Gene THBS1 - ENSG00000137801 | NCBI Gene ID: 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 blood vessel endothelial cell migration
(GO:0043537)
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-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)
Peptide cross-linking
(GO:0018149)
Phosphatidylserine binding
(GO:0001786)
Positive regulation of blood coagulation
(GO:0030194)
Positive regulation of blood vessel endothelial cell migration
(GO:0043536)
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)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: 3.6
Marker Score: 3070
Cell Name: uterine smooth muscle cell (CL0002601)
Fold Change: 3.08
Marker Score: 4012
Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
Fold Change: 2.59
Marker Score: 1080
Cell Name: lung macrophage (CL1001603)
Fold Change: 2.53
Marker Score: 2896
Cell Name: alveolar type 2 fibroblast cell (CL4028006)
Fold Change: 2.45
Marker Score: 1363
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 2.27
Marker Score: 11162
Cell Name: elicited macrophage (CL0000861)
Fold Change: 2.27
Marker Score: 13764
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 2.25
Marker Score: 76621
Cell Name: fibroblast of connective tissue of prostate (CL1000299)
Fold Change: 1.86
Marker Score: 464
Cell Name: alveolar macrophage (CL0000583)
Fold Change: 1.86
Marker Score: 47637
Cell Name: prostate stromal cell (CL0002622)
Fold Change: 1.85
Marker Score: 464
Cell Name: glandular cell of esophagus (CL0002657)
Fold Change: 1.82
Marker Score: 577
Cell Name: duct epithelial cell (CL0000068)
Fold Change: 1.77
Marker Score: 829
Cell Name: supporting cell (CL0000630)
Fold Change: 1.75
Marker Score: 3285
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 1.68
Marker Score: 959
Cell Name: fibroblast of lung (CL0002553)
Fold Change: 1.67
Marker Score: 4378
Cell Name: kidney connecting tubule epithelial cell (CL1000768)
Fold Change: 1.62
Marker Score: 2297
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 1.62
Marker Score: 4090
Cell Name: classical monocyte (CL0000860)
Fold Change: 1.58
Marker Score: 6550
Cell Name: cortical thymic epithelial cell (CL0002364)
Fold Change: 1.56
Marker Score: 5758
Cell Name: kidney interstitial fibroblast (CL1000692)
Fold Change: 1.53
Marker Score: 2934
Cell Name: smooth muscle cell (CL0000192)
Fold Change: 1.51
Marker Score: 991
Cell Name: epithelial cell of proximal tubule (CL0002306)
Fold Change: 1.49
Marker Score: 5303
Cell Name: preosteoblast (CL0007010)
Fold Change: 1.49
Marker Score: 421
Cell Name: mural cell (CL0008034)
Fold Change: 1.46
Marker Score: 168052
Cell Name: skin fibroblast (CL0002620)
Fold Change: 1.46
Marker Score: 379
Cell Name: bronchus fibroblast of lung (CL2000093)
Fold Change: 1.43
Marker Score: 1965
Cell Name: decidual cell (CL2000002)
Fold Change: 1.43
Marker Score: 6163
Cell Name: colon epithelial cell (CL0011108)
Fold Change: 1.39
Marker Score: 4375
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.38
Marker Score: 1380
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 1.36
Marker Score: 1456
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: 1.32
Marker Score: 769
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 1.31
Marker Score: 3192
Cell Name: pericyte (CL0000669)
Fold Change: 1.31
Marker Score: 763
Cell Name: stromal cell (CL0000499)
Fold Change: 1.27
Marker Score: 1486
Cell Name: fibroblast (CL0000057)
Fold Change: 1.26
Marker Score: 1219
Cell Name: chondrocyte (CL0000138)
Fold Change: 1.25
Marker Score: 561
Cell Name: CD14-positive monocyte (CL0001054)
Fold Change: 1.24
Marker Score: 3090
Cell Name: pancreatic stellate cell (CL0002410)
Fold Change: 1.23
Marker Score: 773.5
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 1.22
Marker Score: 1511
Cell Name: muscle cell (CL0000187)
Fold Change: 1.21
Marker Score: 343
Cell Name: corneal endothelial cell (CL0000132)
Fold Change: 1.2
Marker Score: 701
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 1.2
Marker Score: 67077
Cell Name: pulmonary ionocyte (CL0017000)
Fold Change: 1.2
Marker Score: 734
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 1.19
Marker Score: 1835
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.17
Marker Score: 1723
Cell Name: reticular cell (CL0000432)
Fold Change: 1.16
Marker Score: 423
Cell Name: inflammatory cell (CL0009002)
Fold Change: 1.15
Marker Score: 495
Cell Name: smooth muscle cell of prostate (CL1000487)
Fold Change: 1.13
Marker Score: 288
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 1.13
Marker Score: 471.5
Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
Fold Change: 1.1
Marker Score: 2597
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.09
Marker Score: 17005
Cell Name: adventitial cell (CL0002503)
Fold Change: 1.08
Marker Score: 267
Cell Name: endothelial cell of sinusoid (CL0002262)
Fold Change: 1.06
Marker Score: 258
Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
Fold Change: 1
Marker Score: 1019
Cell Name: parietal epithelial cell (CL1000452)
Fold Change: 1
Marker Score: 363
Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
Fold Change: 1
Marker Score: 71729
Cell Name: forebrain radial glial cell (CL0013000)
Fold Change: 1
Marker Score: 47952
Cell Name: absorptive cell (CL0000212)
Fold Change: 0.98
Marker Score: 30399
Cell Name: theca cell (CL0000503)
Fold Change: 0.97
Marker Score: 697
Cell Name: respiratory epithelial cell (CL0002368)
Fold Change: 0.96
Marker Score: 529
Cell Name: acinar cell (CL0000622)
Fold Change: 0.96
Marker Score: 675
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.95
Marker Score: 492
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.95
Marker Score: 2163
Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
Fold Change: 0.95
Marker Score: 447
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.95
Marker Score: 2402
Cell Name: tracheobronchial smooth muscle cell (CL0019019)
Fold Change: 0.92
Marker Score: 271
Cell Name: transit amplifying cell (CL0009010)
Fold Change: 0.92
Marker Score: 5264
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.91
Marker Score: 2729
Cell Name: kidney loop of Henle epithelial cell (CL1000909)
Fold Change: 0.89
Marker Score: 556
Cell Name: mammary gland epithelial cell (CL0002327)
Fold Change: 0.88
Marker Score: 314
Cell Name: smooth muscle cell of large intestine (CL1000279)
Fold Change: 0.88
Marker Score: 332
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 0.88
Marker Score: 1752
Cell Name: stem cell of epidermis (CL1000428)
Fold Change: 0.88
Marker Score: 297
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.88
Marker Score: 5264
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.88
Marker Score: 315
Cell Name: immature innate lymphoid cell (CL0001082)
Fold Change: 0.87
Marker Score: 1778
Cell Name: vascular leptomeningeal cell (CL4023051)
Fold Change: 0.87
Marker Score: 998
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.87
Marker Score: 5251
Cell Name: renal interstitial pericyte (CL1001318)
Fold Change: 0.86
Marker Score: 821
Cell Name: medullary thymic epithelial cell (CL0002365)
Fold Change: 0.86
Marker Score: 1409
Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
Fold Change: 0.85
Marker Score: 1664
Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
Fold Change: 0.85
Marker Score: 914
Cell Name: stromal cell of lamina propria of small intestine (CL0009022)
Fold Change: 0.82
Marker Score: 185
Cell Name: CD1c-positive myeloid dendritic cell (CL0002399)
Fold Change: 0.82
Marker Score: 2128
Cell Name: early T lineage precursor (CL0002425)
Fold Change: 0.82
Marker Score: 623
Cell Name: non-classical monocyte (CL0000875)
Fold Change: 0.81
Marker Score: 1961
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.8
Marker Score: 322
Cell Name: mesenchymal lymphangioblast (CL0005021)
Fold Change: 0.79
Marker Score: 177
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 0.78
Marker Score: 295
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: 0.78
Marker Score: 1266
Cell Name: kidney interstitial cell (CL1000500)
Fold Change: 0.77
Marker Score: 550
Cell Name: paneth cell of colon (CL0009009)
Fold Change: 0.77
Marker Score: 220
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: 0.76
Marker Score: 297
Cell Name: osteoblast (CL0000062)
Fold Change: 0.75
Marker Score: 403
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 0.75
Marker Score: 2008
Cell Name: Cajal-Retzius cell (CL0000695)
Fold Change: 0.74
Marker Score: 384
Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: 0.74
Marker Score: 1744
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.74
Marker Score: 471
Cell Name: macrophage (CL0000235)
Fold Change: 0.74
Marker Score: 818

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**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: 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. 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

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