Dok3
entrez
27261
canonical
uniprot
Q9QZK7
canonical
ensembl
ENSMUSG00000035711
resolver
ensp
ENSMUSP00000046695
resolver
ensp
ENSMUSP00000153308
resolver
enst
ENSMUST00000047877
resolver
enst
ENSMUST00000223563
resolver
genesymbol
Dok3
resolver
genesymbol_syn
Dokl
resolver
uniprot
Q14AA1
resolver
uniprot_entry
DOK3_MOUSE
resolver
uniprot_entry
Q14AA1_MOUSE
resolver
amino_acid_sequence
MESVEPPVKDGILYQQHVKFGKKCWRKVWALLYAGGPSGVARLESWDVRDGGLGPAGDRSTGPSRRGERRVIRLADCVSVLPADGESCPRDTGAFLITTTERSHLLAAQHRQSWVDPICQLAFPGTGECSSGSGQAESPKRGFVPMEENSIYSSWQEVTEFPVIVQRTEATSRCQLKGPYLLVLGQDDIQLRETSKPQACFSWPYRFLRKYGSDKGVFSFEAGRRCDSGEGLFAFSSPRAPDICGVVAAAIARQRERLPELAMSPPCPLPRALSLPSLEPPGELREVAPGFELPTPRKLPLTDPGPQSLPLLLSPTQEGPASGLYASVCKQTSKHTGTAEHLYENVCMLEASPGLTNGGPEAQEGPPGGRSPLGSPIYHNTEDLSWPGSAQDSNLEAQYRRLLELELDEAGSAGRSGAQAGIKAKLVTLLTRERKKGPAPCDRP
uniprot
proteins
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. {ECO:0000269|PubMed:14993273}.
uniprot
proteins
mass_dalton
48027
uniprot
proteins
mutagenesis
MUTAGEN 209; /note="R->A: Greatly reduced ABL1-binding; reduced tyrosine phosphorylation."; /evidence="ECO:0000269|PubMed:10567556"; MUTAGEN 224; /note="R->A: Greatly reduced ABL1-binding; reduced tyrosine phosphorylation."; /evidence="ECO:0000269|PubMed:10567556"; MUTAGEN 325; /note="Y->F: Enhanced reduction of BCR-induced IL2 secretion. No effect on interaction with INPP5DSH2 domain. Abolishes interaction with CSKSH2 domain. No effect on BCR-triggered tyrosine phosphorylation. Abolishes reduction of BCR-induced IL2 secretion, the interaction with INPP5DSH2 domain and BCR-triggered tyrosine phosphorylation; when associated with F-343."; /evidence="ECO:0000269|PubMed:14993273"; MUTAGEN 343; /note="Y->F: Some reduction of BCR-induced IL2 secretion. Some interaction with INPP5DSH2 domain. Some decrease in BCR-triggered tyrosine phosphorylation. Abolishes reduction of BCR-induced IL2 secretion, the interaction with INPP5DSH2 domain and BCR-triggered tyrosine phosphorylation; when associated with F-325."; /evidence="ECO:0000269|PubMed:14993273"; MUTAGEN 378; /note="Y->F: No effect on the reduction of BCR-induced IL2 secretion, nor on the interaction with the SH2 domain of INPP5D or CSK nor on BCR-triggered tyrosine phosphorylation; when associated with F-399."; /evidence="ECO:0000269|PubMed:14993273"; MUTAGEN 399; /note="Y->F: No effect on the reduction of BCR-induced IL2 secretion, nor on the interaction with the SH2 domain of INPP5D or CSK nor on BCR-triggered tyrosine phosphorylation; when associated with F-378."; /evidence="ECO:0000269|PubMed:14993273
uniprot
proteins
post_translational_modification
PTM: Constitutively tyrosine-phosphorylated.; PTM: On IL2 stimulation, phosphorylated on C-terminal tyrosine residues possibly by Src kinases. Can also be phosphorylated by ABL1 kinase.
uniprot
proteins
protein_family
DOK family
uniprot
proteins
protein_family
Type A subfamily
uniprot
proteins
pubmed
10567556
uniprot
proteins
pubmed
10733577
uniprot
proteins
pubmed
14993273
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
uniprot
proteins