Tag Content
SG ID
SG00000355 
UniProt Accession
Theoretical PI
9.15  
Molecular Weight
106858 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Cul-3 
Gene Synonyms/Alias
cul-3, Cul-3-RF 
Protein Name
 
Protein Synonyms/Alias
SubName: Cullin 3, isoform FEC=6.3.2.19SubName: FI19425p1 
Organism
Drosophila melanogaster (Fruit fly) 
NCBI Taxonomy ID
7227 
Chromosome Location
chr:2L;15266029-15272011;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. 

Abstract
In both insects and mammals, spermatids eliminate their bulk cytoplasm as they undergo terminal differentiation. In Drosophila, this process of dramatic cellular remodeling requires apoptotic proteins, including caspases. To gain further insight into the regulation of caspases, we screened a large collection of sterile male flies for mutants that block effector caspase activation at the onset of spermatid individualization. Here, we describe the identification and characterization of a testis-specific, Cullin-3-dependent ubiquitin ligase complex that is required for caspase activation in spermatids. Mutations in either a testis-specific isoform of Cullin-3 (Cul3(Testis)), the small RING protein Roc1b, or a Drosophila orthologue of the mammalian BTB-Kelch protein Klhl10 all reduce or eliminate effector caspase activation in spermatids. Importantly, all three genes encode proteins that can physically interact to form a ubiquitin ligase complex. Roc1b binds to the catalytic core of Cullin-3, and Klhl10 binds specifically to a unique testis-specific N-terminal Cullin-3 (TeNC) domain of Cul3(Testis) that is required for activation of effector caspase in spermatids. Finally, the BIR domain region of the giant inhibitor of apoptosis-like protein dBruce is sufficient to bind to Klhl10, which is consistent with the idea that dBruce is a substrate for the Cullin-3-based E3-ligase complex. These findings reveal a novel role of Cullin-based ubiquitin ligases in caspase regulation. PMID: [17880263] 

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Figures for illustrating the function of this protein/gene
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Ref: E. Arama, M. Bader, G. E. Rieckhof and H. Steller (2007) A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 5(10): e251. PMID: [17880263]
Function
 
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Subcellular Location
 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0031463 C:Cul3-RING ubiquitin ligase complex IPI:FlyBase.
GO:0019005 C:SCF ubiquitin ligase complex NAS:FlyBase.
GO:0004842 F:ubiquitin-protein ligase activity NAS:FlyBase.
GO:0006919 P:activation of cysteine-type endopeptidase activity involved in apoptotic process IMP:FlyBase.
GO:0007409 P:axonogenesis IMP:FlyBase.
GO:0001745 P:compound eye morphogenesis NAS:FlyBase.
GO:0048813 P:dendrite morphogenesis IMP:FlyBase.
GO:0007476 P:imaginal disc-derived wing morphogenesis IMP:FlyBase.
GO:0030162 P:regulation of proteolysis NAS:FlyBase.
GO:0030431 P:sleep IMP:FlyBase.
GO:0007291 P:sperm individualization IMP:FlyBase.
GO:0006511 P:ubiquitin-dependent protein catabolic process IEA:InterPro.
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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.
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Pfam
PF00888;    Cullin;    1.
PF10557;    Cullin_Nedd8;    1.
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SMART
SM00182;    CULLIN;    1.
SM00884;    Cullin_Nedd8;    1.
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PROSITE
PS01256;    CULLIN_1;    1.
PS50069;    CULLIN_2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
Nucleotide Sequence
Length: bp   Go to nucleotide: FASTA
Protein Sequence
Length: 934 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data
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