THBS1 | ENSG00000137801 | NCBI 7057

Details for: THBS1

Gene ID: 7057

Symbol: THBS1

Ensembl ID: ENSG00000137801

Description: thrombospondin 1

Associated with

Defective b3galtl causes pps
(R-HSA-5083635)
Disease
(R-HSA-1643685)
Diseases associated with o-glycosylation of proteins
(R-HSA-3906995)
Diseases of glycosylation
(R-HSA-3781865)
Diseases of metabolism
(R-HSA-5668914)
Extracellular matrix organization
(R-HSA-1474244)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hemostasis
(R-HSA-109582)
Integrin cell surface interactions
(R-HSA-216083)
Metabolism of proteins
(R-HSA-392499)
Non-integrin membrane-ecm interactions
(R-HSA-3000171)
O-glycosylation of tsr domain-containing proteins
(R-HSA-5173214)
O-linked glycosylation
(R-HSA-5173105)
Platelet activation, signaling and aggregation
(R-HSA-76002)
Platelet degranulation
(R-HSA-114608)
Post-translational protein modification
(R-HSA-597592)
Response to elevated platelet cytosolic ca2+
(R-HSA-76005)
Rna polymerase ii transcription
(R-HSA-73857)
Runx1 regulates genes involved in megakaryocyte differentiation and platelet function
(R-HSA-8936459)
Signaling by pdgf
(R-HSA-186797)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signal transduction
(R-HSA-162582)
Syndecan interactions
(R-HSA-3000170)
Transcriptional regulation by runx1
(R-HSA-8878171)
Apoptotic process
(GO:0006915)
Calcium ion binding
(GO:0005509)
Cell adhesion
(GO:0007155)
Cell migration
(GO:0016477)
Cellular response to heat
(GO:0034605)
Chronic inflammatory response
(GO:0002544)
Collagen v binding
(GO:0070052)
Endopeptidase inhibitor activity
(GO:0004866)
Extracellular matrix structural constituent
(GO:0005201)
Fibrinogen binding
(GO:0070051)
Fibroblast growth factor binding
(GO:0017134)
Fibronectin binding
(GO:0001968)
Heparin binding
(GO:0008201)
Immune response
(GO:0006955)
Inflammatory response
(GO:0006954)
Integrin binding
(GO:0005178)
Laminin binding
(GO:0043236)
Low-density lipoprotein particle binding
(GO:0030169)
Negative regulation of angiogenesis
(GO:0016525)
Negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via mhc class ii
(GO:0002581)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of cell-matrix adhesion
(GO:0001953)
Negative regulation of cell population proliferation
(GO:0008285)
Negative regulation of cgmp-mediated signaling
(GO:0010754)
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
(GO:0043154)
Negative regulation of dendritic cell antigen processing and presentation
(GO:0002605)
Negative regulation of endothelial cell migration
(GO:0010596)
Negative regulation of endothelial cell proliferation
(GO:0001937)
Negative regulation of fibroblast growth factor receptor signaling pathway
(GO:0040037)
Negative regulation of interleukin-10 production
(GO:0032693)
Negative regulation of interleukin-12 production
(GO:0032695)
Negative regulation of long-chain fatty acid import across plasma membrane
(GO:0010748)
Negative regulation of nitric oxide mediated signal transduction
(GO:0010751)
Negative regulation of plasminogen activation
(GO:0010757)
Negative regulation of tumor necrosis factor production
(GO:0032720)
Nitric oxide-cgmp-mediated signaling
(GO:0038060)
Peptide cross-linking
(GO:0018149)
Phosphatidylserine binding
(GO:0001786)
Positive regulation of blood coagulation
(GO:0030194)
Positive regulation of cell migration
(GO:0030335)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of endothelial cell migration
(GO:0010595)
Positive regulation of fibroblast migration
(GO:0010763)
Positive regulation of macrophage activation
(GO:0043032)
Positive regulation of macrophage chemotaxis
(GO:0010759)
Positive regulation of map kinase activity
(GO:0043406)
Positive regulation of phosphorylation
(GO:0042327)
Positive regulation of transforming growth factor beta1 production
(GO:0032914)
Positive regulation of transforming growth factor beta receptor signaling pathway
(GO:0030511)
Positive regulation of tumor necrosis factor production
(GO:0032760)
Protease binding
(GO:0002020)
Protein binding
(GO:0005515)
Protein homodimerization activity
(GO:0042803)
Proteoglycan binding
(GO:0043394)
Response to endoplasmic reticulum stress
(GO:0034976)
Response to glucose
(GO:0009749)
Response to hypoxia
(GO:0001666)
Response to magnesium ion
(GO:0032026)
Response to mechanical stimulus
(GO:0009612)
Response to progesterone
(GO:0032570)
Response to testosterone
(GO:0033574)
Response to unfolded protein
(GO:0006986)
Response to xenobiotic stimulus
(GO:0009410)
Sprouting angiogenesis
(GO:0002040)
Transforming growth factor beta binding
(GO:0050431)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 221.0290
Cell Significance Index: -34.3800
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 136.2543
Cell Significance Index: -34.5600
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 75.1741
Cell Significance Index: -30.5400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 67.2259
Cell Significance Index: -34.5800
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 31.9877
Cell Significance Index: -30.5400
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 27.8842
Cell Significance Index: -34.3800
Cell Name: decidual cell (CL2000002)
Fold Change: 10.9724
Cell Significance Index: 176.0400
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 8.6352
Cell Significance Index: -34.0800
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 3.7480
Cell Significance Index: 107.4400
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 2.4028
Cell Significance Index: 457.2700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 1.9258
Cell Significance Index: 136.2000
Cell Name: perivascular cell (CL4033054)
Fold Change: 1.8669
Cell Significance Index: 8.6200
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.3842
Cell Significance Index: 62.7400
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 1.0548
Cell Significance Index: 19.5000
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.8357
Cell Significance Index: 21.9800
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.8251
Cell Significance Index: 63.3200
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: 0.7950
Cell Significance Index: 12.3000
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.7652
Cell Significance Index: 124.4600
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.7462
Cell Significance Index: 73.8200
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 0.7368
Cell Significance Index: 8.3700
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.7110
Cell Significance Index: 97.6400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.6982
Cell Significance Index: 85.8600
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.6349
Cell Significance Index: 13.2900
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.6223
Cell Significance Index: 67.6900
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.4545
Cell Significance Index: 21.3600
Cell Name: monocyte-derived dendritic cell (CL0011031)
Fold Change: 0.4488
Cell Significance Index: 7.7100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.3669
Cell Significance Index: 22.0300
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.2727
Cell Significance Index: 120.5800
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.2498
Cell Significance Index: 17.2800
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.2222
Cell Significance Index: 40.0500
Cell Name: lactocyte (CL0002325)
Fold Change: 0.1752
Cell Significance Index: 22.6400
Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: 0.1237
Cell Significance Index: 1.3500
Cell Name: odontoblast (CL0000060)
Fold Change: 0.1086
Cell Significance Index: 13.9200
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.0944
Cell Significance Index: 2.7200
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.0484
Cell Significance Index: 9.6000
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0322
Cell Significance Index: 1.1300
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.0008
Cell Significance Index: 0.5300
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.0096
Cell Significance Index: -0.1600
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.0120
Cell Significance Index: -0.3000
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0153
Cell Significance Index: -20.8100
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0177
Cell Significance Index: -33.2600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0179
Cell Significance Index: -13.2500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0223
Cell Significance Index: -13.9400
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0224
Cell Significance Index: -41.2800
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0230
Cell Significance Index: -2.3500
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0231
Cell Significance Index: -35.4900
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0238
Cell Significance Index: -1.1100
Cell Name: cell in vitro (CL0001034)
Fold Change: -0.0272
Cell Significance Index: -14.8500
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0282
Cell Significance Index: -20.6700
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0334
Cell Significance Index: -18.8200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0338
Cell Significance Index: -25.6100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0374
Cell Significance Index: -1.9400
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.0395
Cell Significance Index: -2.9500
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0414
Cell Significance Index: -26.3100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0636
Cell Significance Index: -10.8600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0716
Cell Significance Index: -32.4800
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: -0.0876
Cell Significance Index: -31.4300
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0946
Cell Significance Index: -19.9300
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.1015
Cell Significance Index: -11.8300
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1030
Cell Significance Index: -29.6300
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.1260
Cell Significance Index: -3.4300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: -0.1294
Cell Significance Index: -25.9500
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1474
Cell Significance Index: -16.8900
Cell Name: preadipocyte (CL0002334)
Fold Change: -0.1819
Cell Significance Index: -3.5500
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.1953
Cell Significance Index: -4.1600
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.2071
Cell Significance Index: -23.6400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2221
Cell Significance Index: -32.2900
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.2474
Cell Significance Index: -12.5100
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.2631
Cell Significance Index: -5.7000
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.2802
Cell Significance Index: -4.7200
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.2878
Cell Significance Index: -5.0900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.3343
Cell Significance Index: -34.8100
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: -0.3577
Cell Significance Index: -3.0100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.3709
Cell Significance Index: -10.3700
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.4032
Cell Significance Index: -24.7200
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.4091
Cell Significance Index: -32.4000
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: -0.4133
Cell Significance Index: -2.8000
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.4746
Cell Significance Index: -13.9800
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.4969
Cell Significance Index: -32.0600
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.4987
Cell Significance Index: -33.5300
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.5114
Cell Significance Index: -3.0900
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.5206
Cell Significance Index: -27.1200
Cell Name: duct epithelial cell (CL0000068)
Fold Change: -0.5229
Cell Significance Index: -7.2300
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: -0.5265
Cell Significance Index: -3.2400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.5574
Cell Significance Index: -34.2600
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.5625
Cell Significance Index: -5.1800
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.5814
Cell Significance Index: -18.6200
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.5817
Cell Significance Index: -36.6600
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.5821
Cell Significance Index: -21.3700
Cell Name: theca cell (CL0000503)
Fold Change: -0.6162
Cell Significance Index: -3.6200
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.6355
Cell Significance Index: -35.6600
Cell Name: inflammatory cell (CL0009002)
Fold Change: -0.6505
Cell Significance Index: -3.7300
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.6533
Cell Significance Index: -26.7700
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.6624
Cell Significance Index: -14.5100
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.6788
Cell Significance Index: -5.5400
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: -0.6804
Cell Significance Index: -9.7700
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.7043
Cell Significance Index: -31.1600
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.7272
Cell Significance Index: -38.1800
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: -0.7344
Cell Significance Index: -7.6000
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -0.7428
Cell Significance Index: -8.0800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** TSP1 exhibits several key characteristics that distinguish it from other glycoproteins: 1. **Extracellular matrix-binding properties**: TSP1 interacts with various components of the extracellular matrix, including collagen, laminin, and fibronectin, which regulates cell adhesion, migration, and differentiation. 2. **Receptor-mediated signaling**: TSP1 binds to specific receptors, such as integrins, which triggers signaling pathways that regulate cell behavior, including proliferation, migration, and survival. 3. **Glycosylation and post-translational modifications**: TSP1 undergoes O-glycosylation and other post-translational modifications, which affect its function and interactions with other molecules. 4. **Diverse expression patterns**: TSP1 is expressed in various cell types, including fibroblasts, smooth muscle cells, macrophages, and epithelial cells. **Pathways and Functions** TSP1 is involved in numerous signaling pathways and regulates various cellular processes, including: 1. **Cell adhesion and migration**: TSP1 regulates cell adhesion to the extracellular matrix and promotes cell migration through interactions with integrins and other receptors. 2. **Apoptosis regulation**: TSP1 modulates apoptosis by interacting with pro-apoptotic and anti-apoptotic proteins, such as Bcl-2 and Bax. 3. **Angiogenesis regulation**: TSP1 inhibits angiogenesis by binding to vascular endothelial growth factor (VEGF) and other angiogenic factors. 4. **Inflammation regulation**: TSP1 modulates inflammatory responses by interacting with immune cells, such as macrophages and dendritic cells. 5. **Cancer regulation**: TSP1 is involved in cancer progression and metastasis by regulating cell migration, invasion, and angiogenesis. **Clinical Significance** TSP1's dysregulation has been implicated in various diseases, including: 1. **Cancer**: TSP1 overexpression is associated with cancer progression and metastasis. 2. **Cardiovascular disease**: TSP1 dysregulation contributes to atherosclerosis and cardiovascular disease. 3. **Neurological disorders**: TSP1 is involved in neuroinflammation and neurodegenerative diseases, such as Alzheimer's and Parkinson's. 4. **Wound healing**: TSP1 regulates wound healing by modulating cell migration, differentiation, and angiogenesis. In conclusion, TSP1 is a multifunctional glycoprotein that plays a crucial role in regulating various cellular processes, including cell adhesion, migration, and differentiation. Its dysregulation has been implicated in various diseases, highlighting the importance of understanding its biology and potential therapeutic applications.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Thrombospondin-1

Genular Protein ID: 59426331

Symbol: TSP1_HUMAN

Name: Thrombospondin-1

UniProtKB Accession Codes:

P07996 A8K6H4 B4E3J7 B9EGH6 Q15667 Q59E99

Database IDs:

Citations:

PubMed ID: 2430973

Title: The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.

PubMed ID: 2430973

DOI: 10.1083/jcb.103.5.1635

PubMed ID: 2918029

Title: Complete thrombospondin mRNA sequence includes potential regulatory sites in the 3' untranslated region.

PubMed ID: 2918029

DOI: 10.1083/jcb.108.2.729

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3030396

Title: Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins.

PubMed ID: 3030396

DOI: 10.1021/bi00374a014

PubMed ID: 3461443

Title: Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin.

PubMed ID: 3461443

DOI: 10.1073/pnas.83.15.5449

PubMed ID: 2544587

Title: Characterization of the promoter region of the human thrombospondin gene. DNA sequences within the first intron increase transcription.

PubMed ID: 2544587

DOI: 10.1016/s0021-9258(18)60452-1

PubMed ID: 101549

Title: Isolation and characterization of a high molecular weight glycoprotein from human blood platelets.

PubMed ID: 101549

DOI: 10.1016/s0021-9258(17)34336-3

PubMed ID: 6777381

Title: Ca2+-mediated association of glycoprotein G (thrombin-sensitive protein, thrombospondin) with human platelets.

PubMed ID: 6777381

DOI: 10.1016/s0021-9258(19)70174-4

PubMed ID: 6341993

Title: Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

PubMed ID: 6341993

DOI: 10.1073/pnas.80.4.998

PubMed ID: 6489349

Title: Thrombospondin interactions with fibronectin and fibrinogen. Mutual inhibition in binding.

PubMed ID: 6489349

DOI: 10.1111/j.1432-1033.1984.tb08534.x

PubMed ID: 6693501

Title: Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen.

PubMed ID: 6693501

DOI: 10.1083/jcb.98.2.646

PubMed ID: 2478219

Title: An integrin receptor on normal and thrombasthenic platelets that binds thrombospondin.

PubMed ID: 2478219

PubMed ID: 1371676

Title: Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.

PubMed ID: 1371676

DOI: 10.1016/0006-291x(92)91860-s

PubMed ID: 8550562

Title: Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin.

PubMed ID: 8550562

DOI: 10.1074/jbc.271.1.21

PubMed ID: 10613822

Title: Signals leading to apoptosis-dependent inhibition of neovascularization by thrombospondin-1.

PubMed ID: 10613822

DOI: 10.1038/71517

PubMed ID: 11067851

Title: C-mannosylation and O-fucosylation of the thrombospondin type 1 module.

PubMed ID: 11067851

DOI: 10.1074/jbc.m008073200

PubMed ID: 11134179

Title: Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1.

PubMed ID: 11134179

DOI: 10.1172/jci9061

PubMed ID: 12450399

Title: Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1.

PubMed ID: 12450399

DOI: 10.1021/bi026463u

PubMed ID: 14568985

Title: Thrombospondin 1 is an autocrine negative regulator of human dendritic cell activation.

PubMed ID: 14568985

DOI: 10.1084/jem.20030705

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 16740002

Title: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.

PubMed ID: 16740002

DOI: 10.1021/pr050492k

PubMed ID: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

PubMed ID: 18285447

Title: Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region.

PubMed ID: 18285447

DOI: 10.1242/jcs.021006

PubMed ID: 18042364

Title: TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly.

PubMed ID: 18042364

DOI: 10.1016/j.matbio.2007.10.003

PubMed ID: 19004835

Title: Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses.

PubMed ID: 19004835

DOI: 10.1074/jbc.m804860200

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24511121

Title: Thrombospondin-1 activation of signal-regulatory protein-alpha stimulates reactive oxygen species production and promotes renal ischemia reperfusion injury.

PubMed ID: 24511121

DOI: 10.1681/asn.2013040433

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 27742621

Title: TSP1-CD47 signaling is upregulated in clinical pulmonary hypertension and contributes to pulmonary arterial vasculopathy and dysfunction.

PubMed ID: 27742621

DOI: 10.1093/cvr/cvw218

PubMed ID: 29042481

Title: The matricellular protein TSP1 promotes human and mouse endothelial cell senescence through CD47 and Nox1.

PubMed ID: 29042481

DOI: 10.1126/scisignal.aaj1784

PubMed ID: 32679764

Title: CD47 Promotes Age-Associated Deterioration in Angiogenesis, Blood Flow and Glucose Homeostasis.

PubMed ID: 32679764

DOI: 10.3390/cells9071695

PubMed ID: 38237698

Title: Analysis of the Healthy Platelet Proteome Identifies a New Form of Domain-Specific O-Fucosylation.

PubMed ID: 38237698

DOI: 10.1016/j.mcpro.2024.100717

PubMed ID: 12391027

Title: Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication.

PubMed ID: 12391027

DOI: 10.1083/jcb.200206062

PubMed ID: 15014436

Title: Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.

PubMed ID: 15014436

DOI: 10.1038/sj.emboj.7600166

PubMed ID: 16407063

Title: The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin.

PubMed ID: 16407063

DOI: 10.1016/j.str.2005.09.017

PubMed ID: 18065761

Title: Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.

PubMed ID: 18065761

DOI: 10.1074/jbc.m705203200

Sequence Information:

Length: 1170
Mass: 129383
Checksum: 74749B2418E0943B
Sequence:

MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK GPDPSSPAFR 
IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLALERK DHSGQVFSVV 
SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD 
VPIQSVFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL 
TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK 
VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN 
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ QRGRSCDSLN NRCEGSSVQT 
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE 
TKACKKDACP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI 
CNKQDCPIDG CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF 
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC TDGTHDCNKN 
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN 
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN 
HNPDQADTDN NGEGDACAAD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH 
NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN 
DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV DISETDFRRF 
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD 
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL 
WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD 
KTYAGGRLGL FVFSQEMVFF SDLKYECRDP

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: THBS1

Associated with

Cells (max top 100)

Other Information

The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. PubMed ID: 2430973

Complete thrombospondin mRNA sequence includes potential regulatory sites in the 3' untranslated region. PubMed ID: 2918029

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Analysis of the DNA sequence and duplication history of human chromosome 15. PubMed ID: 16572171

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins. PubMed ID: 3030396

Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin. PubMed ID: 3461443

Characterization of the promoter region of the human thrombospondin gene. DNA sequences within the first intron increase transcription. PubMed ID: 2544587

Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. PubMed ID: 101549

Ca2+-mediated association of glycoprotein G (thrombin-sensitive protein, thrombospondin) with human platelets. PubMed ID: 6777381

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix. PubMed ID: 6341993

Thrombospondin interactions with fibronectin and fibrinogen. Mutual inhibition in binding. PubMed ID: 6489349

Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen. PubMed ID: 6693501

An integrin receptor on normal and thrombasthenic platelets that binds thrombospondin. PubMed ID: 2478219

Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding. PubMed ID: 1371676

Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin. PubMed ID: 8550562

Signals leading to apoptosis-dependent inhibition of neovascularization by thrombospondin-1. PubMed ID: 10613822

C-mannosylation and O-fucosylation of the thrombospondin type 1 module. PubMed ID: 11067851

Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1. PubMed ID: 11134179

Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1. PubMed ID: 12450399

Thrombospondin 1 is an autocrine negative regulator of human dendritic cell activation. PubMed ID: 14568985

Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. PubMed ID: 16335952

Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. PubMed ID: 16740002

Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. PubMed ID: 16263699

Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region. PubMed ID: 18285447

TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. PubMed ID: 18042364

Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses. PubMed ID: 19004835

Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. PubMed ID: 19159218

Initial characterization of the human central proteome. PubMed ID: 21269460

Thrombospondin-1 activation of signal-regulatory protein-alpha stimulates reactive oxygen species production and promotes renal ischemia reperfusion injury. PubMed ID: 24511121

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

TSP1-CD47 signaling is upregulated in clinical pulmonary hypertension and contributes to pulmonary arterial vasculopathy and dysfunction. PubMed ID: 27742621

The matricellular protein TSP1 promotes human and mouse endothelial cell senescence through CD47 and Nox1. PubMed ID: 29042481

CD47 Promotes Age-Associated Deterioration in Angiogenesis, Blood Flow and Glucose Homeostasis. PubMed ID: 32679764

Analysis of the Healthy Platelet Proteome Identifies a New Form of Domain-Specific O-Fucosylation. PubMed ID: 38237698

Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication. PubMed ID: 12391027

Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats. PubMed ID: 15014436

The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin. PubMed ID: 16407063

Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain. PubMed ID: 18065761