Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thrombospondin-1  

UniProtKB / Swiss-Prot ID :  TSP1_HUMAN

Gene Name (Synonyms) : 
THBS1, TSP, TSP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  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. 

Protein Sequence MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPV...
Predicted Secondary Structure CCHHHHHHHHHHHHCCCCCCCCCCCCCCCCEEEEEEECCCCCCCCEEECCCCCCCCCCCEEECCCCCCCC...
Protein Variant
LocationDescription
24S -> A (in dbSNP:rs41515347). VAR_052657
523T -> A (in dbSNP:rs2292305). VAR_028938
700N -> S (in dbSNP:rs2228262). VAR_028939
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
248N-linked (GlcNAc...)NNVVNGSSP
CCEEECCCC
40.10SysPTM
Link-
385C-linked (Man)GWSPWSEWT
CCCCCCCCC
11.90HPRD
Link-
385C-linked (Man).GWSPWSEWT
CCCCCCCCC
11.90UniProtKB
Link-
394O-linked (Fuc...).SCSTSCGNG
CCCCCCCCC
12.06UniProtKB
Link-
394O-linked (GalNAc...)SCSTSCGNG
CCCCCCCCC
12.06HPRD
Link-
438C-linked (Man)QDGGWSHWS
ECCCCCCCC
7.80HPRD
Link
438C-linked (Man).QDGGWSHWS
ECCCCCCCC
7.80UniProtKB
Link
441C-linked (Man)GWSHWSPWS
CCCCCCCCC
10.69HPRD
Link
441C-linked (Man).GWSHWSPWS
CCCCCCCCC
10.69UniProtKB
Link
447S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)PWSSCSVTC
CCCCCCCCC
2.94HPRD
Link
450O-linked (Fuc...).SCSVTCGDG
CCCCCCCCC
8.42UniProtKB
Link
450O-linked (GalNAc...)SCSVTCGDG
CCCCCCCCC
8.42HPRD
Link
451S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)CSVTCGDGV
CCCCCCCCE
4.36HPRD
Link
462S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)RIRLCNSPS
CCEEECCCC
3.21HPRD
Link
474S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NGKPCEGEA
CCCCCCCCC
13.79HPRD
Link
484S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)ETKACKKDA
CCCCCCCCC
6.32HPRD
Link
489S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)KKDACPING
CCCCCCCCC
5.08HPRD
Link
498C-linked (Man)GWGPWSPWD
CCCCCCCCC
17.06HPRD
Link
498C-linked (Man).GWGPWSPWD
CCCCCCCCC
17.06UniProtKB
Link
507O-linked (Fuc...).ICSVTCGGG
CCCCCCCCC
6.80UniProtKB
Link
507O-linked (GalNAc...)ICSVTCGGG
CCCCCCCCC
6.80HPRD
Link
1067N-linked (Glc...)VKVVNSTTG
EEEEECCCC
36.30HPRD
Link-
1067N-linked (GlcNAc...)VKVVNSTTG
EEEEECCCC
36.30SysPTM
Link-
1067N-linked (GlcNAc...).VKVVNSTTG
EEEEECCCC
36.30UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LRP1_HUMANin vitro
in vivo
HPRD:01765HPRD9045712
14991768
CALR_HUMANin vitroHPRD:01765HPRD12147682
CATG_HUMANin vitroHPRD:01765HPRD8408036
CO7A1_HUMANyeast 2-hybridHPRD:01765HPRD9840442
CO2A1_HUMANin vitroHPRD:01765HPRD3571333
CO1A1_HUMANin vitroHPRD:01765HPRD3571333
CO3A1_HUMANin vitroHPRD:01765HPRD3571333
CO5A1_HUMANin vivoHPRD:01765HPRD6693501
9840442
MMP2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01765HPRD10900205
MMP9_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01765HPRD10900205
11606713
ELNE_HUMANin vitroHPRD:01765HPRD8463250
PGS2_HUMANin vitro
in vivo
HPRD:01765HPRD9328841
1550960
DYR_HUMANin vitroHPRD:01765HPRD10749676
FIBA_HUMANin vitroHPRD:01765HPRD9867861
FINC_HUMANin vitroHPRD:01765HPRD11773026
HRG_HUMANin vivoHPRD:01765HPRD6438154
IBP5_HUMANin vivoHPRD:01765HPRD10698186
PLMN_HUMANin vitroHPRD:01765HPRD2522013
ITB3_HUMANin vitroHPRD:01765HPRD2478219
LAMB3_HUMANin vivo
yeast 2-hybrid
HPRD:01765HPRD9840442
CD36_HUMANin vivoHPRD:01765HPRD10772961
10487979
TFPI1_HUMANin vitroHPRD:01765HPRD10922378
THRB_HUMANin vivoHPRD:01765HPRD2435757
SPRC_HUMANin vitroHPRD:01765HPRD2745554
ITA3_HUMANENSP00000260356STRING
PGS2_HUMANENSP00000260356STRING
CATG_HUMANENSP00000260356STRING
TIMP1_HUMANENSP00000260356STRING
MMP2_HUMANENSP00000260356STRING
TGFB1_HUMANENSP00000260356STRING
SPRC_HUMANENSP00000260356STRING
HRG_HUMANENSP00000260356STRING
TFPI1_HUMANENSP00000260356STRING
IBP5_HUMANENSP00000260356STRING
LRP1_HUMANENSP00000260356STRING
TSG6_HUMANENSP00000260356STRING
ITAV_HUMANENSP00000260356STRING
ITB3_HUMANENSP00000260356STRING
ELNE_HUMANENSP00000260356STRING
FGF2_HUMANENSP00000260356STRING
P53_HUMANENSP00000260356STRING
VEGFA_HUMANENSP00000260356STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
"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.
O-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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures