Q9BW61 · DDA1_HUMAN
- ProteinDET1- and DDB1-associated protein 1
- GeneDDA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids102 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:17452440, PubMed:28302793, PubMed:28437394, PubMed:31686031, PubMed:31819272).
In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex (PubMed:31686031, PubMed:31819272).
In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex (PubMed:31686031, PubMed:31819272).
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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Aspect | Term | |
---|---|---|
Cellular Component | Cul4-RING E3 ubiquitin ligase complex | |
Cellular Component | nucleoplasm | |
Biological Process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | protein polyubiquitination |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDET1- and DDB1-associated protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BW61
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 98 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000310270 | 2-102 | UniProt | DET1- and DDB1-associated protein 1 | |||
Sequence: ADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYLPTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVELEGESSAPPRKVARTDSPDMHEDT | |||||||
Modified residue | 33 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 95 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and RBX1 (PubMed:28302793, PubMed:28437394, PubMed:31686031, PubMed:31693891, PubMed:31693911, PubMed:31819272).
Component of the DCX(DCAF15) complex, also named CLR4(DCAF15) complex, composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and RBX1 (PubMed:28302793, PubMed:28437394, PubMed:31686031, PubMed:31693891, PubMed:31693911, PubMed:31819272).
Part of the DDD core complex containing DET1, DDA1 and DDB1; the DDD core complex recruits a specific UBE2E enzyme, such as UBE2E1, UBE2E2 UBE2E3, to form specific DDD-E2 complexes (PubMed:17452440).
Component of the DCX(DCAF15) complex, also named CLR4(DCAF15) complex, composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and RBX1 (PubMed:28302793, PubMed:28437394, PubMed:31686031, PubMed:31693891, PubMed:31693911, PubMed:31819272).
Part of the DDD core complex containing DET1, DDA1 and DDB1; the DDD core complex recruits a specific UBE2E enzyme, such as UBE2E1, UBE2E2 UBE2E3, to form specific DDD-E2 complexes (PubMed:17452440).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BW61 | AGTRAP Q6RW13 | 3 | EBI-2510241, EBI-741181 | |
BINARY | Q9BW61 | CMTM5 Q96DZ9 | 3 | EBI-2510241, EBI-2548702 | |
BINARY | Q9BW61 | CMTM5 Q96DZ9-2 | 3 | EBI-2510241, EBI-11522780 | |
BINARY | Q9BW61 | DDB1 Q16531 | 5 | EBI-2510241, EBI-350322 | |
BINARY | Q9BW61 | PKNOX2 Q96KN3 | 5 | EBI-2510241, EBI-2692890 | |
BINARY | Q9BW61 | PRKN O60260-5 | 3 | EBI-2510241, EBI-21251460 | |
BINARY | Q9BW61 | RDH10 Q8IZV5 | 3 | EBI-2510241, EBI-11913715 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 66-102 | Disordered | ||||
Sequence: KNAAKKRDQEQVELEGESSAPPRKVARTDSPDMHEDT |
Sequence similarities
Belongs to the DDA1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length102
- Mass (Da)11,835
- Last updated2001-06-01 v1
- Checksum94E43C3528589F01
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ090952 EMBL· GenBank· DDBJ | AAZ41375.1 EMBL· GenBank· DDBJ | mRNA | ||
AY563006 EMBL· GenBank· DDBJ | AAS66629.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471106 EMBL· GenBank· DDBJ | EAW84593.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000615 EMBL· GenBank· DDBJ | AAH00615.1 EMBL· GenBank· DDBJ | mRNA |