SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00000309 
UniProt Accession
Theoretical PI
4.8  
Molecular Weight
14225 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Roc1b 
Gene Synonyms/Alias
ROC2 
Protein Name
RING-box protein 1B 
Protein Synonyms/Alias
Regulator of cullins 1b; 
Organism
Drosophila melanogaster (Fruit fly) 
NCBI Taxonomy ID
7227 
Chromosome Location
chr:3L;357981-358486;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
Component of the SCF (SKP1-CUL1-F-box protein) E3ubiquitin ligase complex, which mediates the ubiquitination andsubsequent proteasomal degradation of target proteins. Through theRING-type zinc finger, seems to recruit the E2 ubiquitinationenzyme to the complex and brings it into close proximity to thesubstrate (By similarity). 
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Subcellular Location
Cytoplasm. Nucleus. 
Tissue Specificity
Highly expressed in early embryos, and inpupae. Widely expressed in adult males, while it is weaklyexpressed in adult females. 
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell.
GO:0005634 C:nucleus ISS:UniProtKB.
GO:0019005 C:SCF ubiquitin ligase complex ISS:UniProtKB.
GO:0004842 F:ubiquitin-protein ligase activity IDA:FlyBase.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0006919 P:activation of cysteine-type endopeptidase activity involved in apoptotic process IGI:FlyBase.
GO:0008283 P:cell proliferation ISS:UniProtKB.
GO:0019915 P:lipid storage IDA:FlyBase.
GO:0030317 P:sperm motility IMP:FlyBase.
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Interpro
IPR001841;    Znf_RING.
IPR013083;    Znf_RING/FYVE/PHD.
IPR024766;    Znf_RING_H2.
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Pfam
PF12678;    zf-rbx1;    1.
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SMART
SM00184;    RING;    1.
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PROSITE
PS50089;    ZF_RING_2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    122       RING-box protein 1B.
                             /FTId=PRO_0000056018.
ZN_FING      57    112       RING-type.
METAL        57     57       Zinc 1 (By similarity).
METAL        60     60       Zinc 1 (By similarity).
METAL        68     68       Zinc 3 (By similarity).
METAL        71     71       Zinc 3 (By similarity).
METAL        82     82       Zinc 3 (By similarity).
METAL        89     89       Zinc 2 (By similarity).
METAL        91     91       Zinc 2 (By similarity).
METAL        94     94       Zinc 1 (By similarity).
METAL        96     96       Zinc 3 (By similarity).
METAL        97     97       Zinc 1 (By similarity).
METAL       108    108       Zinc 2 (By similarity).
METAL       111    111       Zinc 2 (By similarity).
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Nucleotide Sequence
Length: 750 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 122 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Cul-3BioGRID 
Cul-3BioGRID 
CG7375BioGRID 
CG7375MINT 
Other Protein-Protein interaction resources
String database  
View Microarray data
Temporarily unavailable 
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