Q9UJU6 · DBNL_HUMAN
- ProteinDrebrin-like protein
- GeneDBNL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 361-362 | Cleavage; by caspase-3 | ||||
Sequence: DH |
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
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDrebrin-like protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UJU6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 361 | Abolishes cleavage by caspase-3. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 502 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_0000079793 | 1-430 | UniProt | Drebrin-like protein | |||
Sequence: MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPSTPPCLVQAEEEAVYEEPPEQETFYEQPPLVQQQGAGSEHIDHHIQGQGLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 26 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 137 | UniProt | In isoform Q9UJU6-4; Phosphoserine | ||||
Sequence: G | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 176 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 183 | UniProt | In isoform Q9UJU6-6; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | In isoform Q9UJU6-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | In isoform Q9UJU6-3; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 269 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 272 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 275 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 283 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 288 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 291 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 334 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 344 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Interacts with MAP4K1 and PRAM1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UJU6 | ACD Q96AP0 | 2 | EBI-751783, EBI-717666 | |
BINARY | Q9UJU6 | BAG6 P46379-2 | 3 | EBI-751783, EBI-10988864 | |
BINARY | Q9UJU6 | DNALI1 O14645 | 3 | EBI-751783, EBI-395638 | |
BINARY | Q9UJU6 | FGFR3 P22607 | 3 | EBI-751783, EBI-348399 | |
BINARY | Q9UJU6 | GRIN2C Q14957 | 3 | EBI-751783, EBI-8285963 | |
BINARY | Q9UJU6 | GSN P06396 | 3 | EBI-751783, EBI-351506 | |
BINARY | Q9UJU6 | HTT P42858 | 3 | EBI-751783, EBI-466029 | |
BINARY | Q9UJU6 | KLF11 O14901 | 3 | EBI-751783, EBI-948266 | |
BINARY | Q9UJU6 | SH2D4A Q9H788 | 6 | EBI-751783, EBI-747035 | |
BINARY | Q9UJU6 | SH2D4A Q9H788-2 | 3 | EBI-751783, EBI-10308083 | |
BINARY | Q9UJU6 | SH3BP2 P78314 | 7 | EBI-751783, EBI-727062 | |
BINARY | Q9UJU6 | UBQLN1 Q9UMX0 | 3 | EBI-751783, EBI-741480 | |
BINARY | Q9UJU6-2 | SH2D4A Q9H788 | 3 | EBI-12192777, EBI-747035 | |
BINARY | Q9UJU6-2 | SH3BP2 P78314-3 | 3 | EBI-12192777, EBI-12304031 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-133 | ADF-H | ||||
Sequence: NLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVA | ||||||
Coiled coil | 176-231 | |||||
Sequence: KDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEA | ||||||
Region | 219-283 | Disordered | ||||
Sequence: RREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRS | ||||||
Compositional bias | 227-248 | Polar residues | ||||
Sequence: QGGEASPQRTWEQQQEVVSRNR | ||||||
Compositional bias | 249-265 | Basic and acidic residues | ||||
Sequence: NEQESAVHPREIFKQKE | ||||||
Compositional bias | 266-283 | Polar residues | ||||
Sequence: RAMSTTSISSPQPGKLRS | ||||||
Domain | 371-430 | SH3 | ||||
Sequence: GQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q9UJU6-1
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
- Length430
- Mass (Da)48,207
- Last updated2000-05-01 v1
- Checksum7E8C42ED047257AE
Q9UJU6-2
- Name2
- Differences from canonical
- 234-234: Q → QS
Q9UJU6-3
- Name3
Q9UJU6-4
- Name4
Q9UJU6-5
- Name5
- Differences from canonical
- 1-103: Missing
Q9UJU6-6
- Name6
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054780 | 1-103 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_054779 | 1-109 | in isoform 4 | |||
Sequence: MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLK → MKATAMTSAWLAQG | ||||||
Sequence conflict | 8 | in Ref. 4; AAG17262 | ||||
Sequence: N → K | ||||||
Sequence conflict | 98 | in Ref. 3; AAF81273/AAG13120 | ||||
Sequence: A → S | ||||||
Alternative sequence | VSP_057346 | 110-158 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 227-248 | Polar residues | ||||
Sequence: QGGEASPQRTWEQQQEVVSRNR | ||||||
Alternative sequence | VSP_011398 | 234 | in isoform 2, isoform 3, isoform 4 and isoform 6 | |||
Sequence: Q → QS | ||||||
Sequence conflict | 235 | in Ref. 3; AAF81273/AAG13120 | ||||
Sequence: R → S | ||||||
Compositional bias | 249-265 | Basic and acidic residues | ||||
Sequence: NEQESAVHPREIFKQKE | ||||||
Alternative sequence | VSP_011399 | 251 | in isoform 3 | |||
Sequence: Q → QGSTCASLQ | ||||||
Compositional bias | 266-283 | Polar residues | ||||
Sequence: RAMSTTSISSPQPGKLRS | ||||||
Sequence conflict | 430 | in Ref. 6; CAG33448 | ||||
Sequence: E → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF197060 EMBL· GenBank· DDBJ | AAF13701.1 EMBL· GenBank· DDBJ | mRNA | ||
AF077353 EMBL· GenBank· DDBJ | AAF80228.1 EMBL· GenBank· DDBJ | mRNA | ||
AF250287 EMBL· GenBank· DDBJ | AAF81273.1 EMBL· GenBank· DDBJ | mRNA | ||
AF151364 EMBL· GenBank· DDBJ | AAG13120.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218020 EMBL· GenBank· DDBJ | AAG17262.2 EMBL· GenBank· DDBJ | mRNA | ||
AK027367 EMBL· GenBank· DDBJ | BAB55065.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293279 EMBL· GenBank· DDBJ | BAG56807.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293698 EMBL· GenBank· DDBJ | BAG57133.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457167 EMBL· GenBank· DDBJ | CAG33448.1 EMBL· GenBank· DDBJ | mRNA | ||
AC017116 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236960 EMBL· GenBank· DDBJ | EAL23770.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471128 EMBL· GenBank· DDBJ | EAW61132.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011677 EMBL· GenBank· DDBJ | AAH11677.1 EMBL· GenBank· DDBJ | mRNA | ||
BC031687 EMBL· GenBank· DDBJ | AAH31687.1 EMBL· GenBank· DDBJ | mRNA |