THBS1
entrez
7057
canonical
uniprot
P07996
canonical
ensembl
ENSG00000137801
resolver
ensp
ENSP00000260356
resolver
ensp
ENSP00000550811
resolver
genesymbol
THBS1
resolver
genesymbol_syn
TSP
resolver
genesymbol_syn
TSP1
resolver
hgnc
HGNC:11785
resolver
uniprot
A8K6H4
resolver
uniprot
B4E3J7
resolver
uniprot
B9EGH6
resolver
uniprot
Q15667
resolver
uniprot
Q59E99
resolver
uniprot_entry
TSP1_HUMAN
resolver
uniprot_sec
A8K6H4
resolver
uniprot_sec
B4E3J7
resolver
uniprot_sec
B9EGH6
resolver
uniprot_sec
Q15667
resolver
uniprot_sec
Q59E99
resolver
amino_acid_sequence
MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRKVTEENKELANELRRPPLCYHNGVQYRNNEEWTVDSCTECHCQNSVTICKKVSCPIMPCSNATVPDGECCPRCWPSDSADDGWSPWSEWTSCSTSCGNGIQQRGRSCDSLNNRCEGSSVQTRTCHIQECDKRFKQDGGWSHWSPWSSCSVTCGDGVITRIRLCNSPSPQMNGKPCEGEARETKACKKDACPINGGWGPWSPWDICSVTCGGGVQKRSRLCNNPTPQFGGKDCVGDVTENQICNKQDCPIDGCLSNPCFAGVKCTSYPDGSWKCGACPPGYSGNGIQCTDVDECKEVPDACFNHNGEHRCENTDPGYNCLPCPPRFTGSQPFGQGVEHATANKQVCKPRNPCTDGTHDCNKNAKCNYLGHYSDPMYRCECKPGYAGNGIICGEDTDLDGWPNENLVCVANATYHCKKDNCPNLPNSGQEDYDKDGIGDACDDDDDNDKIPDDRDNCPFHYNPAQYDYDRDDVGDRCDNCPYNHNPDQADTDNNGEGDACAADIDGDGILNERDNCQYVYNVDQRDTDMDGVGDQCDNCPLEHNPDQLDSDSDRIGDTCDNNQDIDEDGHQNNLDNCPYVPNANQADHDKDGKGDACDHDDDNDGIPDDKDNCRLVPNPDQKDSDGDGRGDACKDDFDHDSVPDIDDICPENVDISETDFRRFQMIPLDPKGTSQNDPNWVVRHQGKELVQTVNCDPGLAVGYDEFNAVDFSGTFFINTERDDDYAGFVFGYQSSSRFYVVMWKQVTQSYWDTNPTRAQGYSGLSVKVVNSTTGPGEHLRNALWHTGNTPGQVRTLWHDPRHIGWKDFTAYRWRLSHRPKTGFIRVVMYEGKKIMADSGPIYDKTYAGGRLGLFVFSQEMVFFSDLKYECRDP
uniprot
proteins
function
FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions (PubMed:15014436, PubMed:18285447, PubMed:2430973, PubMed:6489349). Multifunctional, involved in inflammation, angiogenesis, wound healing, reactive oxygen species (ROS) signaling, nitrous oxide (NO) signaling, apoptosis, senescence, aging, cellular self-renewal, stemness, and cardiovascular and metabolic homeostasis (PubMed:10613822, PubMed:11134179, PubMed:1371676, PubMed:14568985, PubMed:24511121, PubMed:29042481, PubMed:32679764). Negatively modulates dendritic cell activation and cytokine release, as part of an autocrine feedback loop, contributing to the resolution of inflammation and immune homeostasis (PubMed:14568985). Ligand for receptor CD47 (PubMed:19004835, PubMed:8550562). Modulates nitrous oxide (NO) signaling via CD47, hence playing a role as a pressor agent, supporting blood pressure (By similarity). Plays a role in endothelial cell senescence, acting via CD47, by increasing the abundance and activation of NADPH oxidase NOX1, and so generating excess ROS (PubMed:29042481). Inhibits stem cell self-renewal, acting via CD47 signaling, probably by regulation of the stem cell transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 (By similarity). Negatively modulates wound healing, acting via CD47 (By similarity). Ligand for receptor CD36 (PubMed:10613822, PubMed:11134179, PubMed:1371676). Involved in inducing apoptosis in podocytes in response to elevated free fatty acids, acting via CD36 (By similarity). Plays a role in suppressing angiogenesis, acting, depending on context, via CD36 or CD47 (PubMed:10613822, PubMed:11134179, PubMed:1371676, PubMed:32679764). Promotes cellular senescence in a TP53-CDKN1A-RB1 signaling-dependent manner (PubMed:29042481). Ligand for immunoglobulin-like cell surface receptor SIRPA (PubMed:24511121). Involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production, acting via interaction with SIRPA (PubMed:24511121). Plays a role in metabolic dysfunction in diet-induced obesity, perhaps acting by exacerbating adipose inflammatory activity; its effects may be mediated, at least in part, through enhanced adipocyte proliferation (By similarity). 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). May be involved in age-related conditions, including metabolic dysregulation, during normal aging (PubMed:29042481, PubMed:32679764). {ECO:0000250|UniProtKB:P35441, ECO:0000269|PubMed:10613822, ECO:0000269|PubMed:11134179, ECO:0000269|PubMed:1371676, ECO:0000269|PubMed:14568985, ECO:0000269|PubMed:15014436, ECO:0000269|PubMed:18285447, ECO:0000269|PubMed:19004835, ECO:0000269|PubMed:2430973, ECO:0000269|PubMed:24511121, ECO:0000269|PubMed:29042481, ECO:0000269|PubMed:32679764, ECO:0000269|PubMed:6489349, ECO:0000269|PubMed:8550562}.
uniprot
proteins
mass_dalton
129383
uniprot
proteins
mutagenesis
MUTAGEN 926; /note="R->V: Reduces attachment to cells and retention in extracellular matrix (ECM); retention in ECM partially dependent on beta-1 integrin."; /evidence="ECO:0000269|PubMed:18285447"; MUTAGEN 1019..1021; /note="DDD->AAA: Reduces attachment to cells and retention in extracellular matrix."; /evidence="ECO:0000269|PubMed:18285447"; MUTAGEN 1067; /note="N->K: Loss of N-glycosylation site."; /evidence="ECO:0000269|PubMed:15014436
uniprot
proteins
protein_family
Thrombospondin family
uniprot
proteins
pubmed
101549
uniprot
proteins
pubmed
10613822
uniprot
proteins
pubmed
11067851
uniprot
proteins
pubmed
11134179
uniprot
proteins
pubmed
12391027
uniprot
proteins
pubmed
12450399
uniprot
proteins
pubmed
1371676
uniprot
proteins
pubmed
14568985
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15014436
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16407063
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16740002
uniprot
proteins
pubmed
18042364
uniprot
proteins
pubmed
18065761
uniprot
proteins
pubmed
18285447
uniprot
proteins
pubmed
19004835
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2430973
uniprot
proteins
pubmed
24511121
uniprot
proteins
pubmed
2478219
uniprot
proteins
pubmed
2544587
uniprot
proteins
pubmed
27742621
uniprot
proteins
pubmed
29042481
uniprot
proteins
pubmed
2918029
uniprot
proteins
pubmed
3030396
uniprot
proteins
pubmed
32679764
uniprot
proteins
pubmed
3461443
uniprot
proteins
pubmed
38237698
uniprot
proteins
pubmed
6341993
uniprot
proteins
pubmed
6489349
uniprot
proteins
pubmed
6693501
uniprot
proteins
pubmed
6777381
uniprot
proteins
pubmed
8550562
uniprot
proteins
sequence_length
1170
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:101549, ECO:0000269|PubMed:14568985, ECO:0000269|PubMed:6777381}. Cell surface {ECO:0000269|PubMed:6777381}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18285447, ECO:0000269|PubMed:6341993}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35441}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P35441}. Note=Secreted by thrombin-activated platelets and binds to the cell surface in the presence of extracellular Ca(2+) (PubMed:101549, PubMed:6777381). Incorporated into the extracellular matrix (ECM) of fibroblasts (PubMed:6341993). The C-terminal region in trimeric form is required for retention in the ECM (PubMed:18285447). Also detected in the endoplasmic reticulum and sarcoplasmic reticulum where it plays a role in the ER stress response (By similarity). {ECO:0000250|UniProtKB:P35441, ECO:0000269|PubMed:6341993, ECO:0000269|PubMed:6777381}.
uniprot
proteins