TENX_HUMAN - dbPTM
TENX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TENX_HUMAN
UniProt AC P22105
Protein Name Tenascin-X
Gene Name TNXB
Organism Homo sapiens (Human).
Sequence Length 4242
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors..
Protein Sequence MMPAQYALTSSLVLLVLLSTARAGPFSSRSNVTLPAPRPPPQPGGHTVGAGVGSPSSQLYEHTVEGGEKQVVFTHRINLPPSTGCGCPPGTEPPVLASEVQALRVRLEILEELVKGLKEQCTGGCCPASAQAGTGQTDVRTLCSLHGVFDLSRCTCSCEPGWGGPTCSDPTDAEIPPSSPPSASGSCPDDCNDQGRCVRGRCVCFPGYTGPSCGWPSCPGDCQGRGRCVQGVCVCRAGFSGPDCSQRSCPRGCSQRGRCEGGRCVCDPGYTGDDCGMRSCPRGCSQRGRCENGRCVCNPGYTGEDCGVRSCPRGCSQRGRCKDGRCVCDPGYTGEDCGTRSCPWDCGEGGRCVDGRCVCWPGYTGEDCSTRTCPRDCRGRGRCEDGECICDTGYSGDDCGVRSCPGDCNQRGRCEDGRCVCWPGYTGTDCGSRACPRDCRGRGRCENGVCVCNAGYSGEDCGVRSCPGDCRGRGRCESGRCMCWPGYTGRDCGTRACPGDCRGRGRCVDGRCVCNPGFTGEDCGSRRCPGDCRGHGLCEDGVCVCDAGYSGEDCSTRSCPGGCRGRGQCLDGRCVCEDGYSGEDCGVRQCPNDCSQHGVCQDGVCICWEGYVSEDCSIRTCPSNCHGRGRCEEGRCLCDPGYTGPTCATRMCPADCRGRGRCVQGVCLCHVGYGGEDCGQEEPPASACPGGCGPRELCRAGQCVCVEGFRGPDCAIQTCPGDCRGRGECHDGSCVCKDGYAGEDCGEEVPTIEGMRMHLLEETTVRTEWTPAPGPVDAYEIQFIPTTEGASPPFTARVPSSASAYDQRGLAPGQEYQVTVRALRGTSWGLPASKTITTMIDGPQDLRVVAVTPTTLELGWLRPQAEVDRFVVSYVSAGNQRVRLEVPPEADGTLLTDLMPGVEYVVTVTAERGRAVSYPASVRANTGSSPLGLLGTTDEPPPSGPSTTQGAQAPLLQQRPQELGELRVLGRDETGRLRVVWTAQPDTFAYFQLRMRVPEGPGAHEEVLPGDVRQALVPPPPPGTPYELSLHGVPPGGKPSDPIIYQGIMDKDEEKPGKSSGPPRLGELTVTDRTSDSLLLRWTVPEGEFDSFVIQYKDRDGQPQVVPVEGPQRSAVITSLDPGRKYKFVLYGFVGKKRHGPLVAEAKILPQSDPSPGTPPHLGNLWVTDPTPDSLHLSWTVPEGQFDTFMVQYRDRDGRPQVVPVEGPERSFVVSSLDPDHKYRFTLFGIANKKRYGPLTADGTTAPERKEEPPRPEFLEQPLLGELTVTGVTPDSLRLSWTVAQGPFDSFMVQYKDAQGQPQAVPVAGDENEVTVPGLDPDRKYKMNLYGLRGRQRVGPESVVAKTAPQEDVDETPSPTELGTEAPESPEEPLLGELTVTGSSPDSLSLFWTVPQGSFDSFTVQYKDRDGRPRAVRVGGKESEVTVGGLEPGHKYKMHLYGLHEGQRVGPVSAVGVTAPQQEETPPATESPLEPRLGELTVTDVTPNSVGLSWTVPEGQFDSFIVQYKDKDGQPQVVPVAADQREVTVYNLEPERKYKMNMYGLHDGQRMGPLSVVIVTAPLPPAPATEASKPPLEPRLGELTVTDITPDSVGLSWTVPEGEFDSFVVQYKDRDGQPQVVPVAADQREVTIPDLEPSRKYKFLLFGIQDGKRRSPVSVEAKTVARGDASPGAPPRLGELWVTDPTPDSLRLSWTVPEGQFDSFVVQFKDKDGPQVVPVEGHERSVTVTPLDAGRKYRFLLYGLLGKKRHGPLTADGTTEARSAMDDTGTKRPPKPRLGEELQVTTVTQNSVGLSWTVPEGQFDSFVVQYKDRDGQPQVVPVEGSLREVSVPGLDPAHRYKLLLYGLHHGKRVGPISAVAITAGREETETETTAPTPPAPEPHLGELTVEEATSHTLHLSWMVTEGEFDSFEIQYTDRDGQLQMVRIGGDRNDITLSGLESDHRYLVTLYGFSDGKHVGPVHVEALTVPEEEKPSEPPTATPEPPIKPRLGELTVTDATPDSLSLSWTVPEGQFDHFLVQYRNGDGQPKAVRVPGHEEGVTISGLEPDHKYKMNLYGFHGGQRMGPVSVVGVTAAEEETPSPTEPSMEAPEPAEEPLLGELTVTGSSPDSLSLSWTVPQGRFDSFTVQYKDRDGRPQVVRVGGEESEVTVGGLEPGRKYKMHLYGLHEGRRVGPVSAVGVTAPEEESPDAPLAKLRLGQMTVRDITSDSLSLSWTVPEGQFDHFLVQFKNGDGQPKAVRVPGHEDGVTISGLEPDHKYKMNLYGFHGGQRVGPVSAVGLTAPGKDEEMAPASTEPPTPEPPIKPRLEELTVTDATPDSLSLSWTVPEGQFDHFLVQYKNGDGQPKATRVPGHEDRVTISGLEPDNKYKMNLYGFHGGQRVGPVSAIGVTAAEEETPSPTEPSMEAPEPPEEPLLGELTVTGSSPDSLSLSWTVPQGRFDSFTVQYKDRDGRPQVVRVGGEESEVTVGGLEPGRKYKMHLYGLHEGRRVGPVSTVGVTAPQEDVDETPSPTEPGTEAPGPPEEPLLGELTVTGSSPDSLSLSWTVPQGRFDSFTVQYKDRDGRPQAVRVGGQESKVTVRGLEPGRKYKMHLYGLHEGRRLGPVSAVGVTEDEAETTQAVPTMTPEPPIKPRLGELTMTDATPDSLSLSWTVPEGQFDHFLVQYRNGDGQPKAVRVPGHEDGVTISGLEPDHKYKMNLYGFHGGQRVGPISVIGVTAAEEETPSPTELSTEAPEPPEEPLLGELTVTGSSPDSLSLSWTIPQGHFDSFTVQYKDRDGRPQVMRVRGEESEVTVGGLEPGRKYKMHLYGLHEGRRVGPVSTVGVTEDEAETTQAVPTTTPEPPNKPRLGELTVTDATPDSLSLSWMVPEGQFDHFLVQYRNGDGQPKVVRVPGHEDGVTISGLEPDHKYKMNLYGFHGGQRVGPISVIGVTAAEEETPAPTEPSTEAPEPPEEPLLGELTVTGSSPDSLSLSWTIPQGRFDSFTVQYKDRDGRPQVVRVRGEESEVTVGGLEPGCKYKMHLYGLHEGQRVGPVSAVGVTAPKDEAETTQAVPTMTPEPPIKPRLGELTVTDATPDSLSLSWMVPEGQFDHFLVQYRNGDGQPKAVRVPGHEDGVTISGLEPDHKYKMNLYGFHGGQRVGPVSAIGVTEEETPSPTEPSTEAPEAPEEPLLGELTVTGSSPDSLSLSWTVPQGRFDSFTVQYKDRDGQPQVVRVRGEESEVTVGGLEPGRKYKMHLYGLHEGQRVGPVSTVGITAPLPTPLPVEPRLGELAVAAVTSDSVGLSWTVAQGPFDSFLVQYRDAQGQPQAVPVSGDLRAVAVSGLDPARKYKFLLFGLQNGKRHGPVPVEARTAPDTKPSPRLGELTVTDATPDSVGLSWTVPEGEFDSFVVQYKDKDGRLQVVPVAANQREVTVQGLEPSRKYRFLLYGLSGRKRLGPISADSTTAPLEKELPPHLGELTVAEETSSSLRLSWTVAQGPFDSFVVQYRDTDGQPRAVPVAADQRTVTVEDLEPGKKYKFLLYGLLGGKRLGPVSALGMTAPEEDTPAPELAPEAPEPPEEPRLGVLTVTDTTPDSMRLSWSVAQGPFDSFVVQYEDTNGQPQALLVDGDQSKILISGLEPSTPYRFLLYGLHEGKRLGPLSAEGTTGLAPAGQTSEESRPRLSQLSVTDVTTSSLRLNWEAPPGAFDSFLLRFGVPSPSTLEPHPRPLLQRELMVPGTRHSAVLRDLRSGTLYSLTLYGLRGPHKADSIQGTARTLSPVLESPRDLQFSEIRETSAKVNWMPPPSRADSFKVSYQLADGGEPQSVQVDGQARTQKLQGLIPGARYEVTVVSVRGFEESEPLTGFLTTVPDGPTQLRALNLTEGFAVLHWKPPQNPVDTYDVQVTAPGAPPLQAETPGSAVDYPLHDLVLHTNYTATVRGLRGPNLTSPASITFTTGLEAPRDLEAKEVTPRTALLTWTEPPVRPAGYLLSFHTPGGQNQEILLPGGITSHQLLGLFPSTSYNARLQAMWGQSLLPPVSTSFTTGGLRIPFPRDCGEEMQNGAGASRTSTIFLNGNRERPLNVFCDMETDGGGWLVFQRRMDGQTDFWRDWEDYAHGFGNISGEFWLGNEALHSLTQAGDYSMRVDLRAGDEAVFAQYDSFHVDSAAEYYRLHLEGYHGTAGDSMSYHSGSVFSARDRDPNSLLISCAVSYRGAWWYRNCHYANLNGLYGSTVDHQGVSWYHWKGFEFSVPFTEMKLRPRNFRSPAGGG
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
6Phosphorylation--MMPAQYALTSSLV
--CCHHHHHHHHHHH
12.9924043423
19PhosphorylationLVLLVLLSTARAGPF
HHHHHHHHHCCCCCC
18.8324043423
20PhosphorylationVLLVLLSTARAGPFS
HHHHHHHHCCCCCCC
21.8224043423
27PhosphorylationTARAGPFSSRSNVTL
HCCCCCCCCCCCCCC
28.16-
28PhosphorylationARAGPFSSRSNVTLP
CCCCCCCCCCCCCCC
39.8622210691
31N-linked_GlycosylationGPFSSRSNVTLPAPR
CCCCCCCCCCCCCCC
29.68UniProtKB CARBOHYD
33PhosphorylationFSSRSNVTLPAPRPP
CCCCCCCCCCCCCCC
31.1322210691
47O-linked_GlycosylationPPQPGGHTVGAGVGS
CCCCCCCCCCCCCCC
24.74OGP
54O-linked_GlycosylationTVGAGVGSPSSQLYE
CCCCCCCCCHHHEEE
21.14OGP
63PhosphorylationSSQLYEHTVEGGEKQ
HHHEEEEECCCCCEE
14.3322210691
74PhosphorylationGEKQVVFTHRINLPP
CCEEEEEEEEEECCC
9.9126074081
83O-linked_GlycosylationRINLPPSTGCGCPPG
EEECCCCCCCCCCCC
42.12OGP
91O-linked_GlycosylationGCGCPPGTEPPVLAS
CCCCCCCCCCCCHHH
51.60OGP
178O-linked_GlycosylationTDAEIPPSSPPSASG
CCCCCCCCCCCCCCC
50.55OGP
418MethylationRGRCEDGRCVCWPGY
CCCCCCCCEEECCCC
23.24115384867
581PhosphorylationCVCEDGYSGEDCGVR
EEECCCCCCCCCCCE
41.0327251275
643O-linked_GlycosylationCLCDPGYTGPTCATR
EEECCCCCCCCCCCC
42.4728411811
779PhosphorylationAPGPVDAYEIQFIPT
CCCCCCEEEEEEEEC
23.21-
785PhosphorylationAYEIQFIPTTEGASP
EEEEEEEECCCCCCC
28.52-
800PhosphorylationPFTARVPSSASAYDQ
CCEEECCCCCCCCCC
4.16-
801PhosphorylationFTARVPSSASAYDQR
CEEECCCCCCCCCCC
2.61-
803PhosphorylationARVPSSASAYDQRGL
EECCCCCCCCCCCCC
4.44-
819PhosphorylationPGQEYQVTVRALRGT
CCCEEEEEEEHHHCC
7.7824719451
827PhosphorylationVRALRGTSWGLPASK
EEHHHCCCCCCCCCC
2.17-
833PhosphorylationTSWGLPASKTITTMI
CCCCCCCCCEEEEEE
21.37-
901N-linked_GlycosylationLLTDLMPGVEYVVTV
EECCCCCCCEEEEEE
30.28-
930N-linked_GlycosylationRANTGSSPLGLLGTT
ECCCCCCCCCCCCCC
28.44-
936O-linked_GlycosylationSPLGLLGTTDEPPPS
CCCCCCCCCCCCCCC
4.12OGP
937O-linked_GlycosylationPLGLLGTTDEPPPSG
CCCCCCCCCCCCCCC
9.33OGP
943O-linked_GlycosylationTTDEPPPSGPSTTQG
CCCCCCCCCCCCCCC
8.25OGP
946O-linked_GlycosylationEPPPSGPSTTQGAQA
CCCCCCCCCCCCCCC
26.44OGP
947O-linked_GlycosylationPPPSGPSTTQGAQAP
CCCCCCCCCCCCCCC
23.09OGP
948O-linked_GlycosylationPPSGPSTTQGAQAPL
CCCCCCCCCCCCCCH
7.72OGP
1114PhosphorylationPVEGPQRSAVITSLD
ECCCCCCEEEEEECC
32.84-
1131PhosphorylationRKYKFVLYGFVGKKR
CCEEEEEEEECCCCC
2.2718083107
1180O-linked_GlycosylationDSLHLSWTVPEGQFD
CCEEEEEEECCCCCC
2.86OGP
1218PhosphorylationSFVVSSLDPDHKYRF
EEEEEECCCCCCEEE
11.83-
1244PhosphorylationGPLTADGTTAPERKE
CCCCCCCCCCCCCCC
56.0119060867
1245PhosphorylationPLTADGTTAPERKEE
CCCCCCCCCCCCCCC
36.7117924679
1290PhosphorylationVAQGPFDSFMVQYKD
EECCCCCEEEEEEEC
3.56-
1330PhosphorylationRKYKMNLYGLRGRQR
CCCEEEHHCCCCCCC
23.6219060867
1331PhosphorylationKYKMNLYGLRGRQRV
CCEEEHHCCCCCCCC
21.97-
1332PhosphorylationYKMNLYGLRGRQRVG
CEEEHHCCCCCCCCC
45.83-
1364O-linked_GlycosylationPSPTELGTEAPESPE
CCCCCCCCCCCCCCC
9.23OGP
1401PhosphorylationVPQGSFDSFTVQYKD
ECCCCCCEEEEEEEC
11.16-
1403PhosphorylationQGSFDSFTVQYKDRD
CCCCCEEEEEEECCC
4.23-
1406PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
7.66-
1417PhosphorylationDGRPRAVRVGGKESE
CCCCCEEEECCEECE
14.7618083107
1441PhosphorylationHKYKMHLYGLHEGQR
CEEEEEEEECCCCCE
67.39-
1469O-linked_GlycosylationQEETPPATESPLEPR
CCCCCCCCCCCCCCC
23.07OGP
1569O-linked_GlycosylationPLPPAPATEASKPPL
CCCCCCCCCCCCCCC
7.22OGP
1693PhosphorylationTPDSLRLSWTVPEGQ
CCCCEEEEEEECCCC
11.84-
1737PhosphorylationPLDAGRKYRFLLYGL
ECCHHHHHHHHHHHH
33.42-
1872O-linked_GlycosylationREETETETTAPTPPA
CCCCCCEECCCCCCC
29.33OGP
1873O-linked_GlycosylationEETETETTAPTPPAP
CCCCCEECCCCCCCC
14.03OGP
1876O-linked_GlycosylationETETTAPTPPAPEPH
CCEECCCCCCCCCCC
3.46OGP
1981O-linked_GlycosylationPSEPPTATPEPPIKP
CCCCCCCCCCCCCCC
4.88OGP
2008O-linked_GlycosylationDSLSLSWTVPEGQFD
CCEEEEEECCCCCCC
19.25OGP
2083O-linked_GlycosylationEEETPSPTEPSMEAP
CCCCCCCCCCCCCCC
58.83OGP
2124PhosphorylationVPQGRFDSFTVQYKD
ECCCCCCEEEEEEEC
2.60-
2126PhosphorylationQGRFDSFTVQYKDRD
CCCCCEEEEEEECCC
30.15-
2129PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
54.79-
2146PhosphorylationVRVGGEESEVTVGGL
EEECCEECEEEECCC
5.6725850435
2149PhosphorylationGGEESEVTVGGLEPG
CCEECEEEECCCCCC
5.8527732954
2159PhosphorylationGLEPGRKYKMHLYGL
CCCCCCEEEEEEEEC
8.13-
2292O-linked_GlycosylationDEEMAPASTEPPTPE
CCCCCCCCCCCCCCC
38.64OGP
2324O-linked_GlycosylationDSLSLSWTVPEGQFD
CCEEEEEECCCCCCC
7.43OGP
2357O-linked_GlycosylationPGHEDRVTISGLEPD
CCCCCCEEEECCCCC
37.85OGP
2399O-linked_GlycosylationEEETPSPTEPSMEAP
CCCCCCCCCCCCCCC
10.03OGP
2440PhosphorylationVPQGRFDSFTVQYKD
ECCCCCCEEEEEEEC
41.29-
2442PhosphorylationQGRFDSFTVQYKDRD
CCCCCEEEEEEECCC
8.58-
2445PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
5.06-
2462PhosphorylationVRVGGEESEVTVGGL
EEECCEECEEEECCC
24.0325850435
2465PhosphorylationGGEESEVTVGGLEPG
CCEECEEEECCCCCC
12.7127732954
2475PhosphorylationGLEPGRKYKMHLYGL
CCCCCCEEEEEEEEC
35.23-
2514O-linked_GlycosylationPSPTEPGTEAPGPPE
CCCCCCCCCCCCCCC
3.08OGP
2551PhosphorylationVPQGRFDSFTVQYKD
ECCCCCCEEEEEEEC
6.53-
2553PhosphorylationQGRFDSFTVQYKDRD
CCCCCEEEEEEECCC
22.85-
2556PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
3.42-
2586PhosphorylationGLEPGRKYKMHLYGL
CCCCCCEEEEEEEEC
35.23-
2615PhosphorylationTEDEAETTQAVPTMT
CCCCHHHCCCCCCCC
36.18-
2620O-linked_GlycosylationETTQAVPTMTPEPPI
HHCCCCCCCCCCCCC
68.53OGP
2727O-linked_GlycosylationTPSPTELSTEAPEPP
CCCCCCCCCCCCCCC
47.27OGP
2728O-linked_GlycosylationPSPTELSTEAPEPPE
CCCCCCCCCCCCCCC
40.85OGP
2765PhosphorylationIPQGHFDSFTVQYKD
ECCCCCCEEEEEEEC
9.10-
2767PhosphorylationQGHFDSFTVQYKDRD
CCCCCEEEEEEECCC
16.90-
2770PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
4.58-
2787PhosphorylationMRVRGEESEVTVGGL
EEEECCCCEEEECCC
59.8727732954
2790PhosphorylationRGEESEVTVGGLEPG
ECCCCEEEECCCCCC
79.2327732954
2800PhosphorylationGLEPGRKYKMHLYGL
CCCCCCEEEEEEEEC
4.41-
2822PhosphorylationPVSTVGVTEDEAETT
CCEEEEECCCCCHHC
36.8522210691
2828PhosphorylationVTEDEAETTQAVPTT
ECCCCCHHCCCCCCC
15.5422210691
2836PhosphorylationTQAVPTTTPEPPNKP
CCCCCCCCCCCCCCC
40.0322210691
2837O-linked_GlycosylationQAVPTTTPEPPNKPR
CCCCCCCCCCCCCCC
2.68OGP
2838O-linked_GlycosylationAVPTTTPEPPNKPRL
CCCCCCCCCCCCCCC
2.49OGP
2979PhosphorylationIPQGRFDSFTVQYKD
ECCCCCCEEEEEEEC
58.78-
2981PhosphorylationQGRFDSFTVQYKDRD
CCCCCEEEEEEECCC
28.20-
2984PhosphorylationFDSFTVQYKDRDGRP
CCEEEEEEECCCCCC
38.20-
3001PhosphorylationVRVRGEESEVTVGGL
EEEECCCCEEEECCC
35.23-
3158O-linked_GlycosylationPTEPSTEAPEAPEEP
CCCCCCCCCCCCCCC
7.12OGP
3174PhosphorylationLGELTVTGSSPDSLS
CEEEEEECCCCCCEE
16.85-
3193PhosphorylationVPQGRFDSFTVQYKD
ECCCCCCEEEEEEEC
58.78-
3195PhosphorylationQGRFDSFTVQYKDRD
CCCCCEEEEEEECCC
32.14-
3198PhosphorylationFDSFTVQYKDRDGQP
CCEEEEEEECCCCCC
41.82-
3215PhosphorylationVRVRGEESEVTVGGL
EEEECCCCEEEECCC
35.2327732954
3218PhosphorylationRGEESEVTVGGLEPG
ECCCCEEEECCCCCC
16.2427732954
3228PhosphorylationGLEPGRKYKMHLYGL
CCCCCCEEEEEEEEC
25.06-
3257O-linked_GlycosylationTAPLPTPLPVEPRLG
ECCCCCCCCCCCCCC
6.61OGP
3316PhosphorylationDLRAVAVSGLDPARK
CCEEEEEECCCHHHH
7.2123403867
3407PhosphorylationAANQREVTVQGLEPS
ECCCCEEEEECCCCC
19.63-
3541O-linked_GlycosylationAPEEDTPAPELAPEA
CCCCCCCCCCCCCCC
10.15OGP
3639PhosphorylationGPLSAEGTTGLAPAG
CCCCCCCCCCCCCCC
60.4726699800
3640PhosphorylationPLSAEGTTGLAPAGQ
CCCCCCCCCCCCCCC
42.5126699800
3648PhosphorylationGLAPAGQTSEESRPR
CCCCCCCCCHHHCCC
55.7226657352
3649PhosphorylationLAPAGQTSEESRPRL
CCCCCCCCHHHCCCH
27.6423911959
3652PhosphorylationAGQTSEESRPRLSQL
CCCCCHHHCCCHHHC
26.8027130503
3682PhosphorylationAPPGAFDSFLLRFGV
CCCCCCCHHHHHCCC
27.6624719451
3691PhosphorylationLLRFGVPSPSTLEPH
HHHCCCCCCCCCCCC
41.8017924679
3738PhosphorylationLYGLRGPHKADSIQG
EEECCCCCCCCCCCC
29.13-
3751PhosphorylationQGTARTLSPVLESPR
CCCCCCCHHCCCCCC
44.4724667141
3756PhosphorylationTLSPVLESPRDLQFS
CCHHCCCCCCCCCHH
6.5527174698
3763PhosphorylationSPRDLQFSEIRETSA
CCCCCCHHHHHCCCC
9.76-
3768PhosphorylationQFSEIRETSAKVNWM
CHHHHHCCCCCCCCC
3.67-
3769PhosphorylationFSEIRETSAKVNWMP
HHHHHCCCCCCCCCC
37.01-
3825PhosphorylationRYEVTVVSVRGFEES
EEEEEEEEEECCCCC
30.4924719451
3853N-linked_GlycosylationPTQLRALNLTEGFAV
CCCEEEECCCCCEEE
29.78UniProtKB CARBOHYD
3855N-linked_GlycosylationQLRALNLTEGFAVLH
CEEEECCCCCEEEEE
38.62-
3880O-linked_GlycosylationYDVQVTAPGAPPLQA
EEEEEECCCCCCCCC
47.83OGP
3906N-linked_GlycosylationHDLVLHTNYTATVRG
HHEEEECCCCEEECC
17.51UniProtKB CARBOHYD
3908N-linked_GlycosylationLVLHTNYTATVRGLR
EEEECCCCEEECCCC
3.41-
3918N-linked_GlycosylationVRGLRGPNLTSPASI
ECCCCCCCCCCCCEE
40.58UniProtKB CARBOHYD
3920N-linked_GlycosylationGLRGPNLTSPASITF
CCCCCCCCCCCEEEE
15.06-
3921PhosphorylationLRGPNLTSPASITFT
CCCCCCCCCCEEEEE
26.8522210691
3922O-linked_GlycosylationRGPNLTSPASITFTT
CCCCCCCCCEEEEEC
3.29OGP
3923O-linked_GlycosylationGPNLTSPASITFTTG
CCCCCCCCEEEEECC
24.76OGP
3924PhosphorylationPNLTSPASITFTTGL
CCCCCCCEEEEECCC
5.0422210691
3965N-linked_GlycosylationPAGYLLSFHTPGGQN
CCEEEEEEECCCCCC
59.79-
4093N-linked_GlycosylationDYAHGFGNISGEFWL
HHHCCCCCCCCEEEE
7.68UniProtKB CARBOHYD
4095N-linked_GlycosylationAHGFGNISGEFWLGN
HCCCCCCCCEEEECH
36.40-
4179PhosphorylationDPNSLLISCAVSYRG
CCCCEEEEEEEECCC
32.5219413330
4226PhosphorylationFEFSVPFTEMKLRPR
EEEECEECCCEECCC
8.94-

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 TENX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 TENX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BANP_HUMANBANPphysical
25416956
FIGL1_HUMANFIGNL1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606408Ehlers-Danlos syndrome due to tenascin X deficiency (EDSTNXD)
615963Vesicoureteral reflux 8 (VUR8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TENX_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-901 AND ASN-930, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3965, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4226, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1331; THR-1332 ANDSER-3738, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1417, AND MASSSPECTROMETRY.

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