TENA_MOUSE - dbPTM
TENA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TENA_MOUSE
UniProt AC Q80YX1
Protein Name Tenascin
Gene Name Tnc {ECO:0000312|MGI:MGI:101922}
Organism Mus musculus (Mouse).
Sequence Length 2110
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth when provided to neurons in culture. May play a role in supporting the growth of epithelial tumors. Ligand for integrins ITGA8:ITGB1, ITGA9:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (By similarity)..
Protein Sequence MGAVTWLLPGIFLALFALTPEGGVLKKIIRHKRESGLNMTLPEENQPVVFNHIYNIKLPMGSQCSVDLESASGEKDLTPTPESSGSFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELELLVSSLREQCTMGTGCCLQPAEGRLDTRPFCSGRGNFSAEGCGCVCEPGWKGPNCSEPDCPGNCNLRGQCLDGQCICDEGFTGEDCSQLACPNDCNDQGRCVNGVCVCFEGYAGPDCGLEVCPVPCSEEHGMCVDGRCVCKDGFAGEDCNEPLCLNNCYNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGELTCPNDCQGRGQCEEGQCVCNEGFAGADCSEKRCPADCHHRGRCLNGQCECDDGFTGADCGDLQCPNGCSGHGRCVNGQCVCDEGYTGEDCSQRRCPNDCHNRGLCVQGKCICEQGFKGFDCSEMSCPNDCHQHGRCVNGMCICDDDYTGEDCRDRRCPRDCSQRGRCVDGQCICEDGFTGPDCAELSCPSDCHGHGRCVNGQCICHEGFTGKDCKEQRCPSDCHGQGRCEDGQCICHEGFTGLDCGQRSCPNDCSNQGQCVSGRCICNEGYTGIDCSEVSPPKDLIVTEVTEETVNLAWDNEMRVTEYLIMYTPTHADGLEMQFRVPGDQTSTTIRELEPGVEYFIRVFAILENKRSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKKVTTTRLDAPSHIEVKDVTDTTALITWFKPLAEIDSIELSYGIKDVPGDRTTIDLTHEDNQYSIGNLRPDTEYEVSLISRRVDMASNPAKETFITGLDAPRNLRRVSQTDNSITLEWRNVKADIDSYRIKYAPISGGDHAEIDVPKSQQATTKTTLTGLRPGTEYGIGVSAVKGDKESDPATINAATEIDAPKDLRVSETTQDSLTFFWTTPLAKFDRYRLNYSLPTGQSMEVQLPKDATSHVLTDLEPGQEYTVLLIAEKGRHKSKPARVKASTEEVPSLENLTVTEAGWDGLRLNWTADDLAYEYFVIQVQEANNVETAHNFTVPGNLRAADIPGLKVATSYRVSIYGVARGYRTPVLSAETSTGTTPNLGEVTVAEVGWDALTLNWTAPEGAYKNFFIQVLEADTTQTVQNLTVPGGLRSVDLPGLKAATRYYITLRGVTQDFGTAPLSVEVLTEDLPQLGGLSVTEVSWDGLTLNWTTDDLAYKHFVVQVQEANNVEAAQNLTVPGSLRAVDIPGLKADTPYRVSIYGVIQGYRTPMLSTDVSTAREPEIGNLNVSDVTPKSFNLSWTATDGIFDMFTIEIIDSNRLLQTAEHNISGAERTAHISGLPPSTDFIVYLSGIAPSIRTKTISTTATTEALPLLENLTISDTNPYGFTVSWTASENAFDSFLVTVVDSGKLLDPQEFTLSGTQRKLELRGLITGIGYEVLVSGFTQGHQTKPLRAETITEAEPEVDNLLVSDATPDGFRLSWTADEGIFDSFVIRIRDTKKQSEPQEISLPSPERTRDITGLREATEYEIELYGISRGRRSQPVSAIATTAMGSPKEIMFSDITENAATVSWRAPTAQVESFRITYVPMTGGAPSMVTVDGTDTETRLVKLTPGVEYRVSVIAMKGFEESDPVSGTLITALDGPSGLLIANITDSEALAMWQPAIATVDSYVISYTGERVPEVTRTVSGNTVEYELHDLEPATEYILSIFAEKGQQKSSTIATKFTTDLDSPREFTATEVQSETALLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYSARIQALSGSLRSKLIQTIFTTIGLLYPFPRDCSQAMLNGDTTSGLYTIYINGDKTQALEVYCDMTSDGGGWIVFLRRKNGREDFYRNWKAYAAGFGDRREEFWLGLDNLSKITAQGQYELRVDLQDHGESAYAVYDRFSVGDAKSRYKLKVEGYSGTAGDSMNYHNGRSFSTYDKDTDSAITNCALSYKGAFWYKNCHRVNLMGRYGDNNHSQGVNWFHWKGHEYSIQFAEMKLRPSNFRNLEGRRKRA
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 Orthologous
Protein Cluster
38N-linked_GlycosylationHKRESGLNMTLPEEN
HHHHCCCCCCCCCCC		25.56-
62PhosphorylationNIKLPMGSQCSVDLE
EEECCCCCCEEEECH		23.0524925903
65PhosphorylationLPMGSQCSVDLESAS
CCCCCCEEEECHHCC		15.8429899451
70PhosphorylationQCSVDLESASGEKDL
CEEEECHHCCCCCCC		34.7225521595
72PhosphorylationSVDLESASGEKDLTP
EEECHHCCCCCCCCC		57.6825521595
134PhosphorylationEELELLVSSLREQCT
HHHHHHHHHHHHHCC		24.5130635358
135PhosphorylationELELLVSSLREQCTM
HHHHHHHHHHHHCCC		24.7830635358
154MethylationCLQPAEGRLDTRPFC
CCCCCCCCCCCCCCC		22.3958860155
166N-linked_GlycosylationPFCSGRGNFSAEGCG
CCCCCCCCCCCCCCC		26.75-
184N-linked_GlycosylationEPGWKGPNCSEPDCP
CCCCCCCCCCCCCCC		51.09-
327N-linked_GlycosylationFDRGRCINGTCYCEE
CCCCCEECCEEEECC		43.26-
375AcetylationAGADCSEKRCPADCH
CCCCCCCCCCCCCCC		42.907610081
788N-linked_GlycosylationISLHIVKNNTRGPGL
EEEEEEECCCCCCCC		44.18-
807PhosphorylationTTRLDAPSHIEVKDV
ECCCCCCCCEEEECC		38.53-
815PhosphorylationHIEVKDVTDTTALIT
CEEEECCCCCCCEEE		37.4524719451
818PhosphorylationVKDVTDTTALITWFK
EECCCCCCCEEEEEC		23.4424719451
822PhosphorylationTDTTALITWFKPLAE
CCCCCEEEEECCHHH		26.2124719451
891PhosphorylationPAKETFITGLDAPRN
CCHHHEECCCCCCCC		27.74-
903PhosphorylationPRNLRRVSQTDNSIT
CCCCCCCCCCCCCEE		26.08-
905PhosphorylationNLRRVSQTDNSITLE
CCCCCCCCCCCEEEE		29.64-
1018N-linked_GlycosylationKFDRYRLNYSLPTGQ
HCCEEEEEEECCCCC		18.49-
1079N-linked_GlycosylationEEVPSLENLTVTEAG
CCCCCCCCEEEEECC		46.43-
1093N-linked_GlycosylationGWDGLRLNWTADDLA
CCCCEECCCCHHHHH		27.84-
1119N-linked_GlycosylationNNVETAHNFTVPGNL
CCEECCCCCCCCCCC		31.64-
1145PhosphorylationTSYRVSIYGVARGYR
EEEEEEEEEECCCCC		9.68-
1184N-linked_GlycosylationGWDALTLNWTAPEGA
CCCEEECCCCCCCCH		28.90-
1210N-linked_GlycosylationDTTQTVQNLTVPGGL
CCCCEEECCEECCCC		33.09-
1275N-linked_GlycosylationSWDGLTLNWTTDDLA
EECCEEEEEECHHHH		28.90-
1301N-linked_GlycosylationNNVEAAQNLTVPGSL
CCCHHHHHCCCCCCE		32.71-
1354N-linked_GlycosylationEPEIGNLNVSDVTPK
CCCCCCCCHHHCCCC		34.93-
1364N-linked_GlycosylationDVTPKSFNLSWTATD
HCCCCCEEEEEEECC		40.01-
1394N-linked_GlycosylationLLQTAEHNISGAERT
CEEEEECCCCCHHHH		22.9416944957
1443N-linked_GlycosylationEALPLLENLTISDTN
CHHHHHHCCEECCCC		42.31-
1485PhosphorylationLLDPQEFTLSGTQRK
CCCCCEEECCCCHHH		21.1821659605
1570PhosphorylationIRDTKKQSEPQEISL
EECCCCCCCCCCCCC		61.1926026062
1576PhosphorylationQSEPQEISLPSPERT
CCCCCCCCCCCCHHH		33.2126026062
1579PhosphorylationPQEISLPSPERTRDI
CCCCCCCCCHHHCCC		44.6926026062
1608PhosphorylationGISRGRRSQPVSAIA
EECCCCCCCCCCEEE		37.1626239621
1612PhosphorylationGRRSQPVSAIATTAM
CCCCCCCCEEEEECC		22.2026239621
1616PhosphorylationQPVSAIATTAMGSPK
CCCCEEEEECCCCCC		14.6926239621
1617PhosphorylationPVSAIATTAMGSPKE
CCCEEEEECCCCCCE		12.9626239621
1687PhosphorylationPGVEYRVSVIAMKGF
CCCEEEEEEEEECCC		9.9820469934
1718N-linked_GlycosylationPSGLLIANITDSEAL
CCEEEEEECCCHHHH		30.60-
1969N-linked_GlycosylationEFWLGLDNLSKITAQ
EEEEECCCHHHEEEC		51.78-
2000PhosphorylationYAVYDRFSVGDAKSR
EEEEECCCCCCCCCC		26.5322817900
2071N-linked_GlycosylationMGRYGDNNHSQGVNW
EEEECCCCCCCCCEE		40.71-
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

Oops, there are no upstream regulatory protein records of TENA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TENA_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 TENA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TENA_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TENA_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1394, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-72, AND MASSSPECTROMETRY.
"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-72, AND MASSSPECTROMETRY.

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