).SUBUNIT (Microbial infection) Interact with Rift valley fever virus NSs (via omegaXaV motif); this interaction is important for EIF2AK2/PKR degradation.INTERACTION In the embryo, it is expressed in the developing eye, limbs and brain (PubMed:31402090). Expression is observed in the lens, retina, lips of the optic fissure closure and regions of the conjunctiva at Carnegie stages (CS) between CS15 and CS21. As eye development progresses, the stronger signal observed in the retina progressively shifts from the inner toward the outer retinal layers (PubMed:31402090). In the developing hand, expression is strong at CS15. At CS19 and CS21, after the digits have begun to form, strong expression is seen in the mesenchyme surrounding the developing cartilage (PubMed:31402090). In the brain, it is expressed in the primitive ventricles at CS17 and CS19, hypothalamus and medulla at CS17, and metencephalon at CS19 (PubMed:31402090). Strong expression is also observed in the pharyngeal arches, including the mandibular process and tongue at CS17 (PubMed:31402090).INDUCTION Expression is negatively regulated by Wnt/beta-catenin pathway.DOMAIN The N-terminal D domain mediates homodimerization.DISEASE The disease is caused by variants affecting the gene represented in this entry.SEQUENCE CAUTION Extended N-terminus.
descriptionrecommendedName: F-box/WD repeat-containing protein 11 alternativeName: fullName evidence="29"F-box and WD repeats protein beta-TrCP2 alternativeName: F-box/WD repeat-containing protein 1B alternativeName: fullName evidence="28"Homologous to Slimb protein shortName evidence="28"HOS
geneNameFBXW11
BTRCP2
FBW1B
FBXW1B
KIAA0696
identifierQ9UKB1
isSequenceChangedFALSE
keyword3D-structure
Alternative splicing
Biological rhythms
Cell cycle
Cytoplasm
Disease variant
Host-virus interaction
Nucleus
Proteomics identification
Reference proteome
Repeat
Ubl conjugation pathway
WD repeat
Wnt signaling pathway
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9841277] Weiser, Joel
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9862192] Weiser, Joel, 2024-02-26
[InstanceEdit:9917590] Weiser, Joel, 2024-08-09
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
nameFBXW11
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8999480] ENSEMBL:ENSG00000072803 FBXW11 [Homo sapiens]
secondaryIdentifierFBW1B_HUMAN
B2RC98
Q9P2S8
Q9P2S9
Q9Y4C6
sequenceLength542
species[Species:48887] Homo sapiens
(isoformParent)[ReferenceIsoform:147501] UniProt:Q9UKB1-2 FBXW11 [Homo sapiens]
[ReferenceIsoform:147502] UniProt:Q9UKB1-3 FBXW11 [Homo sapiens]
[ReferenceIsoform:415445] UniProt:Q9UKB1-1 FBXW11 [Homo sapiens]
(referenceEntity)[EntityWithAccessionedSequence:976035] FBXW11 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:9953055] FBXW11 [nucleoplasm] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q9UKB1 FBXW11 (55058)