TENA_HUMAN - dbPTM
TENA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TENA_HUMAN
UniProt AC P24821
Protein Name Tenascin
Gene Name TNC
Organism Homo sapiens (Human).
Sequence Length 2201
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 from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. [PubMed: 19884327]
Protein Sequence MGAMTQLLAGVFLAFLALATEGGVLKKVIRHKRQSGVNATLPEENQPVVFNHVYNIKLPVGSQCSVDLESASGEKDLAPPSEPSESFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELENLVSSLREQCTAGAGCCLQPATGRLDTRPFCSGRGNFSTEGCGCVCEPGWKGPNCSEPECPGNCHLRGRCIDGQCICDDGFTGEDCSQLACPSDCNDQGKCVNGVCICFEGYAGADCSREICPVPCSEEHGTCVDGLCVCHDGFAGDDCNKPLCLNNCYNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGKPTCPHACHTQGRCEEGQCVCDEGFAGVDCSEKRCPADCHNRGRCVDGRCECDDGFTGADCGELKCPNGCSGHGRCVNGQCVCDEGYTGEDCSQLRCPNDCHSRGRCVEGKCVCEQGFKGYDCSDMSCPNDCHQHGRCVNGMCVCDDGYTGEDCRDRQCPRDCSNRGLCVDGQCVCEDGFTGPDCAELSCPNDCHGQGRCVNGQCVCHEGFMGKDCKEQRCPSDCHGQGRCVDGQCICHEGFTGLDCGQHSCPSDCNNLGQCVSGRCICNEGYSGEDCSEVSPPKDLVVTEVTEETVNLAWDNEMRVTEYLVVYTPTHEGGLEMQFRVPGDQTSTIIQELEPGVEYFIRVFAILENKKSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKRVTTTRLDAPSQIEVKDVTDTTALITWFKPLAEIDGIELTYGIKDVPGDRTTIDLTEDENQYSIGNLKPDTEYEVSLISRRGDMSSNPAKETFTTGLDAPRNLRRVSQTDNSITLEWRNGKAAIDSYRIKYAPISGGDHAEVDVPKSQQATTKTTLTGLRPGTEYGIGVSAVKEDKESNPATINAATELDTPKDLQVSETAETSLTLLWKTPLAKFDRYRLNYSLPTGQWVGVQLPRNTTSYVLRGLEPGQEYNVLLTAEKGRHKSKPARVKASTEQAPELENLTVTEVGWDGLRLNWTAADQAYEHFIIQVQEANKVEAARNLTVPGSLRAVDIPGLKAATPYTVSIYGVIQGYRTPVLSAEASTGETPNLGEVVVAEVGWDALKLNWTAPEGAYEYFFIQVQEADTVEAAQNLTVPGGLRSTDLPGLKAATHYTITIRGVTQDFSTTPLSVEVLTEEVPDMGNLTVTEVSWDALRLNWTTPDGTYDQFTIQVQEADQVEEAHNLTVPGSLRSMEIPGLRAGTPYTVTLHGEVRGHSTRPLAVEVVTEDLPQLGDLAVSEVGWDGLRLNWTAADNAYEHFVIQVQEVNKVEAAQNLTLPGSLRAVDIPGLEAATPYRVSIYGVIRGYRTPVLSAEASTAKEPEIGNLNVSDITPESFNLSWMATDGIFETFTIEIIDSNRLLETVEYNISGAERTAHISGLPPSTDFIVYLSGLAPSIRTKTISATATTEALPLLENLTISDINPYGFTVSWMASENAFDSFLVTVVDSGKLLDPQEFTLSGTQRKLELRGLITGIGYEVMVSGFTQGHQTKPLRAEIVTEAEPEVDNLLVSDATPDGFRLSWTADEGVFDNFVLKIRDTKKQSEPLEITLLAPERTRDITGLREATEYEIELYGISKGRRSQTVSAIATTAMGSPKEVIFSDITENSATVSWRAPTAQVESFRITYVPITGGTPSMVTVDGTKTQTRLVKLIPGVEYLVSIIAMKGFEESEPVSGSFTTALDGPSGLVTANITDSEALARWQPAIATVDSYVISYTGEKVPEITRTVSGNTVEYALTDLEPATEYTLRIFAEKGPQKSSTITAKFTTDLDSPRDLTATEVQSETALLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYTAKIQALNGPLRSNMIQTIFTTIGLLYPFPKDCSQAMLNGDTTSGLYTIYLNGDKAEALEVFCDMTSDGGGWIVFLRRKNGRENFYQNWKAYAAGFGDRREEFWLGLDNLNKITAQGQYELRVDLRDHGETAFAVYDKFSVGDAKTRYKLKVEGYSGTAGDSMAYHNGRSFSTFDKDTDSAITNCALSYKGAFWYRNCHRVNLMGRYGDNNHSQGVNWFHWKGHEHSIQFAEMKLRPSNFRNLEGRRKRA
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
5Phosphorylation---MGAMTQLLAGVF
---CCHHHHHHHHHH
18.6124043423
20PhosphorylationLAFLALATEGGVLKK
HHHHHHHHCCCHHHH
35.6924043423
38N-linked_GlycosylationHKRQSGVNATLPEEN
HHHHCCCCCCCCCCC
30.63UniProtKB CARBOHYD
62PhosphorylationNIKLPVGSQCSVDLE
EEECCCCCCEEEECH
28.4023927012
65PhosphorylationLPVGSQCSVDLESAS
CCCCCCEEEECHHCC
15.8422777824
70PhosphorylationQCSVDLESASGEKDL
CEEEECHHCCCCCCC
34.7229255136
72PhosphorylationSVDLESASGEKDLAP
EEECHHCCCCCCCCC
57.6829255136
81O-linked_GlycosylationEKDLAPPSEPSESFQ
CCCCCCCCCCCHHHH
62.17OGP
81PhosphorylationEKDLAPPSEPSESFQ
CCCCCCCCCCCHHHH
62.1726657352
84O-linked_GlycosylationLAPPSEPSESFQEHT
CCCCCCCCHHHHEEC
41.65OGP
84PhosphorylationLAPPSEPSESFQEHT
CCCCCCCCHHHHEEC
41.6526657352
86PhosphorylationPPSEPSESFQEHTVD
CCCCCCHHHHEECCC
36.2526657352
91O-linked_GlycosylationSESFQEHTVDGENQI
CHHHHEECCCCCCEE
21.38OGP
91PhosphorylationSESFQEHTVDGENQI
CHHHHEECCCCCCEE
21.3828348404
124PhosphorylationPDVKELLSRLEELEN
CCHHHHHHHHHHHHH
47.6624719451
134PhosphorylationEELENLVSSLREQCT
HHHHHHHHHHHHHHH
27.1624719451
135PhosphorylationELENLVSSLREQCTA
HHHHHHHHHHHHHHC
24.7824719451
166N-linked_GlycosylationPFCSGRGNFSTEGCG
CCCCCCCCCCCCCCC
26.74UniProtKB CARBOHYD
168PhosphorylationCSGRGNFSTEGCGCV
CCCCCCCCCCCCCCE
29.5526657352
169PhosphorylationSGRGNFSTEGCGCVC
CCCCCCCCCCCCCEE
32.0526657352
184N-linked_GlycosylationEPGWKGPNCSEPECP
CCCCCCCCCCCCCCC
51.0918780401
257PhosphorylationEICPVPCSEEHGTCV
EECCCCCCCCCCCEE
39.6927251275
327N-linked_GlycosylationFDRGRCINGTCYCEE
CCCCCCCCCEEEECC
43.26UniProtKB CARBOHYD
453 (in isoform 2)Ubiquitination-15.25-
461 (in isoform 2)Ubiquitination-64.48-
491PhosphorylationMCVCDDGYTGEDCRD
EEEECCCCCCCCCCC
20.68-
616PhosphorylationCICNEGYSGEDCSEV
EEECCCCCCCCCCCC
46.7126657352
719AcetylationLPAPEGLKFKSIKET
ECCCCCCCCCCCEEC
62.7011922513
788N-linked_GlycosylationISLHIVKNNTRGPGL
EEEEEEECCCCCCCC
44.18UniProtKB CARBOHYD
799PhosphorylationGPGLKRVTTTRLDAP
CCCCEEEEECCCCCC
26.8723312004
800PhosphorylationPGLKRVTTTRLDAPS
CCCEEEEECCCCCCC
13.6828857561
801PhosphorylationGLKRVTTTRLDAPSQ
CCEEEEECCCCCCCC
21.6223312004
859PhosphorylationTEDENQYSIGNLKPD
CCCCCEEECCCCCCC
17.7922210691
872PhosphorylationPDTEYEVSLISRRGD
CCCCEEEEEEECCCC
14.1922210691
875PhosphorylationEYEVSLISRRGDMSS
CEEEEEEECCCCCCC
22.6324719451
903PhosphorylationPRNLRRVSQTDNSIT
CCCCCCCCCCCCCEE
26.0828857561
905PhosphorylationNLRRVSQTDNSITLE
CCCCCCCCCCCEEEE
29.6423936043
908PhosphorylationRVSQTDNSITLEWRN
CCCCCCCCEEEEECC
21.5428857561
953PhosphorylationATTKTTLTGLRPGTE
CCCEEECCCCCCCCC
31.8824719451
1007PhosphorylationSLTLLWKTPLAKFDR
HEEEEECCCCHHCCE
16.38-
1018N-linked_GlycosylationKFDRYRLNYSLPTGQ
HCCEEEEEEECCCCC
18.4919159218
1019PhosphorylationFDRYRLNYSLPTGQW
CCEEEEEEECCCCCE
19.04-
1020PhosphorylationDRYRLNYSLPTGQWV
CEEEEEEECCCCCEE
27.14-
1023PhosphorylationRLNYSLPTGQWVGVQ
EEEEECCCCCEEEEE
47.50-
1034N-linked_GlycosylationVGVQLPRNTTSYVLR
EEEECCCCCCCEEEC
45.8519159218
1035O-linked_GlycosylationGVQLPRNTTSYVLRG
EEECCCCCCCEEECC
20.5623301498
1037O-linked_GlycosylationQLPRNTTSYVLRGLE
ECCCCCCCEEECCCC
15.9423301498
1079N-linked_GlycosylationEQAPELENLTVTEVG
CCCCCHHCCEEEEEE
54.3518780401
1093N-linked_GlycosylationGWDGLRLNWTAADQA
ECCCEEEECCHHHHH
27.8418780401
1119N-linked_GlycosylationNKVEAARNLTVPGSL
CCHHHHHCCCCCCCC
35.02UniProtKB CARBOHYD
1138PhosphorylationIPGLKAATPYTVSIY
CCCCCCCCCEEEEEE
22.9928270605
1140PhosphorylationGLKAATPYTVSIYGV
CCCCCCCEEEEEEEE
18.5428270605
1141PhosphorylationLKAATPYTVSIYGVI
CCCCCCEEEEEEEEE
14.6928270605
1143PhosphorylationAATPYTVSIYGVIQG
CCCCEEEEEEEEECC
11.4228270605
1145PhosphorylationTPYTVSIYGVIQGYR
CCEEEEEEEEECCCC
9.6128270605
1184N-linked_GlycosylationGWDALKLNWTAPEGA
ECCEEECCEECCCCC
32.2519159218
1210N-linked_GlycosylationDTVEAAQNLTVPGGL
CCHHHHHCCCCCCCC
32.71UniProtKB CARBOHYD
1261N-linked_GlycosylationEEVPDMGNLTVTEVS
CCCCCCCCEEEEEEE
26.3818780401
1265O-linked_GlycosylationDMGNLTVTEVSWDAL
CCCCEEEEEEEECEE
25.98OGP
1275N-linked_GlycosylationSWDALRLNWTTPDGT
EECEEECCEECCCCC
27.8419159218
1301N-linked_GlycosylationDQVEEAHNLTVPGSL
HHHHHHHCCCCCCCC
44.4418780401
1310PhosphorylationTVPGSLRSMEIPGLR
CCCCCCEECCCCCCC
26.5127251275
1366N-linked_GlycosylationGWDGLRLNWTAADNA
CCCCEEEEEEECCCH
27.8419159218
1392N-linked_GlycosylationNKVEAAQNLTLPGSL
CCEEHHHCCCCCCCE
30.21UniProtKB CARBOHYD
1394PhosphorylationVEAAQNLTLPGSLRA
EEHHHCCCCCCCEEE
38.1626074081
1398PhosphorylationQNLTLPGSLRAVDIP
HCCCCCCCEEEEECC
16.8526074081
1411PhosphorylationIPGLEAATPYRVSIY
CCCCCCCCCEEEEEE
28.0922210691
1413PhosphorylationGLEAATPYRVSIYGV
CCCCCCCEEEEEEEE
21.2022210691
1418PhosphorylationTPYRVSIYGVIRGYR
CCEEEEEEEEECCCC
9.61-
1445N-linked_GlycosylationEPEIGNLNVSDITPE
CCCCCCCCHHHCCCC
34.93UniProtKB CARBOHYD
1455N-linked_GlycosylationDITPESFNLSWMATD
HCCCCCCCEEEEECC
42.30UniProtKB CARBOHYD
1469O-linked_GlycosylationDGIFETFTIEIIDSN
CCCCEEEEEEEECCC
25.72OGP
1485N-linked_GlycosylationLLETVEYNISGAERT
EEEEEEEECCCHHHE
14.4018780401
1492PhosphorylationNISGAERTAHISGLP
ECCCHHHEEECCCCC
17.69-
1502PhosphorylationISGLPPSTDFIVYLS
CCCCCCCCCEEEEEC
40.48-
1534N-linked_GlycosylationEALPLLENLTISDIN
CHHHHHHCCEECCCC
42.31UniProtKB CARBOHYD
1678PhosphorylationPERTRDITGLREATE
CCCCCCCCCCCCCEE
34.1624719451
1699PhosphorylationGISKGRRSQTVSAIA
EECCCCCCCCHHHHH
28.92-
1701PhosphorylationSKGRRSQTVSAIATT
CCCCCCCCHHHHHHH
20.06-
1703PhosphorylationGRRSQTVSAIATTAM
CCCCCCHHHHHHHCC
19.83-
1729PhosphorylationTENSATVSWRAPTAQ
CCCCCEEEEECCCCE
13.3922210691
1751PhosphorylationYVPITGGTPSMVTVD
EEECCCCCCCEEEEC
17.34-
1760PhosphorylationSMVTVDGTKTQTRLV
CEEEECCCCCCEEEE
26.84-
1775PhosphorylationKLIPGVEYLVSIIAM
HHCCCHHHHHHHHHC
15.25-
1778PhosphorylationPGVEYLVSIIAMKGF
CCHHHHHHHHHCCCC
12.9922496350
1809N-linked_GlycosylationPSGLVTANITDSEAL
CCCEEEECCCCHHHH
28.4716335952
1825O-linked_GlycosylationRWQPAIATVDSYVIS
HCCCEEEEECEEEEE
20.80OGP
1842PhosphorylationGEKVPEITRTVSGNT
CCCCCEEEEEECCCE
20.73-
1844PhosphorylationKVPEITRTVSGNTVE
CCCEEEEEECCCEEE
15.46-
1846PhosphorylationPEITRTVSGNTVEYA
CEEEEEECCCEEEEE
26.22-
1864PhosphorylationLEPATEYTLRIFAEK
CCCCCEEEEEEEEEC
11.8824719451
1878PhosphorylationKGPQKSSTITAKFTT
CCCCCCCEEEEEEEC
29.4522817900
1885PhosphorylationTITAKFTTDLDSPRD
EEEEEEECCCCCCCC
37.3822817900
1889PhosphorylationKFTTDLDSPRDLTAT
EEECCCCCCCCCCCC
29.1822817900
1902PhosphorylationATEVQSETALLTWRP
CCEECCCEEEEEECC
28.0520166139
1906PhosphorylationQSETALLTWRPPRAS
CCCEEEEEECCCCCE
21.9320166139
1937PhosphorylationEVIVGPDTTSYSLAD
EEEECCCCCCCCHHC
22.3028270605
1938PhosphorylationVIVGPDTTSYSLADL
EEECCCCCCCCHHCC
32.8028270605
1939PhosphorylationIVGPDTTSYSLADLS
EECCCCCCCCHHCCC
18.1528270605
1940PhosphorylationVGPDTTSYSLADLSP
ECCCCCCCCHHCCCC
12.9528270605
1941PhosphorylationGPDTTSYSLADLSPS
CCCCCCCCHHCCCCC
19.4928270605
1946PhosphorylationSYSLADLSPSTHYTA
CCCHHCCCCCCCHHH
19.8328270605
1948PhosphorylationSLADLSPSTHYTAKI
CHHCCCCCCCHHHHH
25.1728270605
1949PhosphorylationLADLSPSTHYTAKIQ
HHCCCCCCCHHHHHH
23.4528270605
1951PhosphorylationDLSPSTHYTAKIQAL
CCCCCCCHHHHHHHH
14.4228270605
1952PhosphorylationLSPSTHYTAKIQALN
CCCCCCHHHHHHHHC
17.5528270605
2070PhosphorylationKITAQGQYELRVDLR
CEECCCEEEEEEECC
24.61-
2129PhosphorylationFSTFDKDTDSAITNC
CCCCCCCCCCHHHHH
37.28-
2134PhosphorylationKDTDSAITNCALSYK
CCCCCHHHHHHHHCC
24.7825867546
2139PhosphorylationAITNCALSYKGAFWY
HHHHHHHHCCCCEEE
13.2825867546
2140PhosphorylationITNCALSYKGAFWYR
HHHHHHHCCCCEEEC
17.8125867546
2162N-linked_GlycosylationMGRYGDNNHSQGVNW
EEEECCCCCCCCCCE
40.7118780401

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
72SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TENA_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 TENA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCAN_HUMANNCANphysical
9341124

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615629Deafness, autosomal dominant, 56 (DFNA56)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TENA_HUMAN

loading...

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-1018; ASN-1034; ASN-1184;ASN-1275; ASN-1301; ASN-1366 AND ASN-1485, AND MASS SPECTROMETRY.
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-1079; ASN-1093;ASN-1261; ASN-1301; ASN-1485 AND ASN-2162, AND MASS SPECTROMETRY.
"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-1809, AND MASSSPECTROMETRY.

TOP