THBS1
Thrombospondin-1
Also known as: THBS, THBS-1, TSP, TSP-1, TSP1, TSP1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P07996
- Gene
- THBS1
- Ensembl
- ENSG00000137801
- Chromosome
- 15
- Canonical length
- 1170 aa
- Protein class
- Cancer-related genes, Candidate cardiovascular disease genes, Plasma proteins, Predicted secreted proteins
- Subcellular location
- Endoplasmic reticulum,Plasma membrane
- Secretome location
- Secreted to extracellular matrix
- Quaternary structure
- Homotrimer
OverviewNCBI Gene
The protein encoded by this gene is a subunit of a disulfide-linked homotrimeric protein. This protein is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. This protein can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. This protein has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
1170 residues, UniProt reviewed canonical sequence.
>P07996|THBS1
1 MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK GPDPSSPAFR
61 IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLALERK DHSGQVFSVV
121 SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD
181 VPIQSVFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL
241 TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK
301 VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN
361 ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ QRGRSCDSLN NRCEGSSVQT
421 RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE
481 TKACKKDACP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI
541 CNKQDCPIDG CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF
601 NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC TDGTHDCNKN
661 AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN
721 LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
781 HNPDQADTDN NGEGDACAAD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH
841 NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
901 DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV DISETDFRRF
961 QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
1021 DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
1081 WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD
1141 KTYAGGRLGL FVFSQEMVFF SDLKYECRDPLocalizationUniProt · AlphaFold · HPA
Whether an antibody against THBS1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.32
- Highest tissue expression
- 372 nTPM
Expression across tissuesHPA
Tissue
- appendix: 372 nTPM
- urinary bladder: 369 nTPM
- adipose tissue: 340 nTPM
- lung: 290 nTPM
- gallbladder: 258 nTPM
- smooth muscle: 227 nTPM
Single-cell type
- monocytes: 2,455 nCPM
- platelets: 634 nCPM
- salivary myoepithelial cells: 595 nCPM
- salivary ionocytes: 561 nCPM
- smooth muscle cells: 472 nCPM
- vascular smooth muscle cells: 386 nCPM
Immune cell
- eosinophil: 16 nTPM
- total PBMC: 11 nTPM
- classical monocyte: 8.7 nTPM
- NK-cell: 7.9 nTPM
- MAIT T-cell: 2.7 nTPM
- neutrophil: 1.5 nTPM
Brain region
- choroid plexus: 60 nTPM
- thalamus: 37 nTPM
- pons: 28 nTPM
- cerebral cortex: 28 nTPM
- medulla oblongata: 26 nTPM
- basal ganglia: 13 nTPM
ReferencesPubMed · IEDB
Publications for THBS1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
3 publications
- Mass spectrometry-based autoimmune profiling reveals predictive autoantigens in idiopathic pulmonary fibrosis.
2023 · iScience · RCR 1.4 · 14 citations - Decreased serum thrombospondin-1 and elevation of its autoantibody are associated with multiple exacerbated clinical manifestations in systemic lupus erythematosus.
2018 · Clin Rheumatol · RCR 0.6 · 12 citations - Expression of the multifunctional extracellular matrix protein thrombospondin in crescentic glomerulonephritis.
1996 · J Pathol · RCR 0.2 · 7 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.24
- gnomAD pLI
- 1
- gnomAD missense Z
- 2.72
- DepMap mean gene effect
- 0
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- apoptotic process
- behavioral response to pain
- blood coagulation, fibrin clot formation
- cell adhesion
- cell migration
- cellular response to growth factor stimulus
- cellular response to heat
- cellular response to tumor necrosis factor
- chronic inflammatory response
- engulfment of apoptotic cell
- immune response
- inflammatory response
- negative regulation of angiogenesis
- negative regulation of apoptotic process
- negative regulation of blood vessel endothelial cell migration
- negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis
- negative regulation of cell migration involved in sprouting angiogenesis
- negative regulation of cell population proliferation
- negative regulation of cell-matrix adhesion
- negative regulation of cGMP-mediated signaling
- negative regulation of dendritic cell antigen processing and presentation
- negative regulation of endothelial cell chemotaxis
- negative regulation of endothelial cell migration
- negative regulation of endothelial cell proliferation
- negative regulation of extrinsic apoptotic signaling pathway
- negative regulation of fibrinolysis
- negative regulation of fibroblast growth factor receptor signaling pathway
- negative regulation of focal adhesion assembly
- negative regulation of interleukin-10 production
- negative regulation of interleukin-12 production
- negative regulation of long-chain fatty acid import across plasma membrane
- negative regulation of nitric oxide mediated signal transduction
- negative regulation of plasminogen activation
- negative regulation of sprouting angiogenesis
- negative regulation of tumor necrosis factor production
- nitric oxide-cGMP-mediated signaling
- positive regulation of angiogenesis
- positive regulation of blood vessel endothelial cell migration
- positive regulation of cell migration
- positive regulation of cell population proliferation
- positive regulation of chemotaxis
- positive regulation of endothelial cell apoptotic process
- positive regulation of endothelial cell migration
- positive regulation of extrinsic apoptotic signaling pathway via death domain receptors
- positive regulation of fibroblast migration
- positive regulation of macrophage activation
- positive regulation of macrophage chemotaxis
- positive regulation of MAPK cascade
- positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
- positive regulation of phosphorylation
- positive regulation of reactive oxygen species metabolic process
- positive regulation of smooth muscle cell proliferation
- positive regulation of transforming growth factor beta receptor signaling pathway
- positive regulation of transforming growth factor beta1 production
- positive regulation of translation
- positive regulation of tumor necrosis factor production
- response to calcium ion
- response to endoplasmic reticulum stress
- response to glucose
- response to hypoxia
- response to magnesium ion
- response to mechanical stimulus
- response to progesterone
- response to testosterone
- response to unfolded protein
- response to xenobiotic stimulus
- sprouting angiogenesis
- negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II
- negative regulation of nitric oxide-cGMP mediated signal transduction
Molecular functions
- calcium ion binding
- collagen V binding
- endopeptidase inhibitor activity
- extracellular matrix structural constituent
- fibrinogen binding
- fibroblast growth factor binding
- fibronectin binding
- heparin binding
- integrin binding
- laminin binding
- low-density lipoprotein particle binding
- phosphatidylserine binding
- protease binding
- protein homodimerization activity
- proteoglycan binding
- transforming growth factor beta binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- EGF-like domain
- Thrombospondin type-1 (TSP1) repeat
- VWFC domain
- EGF-like calcium-binding domain
- Thrombospondin, type 3-like repeat
- Thrombospondin, C-terminal
- Concanavalin A-like lectin/glucanase domain superfamily
- Thrombospondin, type 3 repeat
- TSP type-3 repeat
- Thrombospondin type-1 repeat superfamily
- Thrombospondin-like, N-terminal domain
- Thrombospondin type 1 domain
- von Willebrand factor type C domain
- Thrombospondin type 3 repeat
- Thrombospondin C-terminal region
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of THBS1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads THBS1 as an antibody target. Whether an autoantibody or antibody against THBS1 could matter depends on whether native THBS1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
THBS1 is annotated at the cell surface, where native THBS1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label THBS1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...