TSP1_HUMAN - dbPTM
TSP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSP1_HUMAN
UniProt AC P07996
Protein Name Thrombospondin-1
Gene Name THBS1
Organism Homo sapiens (Human).
Sequence Length 1170
Subcellular Localization Secreted . Cell surface . Secreted, extracellular space, extracellular matrix . Endoplasmic reticulum . Sarcoplasmic reticulum . Secreted by thrombin-activated platelets and binds to the cell surface in the presence of extracellular Ca(2+) (PubMed:67
Protein Description Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Binds heparin. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp (By similarity). Ligand for CD36 mediating antiangiogenic properties. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors (By similarity)..
Protein Sequence MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRKVTEENKELANELRRPPLCYHNGVQYRNNEEWTVDSCTECHCQNSVTICKKVSCPIMPCSNATVPDGECCPRCWPSDSADDGWSPWSEWTSCSTSCGNGIQQRGRSCDSLNNRCEGSSVQTRTCHIQECDKRFKQDGGWSHWSPWSSCSVTCGDGVITRIRLCNSPSPQMNGKPCEGEARETKACKKDACPINGGWGPWSPWDICSVTCGGGVQKRSRLCNNPTPQFGGKDCVGDVTENQICNKQDCPIDGCLSNPCFAGVKCTSYPDGSWKCGACPPGYSGNGIQCTDVDECKEVPDACFNHNGEHRCENTDPGYNCLPCPPRFTGSQPFGQGVEHATANKQVCKPRNPCTDGTHDCNKNAKCNYLGHYSDPMYRCECKPGYAGNGIICGEDTDLDGWPNENLVCVANATYHCKKDNCPNLPNSGQEDYDKDGIGDACDDDDDNDKIPDDRDNCPFHYNPAQYDYDRDDVGDRCDNCPYNHNPDQADTDNNGEGDACAADIDGDGILNERDNCQYVYNVDQRDTDMDGVGDQCDNCPLEHNPDQLDSDSDRIGDTCDNNQDIDEDGHQNNLDNCPYVPNANQADHDKDGKGDACDHDDDNDGIPDDKDNCRLVPNPDQKDSDGDGRGDACKDDFDHDSVPDIDDICPENVDISETDFRRFQMIPLDPKGTSQNDPNWVVRHQGKELVQTVNCDPGLAVGYDEFNAVDFSGTFFINTERDDDYAGFVFGYQSSSRFYVVMWKQVTQSYWDTNPTRAQGYSGLSVKVVNSTTGPGEHLRNALWHTGNTPGQVRTLWHDPRHIGWKDFTAYRWRLSHRPKTGFIRVVMYEGKKIMADSGPIYDKTYAGGRLGLFVFSQEMVFFSDLKYECRDP
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
18PhosphorylationFLMHVCGTNRIPESG
HHHHHHCCCCCCCCC		19.0524043423
55PhosphorylationLVKGPDPSSPAFRIE
CCCCCCCCCCCCEEE		57.2328060719
56PhosphorylationVKGPDPSSPAFRIED
CCCCCCCCCCCEEEC		26.1524719451
93PhosphorylationKGFLLLASLRQMKKT
CHHHHHHHHHHHHHH		24.8524719451
150O-linked_GlycosylationVEEALLATGQWKSIT
HHHHHHHCCCCEEEE		29.8522403705
173UbiquitinationQLYIDCEKMENAELD
EEEEEHHHHHCCCCC		58.82-
174SulfoxidationLYIDCEKMENAELDV
EEEEHHHHHCCCCCC		1.9330846556
193PhosphorylationVFTRDLASIARLRIA
HHHHHHHHHHHHHHH		24.8728060719
221PhosphorylationNVRFVFGTTPEDILR
HCEEEECCCHHHHHH		27.9330087585
248N-linked_GlycosylationTLDNNVVNGSSPAIR
EECCCCCCCCCCCCC		40.1018065761
262UbiquitinationRTNYIGHKTKDLQAI
CCCCCCCCCCCHHHH		52.6529967540
289O-linked_GlycosylationLELRGLRTIVTTLQD
HHHCCHHHHHHHHHH		25.4955826671
292O-linked_GlycosylationRGLRTIVTTLQDSIR
CCHHHHHHHHHHHHH		20.2455826677
293O-linked_GlycosylationGLRTIVTTLQDSIRK
CHHHHHHHHHHHHHH		16.1355826683
302O-linked_GlycosylationQDSIRKVTEENKELA
HHHHHHHHHHHHHHH		40.3955833239
306UbiquitinationRKVTEENKELANELR
HHHHHHHHHHHHHHC		58.3429967540
319PhosphorylationLRRPPLCYHNGVQYR
HCCCCCCEECCEECC		13.15-
360N-linked_GlycosylationCPIMPCSNATVPDGE
CCEECCCCCCCCCCC		46.47UniProtKB CARBOHYD
385C-linked_GlycosylationADDGWSPWSEWTSCS
CCCCCCCHHHCCCCC		11.9011067851
385C-linked_GlycosylationADDGWSPWSEWTSCS
CCCCCCCHHHCCCCC		11.9011067851
394O-linked_GlycosylationEWTSCSTSCGNGIQQ
HCCCCCCCCCCCHHH		12.0611067851
394O-linked_GlycosylationEWTSCSTSCGNGIQQ
HCCCCCCCCCCCHHH		12.0611067851
405PhosphorylationGIQQRGRSCDSLNNR
CHHHCCCCCHHCCCC		25.7128270605
408PhosphorylationQRGRSCDSLNNRCEG
HCCCCCHHCCCCCCC		37.0128270605
416PhosphorylationLNNRCEGSSVQTRTC
CCCCCCCCCCCCCEE		12.6828270605
417PhosphorylationNNRCEGSSVQTRTCH
CCCCCCCCCCCCEEC		29.1528270605
438C-linked_GlycosylationRFKQDGGWSHWSPWS
HHCCCCCCCCCCCCC		7.8011067851
438C-linked_GlycosylationRFKQDGGWSHWSPWS
HHCCCCCCCCCCCCC		7.8011067851
441C-linked_GlycosylationQDGGWSHWSPWSSCS
CCCCCCCCCCCCCCE		10.6911067851
441C-linked_GlycosylationQDGGWSHWSPWSSCS
CCCCCCCCCCCCCCE		10.6911067851
442PhosphorylationDGGWSHWSPWSSCSV
CCCCCCCCCCCCCEE		15.8622210691
445PhosphorylationWSHWSPWSSCSVTCG
CCCCCCCCCCEEEEC		25.5022210691
446PhosphorylationSHWSPWSSCSVTCGD
CCCCCCCCCEEEECC		13.4222210691
450O-linked_GlycosylationPWSSCSVTCGDGVIT
CCCCCEEEECCCEEE		8.4211067851
450O-linked_GlycosylationPWSSCSVTCGDGVIT
CCCCCEEEECCCEEE		8.4211067851
464PhosphorylationTRIRLCNSPSPQMNG
EEEEECCCCCCCCCC		26.2624114839
466PhosphorylationIRLCNSPSPQMNGKP
EEECCCCCCCCCCCC		27.8228270605
472UbiquitinationPSPQMNGKPCEGEAR
CCCCCCCCCCCCCHH		41.30-
481PhosphorylationCEGEARETKACKKDA
CCCCHHCCHHCCCCC		20.56-
498C-linked_GlycosylationINGGWGPWSPWDICS
CCCCCCCCCCCHHEE		17.0611067851
498C-linked_GlycosylationINGGWGPWSPWDICS
CCCCCCCCCCCHHEE		17.0611067851
507O-linked_GlycosylationPWDICSVTCGGGVQK
CCHHEEEECCCCHHH		6.8011067851
507O-linked_GlycosylationPWDICSVTCGGGVQK
CCHHEEEECCCCHHH		6.8011067851
563PhosphorylationCFAGVKCTSYPDGSW
CEECCEEECCCCCCC		26.10-
564PhosphorylationFAGVKCTSYPDGSWK
EECCEEECCCCCCCC		44.10-
565PhosphorylationAGVKCTSYPDGSWKC
ECCEEECCCCCCCCC		6.28-
569PhosphorylationCTSYPDGSWKCGACP
EECCCCCCCCCCCCC		30.6428985074
579PhosphorylationCGACPPGYSGNGIQC
CCCCCCCCCCCCCCC		21.1228985074
580PhosphorylationGACPPGYSGNGIQCT
CCCCCCCCCCCCCCC		31.5328985074
580O-linked_GlycosylationGACPPGYSGNGIQCT
CCCCCCCCCCCCCCC		31.5322403705
625PhosphorylationLPCPPRFTGSQPFGQ
CCCCCCCCCCCCCCC		36.8823312004
627PhosphorylationCPPRFTGSQPFGQGV
CCCCCCCCCCCCCCC		31.4623312004
638O-linked_GlycosylationGQGVEHATANKQVCK
CCCCCHHHCCCCCCC		32.4455834391
670PhosphorylationCNYLGHYSDPMYRCE
CCCCCCCCCCCEEEE		29.5723403867
708N-linked_GlycosylationENLVCVANATYHCKK
CCEEEEECEEEEECC		16.65UniProtKB CARBOHYD
724PhosphorylationNCPNLPNSGQEDYDK
CCCCCCCCCCCCCCC		39.6628270605
817PhosphorylationRDNCQYVYNVDQRDT
CCCEEEEEECCCCCC		12.44-
824PhosphorylationYNVDQRDTDMDGVGD
EECCCCCCCCCCCCC		35.1028060719
847PhosphorylationHNPDQLDSDSDRIGD
CCHHHCCCCCCCCCC		47.8328060719
849PhosphorylationPDQLDSDSDRIGDTC
HHHCCCCCCCCCCCC		32.5128060719
855PhosphorylationDSDRIGDTCDNNQDI
CCCCCCCCCCCCCCC		19.2929970186
921PhosphorylationPNPDQKDSDGDGRGD
CCCCCCCCCCCCCCC		50.9928060719
938PhosphorylationKDDFDHDSVPDIDDI
CCCCCCCCCCCHHHH		31.9328060719
970PhosphorylationIPLDPKGTSQNDPNW
EECCCCCCCCCCCCC		33.0128270605
971PhosphorylationPLDPKGTSQNDPNWV
ECCCCCCCCCCCCCE		35.3428270605
1022PhosphorylationNTERDDDYAGFVFGY
ECCCCCCCCEEEEEE		18.67-
1029PhosphorylationYAGFVFGYQSSSRFY
CCEEEEEEECCCCEE		8.18-
1033PhosphorylationVFGYQSSSRFYVVMW
EEEEECCCCEEEEEE		31.49-
1036PhosphorylationYQSSSRFYVVMWKQV
EECCCCEEEEEEEEH		7.33-
1044PhosphorylationVVMWKQVTQSYWDTN
EEEEEEHHHHHHCCC		14.8728060719
1046PhosphorylationMWKQVTQSYWDTNPT
EEEEHHHHHHCCCCC		20.8728060719
1047PhosphorylationWKQVTQSYWDTNPTR
EEEHHHHHHCCCCCC		9.4828060719
1053O-linked_GlycosylationSYWDTNPTRAQGYSG
HHHCCCCCCCCCCCC		40.48OGP
1058PhosphorylationNPTRAQGYSGLSVKV
CCCCCCCCCCEEEEE		6.3628060719
1059PhosphorylationPTRAQGYSGLSVKVV
CCCCCCCCCEEEEEE		39.8328060719
1062PhosphorylationAQGYSGLSVKVVNST
CCCCCCEEEEEEECC		24.3428060719
1067N-linked_GlycosylationGLSVKVVNSTTGPGE
CEEEEEEECCCCCCH		36.3019522481
1067N-linked_GlycosylationGLSVKVVNSTTGPGE
CEEEEEEECCCCCCH		36.3016263699
1118PhosphorylationRLSHRPKTGFIRVVM
HHHCCCCCCCEEEEE		39.7529083192
1126PhosphorylationGFIRVVMYEGKKIMA
CCEEEEEECCCEEEC		15.2129083192
1130AcetylationVVMYEGKKIMADSGP
EEEECCCEEECCCCC		48.8721339330
1132SulfoxidationMYEGKKIMADSGPIY
EECCCEEECCCCCCC		4.6830846556
1139PhosphorylationMADSGPIYDKTYAGG
ECCCCCCCCCCCCCC		17.9629083192
1142PhosphorylationSGPIYDKTYAGGRLG
CCCCCCCCCCCCCEE		18.7329083192
1143PhosphorylationGPIYDKTYAGGRLGL
CCCCCCCCCCCCEEE		14.6929083192
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 TSP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSP1_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 TSP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP1_HUMANLRP1physical
14991768
IBP5_HUMANIGFBP5physical
10698186
PLMN_HUMANPLGphysical
6438154
CO3A1_HUMANCOL3A1physical
3571333
CO2A1_HUMANCOL2A1physical
3571333
CO1A1_HUMANCOL1A1physical
3571333
CO4A1_HUMANCOL4A1physical
3571333
CO5A1_HUMANCOL5A1physical
3571333
ITB3_HUMANITGB3physical
2478219
THRB_HUMANF2physical
2435757
LRP1_HUMANLRP1physical
9045712
PDGFB_HUMANPDGFBphysical
9334164
ELNE_HUMANELANEphysical
8463250
FIBA_HUMANFGAphysical
9867861
CO7A1_HUMANCOL7A1physical
9840442
MMP2_HUMANMMP2physical
10900205
FGF2_HUMANFGF2physical
17996481
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 TSP1_HUMAN

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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"C-mannosylation and O-fucosylation of the thrombospondin type 1module.";
Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J.,Mosher D.F., Peter-Katalinic J.;
J. Biol. Chem. 276:6485-6498(2001).
Cited for: GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498AND THR-507.
N-linked Glycosylation
ReferencePubMed
"Structure of a thrombospondin C-terminal fragment reveals a novelcalcium core in the type 3 repeats.";
Kvansakul M., Adams J.C., Hohenester E.;
EMBO J. 23:1223-1233(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 834-1170 IN COMPLEX WITHCALCIUM IONS, DISULFIDE BONDS, MUTAGENESIS OF ASN-1067, GLYCOSYLATIONAT ASN-1067, CELL ATTACHMENT SITE, AND FUNCTION.
"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-1067, AND MASSSPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, 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-248 AND ASN-1067, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Crystal structure of the TSP-1 type 1 repeats: a novel layered foldand its biological implication.";
Tan K., Duquette M., Liu J.-H., Dong Y., Zhang R., Joachimiak A.,Lawler J., Wang J.-H.;
J. Cell Biol. 159:373-382(2002).
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 434-546, DISULFIDE BONDS, ANDGLYCOSYLATION AT THR-450 AND THR-507.
"C-mannosylation and O-fucosylation of the thrombospondin type 1module.";
Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J.,Mosher D.F., Peter-Katalinic J.;
J. Biol. Chem. 276:6485-6498(2001).
Cited for: GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498AND THR-507.

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