Tyrobp
entrez
22177
canonical
uniprot
O54885
canonical
ensembl
ENSMUSG00000030579
resolver
ensp
ENSMUSP00000032800
resolver
enst
ENSMUST00000032800
resolver
genesymbol
Tyrobp
resolver
genesymbol_syn
Dap12
resolver
genesymbol_syn
Karap
resolver
uniprot
O88603
resolver
uniprot
Q3U419
resolver
uniprot_entry
Q3U419_MOUSE
resolver
uniprot_entry
TYOBP_MOUSE
resolver
uniprot_sec
O88603
resolver
amino_acid_sequence
MGALEPSWCLLFLPVLLTVGGLSPVQAQSDTFPRCDCSSVSPGVLAGIVLGDLVLTLLIALAVYSLGRLVSRGQGTAEGTRKQHIAETESPYQELQGQRPEVYSDLNTQRQYYR
uniprot
proteins
function
FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (PubMed:15471863, PubMed:9647200). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (PubMed:15728241, PubMed:16715077). Also has an inhibitory role in some cells (PubMed:21727189). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (PubMed:15471863). Required for neutrophil activation mediated by integrin (PubMed:17086186). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Also associates non-covalently with the NK cell receptors KLRA4/LY49D and KLRA8/LY49H which leads to NK cell activation (PubMed:9647200). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (PubMed:18957693). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) which is produced by TREM2 ectodomain shedding (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (PubMed:15728241). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (PubMed:18685038). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (PubMed:25690660). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability (PubMed:21257958). Negatively regulates B cell proliferation (PubMed:21727189). Required for CSF1-mediated osteoclast cytoskeletal organization (PubMed:18691974). Positively regulates multinucleation during osteoclast development (PubMed:12569157, PubMed:14969392). {ECO:0000250|UniProtKB:O43914, ECO:0000269|PubMed:12569157, ECO:0000269|PubMed:14969392, ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:15728241, ECO:0000269|PubMed:16715077, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:18685038, ECO:0000269|PubMed:18691974, ECO:0000269|PubMed:18957693, ECO:0000269|PubMed:21257958, ECO:0000269|PubMed:21727189, ECO:0000269|PubMed:25690660, ECO:0000269|PubMed:9647200}.
uniprot
proteins
mass_dalton
12367
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="D->A: Failure to rescue cytoskeletal defects when introduced into TYROBP-deficient cells."; /evidence="ECO:0000269|PubMed:18691974"; MUTAGEN 92; /note="Y->F: Abolishes phosphorylation and ability to regulate cytoskeletal organization; when associated with F-103."; /evidence="ECO:0000269|PubMed:18691974, ECO:0000269|PubMed:24078628"; MUTAGEN 103; /note="Y->F: Abolishes phosphorylation and ability to regulate cytoskeletal organization; when associated with F-92."; /evidence="ECO:0000269|PubMed:18691974, ECO:0000269|PubMed:24078628
uniprot
proteins
post_translational_modification
PTM: Tyrosine phosphorylated (PubMed:11754004, PubMed:12426565, PubMed:15728241, PubMed:17086186, PubMed:18691974, PubMed:9490415, PubMed:9852069). Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). {ECO:0000250|UniProtKB:O43914, ECO:0000269|PubMed:11754004, ECO:0000269|PubMed:12426565, ECO:0000269|PubMed:17086186, ECO:0000269|PubMed:9490415, ECO:0000269|PubMed:9852069}.
uniprot
proteins
protein_family
TYROBP family
uniprot
proteins
pubmed
10449773
uniprot
proteins
pubmed
11754004
uniprot
proteins
pubmed
12426564
uniprot
proteins
pubmed
12426565
uniprot
proteins
pubmed
12569157
uniprot
proteins
pubmed
12874256
uniprot
proteins
pubmed
12893283
uniprot
proteins
pubmed
14969392
uniprot
proteins
pubmed
15294961
uniprot
proteins
pubmed
15471863
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15728241
uniprot
proteins
pubmed
16715077
uniprot
proteins
pubmed
17086186
uniprot
proteins
pubmed
17202337
uniprot
proteins
pubmed
17928527
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
18685038
uniprot
proteins
pubmed
18691974
uniprot
proteins
pubmed
18957693
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21257958
uniprot
proteins
pubmed
21727189
uniprot
proteins
pubmed
24078628
uniprot
proteins
pubmed
25690660
uniprot
proteins
pubmed
29518356
uniprot
proteins
pubmed
9490415
uniprot
proteins
pubmed
9647200
uniprot
proteins
pubmed
9852069
uniprot
proteins
sequence_length
114
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9647200}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 43..63; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O43914
uniprot
proteins