ID   CUL3_MOUSE              Reviewed;         768 AA.
AC   Q9JLV5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   22-JUL-2008, entry version 54.
DE   RecName: Full=Cullin-3;
DE            Short=CUL-3;
GN   Name=Cul3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Levy N., Agulnik A.I., Boettger-Tong H., Bishop C.E.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, INTERACTION WITH CYCE, AND TISSUE SPECIFICITY.
RX   MEDLINE=99431971; PubMed=10500095; DOI=10.1101/gad.13.18.2375;
RA   Singer J.D., Gurian-West M., Clurman B., Roberts J.M.;
RT   "Cullin-3 targets cyclin E for ubiquitination and controls S phase in
RT   mammalian cells.";
RL   Genes Dev. 13:2375-2387(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 678-768.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the cullin-3 homologue.";
RL   Submitted (OCT-2003) to the PDB data bank.
CC   -!- FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-
CC       CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. As a scaffold protein may contribute to catalysis
CC       through positioning of the substrate and the ubiquitin-conjugating
CC       enzyme. The E3 ubiquitin-protein ligase activity of the complex is
CC       dependent on the neddylation of the cullin subunit and is
CC       inhibited by the association of the deneddylated cullin subunit
CC       with TIP120A/CAND1 (By similarity). The functional specificity of
CC       the BCR complex depends on the BTB domain-containing protein as
CC       the susbstrate recognition component. BCR(SPOP) is involved in
CC       ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or
CC       GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on
CC       mitotic chromosomes and thereby coordinates faithful mitotic
CC       progression and completion of cytokinesis. Involved in
CC       ubiquitination of cyclin E and of cyclin D1 (in vitro) thus
CC       involved in regulation of G1/S transition (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Forms neddylation-dependent homodimers. Component of
CC       multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC       formed of CUL3, RBX1 and a variable BTB domain-containing protein
CC       acting as both, asapter to cullin and substrate recognition
CC       subunit. The BCR complex may be active as a heterodimeric complex,
CC       in which NEDD8, covalently attached to one CUL3 molecule, binds to
CC       the C-terminus of a second CUL3 molecule. Interacts with RBX1,
CC       RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing
CC       SPOP. Part of the probable BCR(KLHL9-KLHL13) complex with BTB
CC       domain proteins KLHL9 and KLHL13. Part of the BCR(KBTBD10) complex
CC       containing KBTBD10. Part of the BCR(ENC1) complex containing ENC1.
CC       Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of
CC       a complex consisting of H2AFY, CUL3 and SPOP. Interacts with
CC       KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20,
CC       C16orf44, GMCL1L, BTBD1. Part of a complex that contains CUL3,
CC       RBX1 and GAN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       brain, spleen and testis.
CC   -!- PTM: Neddylated. Attachment of NEDD8 is required for the E3
CC       ubiquitin-protein ligase activity of the BCR E3 ligase complex.
CC       Deneddylated via its interaction with the COP9 signalosome (CSN)
CC       complex (By similarity).
CC   -!- MISCELLANEOUS: Null deficient mice are not viable. Extraembryonic
CC       ectoderm shows a greatly increased number of cells in S phase. In
CC       the trophectoderm cells are blocked to entry into S phase.
CC   -!- SIMILARITY: Belongs to the cullin family.
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DR   EMBL; AF129738; AAF36500.1; -; mRNA.
DR   EMBL; BC027304; AAH27304.1; -; mRNA.
DR   RefSeq; NP_057925.1; -.
DR   UniGene; Mm.12665; -.
DR   PDB; 1IUY; NMR; -; A=678-768.
DR   PDBsum; 1IUY; -.
DR   PhosphoSite; Q9JLV5; -.
DR   Ensembl; ENSMUSG00000004364; Mus musculus.
DR   GeneID; 26554; -.
DR   KEGG; mmu:26554; -.
DR   MGI; MGI:1347360; Cul3.
DR   HOVERGEN; Q9JLV5; -.
DR   ArrayExpress; Q9JLV5; -.
DR   CleanEx; MM_CUL3; -.
DR   GermOnline; ENSMUSG00000004364; Mus musculus.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Golgi apparatus; Nucleus; Phosphoprotein;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    768       Cullin-3.
FT                                /FTId=PRO_0000119794.
FT   MOD_RES      58     58       Phosphotyrosine (By similarity).
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   CROSSLNK    712    712       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in NEDD8) (By
FT                                similarity).
FT   TURN        699    701
FT   HELIX       702    714
FT   STRAND      716    718
FT   HELIX       719    729
FT   HELIX       738    750
FT   STRAND      753    756
FT   STRAND      761    766
SQ   SEQUENCE   768 AA;  88948 MW;  841E20407BD076A3 CRC64;
     MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
     AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
     DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
     GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
     INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY
     KLFSRVPNGL KTMCECMSCY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF
     NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
     FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
     NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
     AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
     ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHIFT
     VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
     VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
//