dbPTM

TYRO3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TYRO3_MOUSE
UniProt AC	P55144
Protein Name	Tyrosine-protein kinase receptor TYRO3
Gene Name	Tyro3
Organism	Mus musculus (Mouse).
Sequence Length	880
Subcellular Localization	Cell membrane Single-pass type I membrane protein.
Protein Description	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including 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..
Protein Sequence	MALRRSMGWPGLRPLLLAGLASLLLPGSAAAGLKLMGAPVKMTVSQGQPVKLNCSVEGMEDPDIHWMKDGTVVQNASQVSISISEHSWIGLLSLKSVERSDAGLYWCQVKDGEETKISQSVWLTVEGVPFFTVEPKDLAVPPNAPFQLSCEAVGPPEPVTIYWWRGLTKVGGPAPSPSVLNVTGVTQRTEFSCEARNIKGLATSRPAIVRLQAPPAAPFNTTVTTISSYNASVAWVPGADGLALLHSCTVQVAHAPGEWEALAVVVPVPPFTCLLRNLAPATNYSLRVRCANALGPSPYGDWVPFQTKGLAPARAPQNFHAIRTDSGLILEWEEVIPEDPGEGPLGPYKLSWVQENGTQDELMVEGTRANLTDWDPQKDLILRVCASNAIGDGPWSQPLVVSSHDHAGRQGPPHSRTSWVPVVLGVLTALITAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLVRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVHSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEEVYDLMYQCWSADPKQRPSFTCLRMELENILGHLSVLSTSQDPLYINIERAEQPTESGSPEVHCGERSSSEAGDGSGVGAVGGIPSDSRYIFSPGGLSESPGQLEQQPESPLNENQRLLLLQQGLLPHSSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	LLLAGLASLLLPGSA HHHHHHHHHHCCCCH	25.29	26239621
53	N-linked_Glycosylation	QGQPVKLNCSVEGME CCCCEEEEEEECCCC	15.42	-
75	N-linked_Glycosylation	KDGTVVQNASQVSIS CCCEEEECCEEEEEE	29.92	-
181	N-linked_Glycosylation	APSPSVLNVTGVTQR CCCCCEEECCCCCCC	27.44	19349973
220	N-linked_Glycosylation	APPAAPFNTTVTTIS CCCCCCCCCEEEEEE	33.51	-
230	N-linked_Glycosylation	VTTISSYNASVAWVP EEEEECCCCEEEEEC	27.90	-
282	Phosphorylation	LRNLAPATNYSLRVR HHHCCCCCCCEEEEE	33.36	-
283	N-linked_Glycosylation	RNLAPATNYSLRVRC HHCCCCCCCEEEEEE	26.88	-
285	Phosphorylation	LAPATNYSLRVRCAN CCCCCCCEEEEEEHH	16.27	22807455
356	N-linked_Glycosylation	KLSWVQENGTQDELM EEEEEECCCCCCEEE	41.54	-
370	N-linked_Glycosylation	MVEGTRANLTDWDPQ EEECCCCCCCCCCCC	39.93	-
456	Phosphorylation	RFGQAFDSVMARGEP HHHHHHHHHHHCCCC	13.82	22324799
472	Phosphorylation	VHFRAARSFNRERPE HHHHHCCCCCCCCHH	23.34	22324799
495	Acetylation	LGISDELKEKLEDVL CCCCHHHHHHHHHCC	51.24	6571709
497 (in isoform 2)	Ubiquitination	-	56.44	22790023
497	Ubiquitination	ISDELKEKLEDVLIP CCHHHHHHHHHCCCC	56.44	22790023
509	Phosphorylation	LIPEQQFTLGRMLGK CCCHHHCCHHHHCCC	24.78	29899451
511 (in isoform 2)	Ubiquitination	-	15.19	-
536	Acetylation	QEDGSFVKVAVKMLK CCCCCHHHHHHHHHH	23.59	19861503
671	Phosphorylation	FGLSRKIYSGDYYRQ CCCCCCCCCCCHHHC	15.05	22499769
672	Phosphorylation	GLSRKIYSGDYYRQG CCCCCCCCCCHHHCC	28.76	-
675	Phosphorylation	RKIYSGDYYRQGCAS CCCCCCCHHHCCCHH	12.22	18563927
676	Phosphorylation	KIYSGDYYRQGCASK CCCCCCHHHCCCHHC	10.95	-
723	Phosphorylation	MTRGQTPYAGIENAE HHCCCCCCCCCCCHH	22.35	-
756	Phosphorylation	EEVYDLMYQCWSADP HHHHHHHHHHHCCCC	14.07	-
784	Phosphorylation	ENILGHLSVLSTSQD HHHHHHHHHHCCCCC	18.48	20415495
787	Phosphorylation	LGHLSVLSTSQDPLY HHHHHHHCCCCCCEE	24.69	20415495
788	Phosphorylation	GHLSVLSTSQDPLYI HHHHHHCCCCCCEEE	26.67	20415495
789	Phosphorylation	HLSVLSTSQDPLYIN HHHHHCCCCCCEEEE	29.25	20415495
794	Phosphorylation	STSQDPLYINIERAE CCCCCCEEEEEEECC	9.41	20415495
806	Phosphorylation	RAEQPTESGSPEVHC ECCCCCCCCCCCEEC	47.23	29899451
808	Phosphorylation	EQPTESGSPEVHCGE CCCCCCCCCCEECCC	27.45	25521595
817	Phosphorylation	EVHCGERSSSEAGDG CEECCCCCCCCCCCC	33.63	25293948
818	Phosphorylation	VHCGERSSSEAGDGS EECCCCCCCCCCCCC	38.12	25293948
819	Phosphorylation	HCGERSSSEAGDGSG ECCCCCCCCCCCCCC	32.48	25293948
842	Phosphorylation	SDSRYIFSPGGLSES CCCCEEECCCCCCCC	17.05	25293948
847	Phosphorylation	IFSPGGLSESPGQLE EECCCCCCCCCCCCC	39.02	25293948
849	Phosphorylation	SPGGLSESPGQLEQQ CCCCCCCCCCCCCCC	30.84	19060867
859	Phosphorylation	QLEQQPESPLNENQR CCCCCCCCCCCHHHH	41.17	25521595
878	Phosphorylation	QQGLLPHSSC----- HCCCCCCCCC-----	31.31	25293948
879	Phosphorylation	QGLLPHSSC------ CCCCCCCCC------	22.32	20415495

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
723	Y	Phosphorylation	Kinase	TYRO3	P55144	PSP
756	Y	Phosphorylation	Kinase	TYRO3	P55144	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TYRO3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TYRO3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TYRO3_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TYRO3_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181, AND MASSSPECTROMETRY.	19349973 [Abstract]