Aliases for BTRC Gene
- Beta-Transducin Repeat Containing E3 Ubiquitin Protein Ligase 2 3 5
- F-Box And WD Repeats Protein Beta-TrCP 3 4
- PIkappaBalpha-E3 Receptor Subunit 3 4
- Epididymis Tissue Protein Li 2a 3 4
- E3RSIkappaB 3 4
- FBXW1A 3 4
- FBW1A 3 4
- F-Box/WD Repeat-Containing Protein 1A 3
- Beta-Transducin Repeat Containing 2
- F-Box And WD-Repeat Protein 1B 3
External Ids for BTRC Gene
Previous GeneCards Identifiers for BTRC Gene
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbws class; in addition to an F-box, this protein contains multiple WD-40 repeats. The encoded protein mediates degradation of CD4 via its interaction with HIV-1 Vpu. It has also been shown to ubiquitinate phosphorylated NFKBIA (nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha), targeting it for degradation and thus activating nuclear factor kappa-B. Alternatively spliced transcript variants have been described. A related pseudogene exists in chromosome 6. [provided by RefSeq, Mar 2012]
GeneCards Summary for BTRC Gene
BTRC (Beta-Transducin Repeat Containing E3 Ubiquitin Protein Ligase) is a Protein Coding gene. Diseases associated with BTRC include Vaccinia and Isolated Split Hand-Split Foot Malformation. Among its related pathways are Activated TLR4 signalling and Cell Cycle, Mitotic. Gene Ontology (GO) annotations related to this gene include ligase activity and protein dimerization activity. An important paralog of this gene is FBXW11.
UniProtKB/Swiss-Prot for BTRC Gene
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. Recognizes and binds to phosphorylated target proteins (PubMed:10066435, PubMed:10497169, PubMed:10644755, PubMed:10835356, PubMed:11238952, PubMed:11359933, PubMed:11994270, PubMed:12791267, PubMed:12902344, PubMed:14603323, PubMed:14681206, PubMed:14988407, PubMed:15448698, PubMed:15917222, PubMed:16371461, PubMed:25503564, PubMed:25704143, PubMed:9859996). SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling (PubMed:12077367, PubMed:12820959). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2 (PubMed:10835356, PubMed:11238952, PubMed:14681206, PubMed:14603323). SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription (PubMed:10066435, PubMed:10497169, PubMed:10644755). Ubiquitination of NFKBIA occurs at Lys-21 and Lys-22 (PubMed:10066435). SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25704143, PubMed:25503564). SCF(BTRC) mediates the ubiquitination and subsequent degradation of nuclear NFE2L1 (By similarity). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2 (PubMed:15917222). May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3 (PubMed:16371461).
Ubiquitin E3 ligases (EC 220.127.116.11) attach ubiquitin molecules onto lysine residues of proteins in order to target the protein for a specific cellular process, such as proteasomal degradation or an alteration in subcellular localization.