Q24311 · CUL1_DROME
- ProteinCullin homolog 1
- GeneCul1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids774 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Core component of multiple SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. During early metamorphosis, part of the SCF-slmb complex that negatively regulates the InR/PI3K/TOR pathway to activate the pruning of unnecessary larval ddaC dendrites and mushroom body axons (PubMed:24068890).
The SCF-slmb complex also regulates asymmetrical division of neuroblasts and inhibits ectopic neuroblast formation partly through SAK and Akt1 (PubMed:24413555).
Also part of an SCF complex required for caspase activation during sperm differentiation (PubMed:20392747).
Necessary for auditory transduction: plays a role in Johnston's organ organization by acting in the regulation of zip and ck function in scolopidial apical attachment (PubMed:27331610).
May function by acting in a Ubr3-mediated pathway that negatively regulates the ubiquitination of zip, consequently affecting its interaction with ck (PubMed:27331610).
The SCF-slmb complex also regulates asymmetrical division of neuroblasts and inhibits ectopic neuroblast formation partly through SAK and Akt1 (PubMed:24413555).
Also part of an SCF complex required for caspase activation during sperm differentiation (PubMed:20392747).
Necessary for auditory transduction: plays a role in Johnston's organ organization by acting in the regulation of zip and ck function in scolopidial apical attachment (PubMed:27331610).
May function by acting in a Ubr3-mediated pathway that negatively regulates the ubiquitination of zip, consequently affecting its interaction with ck (PubMed:27331610).
Pathway
Protein modification; protein ubiquitination.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCullin homolog 1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ24311
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In the spermatid, colocalizes with ntc at the actin-based individualization complex and the cystic bulge.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Severe dendrite pruning defects in ddaC neurons at 16 hours after puparium formation (APF) and axon pruning defects in mushroom body gamma neurons at 24 hours APF. RNAi-mediated knockdown results in a significant increase in Akt1 protein levels and activity in ddaC somas (PubMed:24068890).
In the larval brain there is a large increase in the number of neuroblasts, 40% of which show a spindle misorientation at metaphase (PubMed:24413555).
RNAi-mediated knockdown results in apical detachment of scolopidial cells in Johnston's organ (PubMed:27331610).
In the larval brain there is a large increase in the number of neuroblasts, 40% of which show a spindle misorientation at metaphase (PubMed:24413555).
RNAi-mediated knockdown results in apical detachment of scolopidial cells in Johnston's organ (PubMed:27331610).
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119786 | 1-774 | Cullin homolog 1 | |||
Sequence: MNRSGNSQTTQKLVNLDDIWSELVEGIMQVFEHEKSLTRSQYMRFYTHVYDYCTSVSAAPSGRSSGKTGGAQLVGKKLYDRLEQFLKSYLSELLTKFKAISGEEVLLSRYTKQWKSYQFSSTVLDGICNYLNRNWVKRECEEGQKGIYKIYRLALVAWKGHLFQVLNEPVTKAVLKSIEEERQGKLINRSLVRDVIECYVELSFNEEDTDAEQQKLSVYKQNFENKFIADTSAFYEKESDAFLSTNTVTEYLKHVENRLEEETQRVRGFNSKNGLSYLHETTADVLKSTCEEVLIEKHLKIFHTEFQNLLNADRNDDLKRMYSLVALSSKNLTDLKSILENHILHQGTEAIAKCCTTDAANDPKTYVQTILDVHKKYNALVLTAFNNDNGFVAALDKACGKFINSNVVTIANSASKSPELLAKYCDLLLKKSSKNPEDKELEDNLNQVMVVFKYIEDKDVFQKYYSKMLAKRLVNHTSASDDAEAMMISKLKQTCGYEYTVKLQRMFQDIGVSKDLNSYFKQYLAEKNLTMEIDFGIEVLSSGSWPFQLSNNFLLPSELERSVRQFNEFYAARHSGRKLNWLYQMCKGELIMNVNRNNSSTYTLQASTFQMSVLLQFNDQLSFTVQQLQDNTQTQQENLIQVLQILLKAKVLTSSDNENSLTPESTVELFLDYKNKKRRININQPLKTELKVEQETVHKHIEEDRKLLIQAAIVRIMKMRKRLNHTNLISEVLNQLSTRFKPKVPVIKKCIDILIEKEYLERMEGHKDTYSYLA | ||||||
Cross-link | 718 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) | ||||
Sequence: K |
Post-translational modification
Neddylated (PubMed:12183637, PubMed:18493598).
Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:12183637).
Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:12183637).
Keywords
- PTM
Proteomic databases
Expression
Interaction
Subunit
Component of SCF E3 ubiquitin-protein ligase complexes consisting of Skpa, Cul1, Roc1a and an F-box protein. In larval neuroblast self renewal and asymmetric division, as well as ddaC dendrite and mushroom body axon pruning, the complex contains the F-box protein slmb (SCF-slmb) (PubMed:24068890, PubMed:24413555).
In caspase activation during sperm differentiation, the complex contains the F-box protein ntc (PubMed:20392747).
Interacts directly with Roc1a (PubMed:11500045).
Interacts with Fsn (PubMed:20123973).
Interacts with Dlish (PubMed:27692068).
Interacts with Cad99C (via the cytoplasmic domain) (PubMed:27331610).
Interacts with Sans (PubMed:27331610).
In caspase activation during sperm differentiation, the complex contains the F-box protein ntc (PubMed:20392747).
Interacts directly with Roc1a (PubMed:11500045).
Interacts with Fsn (PubMed:20123973).
Interacts with Dlish (PubMed:27692068).
Interacts with Cad99C (via the cytoplasmic domain) (PubMed:27331610).
Interacts with Sans (PubMed:27331610).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q24311 | Rca1 P91666 | 2 | EBI-136038, EBI-7085629 | |
BINARY | Q24311 | SkpA O77430 | 2 | EBI-136038, EBI-180180 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length774
- Mass (Da)89,511
- Last updated2001-11-02 v2
- Checksum1AF0D035DE85363C
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 266 | in Ref. 1; AAA85085 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L41642 EMBL· GenBank· DDBJ | AAA85085.1 EMBL· GenBank· DDBJ | mRNA | ||
AF136343 EMBL· GenBank· DDBJ | AAD33676.1 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF59174.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT010290 EMBL· GenBank· DDBJ | AAQ23608.1 EMBL· GenBank· DDBJ | mRNA |