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Q9JLV5 (CUL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-3

Short name=CUL-3
Gene names
Name:Cul3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

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 KCTD5, KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20, C16orf44, GMCL1P1, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the interaction regulates surface GRIK2 expression By similarity. Ref.3

Subcellular location

Nucleus. Golgi apparatus Ref.3.

Tissue specificity

Widely expressed, with highest expression in brain, spleen and testis. Ref.3

Post-translational modification

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.

Sequence similarities

Belongs to the cullin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Cullin-3
PRO_0000119794

Amino acid modifications

Modified residue581Phosphotyrosine By similarity
Modified residue4501Phosphoserine Ref.4
Modified residue7371Phosphoserine By similarity
Cross-link712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Secondary structure

............. 768
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9JLV5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 841E20407BD076A3

FASTA76888,948
        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 

« Hide

References

« Hide 'large scale' references
[1]Levy N., Agulnik A.I., Boettger-Tong H., Bishop C.E.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[3]"Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cells."
Singer J.D., Gurian-West M., Clurman B., Roberts J.M.
Genes Dev. 13:2375-2387(1999) [PubMed: 10500095] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CYCE, TISSUE SPECIFICITY.
[4]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[5]"Solution structure of the cullin-3 homologue."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2003) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 678-768.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129738 mRNA. Translation: AAF36500.1.
BC027304 mRNA. Translation: AAH27304.1.
IPIIPI00467383.
RefSeqNP_057925.1. NM_016716.4.
UniGeneMm.12665.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IUYNMR-A678-768[»]
ProteinModelPortalQ9JLV5.
SMRQ9JLV5. Positions 11-768.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9JLV5. 4 interactions.
STRINGQ9JLV5.

PTM databases

PhosphoSiteQ9JLV5.

Proteomic databases

PRIDEQ9JLV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163119; ENSMUSP00000130738; ENSMUSG00000004364.
GeneID26554.
KEGGmmu:26554.

Organism-specific databases

CTD8452.
MGIMGI:1347360. Cul3.

Phylogenomic databases

GeneTreeENSGT00550000074299.
HOVERGENHBG003619.
InParanoidQ9JLV5.
OMAAKLKTEC.
OrthoDBEOG4JWVCW.
PhylomeDBQ9JLV5.

Gene expression databases

ArrayExpressQ9JLV5.
BgeeQ9JLV5.
CleanExMM_CUL3.
GenevestigatorQ9JLV5.
GermOnlineENSMUSG00000004364. Mus musculus.

Family and domain databases

InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
KOK03869.
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF75632. Cullin_homology. 1 hit.
SSF74788. Cullin_repeat-like. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304599.
SOURCESearch...

Entry information

Entry nameCUL3_MOUSE
AccessionPrimary (citable) accession number: Q9JLV5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families