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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Phosphorylation | ---MGAMTQLLAGVF ---CCHHHHHHHHHH | 18.61 | 24043423 | |
20 | Phosphorylation | LAFLALATEGGVLKK HHHHHHHHCCCHHHH | 35.69 | 24043423 | |
38 | N-linked_Glycosylation | HKRQSGVNATLPEEN HHHHCCCCCCCCCCC | 30.63 | UniProtKB CARBOHYD | |
62 | Phosphorylation | NIKLPVGSQCSVDLE EEECCCCCCEEEECH | 28.40 | 23927012 | |
65 | Phosphorylation | LPVGSQCSVDLESAS CCCCCCEEEECHHCC | 15.84 | 22777824 | |
70 | Phosphorylation | QCSVDLESASGEKDL CEEEECHHCCCCCCC | 34.72 | 29255136 | |
72 | Phosphorylation | SVDLESASGEKDLAP EEECHHCCCCCCCCC | 57.68 | 29255136 | |
81 | O-linked_Glycosylation | EKDLAPPSEPSESFQ CCCCCCCCCCCHHHH | 62.17 | OGP | |
81 | Phosphorylation | EKDLAPPSEPSESFQ CCCCCCCCCCCHHHH | 62.17 | 26657352 | |
84 | O-linked_Glycosylation | LAPPSEPSESFQEHT CCCCCCCCHHHHEEC | 41.65 | OGP | |
84 | Phosphorylation | LAPPSEPSESFQEHT CCCCCCCCHHHHEEC | 41.65 | 26657352 | |
86 | Phosphorylation | PPSEPSESFQEHTVD CCCCCCHHHHEECCC | 36.25 | 26657352 | |
91 | O-linked_Glycosylation | SESFQEHTVDGENQI CHHHHEECCCCCCEE | 21.38 | OGP | |
91 | Phosphorylation | SESFQEHTVDGENQI CHHHHEECCCCCCEE | 21.38 | 28348404 | |
124 | Phosphorylation | PDVKELLSRLEELEN CCHHHHHHHHHHHHH | 47.66 | 24719451 | |
134 | Phosphorylation | EELENLVSSLREQCT HHHHHHHHHHHHHHH | 27.16 | 24719451 | |
135 | Phosphorylation | ELENLVSSLREQCTA HHHHHHHHHHHHHHC | 24.78 | 24719451 | |
166 | N-linked_Glycosylation | PFCSGRGNFSTEGCG CCCCCCCCCCCCCCC | 26.74 | UniProtKB CARBOHYD | |
168 | Phosphorylation | CSGRGNFSTEGCGCV CCCCCCCCCCCCCCE | 29.55 | 26657352 | |
169 | Phosphorylation | SGRGNFSTEGCGCVC CCCCCCCCCCCCCEE | 32.05 | 26657352 | |
184 | N-linked_Glycosylation | EPGWKGPNCSEPECP CCCCCCCCCCCCCCC | 51.09 | 18780401 | |
257 | Phosphorylation | EICPVPCSEEHGTCV EECCCCCCCCCCCEE | 39.69 | 27251275 | |
327 | N-linked_Glycosylation | FDRGRCINGTCYCEE CCCCCCCCCEEEECC | 43.26 | UniProtKB CARBOHYD | |
453 (in isoform 2) | Ubiquitination | - | 15.25 | - | |
461 (in isoform 2) | Ubiquitination | - | 64.48 | - | |
491 | Phosphorylation | MCVCDDGYTGEDCRD EEEECCCCCCCCCCC | 20.68 | - | |
616 | Phosphorylation | CICNEGYSGEDCSEV EEECCCCCCCCCCCC | 46.71 | 26657352 | |
719 | Acetylation | LPAPEGLKFKSIKET ECCCCCCCCCCCEEC | 62.70 | 11922513 | |
788 | N-linked_Glycosylation | ISLHIVKNNTRGPGL EEEEEEECCCCCCCC | 44.18 | UniProtKB CARBOHYD | |
799 | Phosphorylation | GPGLKRVTTTRLDAP CCCCEEEEECCCCCC | 26.87 | 23312004 | |
800 | Phosphorylation | PGLKRVTTTRLDAPS CCCEEEEECCCCCCC | 13.68 | 28857561 | |
801 | Phosphorylation | GLKRVTTTRLDAPSQ CCEEEEECCCCCCCC | 21.62 | 23312004 | |
859 | Phosphorylation | TEDENQYSIGNLKPD CCCCCEEECCCCCCC | 17.79 | 22210691 | |
872 | Phosphorylation | PDTEYEVSLISRRGD CCCCEEEEEEECCCC | 14.19 | 22210691 | |
875 | Phosphorylation | EYEVSLISRRGDMSS CEEEEEEECCCCCCC | 22.63 | 24719451 | |
903 | Phosphorylation | PRNLRRVSQTDNSIT CCCCCCCCCCCCCEE | 26.08 | 28857561 | |
905 | Phosphorylation | NLRRVSQTDNSITLE CCCCCCCCCCCEEEE | 29.64 | 23936043 | |
908 | Phosphorylation | RVSQTDNSITLEWRN CCCCCCCCEEEEECC | 21.54 | 28857561 | |
953 | Phosphorylation | ATTKTTLTGLRPGTE CCCEEECCCCCCCCC | 31.88 | 24719451 | |
1007 | Phosphorylation | SLTLLWKTPLAKFDR HEEEEECCCCHHCCE | 16.38 | - | |
1018 | N-linked_Glycosylation | KFDRYRLNYSLPTGQ HCCEEEEEEECCCCC | 18.49 | 19159218 | |
1019 | Phosphorylation | FDRYRLNYSLPTGQW CCEEEEEEECCCCCE | 19.04 | - | |
1020 | Phosphorylation | DRYRLNYSLPTGQWV CEEEEEEECCCCCEE | 27.14 | - | |
1023 | Phosphorylation | RLNYSLPTGQWVGVQ EEEEECCCCCEEEEE | 47.50 | - | |
1034 | N-linked_Glycosylation | VGVQLPRNTTSYVLR EEEECCCCCCCEEEC | 45.85 | 19159218 | |
1035 | O-linked_Glycosylation | GVQLPRNTTSYVLRG EEECCCCCCCEEECC | 20.56 | 23301498 | |
1037 | O-linked_Glycosylation | QLPRNTTSYVLRGLE ECCCCCCCEEECCCC | 15.94 | 23301498 | |
1079 | N-linked_Glycosylation | EQAPELENLTVTEVG CCCCCHHCCEEEEEE | 54.35 | 18780401 | |
1093 | N-linked_Glycosylation | GWDGLRLNWTAADQA ECCCEEEECCHHHHH | 27.84 | 18780401 | |
1119 | N-linked_Glycosylation | NKVEAARNLTVPGSL CCHHHHHCCCCCCCC | 35.02 | UniProtKB CARBOHYD | |
1138 | Phosphorylation | IPGLKAATPYTVSIY CCCCCCCCCEEEEEE | 22.99 | 28270605 | |
1140 | Phosphorylation | GLKAATPYTVSIYGV CCCCCCCEEEEEEEE | 18.54 | 28270605 | |
1141 | Phosphorylation | LKAATPYTVSIYGVI CCCCCCEEEEEEEEE | 14.69 | 28270605 | |
1143 | Phosphorylation | AATPYTVSIYGVIQG CCCCEEEEEEEEECC | 11.42 | 28270605 | |
1145 | Phosphorylation | TPYTVSIYGVIQGYR CCEEEEEEEEECCCC | 9.61 | 28270605 | |
1184 | N-linked_Glycosylation | GWDALKLNWTAPEGA ECCEEECCEECCCCC | 32.25 | 19159218 | |
1210 | N-linked_Glycosylation | DTVEAAQNLTVPGGL CCHHHHHCCCCCCCC | 32.71 | UniProtKB CARBOHYD | |
1261 | N-linked_Glycosylation | EEVPDMGNLTVTEVS CCCCCCCCEEEEEEE | 26.38 | 18780401 | |
1265 | O-linked_Glycosylation | DMGNLTVTEVSWDAL CCCCEEEEEEEECEE | 25.98 | OGP | |
1275 | N-linked_Glycosylation | SWDALRLNWTTPDGT EECEEECCEECCCCC | 27.84 | 19159218 | |
1301 | N-linked_Glycosylation | DQVEEAHNLTVPGSL HHHHHHHCCCCCCCC | 44.44 | 18780401 | |
1310 | Phosphorylation | TVPGSLRSMEIPGLR CCCCCCEECCCCCCC | 26.51 | 27251275 | |
1366 | N-linked_Glycosylation | GWDGLRLNWTAADNA CCCCEEEEEEECCCH | 27.84 | 19159218 | |
1392 | N-linked_Glycosylation | NKVEAAQNLTLPGSL CCEEHHHCCCCCCCE | 30.21 | UniProtKB CARBOHYD | |
1394 | Phosphorylation | VEAAQNLTLPGSLRA EEHHHCCCCCCCEEE | 38.16 | 26074081 | |
1398 | Phosphorylation | QNLTLPGSLRAVDIP HCCCCCCCEEEEECC | 16.85 | 26074081 | |
1411 | Phosphorylation | IPGLEAATPYRVSIY CCCCCCCCCEEEEEE | 28.09 | 22210691 | |
1413 | Phosphorylation | GLEAATPYRVSIYGV CCCCCCCEEEEEEEE | 21.20 | 22210691 | |
1418 | Phosphorylation | TPYRVSIYGVIRGYR CCEEEEEEEEECCCC | 9.61 | - | |
1445 | N-linked_Glycosylation | EPEIGNLNVSDITPE CCCCCCCCHHHCCCC | 34.93 | UniProtKB CARBOHYD | |
1455 | N-linked_Glycosylation | DITPESFNLSWMATD HCCCCCCCEEEEECC | 42.30 | UniProtKB CARBOHYD | |
1469 | O-linked_Glycosylation | DGIFETFTIEIIDSN CCCCEEEEEEEECCC | 25.72 | OGP | |
1485 | N-linked_Glycosylation | LLETVEYNISGAERT EEEEEEEECCCHHHE | 14.40 | 18780401 | |
1492 | Phosphorylation | NISGAERTAHISGLP ECCCHHHEEECCCCC | 17.69 | - | |
1502 | Phosphorylation | ISGLPPSTDFIVYLS CCCCCCCCCEEEEEC | 40.48 | - | |
1534 | N-linked_Glycosylation | EALPLLENLTISDIN CHHHHHHCCEECCCC | 42.31 | UniProtKB CARBOHYD | |
1678 | Phosphorylation | PERTRDITGLREATE CCCCCCCCCCCCCEE | 34.16 | 24719451 | |
1699 | Phosphorylation | GISKGRRSQTVSAIA EECCCCCCCCHHHHH | 28.92 | - | |
1701 | Phosphorylation | SKGRRSQTVSAIATT CCCCCCCCHHHHHHH | 20.06 | - | |
1703 | Phosphorylation | GRRSQTVSAIATTAM CCCCCCHHHHHHHCC | 19.83 | - | |
1729 | Phosphorylation | TENSATVSWRAPTAQ CCCCCEEEEECCCCE | 13.39 | 22210691 | |
1751 | Phosphorylation | YVPITGGTPSMVTVD EEECCCCCCCEEEEC | 17.34 | - | |
1760 | Phosphorylation | SMVTVDGTKTQTRLV CEEEECCCCCCEEEE | 26.84 | - | |
1775 | Phosphorylation | KLIPGVEYLVSIIAM HHCCCHHHHHHHHHC | 15.25 | - | |
1778 | Phosphorylation | PGVEYLVSIIAMKGF CCHHHHHHHHHCCCC | 12.99 | 22496350 | |
1809 | N-linked_Glycosylation | PSGLVTANITDSEAL CCCEEEECCCCHHHH | 28.47 | 16335952 | |
1825 | O-linked_Glycosylation | RWQPAIATVDSYVIS HCCCEEEEECEEEEE | 20.80 | OGP | |
1842 | Phosphorylation | GEKVPEITRTVSGNT CCCCCEEEEEECCCE | 20.73 | - | |
1844 | Phosphorylation | KVPEITRTVSGNTVE CCCEEEEEECCCEEE | 15.46 | - | |
1846 | Phosphorylation | PEITRTVSGNTVEYA CEEEEEECCCEEEEE | 26.22 | - | |
1864 | Phosphorylation | LEPATEYTLRIFAEK CCCCCEEEEEEEEEC | 11.88 | 24719451 | |
1878 | Phosphorylation | KGPQKSSTITAKFTT CCCCCCCEEEEEEEC | 29.45 | 22817900 | |
1885 | Phosphorylation | TITAKFTTDLDSPRD EEEEEEECCCCCCCC | 37.38 | 22817900 | |
1889 | Phosphorylation | KFTTDLDSPRDLTAT EEECCCCCCCCCCCC | 29.18 | 22817900 | |
1902 | Phosphorylation | ATEVQSETALLTWRP CCEECCCEEEEEECC | 28.05 | 20166139 | |
1906 | Phosphorylation | QSETALLTWRPPRAS CCCEEEEEECCCCCE | 21.93 | 20166139 | |
1937 | Phosphorylation | EVIVGPDTTSYSLAD EEEECCCCCCCCHHC | 22.30 | 28270605 | |
1938 | Phosphorylation | VIVGPDTTSYSLADL EEECCCCCCCCHHCC | 32.80 | 28270605 | |
1939 | Phosphorylation | IVGPDTTSYSLADLS EECCCCCCCCHHCCC | 18.15 | 28270605 | |
1940 | Phosphorylation | VGPDTTSYSLADLSP ECCCCCCCCHHCCCC | 12.95 | 28270605 | |
1941 | Phosphorylation | GPDTTSYSLADLSPS CCCCCCCCHHCCCCC | 19.49 | 28270605 | |
1946 | Phosphorylation | SYSLADLSPSTHYTA CCCHHCCCCCCCHHH | 19.83 | 28270605 | |
1948 | Phosphorylation | SLADLSPSTHYTAKI CHHCCCCCCCHHHHH | 25.17 | 28270605 | |
1949 | Phosphorylation | LADLSPSTHYTAKIQ HHCCCCCCCHHHHHH | 23.45 | 28270605 | |
1951 | Phosphorylation | DLSPSTHYTAKIQAL CCCCCCCHHHHHHHH | 14.42 | 28270605 | |
1952 | Phosphorylation | LSPSTHYTAKIQALN CCCCCCHHHHHHHHC | 17.55 | 28270605 | |
2070 | Phosphorylation | KITAQGQYELRVDLR CEECCCEEEEEEECC | 24.61 | - | |
2129 | Phosphorylation | FSTFDKDTDSAITNC CCCCCCCCCCHHHHH | 37.28 | - | |
2134 | Phosphorylation | KDTDSAITNCALSYK CCCCCHHHHHHHHCC | 24.78 | 25867546 | |
2139 | Phosphorylation | AITNCALSYKGAFWY HHHHHHHHCCCCEEE | 13.28 | 25867546 | |
2140 | Phosphorylation | ITNCALSYKGAFWYR HHHHHHHCCCCEEEC | 17.81 | 25867546 | |
2162 | N-linked_Glycosylation | MGRYGDNNHSQGVNW EEEECCCCCCCCCCE | 40.71 | 18780401 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
72 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TENA_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NCAN_HUMAN | NCAN | physical | 9341124 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615629 | Deafness, autosomal dominant, 56 (DFNA56) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"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. |