FBXL17

F-box/LRR-repeat protein 17

701 amino acids

Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome (PubMed:30190310). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1 (PubMed:24035498, PubMed:30190310). The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction (PubMed:27234298). The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (By similarity).

Belongs to the FBXL17 family.

75.695 kDa

MGHLLSKEPRNRPSQKRPRCCSWCRRRRPLLRLPRRTPAKVPPQPAAPRSRDCFFRGPCMLCFIVHSPGAPAPAGPEEEPPLSPPPRDGAYAAASSSQHLARRYAALAAEDCAAAARRFLLSSAAAAAAAAASASSPASCCKELGLAAAAAWEQQGRSLFLASLGPVRFLGPPAAVQLFRGPTPSPAELPTPPEMVCKRKGAGVPACTPCKQPRCGGGGCGGGGGGGGGGGPAGGGASPPRPPDAGCCQAPEQPPQPLCPPPSSPTSEGAPTEAGGDAVRAGGTAPLSAQQQHECGDADCRESPENPCDCHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLDLSSRQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQLSDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYALIAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS

Fbxl17

F-box/LRR-repeat protein 17

701 amino acids

Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome (By similarity). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1 (By similarity). The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction (PubMed:27234298). The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (PubMed:28883095).

Belongs to the FBXL17 family.

75.683 kDa

MGHLLSKEPRNRPSQKRPRCCSWCRRRRPLLRLPRRALAKASPQPAAPRSRDCFFRGPCMLCFIVHSPGAPASAGLEEEPPLSPPPPPPRDGAYAAVSSQHLARRYAALAAEDCAAAARRFLLSSAAAAAAAASSPASCCKELGLAAAAAWEQQGRSLFLAGVGPVRFLGPLAAVQLFRAPPAPPPQAEPATALEMVCKRKGAGVPACTPCKQPRCGCGGCGGGGGGGGGPAGGGASPPRPPDAGCCQAPEQPPPPLCPAPASPASECAPIVAAAGDTVRAGGTAPSSAQQQPESGDADCQEPPENPCDCHREPPPEIPDINQLPPSILLKIFSNLSLNERCLSASLVCKYWRDLCLDFQFWKQLDLSSRQQVTDELLEKIASRSQNIIEINISDCRSLSDSGVCVLAFKCPGLLRYTAYRCKQLSDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSRCRELKDIHFGQCYKISDEGMIVIAKSCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYALIAIGRYSVTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNELTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAATS

fbxl17

F-box/LRR-repeat protein 17

673 amino acids

Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome (By similarity). The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (PubMed:30190310).

Belongs to the FBXL17 family.

73.081 kDa

MGHVAPHASKKEHVAPHAAEKDHVAPHASKKEHVAPHAAEKGQVAPYAAGEGQVAPNAAGERPVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEGQVAPYAAGEAQVAPHAAGEGRVAPHAAGDGQVEHCTVEDREEGHIGTTEQGHMSHYTSKLEHMAPPSAQTEAVVSYVAGERHAPPDCTVSGPAMCCSAEARQTTPDWTTTGPEISQGTLPGLTVLHVGGTWQTFAAEDEPCVTTLLSPVKPLSSSRKYAPYNLQIPSYSESEPQAHKGLSSETFGPCEPLHINQLPSSLLLKIFSNLSLNERCILASLVCKYWRDLCLDSQFWKQLDLSNRQQIKDNILEEIASRSQNITEINISDCFSVSDQGVCVVALKCPGLVKYTAYRCKQLSDISLIALAAHCPSLQKVHVGNQDKLSDEALIQMGRRCKELKDIHFGQCYKISDEGLIVIAKGCQKLQKIYMQENKLVSDESVKAFAEHCPGLQYVGFMGCSVTSEGVINLTKLKHLSSLDLRHITELDNETVMEIVKQCQHLTSLNLCLNRSINDRCVEVIAKEGRSLKELYLVTCKITDYALIAIGRYSKSIETVDVGWCKEITDYGAKQIAQSSKSIRYLGLMRCDKVNEATVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNASPAT