Q58WW2 · DCAF6_HUMAN
- ProteinDDB1- and CUL4-associated factor 6
- GeneDCAF6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids860 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ligand-dependent coactivator of nuclear receptors. Enhance transcriptional activity of the nuclear receptors NR3C1 and AR. May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | nuclear receptor coactivator activity | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | protein ubiquitination |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDDB1- and CUL4-associated factor 6
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ58WW2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035020 | 547 | in dbSNP:rs11558511 | |||
Sequence: V → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 935 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000304401 | 1-860 | UniProt | DDB1- and CUL4-associated factor 6 | |||
Sequence: MSRGGSYPHLLWDVRKRSLGLEDPSRLRSRYLGRREFIQRLKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRSGHRANIFSAKFLPCTNDKQIVSCSGDGVIFYTNVEQDAETNRQCQFTCHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTKEDCKDDILINCRRAATSVAICPPIPYYLAVGCSDSSVRIYDRRMLGTRATGNYAGRGTTGMVARFIPSHLNNKSCRVTSLCYSEDGQEILVSYSSDYIYLFDPKDDTARELKTPSAEERREELRQPPVKRLRLRGDWSDTGPRARPESERERDGEQSPNVSLMQRMSDMLSRWFEEASEVAQSNRGRGRSRPRGGTSQSDISTLPTVPSSPDLEVSETAMEVDTPAEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHHTHHQSDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVLIPGARYRAGPGDRRSAVARIQEFFRRRKERKEMEELDTLNIRRPLVKMVYKGHRNSRTMIKEANFWGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSPLEESRIFNRKLADEVITRNELMLEETRNTITVPASFMLRMLASLNHIRADRLEGDRSEGSGQENENEDEE | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 467 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 649 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 654 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 654 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 657 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 657 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 847 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 847 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 850 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 850 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in skeletal muscle and testis. Expressed to a lesser degree in heart, prostate, and adrenal gland.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the nuclear receptors NR3C1 and AR in the presence of ligand. Interacts with DDB1, CUL4A and CUL4B.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q58WW2 | BMP15 O95972 | 2 | EBI-2559044, EBI-12594867 | |
BINARY | Q58WW2 | DDB1 Q16531 | 2 | EBI-2559044, EBI-350322 | |
BINARY | Q58WW2 | GTF2IRD1 Q9UHL9 | 2 | EBI-2559044, EBI-372530 | |
BINARY | Q58WW2 | MDFI Q99750 | 3 | EBI-2559044, EBI-724076 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 49-88 | WD 1 | ||||
Sequence: VHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTT | ||||||
Repeat | 92-133 | WD 2 | ||||
Sequence: GHRANIFSAKFLPCTNDKQIVSCSGDGVIFYTNVEQDAETNR | ||||||
Repeat | 139-179 | WD 3 | ||||
Sequence: CHYGTTYEIMTVPNDPYTFLSCGEDGTVRWFDTRIKTSCTK | ||||||
Repeat | 189-229 | WD 4 | ||||
Sequence: NCRRAATSVAICPPIPYYLAVGCSDSSVRIYDRRMLGTRAT | ||||||
Repeat | 251-290 | WD 5 | ||||
Sequence: NKSCRVTSLCYSEDGQEILVSYSSDYIYLFDPKDDTAREL | ||||||
Compositional bias | 288-335 | Basic and acidic residues | ||||
Sequence: RELKTPSAEERREELRQPPVKRLRLRGDWSDTGPRARPESERERDGEQ | ||||||
Region | 288-340 | Disordered | ||||
Sequence: RELKTPSAEERREELRQPPVKRLRLRGDWSDTGPRARPESERERDGEQSPNVS | ||||||
Region | 355-392 | Disordered | ||||
Sequence: EASEVAQSNRGRGRSRPRGGTSQSDISTLPTVPSSPDL | ||||||
Compositional bias | 362-392 | Polar residues | ||||
Sequence: SNRGRGRSRPRGGTSQSDISTLPTVPSSPDL | ||||||
Compositional bias | 407-446 | Polar residues | ||||
Sequence: QFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQ | ||||||
Region | 407-490 | Disordered | ||||
Sequence: QFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHHTHHQSDNNNEKLSPKPGTGEPVLSLHYSTEGTTTST | ||||||
Compositional bias | 447-463 | Basic and acidic residues | ||||
Sequence: SVEASGHHTHHQSDNNN | ||||||
Compositional bias | 502-533 | Polar residues | ||||
Sequence: IASSSRGIGSHCKSEGQEESFVPQSSVQPPEG | ||||||
Region | 502-675 | Disordered | ||||
Sequence: IASSSRGIGSHCKSEGQEESFVPQSSVQPPEGDSETKAPEESSEDVTKYQEGVSAENPVENHINITQSDKFTAKPLDSNSGERNDLNLDRSCGVPEESASSEKAKEPETSDQTSTESATNENNTNPEPQFQTEATGPSAHEETSTRDSALQDTDDSDDDPVLIPGARYRAGPGD | ||||||
Compositional bias | 558-587 | Polar residues | ||||
Sequence: NPVENHINITQSDKFTAKPLDSNSGERNDL | ||||||
Compositional bias | 612-645 | Polar residues | ||||
Sequence: DQTSTESATNENNTNPEPQFQTEATGPSAHEETS | ||||||
Domain | 676-705 | IQ | ||||
Sequence: RRSAVARIQEFFRRRKERKEMEELDTLNIR | ||||||
Repeat | 718-756 | WD 6 | ||||
Sequence: NSRTMIKEANFWGANFVMSGSDCGHIFIWDRHTAEHLML | ||||||
Repeat | 759-798 | WD 7 | ||||
Sequence: ADNHVVNCLQPHPFDPILASSGIDYDIKIWSPLEESRIFN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q58WW2-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length860
- Mass (Da)96,292
- Last updated2005-04-26 v1
- Checksum8C7602D635DAF124
Q58WW2-2
- Name2
- Differences from canonical
- 459-459: S → SDSPSSVVNKQLGSMSLDEQQ
Q58WW2-3
- Name3
Q58WW2-4
- Name4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F2Z305 | F2Z305_HUMAN | DCAF6 | 472 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043312 | 54-84 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 288-335 | Basic and acidic residues | ||||
Sequence: RELKTPSAEERREELRQPPVKRLRLRGDWSDTGPRARPESERERDGEQ | ||||||
Compositional bias | 362-392 | Polar residues | ||||
Sequence: SNRGRGRSRPRGGTSQSDISTLPTVPSSPDL | ||||||
Compositional bias | 407-446 | Polar residues | ||||
Sequence: QFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQ | ||||||
Compositional bias | 447-463 | Basic and acidic residues | ||||
Sequence: SVEASGHHTHHQSDNNN | ||||||
Alternative sequence | VSP_028019 | 459 | in isoform 2 | |||
Sequence: S → SDSPSSVVNKQLGSMSLDEQQ | ||||||
Alternative sequence | VSP_028020 | 459 | in isoform 3 and isoform 4 | |||
Sequence: S → SEFLRGPEIALLRKRLQQLRLKKAEQQRQQELAAHTQQQPSTSDQSSHEGSSQDPHASDSPSSVVNKQLGSMSLDEQQ | ||||||
Compositional bias | 502-533 | Polar residues | ||||
Sequence: IASSSRGIGSHCKSEGQEESFVPQSSVQPPEG | ||||||
Compositional bias | 558-587 | Polar residues | ||||
Sequence: NPVENHINITQSDKFTAKPLDSNSGERNDL | ||||||
Compositional bias | 612-645 | Polar residues | ||||
Sequence: DQTSTESATNENNTNPEPQFQTEATGPSAHEETS | ||||||
Alternative sequence | VSP_028021 | 675 | in isoform 3 and isoform 4 | |||
Sequence: D → DRFNIRGTTIGDRIM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY766164 EMBL· GenBank· DDBJ | AAX09330.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ768089 EMBL· GenBank· DDBJ | ABG76793.1 EMBL· GenBank· DDBJ | mRNA | ||
AF116725 EMBL· GenBank· DDBJ | AAO15301.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297847 EMBL· GenBank· DDBJ | BAG60180.1 EMBL· GenBank· DDBJ | mRNA | ||
Z97876 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL033531 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL031287 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL033532 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471067 EMBL· GenBank· DDBJ | EAW90809.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC025262 EMBL· GenBank· DDBJ | AAH25262.2 EMBL· GenBank· DDBJ | mRNA | ||
AL136738 EMBL· GenBank· DDBJ | CAB66672.2 EMBL· GenBank· DDBJ | mRNA |