TENN_HUMAN - dbPTM
TENN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TENN_HUMAN
UniProt AC Q9UQP3
Protein Name Tenascin-N {ECO:0000312|HGNC:HGNC:22942}
Gene Name TNN {ECO:0000312|HGNC:HGNC:22942}
Organism Homo sapiens (Human).
Sequence Length 1299
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description Extracellular matrix protein that seems to be a ligand for ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity). [PubMed: 17909022 Involved in neurite outgrowth and cell migration in hippocampal explants (By similarity During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (By similarity In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells]
Protein Sequence MSLQEMFRFPMGLLLGSVLLVASAPATLEPPGCSNKEQQVTVSHTYKIDVPKSALVQVDADPQPLSDDGASLLALGEAREEQNIIFRHNIRLQTPQKDCELAGSVQDLLARVKKLEEEMVEMKEQCSAQRCCQGVTDLSRHCSGHGTFSLETCSCHCEEGREGPACERLACPGACSGHGRCVDGRCLCHEPYVGADCGYPACPENCSGHGECVRGVCQCHEDFMSEDCSEKRCPGDCSGHGFCDTGECYCEEGFTGLDCAQVVTPQGLQLLKNTEDSLLVSWEPSSQVDHYLLSYYPLGKELSGKQIQVPKEQHSYEILGLLPGTKYIVTLRNVKNEVSSSPQHLLATTDLAVLGTAWVTDETENSLDVEWENPSTEVDYYKLRYGPMTGQEVAEVTVPKSSDPKSRYDITGLHPGTEYKITVVPMRGELEGKPILLNGRTEIDSPTNVVTDRVTEDTATVSWDPVQAVIDKYVVRYTSADGDTKEMAVHKDESSTVLTGLKPGEAYKVYVWAERGNQGSKKADTNALTEIDSPANLVTDRVTENTATISWDPVQATIDKYVVRYTSADDQETREVLVGKEQSSTVLTGLRPGVEYTVHVWAQKGDRESKKADTNAPTDIDSPKNLVTDRVTENMATVSWDPVQAAIDKYVVRYTSAGGETREVPVGKEQSSTVLTGLRPGMEYMVHVWAQKGDQESKKADTKAQTDIDSPQNLVTDRVTENMATVSWDPVRATIDRYVVRYTSAKDGETREVPVGKEQSSTVLTGLRPGVEYTVHVWAQKGAQESKKADTKAQTDIDSPQNLVTDWVTENTATVSWDPVQATIDRYVVHYTSANGETREVPVGKEQSSTVLTGLRPGMEYTVHVWAQKGNQESKKADTKAQTEIDGPKNLVTDWVTENMATVSWDPVQATIDKYMVRYTSADGETREVPVGKEHSSTVLTGLRPGMEYMVHVWAQKGAQESKKADTKAQTELDPPRNLRPSAVTQSGGILTWTPPSAQIHGYILTYQFPDGTVKEMQLGREDQRFALQGLEQGATYPVSLVAFKGGRRSRNVSTTLSTVGARFPHPSDCSQVQQNSNAASGLYTIYLHGDASRPLQVYCDMETDGGGWIVFQRRNTGQLDFFKRWRSYVEGFGDPMKEFWLGLDKLHNLTTGTPARYEVRVDLQTANESAYAIYDFFQVASSKERYKLTVGKYRGTAGDALTYHNGWKFTTFDRDNDIALSNCALTHHGGWWYKNCHLANPNGRYGETKHSEGVNWEPWKGHEFSIPYVELKIRPHGYSREPVLGRKKRTLRGRLRTF
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
27O-linked_GlycosylationLVASAPATLEPPGCS
HHCCCCCCCCCCCCC		30.51OGP
41PhosphorylationSNKEQQVTVSHTYKI
CCCCEEEEEEEEEEC		16.3820446291
127PhosphorylationVEMKEQCSAQRCCQG
HHHHHHHHHHHHHCC		27.42-
136PhosphorylationQRCCQGVTDLSRHCS
HHHHCCHHHHHHHHC		37.74-
139PhosphorylationCQGVTDLSRHCSGHG
HCCHHHHHHHHCCCC		23.84-
225PhosphorylationQCHEDFMSEDCSEKR
HCCHHHCCCCCCCCC		30.2122468782
229PhosphorylationDFMSEDCSEKRCPGD
HHCCCCCCCCCCCCC		59.4822468782
385PhosphorylationVDYYKLRYGPMTGQE
EEEEEEEECCCCCCE		35.70-
419PhosphorylationGLHPGTEYKITVVPM
CCCCCCEEEEEEEEC		13.9220736484
458PhosphorylationTDRVTEDTATVSWDP
ECCCCCCCCEECCCH		20.28-
479PhosphorylationKYVVRYTSADGDTKE
EEEEEEECCCCCCCE		18.54-
491UbiquitinationTKEMAVHKDESSTVL
CCEEEEECCCCCCEE		57.50-
494PhosphorylationMAVHKDESSTVLTGL
EEEECCCCCCEECCC		41.2524719451
502UbiquitinationSTVLTGLKPGEAYKV
CCEECCCCCCCEEEE		52.93-
507PhosphorylationGLKPGEAYKVYVWAE
CCCCCCEEEEEEEEE		9.1824719451
525PhosphorylationQGSKKADTNALTEID
CCCCCCCCCCCCCCC		27.53-
529PhosphorylationKADTNALTEIDSPAN
CCCCCCCCCCCCCHH		28.60-
543PhosphorylationNLVTDRVTENTATIS
HCCEECCCCCCEEEE		25.14-
565PhosphorylationIDKYVVRYTSADDQE
EEEEEEEECCCCCHH		8.0819664994
588PhosphorylationEQSSTVLTGLRPGVE
CCCCCEECCCCCCCE		29.8124719451
656PhosphorylationKYVVRYTSAGGETRE
EEEEEEECCCCCEEE		18.9125954137
661PhosphorylationYTSAGGETREVPVGK
EECCCCCEEEECCCC		35.0925954137
676PhosphorylationEQSSTVLTGLRPGME
CCCCCEECCCCCCCE		29.8124719451
684PhosphorylationGLRPGMEYMVHVWAQ
CCCCCCEEEEEEEEC		8.78-
706PhosphorylationKADTKAQTDIDSPQN
HCCCCCCCCCCCCHH		39.52-
710PhosphorylationKAQTDIDSPQNLVTD
CCCCCCCCCHHHCCH		28.81-
716PhosphorylationDSPQNLVTDRVTENM
CCCHHHCCHHHHCCC		22.66-
765PhosphorylationEQSSTVLTGLRPGVE
CCCCCEECCCCCCCE		29.8124719451
795PhosphorylationKADTKAQTDIDSPQN
HCCCCCCCCCCCCCC		39.52-
799PhosphorylationKAQTDIDSPQNLVTD
CCCCCCCCCCCCCCC		28.81-
853PhosphorylationEQSSTVLTGLRPGME
CCCCCEECCCCCCCE		29.8124719451
936PhosphorylationVPVGKEHSSTVLTGL
ECCCCCCCCCEECCC		28.8826552605
937PhosphorylationPVGKEHSSTVLTGLR
CCCCCCCCCEECCCC		25.1726552605
938PhosphorylationVGKEHSSTVLTGLRP
CCCCCCCCEECCCCC		23.6626552605
941PhosphorylationEHSSTVLTGLRPGME
CCCCCEECCCCCCCC		29.8124719451
949PhosphorylationGLRPGMEYMVHVWAQ
CCCCCCCHHHHHHHH		8.7826552605
1149N-linked_GlycosylationLGLDKLHNLTTGTPA
HCHHHHCCCCCCCCC		49.9016335952
1172PhosphorylationQTANESAYAIYDFFQ
ECCCHHHHHHHHHHH		11.65-
1187PhosphorylationVASSKERYKLTVGKY
HHCCCCCEEEEEEEC		16.08-
1194PhosphorylationYKLTVGKYRGTAGDA
EEEEEEECCCCCCCC		14.35-
1204PhosphorylationTAGDALTYHNGWKFT
CCCCCEEEECCEEEE		8.30-
1289UbiquitinationEPVLGRKKRTLRGRL
CCCCCCCCCCHHHHC		49.61-
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 TENN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of TENN_HUMAN !!
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 TENN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-1149, AND MASSSPECTROMETRY.

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