Reviewed,
UniProtKB/Swiss-Prot Q9JLV5 (CUL3_MOUSE)
Last modified
July 22, 2008.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cullin-3 Short name(s)=CUL-3 | ||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 768 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| 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 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 | |
| Tissue specificity | Widely expressed, with highest expression in brain, spleen and testis. |
| 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. |
Ontologies
Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Golgi apparatus Nucleus |
| PTM | Phosphoprotein Ubl conjugation |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| None. [Check GOA] | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||||||||||||||
Molecule processing | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 768 | 768 | Cullin-3 | |||||||||||||||||
Amino acid modifications | ||||||||||||||||||||
| Modified residue | 58 | 1 | Phosphotyrosine By similarity | |||||||||||||||||
| Modified residue | 450 | 1 | Phosphoserine | |||||||||||||||||
| Modified residue | 737 | 1 | Phosphoserine By similarity | |||||||||||||||||
| Cross-link | 712 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity | ||||||||||||||||||
Secondary structure | ||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||
| Turn | 699 – 701 | 3 | ||||||||||||||||||
| Helix | 702 – 714 | 13 | ||||||||||||||||||
| Beta strand | 716 – 718 | 3 | ||||||||||||||||||
| Helix | 719 – 729 | 11 | ||||||||||||||||||
| Helix | 738 – 750 | 13 | ||||||||||||||||||
| Beta strand | 753 – 756 | 4 | ||||||||||||||||||
| Beta strand | 761 – 766 | 6 | ||||||||||||||||||
Sequences
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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. |
| [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. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF129738 mRNA. Translation: AAF36500.1. BC027304 mRNA. Translation: AAH27304.1. | |||||||||||||
| RefSeq | NP_057925.1. | ||||||||||||
| UniGene | Mm.12665 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9JLV5. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSMUSG00000004364. Mus musculus. [Contig view] | ||||||||||||
| GeneID | 26554. | ||||||||||||
| KEGG | mmu:26554. | ||||||||||||
Organism-specific databases | |||||||||||||
| MGI | MGI:1347360. Cul3. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | Q9JLV5. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9JLV5. | ||||||||||||
| CleanEx | MM_CUL3. | ||||||||||||
| GermOnline | ENSMUSG00000004364. Mus musculus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR016157. Cullin_CS. IPR016158. Cullin_homology. IPR001373. Cullin_N. IPR011991. Wing_hlx_DNA_bd. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits. | ||||||||||||
| Pfam | PF00888. Cullin. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00182. CULLIN. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS01256. CULLIN_1. 1 hit. PS50069. CULLIN_2. 1 hit. [Graphical view] | ||||||||||||
| ProDom | Q9JLV5. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| BLOCKS | Search... | ||||||||||||
Other Resources | |||||||||||||
| SOURCE | Search... | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CUL3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9JLV5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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 |

Clusters with


