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Protein Page:
Tyro3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Tyro3 Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TUB, TULP1 and GAS6. Interacts with PIK3R1; this interaction increases PI3-kinase activity. Abundant in the brain and lower levels in other tissues. Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Kinase, protein; Protein kinase, TK; EC 2.7.10.1; Protein kinase, tyrosine (receptor); EC 2.7.1.112; TK group; Axl family
Cellular Component: endoplasmic reticulum membrane; integral to plasma membrane; nuclear envelope; nucleus
Molecular Function: protein binding; protein heterodimerization activity; protein-tyrosine kinase activity; phosphoinositide 3-kinase binding; receptor signaling protein tyrosine kinase activity; transmembrane receptor protein tyrosine kinase activity; ATP binding
Biological Process: forebrain cell migration; platelet activation; negative regulation of lymphocyte activation; phosphoinositide 3-kinase cascade; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; vagina development; signal transduction; ovulation cycle; natural killer cell differentiation; negative regulation of innate immune response; negative regulation of inflammatory response; protein kinase B signaling cascade; negative regulation of toll-like receptor signaling pathway; spermatogenesis; negative regulation of neuron apoptosis; cell adhesion; apoptotic cell clearance; secretion by cell
Reference #:  Q06418 (UniProtKB)
Alt. Names/Synonyms: Brt; BYK; DTK; FLJ16467; RSE; SKY; Tif; TYRO3; TYRO3 protein tyrosine kinase; Tyro3 protein tyrosine kinase (sea-related receptor tyrosine kinase); Tyrosine-protein kinase byk; Tyrosine-protein kinase DTK; Tyrosine-protein kinase receptor TYRO3; Tyrosine-protein kinase RSE; Tyrosine-protein kinase SKY
Gene Symbols: TYRO3
Molecular weight: 96,905 Da
Basal Isoelectric point: 5.47  Predict pI for various phosphorylation states
CST Pathways:  Tyrosine Kinases & Substrates
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Tyro3

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T292 LRDLVPATNYSLRVR
0 1 S307-p CANALGPsPYADWVP
0 1 T427-p QGPPHSRtsWVPVVL
0 1 S428-p GPPHSRtsWVPVVLG
0 8 S466-p RFGQAFDsVMARGEP
0 1 K505 LGISDELKEKLEDVL
0 1 K507 ISDELKEKLEDVLIP
0 1 S543-p QLKQEDGsFVKVAVK
0 1 K546 QEDGsFVKVAVKMLK
0 1 K582-ub FDHPHVAkLVGVSLR
0 441 Y681-p FGLSRKIysGDyyRQ
0 68 S682-p GLSRKIysGDyyRQG
0 397 Y685-p RKIysGDyyRQGCAS
0 88 Y686-p KIysGDyyRQGCASK
0 1 S794 ENILGQLSVLSASQD
0 1 Y804 SASQDPLYINIERAE
0 2 S818-p EEPTAGGsLELPGRD
1 18 Y828-p LPGRDQPySGAGDGs
0 1 S835-p ySGAGDGsGMGAVGG
0 3 S869-p QAEHQPEsPLNETQR
0 1 S889 QGLLPHSSC______
  mouse

 
T282-p LRNLAPAtNYSLRVR
S297 CANALGPSPYGDWVP
T417 QGPPHSRTSWVPVVL
S418 GPPHSRTSWVPVVLG
S456-p RFGQAFDsVMARGEP
K495-ac LGISDELkEkLEDVL
K497-ub ISDELkEkLEDVLIP
S533 QLKQEDGSFVkVAVK
K536-ac QEDGSFVkVAVKMLK
K572 FDHPHVAKLVGVSLR
Y671-p FGLSRKIysGDyyRQ
S672-p GLSRKIysGDyyRQG
Y675-p RKIysGDyyRQGCAS
Y676-p KIysGDyyRQGCASK
S784-p ENILGHLsVLSTSQD
Y794-p STSQDPLyINIERAE
S808-p EQPTESGsPEVHCGE
S818 VHCGERSSSEAGDGS
S825 SSEAGDGSGVGAVGG
S859-p QLEQQPEsPLNENQR
S879-p QGLLPHSsC______
  rat

 
T282 LRNLAPATNYSLRVR
S297 CANALGPSPYGDWVP
T417 QGPPHSRTSWVPVVL
S418 GPPHSRTSWVPVVLG
S456 RFGQAFDSVMARGEP
K495 LGISDELKEKLEDVL
K497 ISDELKEKLEDVLIP
S533 QLKQEDGSFVKVAVK
K536 QEDGSFVKVAVKMLK
K572 FDHPHVAKLVGVSLR
Y671-p FGLSRKIySGDyyRQ
S672 GLSRKIySGDyyRQG
Y675-p RKIySGDyyRQGCAS
Y676-p KIySGDyyRQGCASK
S784 ENILGHLSVLSTSQD
Y794 STSQDPLYINIERAG
S808 GQPAENGSPELPCGE
S818 LPCGEQSSSEAGDGS
S825 SSEAGDGSGMGAIGG
S859 QLEQQPESPLNENQR
S879 QGLLPHSSC______
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