Cullin-3 - Mus musculus (Mouse)

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Q9JLV5 (CUL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cullin-3
Short name=CUL-3

Gene names

Name:

Cul3

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 › Mus

Protein attributes

Sequence length	768 AA.
Sequence status	Complete.
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	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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Golgi apparatus Nucleus
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from direct assay. Source: MGI cell migration Inferred from sequence or structural similarity. Source: UniProtKB cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB gastrulation Inferred from mutant phenotype Ref.3. Source: MGI mitotic anaphase Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of Rho protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB stress fiber assembly Inferred from sequence or structural similarity. Source: UniProtKB trophectodermal cellular morphogenesis Inferred from mutant phenotype Ref.3. Source: MGI
Cellular component	Cul3-RING ubiquitin ligase complex Inferred from sequence or structural similarity. Source: UniProtKB Golgi apparatus Inferred from direct assay Ref.3. Source: MGI nucleus Inferred from direct assay Ref.3. Source: MGI polar microtubule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	cyclin binding Inferred from physical interaction Ref.3. Source: MGI ubiquitin protein ligase binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 768

768

Cullin-3

PRO_0000119794

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

450

Phosphoserine Ref.4

Modified residue

737

Phosphoserine By similarity

Cross-link

712

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Secondary structure

768

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JLV5 [UniParc].

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

FASTA

768

88,948

        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' referencesShow '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.

IPI

IPI00467383.

RefSeq

NP_057925.1. NM_016716.4.

UniGene

Mm.12665.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IUY	NMR	-	A	678-768	[»]

ProteinModelPortal

Q9JLV5.

SMR

Q9JLV5. Positions 11-768.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9JLV5. 4 interactions.

STRING

Q9JLV5.

PTM databases

PhosphoSite

Q9JLV5.

Proteomic databases

PRIDE

Q9JLV5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000163119; ENSMUSP00000130738; ENSMUSG00000004364.

GeneID

26554.

KEGG

mmu:26554.

Organism-specific databases

CTD

8452.

MGI

MGI:1347360. Cul3.

Phylogenomic databases

GeneTree

ENSGT00550000074299.

HOVERGEN

HBG003619.

InParanoid

Q9JLV5.

OMA

AKLKTEC.

OrthoDB

EOG4JWVCW.

PhylomeDB

Q9JLV5.

Gene expression databases

ArrayExpress

Q9JLV5.

Bgee

Q9JLV5.

CleanEx

MM_CUL3.

Genevestigator

Q9JLV5.

GermOnline

ENSMUSG00000004364. Mus musculus.

Family and domain databases

InterPro

IPR016157. 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]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.

K03869.

Pfam

PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]

SMART

SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]

SUPFAM

SSF75632. Cullin_homology. 1 hit.
SSF74788. Cullin_repeat-like. 1 hit.

PROSITE

PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

304599.

SOURCE

Search...

Entry information

Entry name

CUL3_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents