Q7L591 · DOK3_HUMAN
- ProteinDocking protein 3
- GeneDOK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids496 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity).
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 | cytoplasm | |
Cellular Component | ficolin-1-rich granule membrane | |
Cellular Component | plasma membrane | |
Cellular Component | secretory granule membrane | |
Biological Process | cell surface receptor protein tyrosine kinase signaling pathway | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | Ras protein signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDocking protein 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7L591
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057525 | 12 | in dbSNP:rs3749728 | |||
Sequence: R → P | ||||||
Natural variant | VAR_062002 | 22 | in dbSNP:rs41275297 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000187272 | 1-496 | UniProt | Docking protein 3 | |||
Sequence: MTRGARLRSDARAQLNQLSLDGGTGSGQKGKCEEFPSSLSSVSPGLEAAALLLAVTMDPLETPIKDGILYQQHVKFGKKCWRKVWALLYAGGPSGVARLESWEVRDGGLGAAGDRSAGPGRRGERRVIRLADCVSVLPADGESCPRDTGAFLLTTTERSHLLAAQHRQAWMGPICQLAFPGTGEASSGSTDAQSPKRGLVPMEENSIYSSWQEVGEFPVVVQRTEAATRCQLKGPALLVLGPDAIQLREAKGTQALYSWPYHFLRKFGSDKGVFSFEAGRRCHSGEGLFAFSTPCAPDLCRAVAGAIARQRERLPELTRPQPCPLPRATSLPSLDTPGELREMPPGPEPPTSRKMHLAEPGPQSLPLLLGPEPNDLASGLYASVCKRASGPPGNEHLYENLCVLEASPTLHGGEPEPHEGPGSRSPTTSPIYHNGQDLSWPGPANDSTLEAQYRRLLELDQVEGTGRPDPQAGFKAKLVTLLSRERRKGPAPCDRP | |||||||
Modified residue | 194 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 330 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 364 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 381 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 398 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 407 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 425 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 425 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Constitutively tyrosine-phosphorylated.
On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL1 kinase (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in spleen.
Gene expression databases
Organism-specific databases
Interaction
Subunit
On tyrosine phosphorylation, interacts with CSK and INPP5D/SHIP1 via their SH2 domains. Both Tyr-381 and Tyr-398 are required for interaction with INPP5D. Only Tyr-381 is required for interaction with CSK. Binds ABL1 through the PTB domain and in a kinase-dependent manner. Does not interact with RasGAP (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-38 | Disordered | ||||
Sequence: LSLDGGTGSGQKGKCEEFPSS | ||||||
Domain | 63-179 | PH | ||||
Sequence: PIKDGILYQQHVKFGKKCWRKVWALLYAGGPSGVARLESWEVRDGGLGAAGDRSAGPGRRGERRVIRLADCVSVLPADGESCPRDTGAFLLTTTERSHLLAAQHRQAWMGPICQLAF | ||||||
Domain | 213-317 | IRS-type PTB | ||||
Sequence: EVGEFPVVVQRTEAATRCQLKGPALLVLGPDAIQLREAKGTQALYSWPYHFLRKFGSDKGVFSFEAGRRCHSGEGLFAFSTPCAPDLCRAVAGAIARQRERLPEL | ||||||
Region | 313-363 | Disordered | ||||
Sequence: RLPELTRPQPCPLPRATSLPSLDTPGELREMPPGPEPPTSRKMHLAEPGPQ | ||||||
Region | 408-447 | Disordered | ||||
Sequence: PTLHGGEPEPHEGPGSRSPTTSPIYHNGQDLSWPGPANDS | ||||||
Compositional bias | 422-446 | Polar residues | ||||
Sequence: GSRSPTTSPIYHNGQDLSWPGPAND |
Domain
PTB domain mediates receptor interaction.
Sequence similarities
Belongs to the DOK family. Type A subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q7L591-1
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
- Length496
- Mass (Da)53,288
- Last updated2005-05-10 v2
- Checksum7E186B998F9F1E24
Q7L591-2
- Name2
Q7L591-3
- Name3
Q7L591-4
- Name4
- Differences from canonical
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013712 | 1-56 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013713 | 1-170 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013714 | 79-180 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 188 | In isoform Q7L591-2; in Ref. 2; AAH04867 | ||||
Sequence: R → C | ||||||
Sequence conflict | 200 | In isoform Q7L591-4; in Ref. 1; BAC04986 | ||||
Sequence: R → C | ||||||
Sequence conflict | 267 | in Ref. 1; BAB15399 | ||||
Sequence: F → L | ||||||
Alternative sequence | VSP_013715 | 272-386 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: GVFSFEAGRRCHSGEGLFAFSTPCAPDLCRAVAGAIARQRERLPELTRPQPCPLPRATSLPSLDTPGELREMPPGPEPPTSRKMHLAEPGPQSLPLLLGPEPNDLASGLYASVCK → ILLGTPGVSLLICKGERTDDVSGIILDESLLRAYSVPGAGGHSRVQDSLGPVLREPTFQGERSFLKTSMLRSLLCSCSWRHPRSQPRTQASCLQGSDCPAPHRNSTSAAHTLGTS | ||||||
Sequence conflict | 302 | In isoform Q7L591-3; in Ref. 3; AAH04564 | ||||
Sequence: R → C | ||||||
Alternative sequence | VSP_013716 | 387-496 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 422-446 | Polar residues | ||||
Sequence: GSRSPTTSPIYHNGQDLSWPGPAND |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK026223 EMBL· GenBank· DDBJ | BAB15399.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097258 EMBL· GenBank· DDBJ | BAC04986.1 EMBL· GenBank· DDBJ | mRNA | ||
AC145098 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC004564 EMBL· GenBank· DDBJ | AAH04564.2 EMBL· GenBank· DDBJ | mRNA | ||
BC004867 EMBL· GenBank· DDBJ | AAH04867.1 EMBL· GenBank· DDBJ | mRNA |