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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Levy N.,
Agulnik A.I.,
Boettger-Tong H.,
Bishop C.E.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[3]
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SUBCELLULAR LOCATION, INTERACTION WITH CYCE, AND TISSUE SPECIFICITY.
DOI=10.1101/gad.13.18.2375; PubMed=10500095 [NCBI, ExPASy, EBI, Israel, Japan]
Singer J.D.,
Gurian-West M.,
Clurman B.,
Roberts J.M.;
"Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells.";
Genes Dev. 13:2375-2387(1999).
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[4]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASS SPECTROMETRY.
DOI=10.1021/pr070122r; PubMed=17622165 [NCBI, ExPASy, EBI, Israel, Japan]
Smith J.C.,
Duchesne M.A.,
Tozzi P.,
Ethier M.,
Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells.";
J. Proteome Res. 6:3174-3186(2007).
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[5]
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STRUCTURE BY NMR OF 678-768.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the cullin-3 homologue.";
Submitted (OCT-2003) to the PDB data bank.
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- FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition (By similarity).
- PATHWAY: Protein modification; protein ubiquitination.
- SUBUNIT: Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, asapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of a second CUL3 molecule. Interacts with RBX1, RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing SPOP. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KBTBD10) complex containing KBTBD10. Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20, C16orf44, GMCL1L, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN (By similarity).
- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus.
- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain, spleen and testis.
- PTM: Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR E3 ligase complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity).
- MISCELLANEOUS: Null deficient mice are not viable. Extraembryonic ectoderm shows a greatly increased number of cells in S phase. In the trophectoderm cells are blocked to entry into S phase.
- SIMILARITY: Belongs to the cullin family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 768 AA [This is the length of the unprocessed precursor] |
Molecular weight: 88948 Da [This is the MW of the unprocessed precursor] |
CRC64: 841E20407BD076A3 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
70 80 90 100 110 120
AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
130 140 150 160 170 180
DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
190 200 210 220 230 240
GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
250 260 270 280 290 300
INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY
310 320 330 340 350 360
KLFSRVPNGL KTMCECMSCY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF
370 380 390 400 410 420
NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
430 440 450 460 470 480
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
490 500 510 520 530 540
NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
550 560 570 580 590 600
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
610 620 630 640 650 660
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHIFT
670 680 690 700 710 720
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
730 740 750 760
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
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Q9JLV5 in FASTA format |
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