TENR_HUMAN - dbPTM
TENR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TENR_HUMAN
UniProt AC Q92752
Protein Name Tenascin-R
Gene Name TNR
Organism Homo sapiens (Human).
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. These 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 mediate 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 MGADGETVVLKNMLIGINLILLGSMIKPSECQLEVTTERVQRQSVEEEGGIANYNTSSKEQPVVFNHVYNINVPLDNLCSSGLEASAEQEVSAEDETLAEYMGQTSDHESQVTFTHRINFPKKACPCASSAQVLQELLSRIEMLEREVSVLRDQCNANCCQESAATGQLDYIPHCSGHGNFSFESCGCICNEGWFGKNCSEPYCPLGCSSRGVCVDGQCICDSEYSGDDCSELRCPTDCSSRGLCVDGECVCEEPYTGEDCRELRCPGDCSGKGRCANGTCLCEEGYVGEDCGQRQCLNACSGRGQCEEGLCVCEEGYQGPDCSAVAPPEDLRVAGISDRSIELEWDGPMAVTEYVISYQPTALGGLQLQQRVPGDWSGVTITELEPGLTYNISVYAVISNILSLPITAKVATHLSTPQGLQFKTITETTVEVQWEPFSFSFDGWEISFIPKNNEGGVIAQVPSDVTSFNQTGLKPGEEYIVNVVALKEQARSPPTSASVSTVIDGPTQILVRDVSDTVAFVEWIPPRAKVDFILLKYGLVGGEGGRTTFRLQPPLSQYSVQALRPGSRYEVSVSAVRGTNESDSATTQFTTEIDAPKNLRVGSRTATSLDLEWDNSEAEVQEYKVVYSTLAGEQYHEVLVPRGIGPTTRATLTDLVPGTEYGVGISAVMNSQQSVPATMNARTELDSPRDLMVTASSETSISLIWTKASGPIDHYRITFTPSSGIASEVTVPKDRTSYTLTDLEPGAEYIISVTAERGRQQSLESTVDAFTGFRPISHLHFSHVTSSSVNITWSDPSPPADRLILNYSPRDEEEEMMEVSLDATKRHAVLMGLQPATEYIVNLVAVHGTVTSEPIVGSITTGIDPPKDITISNVTKDSVMVSWSPPVASFDYYRVSYRPTQVGRLDSSVVPNTVTEFTITRLNPATEYEISLNSVRGREESERICTLVHTAMDNPVDLIATNITPTEALLQWKAPVGEVENYVIVLTHFAVAGETILVDGVSEEFRLVDLLPSTHYTATMYATNGPLTSGTISTNFSTLLDPPANLTASEVTRQSALISWQPPRAEIENYVLTYKSTDGSRKELIVDAEDTWIRLEGLLENTDYTVLLQAAQDTTWSSITSTAFTTGGRVFPHPQDCAQHLMNGDTLSGVYPIFLNGELSQKLQVYCDMTTDGGGWIVFQRRQNGQTDFFRKWADYRVGFGNVEDEFWLGLDNIHRITSQGRYELRVDMRDGQEAAFASYDRFSVEDSRNLYKLRIGSYNGTAGDSLSYHQGRPFSTEDRDNDVAVTNCAMSYKGAWWYKNCHRTNLNGKYGESRHSQGINWYHWKGHEFSIPFVEMKMRPYNHRLMAGRKRQSLQF
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
36O-linked_GlycosylationSECQLEVTTERVQRQ
HHCEEEECCHHHHHH		17.3519838169
37O-linked_GlycosylationECQLEVTTERVQRQS
HCEEEECCHHHHHHC		27.2819838169
44PhosphorylationTERVQRQSVEEEGGI
CHHHHHHCHHHHCCC		33.4122817900
55N-linked_GlycosylationEGGIANYNTSSKEQP
HCCCCCCCCCCCCCC		33.04UniProtKB CARBOHYD
57PhosphorylationGIANYNTSSKEQPVV
CCCCCCCCCCCCCEE		35.4617081983
58PhosphorylationIANYNTSSKEQPVVF
CCCCCCCCCCCCEEE		37.8717081983
92PhosphorylationASAEQEVSAEDETLA
CCCCCCCCCCHHHHH		25.7829759185
139PhosphorylationQVLQELLSRIEMLER
HHHHHHHHHHHHHHH		43.7824719451
180N-linked_GlycosylationPHCSGHGNFSFESCG
CCCCCCCCEECCCCC		24.58UniProtKB CARBOHYD
198N-linked_GlycosylationNEGWFGKNCSEPYCP
CCCCCCCCCCCCCCC		34.62UniProtKB CARBOHYD
278N-linked_GlycosylationSGKGRCANGTCLCEE
CCCCCCCCCCEEECC		50.35UniProtKB CARBOHYD
287PhosphorylationTCLCEEGYVGEDCGQ
CEEECCCCCCCCCCC		14.4622817900
391PhosphorylationELEPGLTYNISVYAV
EECCCCEEEEEEEEH		18.6225332170
392N-linked_GlycosylationLEPGLTYNISVYAVI
ECCCCEEEEEEEEHH		18.15UniProtKB CARBOHYD
394PhosphorylationPGLTYNISVYAVISN
CCCEEEEEEEEHHHH		12.8725332170
425PhosphorylationPQGLQFKTITETTVE
CCCCEEEEEEEEEEE		34.1328450419
427PhosphorylationGLQFKTITETTVEVQ
CCEEEEEEEEEEEEE		32.2928450419
429PhosphorylationQFKTITETTVEVQWE
EEEEEEEEEEEEEEE		27.7328450419
430PhosphorylationFKTITETTVEVQWEP
EEEEEEEEEEEEEEE		14.4028450419
439PhosphorylationEVQWEPFSFSFDGWE
EEEEEEEEEEECCEE		30.6028450419
441PhosphorylationQWEPFSFSFDGWEIS
EEEEEEEEECCEEEE		22.6428450419
448PhosphorylationSFDGWEISFIPKNNE
EECCEEEEEECCCCC		12.9528450419
470N-linked_GlycosylationPSDVTSFNQTGLKPG
CCCCCCCCCCCCCCC		37.97UniProtKB CARBOHYD
538PhosphorylationVDFILLKYGLVGGEG
CCEEEEECCCCCCCC		18.7028674151
548PhosphorylationVGGEGGRTTFRLQPP
CCCCCCCEEEEECCC		33.2924043423
549PhosphorylationGGEGGRTTFRLQPPL
CCCCCCEEEEECCCC		12.8524043423
557PhosphorylationFRLQPPLSQYSVQAL
EEECCCCCEEEEEEC		32.6124043423
559PhosphorylationLQPPLSQYSVQALRP
ECCCCCEEEEEECCC		13.8724043423
560PhosphorylationQPPLSQYSVQALRPG
CCCCCEEEEEECCCC		10.5024043423
581N-linked_GlycosylationVSAVRGTNESDSATT
EEEEECCCCCCCCEE		49.99UniProtKB CARBOHYD
719PhosphorylationPIDHYRITFTPSSGI
CCCEEEEEEECCCCC		16.6826033855
721PhosphorylationDHYRITFTPSSGIAS
CEEEEEEECCCCCCC		17.3820886841
723PhosphorylationYRITFTPSSGIASEV
EEEEEECCCCCCCEE		37.8320886841
724PhosphorylationRITFTPSSGIASEVT
EEEEECCCCCCCEEE		35.1120886841
728PhosphorylationTPSSGIASEVTVPKD
ECCCCCCCEEEECCC		30.5825332170
755 (in isoform 2)Phosphorylation-18.9322210691
767 (in isoform 2)Phosphorylation-17.0322210691
791N-linked_GlycosylationHVTSSSVNITWSDPS
EECCCCEEEEECCCC		28.11UniProtKB CARBOHYD
874N-linked_GlycosylationPKDITISNVTKDSVM
CCCEEEEECCCCCEE		41.44UniProtKB CARBOHYD
1036N-linked_GlycosylationTSGTISTNFSTLLDP
CCCEEECCCHHHCCC		23.29UniProtKB CARBOHYD
1046N-linked_GlycosylationTLLDPPANLTASEVT
HHCCCCCCCCHHHHH		43.64UniProtKB CARBOHYD
1259PhosphorylationLYKLRIGSYNGTAGD
EEEEEEEEECCCCCC		17.0429449344
1260PhosphorylationYKLRIGSYNGTAGDS
EEEEEEEECCCCCCC		16.6422817900
1261N-linked_GlycosylationKLRIGSYNGTAGDSL
EEEEEEECCCCCCCC		42.93UniProtKB CARBOHYD
1263PhosphorylationRIGSYNGTAGDSLSY
EEEEECCCCCCCCCE		24.6729449344
1267PhosphorylationYNGTAGDSLSYHQGR
ECCCCCCCCCEECCC		20.4929449344
1269PhosphorylationGTAGDSLSYHQGRPF
CCCCCCCCEECCCCC		25.2329449344
1270PhosphorylationTAGDSLSYHQGRPFS
CCCCCCCEECCCCCC		11.9429449344
1288O-linked_GlycosylationRDNDVAVTNCAMSYK
CCCCEEEECCCEECC		18.16OGP
1294PhosphorylationVTNCAMSYKGAWWYK
EECCCEECCCCEEEE		10.6022817900
1343PhosphorylationVEMKMRPYNHRLMAG
EEEECCCCCHHHCCC		17.15-
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 TENR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
36TGlycosylation

19838169
37TGlycosylation

19838169
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 TENR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTPRZ_HUMANPTPRZ1physical
9507007
NCAN_HUMANNCANphysical
9507007
NCK2_HUMANNCK2physical
25416956
RPC3_HUMANPOLR3Cphysical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
PPL13_HUMANLGALS14physical
25416956
CC146_HUMANCCDC146physical
25416956
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.
Regulatory Network of TENR_HUMAN

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Related Literatures of Post-Translational Modification

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