Reviewed, UniProtKB/Swiss-Prot Q9JLV5 (CUL3_MOUSE)

Names and origin

Protein names

Recommended name:
    Cullin-3
      Short name(s)=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

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	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 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.
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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

768

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Q9JLV5-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 841E20407BD076A3	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

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.
[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

EMBLGenBankDDBJ

AF129738 mRNA. Translation: AAF36500.1.
BC027304 mRNA. Translation: AAH27304.1.

RefSeq

NP_057925.1.

UniGene

Mm.12665

3D structure databases

PDBMSD

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

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

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ProtoNet

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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:	July 22, 2008
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)