RON_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RON_HUMAN
• UniProt AC: Q04912
• Protein Name: Macrophage-stimulating protein receptor
• Gene Name: MST1R
• Organism: Homo sapiens (Human).
• Sequence Length: 1400
• Subcellular Localization: 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 MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Plays also a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand..
• Protein Sequence: MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTVGGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQFSPMPGNVRRPRPLSEPPRPT

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
66	N-linked_Glycosylation	VTYEGDRNESAVFVA EEEECCCCCEEEEEE	52.92	UniProtKB CARBOHYD
215	Phosphorylation	AASFSPRSVSIRRLK HHHCCCCEEEEEEEE	24.49	22210691
217	Phosphorylation	SFSPRSVSIRRLKAD HCCCCEEEEEEEECC	16.18	24719451
222 (in isoform 2)	Ubiquitination	-	42.27	21906983
222 (in isoform 1)	Ubiquitination	-	42.27	21906983
222	Ubiquitination	SVSIRRLKADASGFA EEEEEEEECCCCCCC	42.27	2190698
226	Phosphorylation	RRLKADASGFAPGFV EEEECCCCCCCCCEE	34.68	-
236	Phosphorylation	APGFVALSVLPKHLV CCCEEEEEECCHHHH	16.33	-
419	N-linked_Glycosylation	GLEALSPNTSCRHFP CCCCCCCCCCCCCCC	41.05	UniProtKB CARBOHYD
458	N-linked_Glycosylation	LYVTRLDNVTVAHMG EEEEECCCEEEEECC	35.63	UniProtKB CARBOHYD
488	N-linked_Glycosylation	NYLLYVSNFSLGDSG CCEEEEECCCCCCCC	22.08	22848655
654	N-linked_Glycosylation	TQAVGPTNVSLTVTN CCCCCCCEEEEEEEC	25.23	UniProtKB CARBOHYD
720	N-linked_Glycosylation	TSRAVLVNGTECLLA CCEEEEECCCEEEEE	47.73	UniProtKB CARBOHYD
841	N-linked_Glycosylation	PQGWVAGNLSARGDG CCCCEECCCCCCCCC	22.53	UniProtKB CARBOHYD
897	N-linked_Glycosylation	VADCVGINVTVGGES HCCEEEEEEEECCCC	19.92	UniProtKB CARBOHYD
956	Phosphorylation	GPDGVPQSTLLGILL CCCCCCHHHHHHHHH	18.23	26853621
957	Phosphorylation	PDGVPQSTLLGILLP CCCCCHHHHHHHHHH	22.28	26853621
1012	Phosphorylation	ATPLPILYSGSDYRS CCCCCEEECCCCCCC	16.23	26356563
1013	Phosphorylation	TPLPILYSGSDYRSG CCCCEEECCCCCCCC	28.51	26356563
1015	Phosphorylation	LPILYSGSDYRSGLA CCEEECCCCCCCCCC	26.06	26356563
1017	Phosphorylation	ILYSGSDYRSGLALP EEECCCCCCCCCCCC	14.36	26356563
1031	Phosphorylation	PAIDGLDSTTCVHGA CCCCCCCCCCCCCCC	30.56	24144214
1032	Phosphorylation	AIDGLDSTTCVHGAS CCCCCCCCCCCCCCC	24.71	28102081
1033	Phosphorylation	IDGLDSTTCVHGASF CCCCCCCCCCCCCCC	19.24	26657352
1039	Phosphorylation	TTCVHGASFSDSEDE CCCCCCCCCCCCCCC	29.85	26657352
1041	Phosphorylation	CVHGASFSDSEDESC CCCCCCCCCCCCCCC	37.42	26657352
1043	Phosphorylation	HGASFSDSEDESCVP CCCCCCCCCCCCCHH	45.83	26657352
1047	Phosphorylation	FSDSEDESCVPLLRK CCCCCCCCCHHHHCC	32.51	24144214
1056	Phosphorylation	VPLLRKESIQLRDLD HHHHCCCCEECCCCC	20.76	29496963
1071	Ubiquitination	SALLAEVKDVLIPHE HHHHHHHHHEEECCC	33.36	-
1092	Phosphorylation	DRVIGKGHFGVVYHG CCEEECCCEEEEECH	21.55	-
1101	Phosphorylation	GVVYHGEYIDQAQNR EEEECHHHHHHHHHH	17.87	-
1198	Phosphorylation	QVARGMEYLAEQKFV HHHHHHHHHHHCCCH	11.54	-
1223	Ubiquitination	LDESFTVKVADFGLA CCCCEEEEEHHHCHH	28.75	-
1237	Phosphorylation	ARDILDREYYSVQQH HHHHHCCCCCCHHHH	48.79	17016520
1238	Phosphorylation	RDILDREYYSVQQHR HHHHCCCCCCHHHHC	11.26	21945579
1239	Phosphorylation	DILDREYYSVQQHRH HHHCCCCCCHHHHCC	9.52	21945579
1240	Phosphorylation	ILDREYYSVQQHRHA HHCCCCCCHHHHCCC	16.73	21945579
1317	Phosphorylation	EYCPDSLYQVMQQCW CCCCHHHHHHHHHHH	11.74	22817900
1353	Phosphorylation	SALLGDHYVQLPATY HHHHCCCEEECCEEE	8.47	15632155
1360	Phosphorylation	YVQLPATYMNLGPST EEECCEEEEECCCCC	6.01	15632155
1394	Phosphorylation	VRRPRPLSEPPRPT- CCCCCCCCCCCCCC-	51.22	12919677
1400	Phosphorylation	LSEPPRPT------- CCCCCCCC-------	53.15	20639409

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
1238	Y	Phosphorylation	Kinase	MET	P08581	PSP
1238	Y	Phosphorylation	Kinase	MST1R	Q04912	GPS
1239	Y	Phosphorylation	Kinase	MET	P08581	PSP
1239	Y	Phosphorylation	Kinase	MST1R	Q04912	GPS
1353	Y	Phosphorylation	Kinase	MET	P08581	PSP
1353	Y	Phosphorylation	Kinase	MST1R	Q04912	GPS
1360	Y	Phosphorylation	Kinase	MET	P08581	PSP
1360	Y	Phosphorylation	Kinase	MST1R	Q04912	GPS
1394	S	Phosphorylation	Kinase	AKT1	P31749	PSP
1394	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
1394	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:16740632
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:12802274

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RON_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 RON_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHC1_HUMAN	SHC1	physical	8918464
GRB2_HUMAN	GRB2	physical	8918464
PLCG1_HUMAN	PLCG1	physical	8918464
CHIP_HUMAN	STUB1	physical	16740632
HSP7C_HUMAN	HSPA8	physical	16740632
HS90A_HUMAN	HSP90AA1	physical	16740632
GAB1_HUMAN	GAB1	physical	14982882
PP1A_HUMAN	PPP1CA	physical	14505491
1433B_HUMAN	YWHAB	physical	14505491
1433E_HUMAN	YWHAE	physical	14505491
1433F_HUMAN	YWHAH	physical	14505491
1433G_HUMAN	YWHAG	physical	14505491
1433T_HUMAN	YWHAQ	physical	14505491
1433Z_HUMAN	YWHAZ	physical	14505491
1433S_HUMAN	SFN	physical	14505491
PTPRR_HUMAN	PTPRR	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
• D10074: Narnatumab (USAN)
• DrugBank
• There are no disease associations of PTM sites.