TYRO3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TYRO3_HUMAN
• UniProt AC: Q06418
• Protein Name: Tyrosine-protein kinase receptor TYRO3
• Gene Name: TYRO3
• Organism: Homo sapiens (Human).
• Sequence Length: 890
• 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.; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope.; (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope..
• Protein Sequence: MALRRSMGRPGLPPLPLPPPPRLGLLLAALASLLLPESAAAGLKLMGAPVKLTVSQGQPVKLNCSVEGMEEPDIQWVKDGAVVQNLDQLYIPVSEQHWIGFLSLKSVERSDAGRYWCQVEDGGETEISQPVWLTVEGVPFFTVEPKDLAVPPNAPFQLSCEAVGPPEPVTIVWWRGTTKIGGPAPSPSVLNVTGVTQSTMFSCEAHNLKGLASSRTATVHLQALPAAPFNITVTKLSSSNASVAWMPGADGRALLQSCTVQVTQAPGGWEVLAVVVPVPPFTCLLRDLVPATNYSLRVRCANALGPSPYADWVPFQTKGLAPASAPQNLHAIRTDSGLILEWEEVIPEAPLEGPLGPYKLSWVQDNGTQDELTVEGTRANLTGWDPQKDLIVRVCVSNAVGCGPWSQPLVVSSHDRAGQQGPPHSRTSWVPVVLGVLTALVTAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLIRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVQSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEDVYDLMYQCWSADPKQRPSFTCLRMELENILGQLSVLSASQDPLYINIERAEEPTAGGSLELPGRDQPYSGAGDGSGMGAVGGTPSDCRYILTPGGLAEQPGQAEHQPESPLNETQRLLLLQQGLLPHSSC

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MALRRSMGRPGLP --CCCCCCCCCCCCC	21.10	30631047
63	N-linked_Glycosylation	QGQPVKLNCSVEGME CCCCEEEEEEECCCC	15.42	UniProtKB CARBOHYD
191	N-linked_Glycosylation	APSPSVLNVTGVTQS CCCCCEEEEECCCCC	27.44	UniProtKB CARBOHYD
230	N-linked_Glycosylation	ALPAAPFNITVTKLS ECCCCCEEEEEEECC	28.14	UniProtKB CARBOHYD
240	N-linked_Glycosylation	VTKLSSSNASVAWMP EEECCCCCCEEEECC	37.88	UniProtKB CARBOHYD
293	N-linked_Glycosylation	RDLVPATNYSLRVRC HHHCCCCCCEEEEEE	26.88	UniProtKB CARBOHYD
295	Phosphorylation	LVPATNYSLRVRCAN HCCCCCCEEEEEEHH	16.27	24719451
307	Phosphorylation	CANALGPSPYADWVP EHHHCCCCCCCCCCC	28.83	-
366	N-linked_Glycosylation	KLSWVQDNGTQDELT EEEEEEECCCCCEEE	38.02	UniProtKB CARBOHYD
380	N-linked_Glycosylation	TVEGTRANLTGWDPQ EEEECCCCCCCCCCC	34.54	UniProtKB CARBOHYD
427	Phosphorylation	QGPPHSRTSWVPVVL CCCCCCCCCHHHHHH	29.92	-
428	Phosphorylation	GPPHSRTSWVPVVLG CCCCCCCCHHHHHHH	25.60	-
466	Phosphorylation	RFGQAFDSVMARGEP HHHHHHHHHHHCCCC	13.82	30266825
482	Phosphorylation	VHFRAARSFNRERPE HHHHHCCCCCCCCHH	23.34	28102081
507	Ubiquitination	ISDELKEKLEDVLIP CCHHHHHHHHHCCCC	56.44	-
526	Ubiquitination	TLGRMLGKGEFGSVR CHHHHCCCCCCCCCE	51.83	-
543	Phosphorylation	QLKQEDGSFVKVAVK HHHCCCCCHHHHHHH	38.91	21815630
582	Ubiquitination	FDHPHVAKLVGVSLR CCCHHHHHHHHHHHH	42.49	21890473
681	Phosphorylation	FGLSRKIYSGDYYRQ CCCCCCCCCCCHHHC	15.05	27273156
682	Phosphorylation	GLSRKIYSGDYYRQG CCCCCCCCCCHHHCC	28.76	28796482
685	Phosphorylation	RKIYSGDYYRQGCAS CCCCCCCHHHCCCHH	12.22	27273156
686	Phosphorylation	KIYSGDYYRQGCASK CCCCCCHHHCCCHHC	10.95	22322096
731	Phosphorylation	EIMTRGQTPYAGIEN HHHHCCCCCCCCCCC	22.53	30622161
733	Phosphorylation	MTRGQTPYAGIENAE HHCCCCCCCCCCCHH	22.35	30622161
804	Phosphorylation	SASQDPLYINIERAE CCCCCCEEEEEEECC	9.41	-
814	Phosphorylation	IERAEEPTAGGSLEL EEECCCCCCCCCEEC	41.01	29255136
818	Phosphorylation	EEPTAGGSLELPGRD CCCCCCCCEECCCCC	20.11	23401153
828	Phosphorylation	LPGRDQPYSGAGDGS CCCCCCCCCCCCCCC	17.69	19702290
829	Phosphorylation	PGRDQPYSGAGDGSG CCCCCCCCCCCCCCC	28.93	29978859
835	Phosphorylation	YSGAGDGSGMGAVGG CCCCCCCCCCCCCCC	30.28	29978859
849	Phosphorylation	GTPSDCRYILTPGGL CCHHCCCEEECCCCH	13.45	28152594
852	Phosphorylation	SDCRYILTPGGLAEQ HCCCEEECCCCHHCC	15.44	30266825
869	Phosphorylation	QAEHQPESPLNETQR CCCCCCCCCCCHHHH	41.17	30266825
874	Phosphorylation	PESPLNETQRLLLLQ CCCCCCHHHHHHHHH	20.23	30266825
888	Phosphorylation	QQGLLPHSSC----- HCCCCCCCCC-----	31.31	29978859
889	Phosphorylation	QGLLPHSSC------ CCCCCCCCC------	22.32	24719451

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

Oops, there are no upstream regulatory protein records of TYRO3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TYRO3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TYRO3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRC_HUMAN	SRC	physical	7537495
P85A_HUMAN	PIK3R1	physical	10627473
GAS6_HUMAN	GAS6	physical	8621659
VIGLN_HUMAN	HDLBP	physical	22939629
KLK4_HUMAN	KLK4	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
CTDS1_HUMAN	CTDSP1	physical	28065597
CTDS2_HUMAN	CTDSP2	physical	28065597

Drug and Disease Associations

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