TENR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TENR_MOUSE
• UniProt AC: Q8BYI9
• Protein Name: Tenascin-R
• Gene Name: Tnr
• Organism: Mus musculus (Mouse).
• Sequence Length: 1358
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Description: Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity)..
• Protein Sequence: MGIDGETVVLKNMLIGVNLILLGSMLKPSECRLEVTTERAQRQTVEEEGGASSYNTSSKEQPMVFNHVYNINVPLESLCSSGLEASAEQDMSAEDDTLAEYIGQTSDHESQVTFTHKINLPKKACPCASSSQVLQELLSRIEMLEREVSLLRDQCNTNCCQESAATGQLDYVPHCSGHGNFSFESCGCICNEGWFGKNCSEPYCPLGCSSRGVCVDGQCICDSEYSGDDCSELRCPTDCSSRGLCVDGECVCEEPYTGEDCRELRCPGDCSGKGQCANGTCLCQEGYAGEDCSQRRCLNACSGRGHCQEGLCICEEGYQGPDCSAVAPPEDLRVAGISDRSIELEWDGPMAVTEYVISYQPTALGGLQLQQRVPGDWSGVTIMELEPGLTYNISVYAVISNILSLPITAKVATHLSTPQGLQFKTITETTVEVQWEPFSFSFDGWEISFIPKNNEGGVIAQLPSDVTSFNQTGLKPGEEYIVNVVALKEQARSPPTSASVSTVIDGPTQILVRDVSDTVAFVEWTPPRAKVDFILLKYGLVGGEGGKTTFRLQPPLSQYSVQALRPGSRYEVSISAVRGTNESEASSTQFTTEIDAPKNLRVGSRTATSLDLEWDNSEAEAQEYKVVYSTLAGEQYHEVLVPKGIGPTTKTTLTDLVPGTEYGVGISAVMNSKQSIPATMNARTELDSPRDLMVTASSETSISLIWTKASGPIDHYRITFTPSSGISSEVTVPRDRTSYTLTDLEPGAEYIISITAERGRQQSLESTVDAFTGFRPISHLHFSHVTSSSVNITWSDPSPPADRLILNYSPRDKEEDMLEVLLDATKRHAVLMGLQPATEYIVNLVAVHGTVTSEPIVGSITTGIDPPKNITISNVTKDSLTVSWSSPVAPFDYYRVSYRPTQVGRLDSSVVPNTVTEFAITRLYPATEYEISLNSVRGREESERICTLVHTAMDSPMDLIATNITPTEALLQWKAPMGEVENYVIVLTHFAIAGETILVDGVSEEFQLVDLLPSTHYTVTMYATSGPLMSGTIATNFSTLLDPPDNLTASEVTRQSALISWQPPRAAIENYVLTYKSTDGSRKELIVDAEDTWIRLEGLSENTDYTVLLQAAQEATRSSLTSTVFTTGGRVFSHPQDCAQHLMNGDTLSGVYTIFLNGELSHKLQVYCDMTTDGGGWIVFQRRQNGQTDFFRKWADYRVGFGNLEDEFWLGLDNIHRITAQGRYELRVDMRDGQEAVFAYYDKFAVEDSRSLYKIRIGSYNGTAGDSLSYHQGRPFSTEDRDNDVAVTNCAMSYKGAWWYKNCHRTNLNGKYGESRHSQGINWYHWKGHEFSIPFVEMKMRPYIHRLTAGRKRRALKF

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
55	N-linked_Glycosylation	EGGASSYNTSSKEQP CCCCCCCCCCCCCCC	35.12	-
58	Phosphorylation	ASSYNTSSKEQPMVF CCCCCCCCCCCCEEE	37.87	27708245
180	N-linked_Glycosylation	PHCSGHGNFSFESCG CCCCCCCCEECCCCC	24.58	-
198	N-linked_Glycosylation	NEGWFGKNCSEPYCP CCCCCCCCCCCCCCC	34.62	-
278	N-linked_Glycosylation	SGKGQCANGTCLCQE CCCCCCCCCEEEECC	54.67	-
312	S-palmitoylation	GHCQEGLCICEEGYQ CCCCCCEEEECCCCC	5.00	28680068
392	N-linked_Glycosylation	LEPGLTYNISVYAVI ECCCCEEEEEEEHHH	18.15	-
400	Phosphorylation	ISVYAVISNILSLPI EEEEHHHHHHHCCCC	15.95	-
404	Phosphorylation	AVISNILSLPITAKV HHHHHHHCCCCCCHH	28.44	-
408	Phosphorylation	NILSLPITAKVATHL HHHCCCCCCHHHHCC	20.63	-
470	N-linked_Glycosylation	PSDVTSFNQTGLKPG CCCCCCCCCCCCCCC	37.97	-
557	Phosphorylation	FRLQPPLSQYSVQAL EEECCCCCEEEEEEC	32.61	26643407
559	Phosphorylation	LQPPLSQYSVQALRP ECCCCCEEEEEECCC	13.87	26643407
560	Phosphorylation	QPPLSQYSVQALRPG CCCCCEEEEEECCCC	10.50	26643407
581	N-linked_Glycosylation	ISAVRGTNESEASST EEEEECCCCCCCCCC	54.33	-
719	Phosphorylation	PIDHYRITFTPSSGI CCCEEEEEEECCCCC	16.68	25521595
721	Phosphorylation	DHYRITFTPSSGISS CEEEEEEECCCCCCC	17.38	25521595
723	Phosphorylation	YRITFTPSSGISSEV EEEEEECCCCCCCEE	37.83	24925903
724	Phosphorylation	RITFTPSSGISSEVT EEEEECCCCCCCEEE	41.15	25521595
727	Phosphorylation	FTPSSGISSEVTVPR EECCCCCCCEEEECC	24.79	24925903
728	Phosphorylation	TPSSGISSEVTVPRD ECCCCCCCEEEECCC	33.88	22324799
731	Phosphorylation	SGISSEVTVPRDRTS CCCCCEEEECCCCCE	22.27	29899451
791	N-linked_Glycosylation	HVTSSSVNITWSDPS EECCCCEEEEECCCC	28.11	-
869	N-linked_Glycosylation	TGIDPPKNITISNVT CCCCCCCCEEEEECC	42.27	-
874	N-linked_Glycosylation	PKNITISNVTKDSLT CCCEEEEECCCCCEE	41.44	-
876	Phosphorylation	NITISNVTKDSLTVS CEEEEECCCCCEEEE	33.13	26239621
879	Phosphorylation	ISNVTKDSLTVSWSS EEECCCCCEEEEECC	27.74	26239621
881	Phosphorylation	NVTKDSLTVSWSSPV ECCCCCEEEEECCCC	19.22	26239621
883	Phosphorylation	TKDSLTVSWSSPVAP CCCCEEEEECCCCCC	18.92	26239621
908	Phosphorylation	TQVGRLDSSVVPNTV CCCCCCCCCCCCCCC	29.62	29899451
947	Phosphorylation	EESERICTLVHTAMD HHHHHHHHHHHHHCC	29.46	21183079
951	Phosphorylation	RICTLVHTAMDSPMD HHHHHHHHHCCCCCH	19.05	21183079
1036	N-linked_Glycosylation	MSGTIATNFSTLLDP CCCEEEECHHHHCCC	21.61	-
1046	N-linked_Glycosylation	TLLDPPDNLTASEVT HHCCCCCCCCHHHHH	45.10	-
1251	Phosphorylation	FAVEDSRSLYKIRIG CEECCCCCCEEEEEE	39.75	-
1261	N-linked_Glycosylation	KIRIGSYNGTAGDSL EEEEEEECCCCCCCC	42.93	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of TENR_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND MASSSPECTROMETRY.
PubMed: 17114649