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Thrombospondin-1 (Glycoprotein G)

 TSP1_HUMAN              Reviewed;        1170 AA.
P07996; A8K6H4; B4E3J7; B9EGH6; Q15667; Q59E99;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 2.
17-JUN-2020, entry version 241.
RecName: Full=Thrombospondin-1;
AltName: Full=Glycoprotein G {ECO:0000303|PubMed:6777381};
Flags: Precursor;
Name=THBS1; Synonyms=TSP, TSP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Endothelial cell;
PubMed=2430973; DOI=10.1083/jcb.103.5.1635;
Lawler J., Hynes R.O.;
"The structure of human thrombospondin, an adhesive glycoprotein with
multiple calcium-binding sites and homologies with several different
proteins.";
J. Cell Biol. 103:1635-1648(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-523.
PubMed=2918029; DOI=10.1083/jcb.108.2.729;
Hennessy S.W., Frazier B.A., Kim D.D., Deckwerth T.L., Baumgartel D.M.,
Rotwein P., Frazier W.A.;
"Complete thrombospondin mRNA sequence includes potential regulatory sites
in the 3' untranslated region.";
J. Cell Biol. 108:729-736(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ALA-523.
TISSUE=Placenta, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-700.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human chromosome
15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-397 (ISOFORM 1).
PubMed=3030396; DOI=10.1021/bi00374a014;
Kobayashi S., Eden-Mccutchan F., Framson P., Bornstein P.;
"Partial amino acid sequence of human thrombospondin as determined by
analysis of cDNA clones: homology to malarial circumsporozoite proteins.";
Biochemistry 25:8418-8425(1986).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-374 (ISOFORM 1).
PubMed=3461443; DOI=10.1073/pnas.83.15.5449;
Dixit V.M., Hennessy S.W., Grant G.A., Rotwein P., Frazier W.A.;
"Characterization of a cDNA encoding the heparin and collagen binding
domains of human thrombospondin.";
Proc. Natl. Acad. Sci. U.S.A. 83:5449-5453(1986).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
PubMed=2544587;
Laherty C.D., Gierman T.M., Dixit V.M.;
"Characterization of the promoter region of the human thrombospondin gene.
DNA sequences within the first intron increase transcription.";
J. Biol. Chem. 264:11222-11227(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1170 (ISOFORM 1).
la Fleur M., Jobin C., Gauthier J., Kreis C.G.;
"Expression of thrombospondin in chronic inflammation: neutrophils from
synovial fluids synthesize a novel 3.9 kb TSP mRNA.";
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[11]
SUBCELLULAR LOCATION.
PubMed=6777381;
Phillips D.R., Jennings L.K., Prasanna H.R.;
"Ca2+-mediated association of glycoprotein G (thrombin-sensitive protein,
thrombospondin) with human platelets.";
J. Biol. Chem. 255:11629-11632(1980).
[12]
SUBCELLULAR LOCATION.
PubMed=6341993; DOI=10.1073/pnas.80.4.998;
Jaffe E.A., Ruggiero J.T., Leung L.K., Doyle M.J., McKeown-Longo P.J.,
Mosher D.F.;
"Cultured human fibroblasts synthesize and secrete thrombospondin and
incorporate it into extracellular matrix.";
Proc. Natl. Acad. Sci. U.S.A. 80:998-1002(1983).
[13]
INTERACTION WITH CD36.
PubMed=1371676; DOI=10.1016/0006-291x(92)91860-s;
Asch A.S., Silbiger S., Heimer E., Nachman R.L.;
"Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.";
Biochem. Biophys. Res. Commun. 182:1208-1217(1992).
[14]
GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498 AND
THR-507.
TISSUE=Platelet;
PubMed=11067851; DOI=10.1074/jbc.m008073200;
Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F.,
Peter-Katalinic J.;
"C-mannosylation and O-fucosylation of the thrombospondin type 1 module.";
J. Biol. Chem. 276:6485-6498(2001).
[15]
INTERACTION WITH HRG, AND FUNCTION.
PubMed=11134179; DOI=10.1172/jci9061;
Simantov R., Febbraio M., Crombie R., Asch A.S., Nachman R.L.,
Silverstein R.L.;
"Histidine-rich glycoprotein inhibits the antiangiogenic effect of
thrombospondin-1.";
J. Clin. Invest. 107:45-52(2001).
[16]
DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
PubMed=12450399; DOI=10.1021/bi026463u;
Huwiler K.G., Vestling M.M., Annis D.S., Mosher D.F.;
"Biophysical characterization, including disulfide bond assignments, of the
anti-angiogenic type 1 domains of human thrombospondin-1.";
Biochemistry 41:14329-14339(2002).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248 AND ASN-1067.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by glycoprotein
capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple
enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 434-546, DISULFIDE BONDS, AND
GLYCOSYLATION AT THR-450 AND THR-507.
PubMed=12391027; DOI=10.1083/jcb.200206062;
Tan K., Duquette M., Liu J.-H., Dong Y., Zhang R., Joachimiak A.,
Lawler J., Wang J.-H.;
"Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and
its biological implication.";
J. Cell Biol. 159:373-382(2002).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 834-1170 IN COMPLEX WITH CALCIUM
IONS, DISULFIDE BONDS, MUTAGENESIS OF ASN-1067, GLYCOSYLATION AT ASN-1067,
CELL ATTACHMENT SITE, AND FUNCTION.
PubMed=15014436; DOI=10.1038/sj.emboj.7600166;
Kvansakul M., Adams J.C., Hohenester E.;
"Structure of a thrombospondin C-terminal fragment reveals a novel calcium
core in the type 3 repeats.";
EMBO J. 23:1223-1233(2004).
[25]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-233 IN COMPLEX WITH SYNTHETIC
PENTAMERIC HEPARIN, AND DISULFIDE BOND.
PubMed=16407063; DOI=10.1016/j.str.2005.09.017;
Tan K., Duquette M., Liu J.-H., Zhang R., Joachimiak A., Wang J.-H.,
Lawler J.;
"The structures of the thrombospondin-1 N-terminal domain and its complex
with a synthetic pentameric heparin.";
Structure 14:33-42(2006).
[26]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-257 IN COMPLEXES WITH HEPARIN,
IDENTIFICATION BY MASS SPECTROMETRY, AND GLYCOSYLATION AT ASN-248.
PubMed=18065761; DOI=10.1074/jbc.m705203200;
Tan K., Duquette M., Liu J.-H., Shanmugasundaram K., Joachimiak A.,
Gallagher J.T., Rigby A.C., Wang J.-H., Lawler J.;
"Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1
N-terminal domain.";
J. Biol. Chem. 283:3932-3941(2008).
-!- 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. 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). {ECO:0000250, ECO:0000269|PubMed:11134179,
ECO:0000269|PubMed:15014436}.
-!- SUBUNIT: Homotrimer; disulfide-linked. Interacts (via the TSP type I
repeats) with HRG; the interaction blocks the antiangiogenic effect of
THBS1 with CD36 (By similarity). Can bind to fibrinogen, fibronectin,
laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3
and alpha-IIb/beta-3. Interacts (via the TSP type I repeats) with CD36;
the interaction conveys an antiangiogenic effect. Interacts with ATF6
(via lumenal domain) (By similarity). {ECO:0000250}.
-!- INTERACTION:
P07996; P02751: FN1; NbExp=2; IntAct=EBI-2530274, EBI-1220319;
P07996; Q15113: PCOLCE; NbExp=3; IntAct=EBI-2530274, EBI-8869614;
P07996; P01137: TGFB1; NbExp=2; IntAct=EBI-2530274, EBI-779636;
PRO_0000035842; P16671: CD36; NbExp=2; IntAct=EBI-13915509, EBI-2808214;
PRO_0000035842; Q92743: HTRA1; NbExp=2; IntAct=EBI-13915509, EBI-352256;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6777381}. Cell
surface {ECO:0000269|PubMed:6777381}. Secreted, extracellular space,
extracellular matrix {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:6777381). Incorporated into the
extracellular matrix of fibroblasts (PubMed:6341993). 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07996-1; Sequence=Displayed;
Name=2;
IsoId=P07996-2; Sequence=VSP_055757;
-!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/THBS1ID42548ch15q15.html";
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EMBL; X04665; CAA28370.1; -; mRNA.
EMBL; X14787; CAA32889.1; -; mRNA.
EMBL; AK291639; BAF84328.1; -; mRNA.
EMBL; AK304754; BAG65509.1; -; mRNA.
EMBL; AB209912; BAD93149.1; ALT_INIT; mRNA.
EMBL; AC037198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC136469; AAI36470.1; -; mRNA.
EMBL; BC136470; AAI36471.1; -; mRNA.
EMBL; M25631; AAA36741.1; -; mRNA.
EMBL; M14326; AAA61237.1; ALT_SEQ; mRNA.
EMBL; J04835; AAA61178.1; -; Genomic_DNA.
EMBL; M99425; AAB59366.1; -; mRNA.
CCDS; CCDS32194.1; -. [P07996-1]
PIR; A26155; TSHUP1.
RefSeq; NP_003237.2; NM_003246.3. [P07996-1]
PDB; 1LSL; X-ray; 1.90 A; A=434-546.
PDB; 1UX6; X-ray; 1.90 A; A=834-1170.
PDB; 1Z78; X-ray; 1.80 A; A=19-233.
PDB; 1ZA4; X-ray; 1.90 A; A=19-257.
PDB; 2ERF; X-ray; 1.45 A; A=25-233.
PDB; 2ES3; X-ray; 1.85 A; A/B=25-233.
PDB; 2OUH; X-ray; 2.40 A; A/B=19-257.
PDB; 2OUJ; X-ray; 1.90 A; A=19-257.
PDB; 3R6B; X-ray; 2.40 A; A=434-547.
PDB; 5FOE; X-ray; 1.98 A; A/B=378-429.
PDBsum; 1LSL; -.
PDBsum; 1UX6; -.
PDBsum; 1Z78; -.
PDBsum; 1ZA4; -.
PDBsum; 2ERF; -.
PDBsum; 2ES3; -.
PDBsum; 2OUH; -.
PDBsum; 2OUJ; -.
PDBsum; 3R6B; -.
PDBsum; 5FOE; -.
SMR; P07996; -.
BioGRID; 112915; 42.
ComplexPortal; CPX-1785; Thrombospondin 1 complex.
CORUM; P07996; -.
DIP; DIP-1037N; -.
IntAct; P07996; 26.
MINT; P07996; -.
STRING; 9606.ENSP00000260356; -.
GlyConnect; 594; -.
GlyConnect; 595; -.
GlyConnect; 596; -.
iPTMnet; P07996; -.
MetOSite; P07996; -.
PhosphoSitePlus; P07996; -.
SwissPalm; P07996; -.
UniCarbKB; P07996; -.
BioMuta; THBS1; -.
DMDM; 117949802; -.
OGP; P07996; -.
CPTAC; non-CPTAC-1162; -.
EPD; P07996; -.
jPOST; P07996; -.
MassIVE; P07996; -.
MaxQB; P07996; -.
PaxDb; P07996; -.
PeptideAtlas; P07996; -.
PRIDE; P07996; -.
ProteomicsDB; 52058; -. [P07996-1]
ABCD; P07996; 6 sequenced antibodies.
Antibodypedia; 9950; 687 antibodies.
Ensembl; ENST00000260356; ENSP00000260356; ENSG00000137801. [P07996-1]
GeneID; 7057; -.
KEGG; hsa:7057; -.
UCSC; uc001zkh.4; human. [P07996-1]
CTD; 7057; -.
DisGeNET; 7057; -.
EuPathDB; HostDB:ENSG00000137801.10; -.
GeneCards; THBS1; -.
HGNC; HGNC:11785; THBS1.
HPA; ENSG00000137801; Low tissue specificity.
MIM; 188060; gene.
neXtProt; NX_P07996; -.
OpenTargets; ENSG00000137801; -.
PharmGKB; PA36497; -.
eggNOG; ENOG410IFQQ; Eukaryota.
eggNOG; ENOG410XQKE; LUCA.
GeneTree; ENSGT00940000155832; -.
HOGENOM; CLU_009257_0_0_1; -.
InParanoid; P07996; -.
KO; K16857; -.
OMA; CIHNGIL; -.
OrthoDB; 120983at2759; -.
PhylomeDB; P07996; -.
TreeFam; TF324917; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-5083635; Defective B3GALTL causes Peters-plus syndrome (PpS).
Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SIGNOR; P07996; -.
BioGRID-ORCS; 7057; 3 hits in 790 CRISPR screens.
ChiTaRS; THBS1; human.
EvolutionaryTrace; P07996; -.
GeneWiki; Thrombospondin_1; -.
GenomeRNAi; 7057; -.
Pharos; P07996; Tbio.
PRO; PR:P07996; -.
Proteomes; UP000005640; Chromosome 15.
RNAct; P07996; protein.
Bgee; ENSG00000137801; Expressed in upper lobe of left lung and 217 other tissues.
ExpressionAtlas; P07996; baseline and differential.
Genevisible; P07996; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL.
GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; NAS:BHF-UCL.
GO; GO:0070052; F:collagen V binding; IDA:BHF-UCL.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
GO; GO:0070051; F:fibrinogen binding; IDA:BHF-UCL.
GO; GO:0017134; F:fibroblast growth factor binding; IDA:BHF-UCL.
GO; GO:0001968; F:fibronectin binding; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; NAS:BHF-UCL.
GO; GO:0005178; F:integrin binding; IMP:BHF-UCL.
GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0043394; F:proteoglycan binding; TAS:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
GO; GO:0000187; P:activation of MAPK activity; IMP:BHF-UCL.
GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; NAS:BHF-UCL.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0002544; P:chronic inflammatory response; IEP:BHF-UCL.
GO; GO:0043652; P:engulfment of apoptotic cell; IDA:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006955; P:immune response; IEP:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IDA:CACAO.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0002581; P:negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IDA:BHF-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; IDA:BHF-UCL.
GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; IDA:MGI.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL.
GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; TAS:BHF-UCL.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; IDA:BHF-UCL.
GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IDA:BHF-UCL.
GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL.
GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IGI:BHF-UCL.
GO; GO:0018149; P:peptide cross-linking; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:BHF-UCL.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:BHF-UCL.
GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:BHF-UCL.
GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; ISS:BHF-UCL.
GO; GO:0045727; P:positive regulation of translation; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; IEP:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; NAS:BHF-UCL.
GO; GO:0032026; P:response to magnesium ion; IDA:BHF-UCL.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; TAS:BHF-UCL.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
GO; GO:0002040; P:sprouting angiogenesis; IMP:BHF-UCL.
Gene3D; 2.20.100.10; -; 3.
Gene3D; 4.10.1080.10; -; 2.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR001791; Laminin_G.
InterPro; IPR028499; Thrombospondin-1.
InterPro; IPR003367; Thrombospondin_3-like_rpt.
InterPro; IPR017897; Thrombospondin_3_rpt.
InterPro; IPR008859; Thrombospondin_C.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
InterPro; IPR028974; TSP_type-3_rpt.
InterPro; IPR001007; VWF_dom.
PANTHER; PTHR10199:SF78; PTHR10199:SF78; 1.
Pfam; PF00090; TSP_1; 3.
Pfam; PF02412; TSP_3; 7.
Pfam; PF05735; TSP_C; 1.
Pfam; PF00093; VWC; 1.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00209; TSP1; 3.
SMART; SM00210; TSPN; 1.
SMART; SM00214; VWC; 1.
SUPFAM; SSF103647; SSF103647; 3.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF82895; SSF82895; 3.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS50092; TSP1; 3.
PROSITE; PS51234; TSP3; 8.
PROSITE; PS51236; TSP_CTER; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion; Disulfide bond;
EGF-like domain; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
Heparin-binding; Polymorphism; Reference proteome; Repeat;
Sarcoplasmic reticulum; Secreted; Signal; Unfolded protein response.
SIGNAL 1..18
CHAIN 19..1170
/note="Thrombospondin-1"
/id="PRO_0000035842"
DOMAIN 65..270
/note="Laminin G-like"
DOMAIN 316..373
/note="VWFC"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
DOMAIN 379..429
/note="TSP type-1 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
DOMAIN 435..490
/note="TSP type-1 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
DOMAIN 492..547
/note="TSP type-1 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
DOMAIN 547..587
/note="EGF-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 646..690
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REPEAT 691..726
/note="TSP type-3 1"
REPEAT 727..762
/note="TSP type-3 2"
REPEAT 763..785
/note="TSP type-3 3"
REPEAT 786..821
/note="TSP type-3 4"
REPEAT 822..844
/note="TSP type-3 5"
REPEAT 845..882
/note="TSP type-3 6"
REPEAT 883..918
/note="TSP type-3 7"
REPEAT 919..954
/note="TSP type-3 8"
DOMAIN 958..1170
/note="TSP C-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
REGION 47..95
/note="Heparin-binding"
MOTIF 926..928
/note="Cell attachment site"
/evidence="ECO:0000305"
CARBOHYD 248
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000305|PubMed:16263699,
ECO:0000305|PubMed:16335952, ECO:0000305|PubMed:18065761"
CARBOHYD 360
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 385
/note="C-linked (Man) tryptophan"
/evidence="ECO:0000269|PubMed:11067851"
/id="CAR_000205"
CARBOHYD 394
/note="O-linked (Fuc...) serine"
/evidence="ECO:0000269|PubMed:11067851"
/id="CAR_000206"
CARBOHYD 438
/note="C-linked (Man) tryptophan"
/evidence="ECO:0000269|PubMed:11067851"
/id="CAR_000207"
CARBOHYD 441
/note="C-linked (Man) tryptophan"
/evidence="ECO:0000269|PubMed:11067851"
/id="CAR_000208"
CARBOHYD 450
/note="O-linked (Fuc...) threonine"
/evidence="ECO:0000269|PubMed:11067851,
ECO:0000269|PubMed:12391027"
/id="CAR_000209"
CARBOHYD 498
/note="C-linked (Man) tryptophan"
/evidence="ECO:0000269|PubMed:11067851"
/id="CAR_000210"
CARBOHYD 507
/note="O-linked (Fuc...) threonine"
/evidence="ECO:0000269|PubMed:11067851,
ECO:0000269|PubMed:12391027"
/id="CAR_000211"
CARBOHYD 708
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1067
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15014436,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218"
DISULFID 171..232
/evidence="ECO:0000244|PDB:1Z78, ECO:0000244|PDB:2ERF,
ECO:0000244|PDB:2ES3, ECO:0000244|PDB:2OUH,
ECO:0000244|PDB:2OUJ, ECO:0000269|PubMed:16407063,
ECO:0000269|PubMed:18065761"
DISULFID 270
/note="Interchain"
/evidence="ECO:0000305"
DISULFID 274
/note="Interchain"
/evidence="ECO:0000305"
DISULFID 391..423
DISULFID 395..428
DISULFID 406..413
DISULFID 447..484
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 451..489
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 462..474
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 504..541
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 508..546
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 519..531
/evidence="ECO:0000244|PDB:1LSL,
ECO:0000269|PubMed:12391027"
DISULFID 551..562
/evidence="ECO:0000250"
DISULFID 556..572
/evidence="ECO:0000250"
DISULFID 575..586
/evidence="ECO:0000250"
DISULFID 592..608
/evidence="ECO:0000250"
DISULFID 599..617
/evidence="ECO:0000250"
DISULFID 620..644
/evidence="ECO:0000250"
DISULFID 650..663
/evidence="ECO:0000250"
DISULFID 657..676
/evidence="ECO:0000250"
DISULFID 678..689
/evidence="ECO:0000250"
DISULFID 705..713
/evidence="ECO:0000250"
DISULFID 718..738
/evidence="ECO:0000250"
DISULFID 754..774
/evidence="ECO:0000250"
DISULFID 777..797
/evidence="ECO:0000250"
DISULFID 813..833
/evidence="ECO:0000250"
DISULFID 836..856
/evidence="ECO:0000244|PDB:1UX6,
ECO:0000269|PubMed:15014436"
DISULFID 874..894
/evidence="ECO:0000244|PDB:1UX6,
ECO:0000269|PubMed:15014436"
DISULFID 910..930
/evidence="ECO:0000244|PDB:1UX6,
ECO:0000269|PubMed:15014436"
DISULFID 946..1167
/evidence="ECO:0000244|PDB:1UX6,
ECO:0000269|PubMed:15014436"
VAR_SEQ 17..101
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_055757"
VARIANT 24
/note="S -> A (in dbSNP:rs41515347)"
/id="VAR_052657"
VARIANT 523
/note="T -> A (in dbSNP:rs2292305)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:2918029"
/id="VAR_028938"
VARIANT 700
/note="N -> S (in dbSNP:rs2228262)"
/evidence="ECO:0000269|Ref.4"
/id="VAR_028939"
MUTAGEN 1067
/note="N->K: Loss of N-glycosylation site."
/evidence="ECO:0000269|PubMed:15014436"
CONFLICT 4
/note="A -> S (in Ref. 3; BAG65509)"
/evidence="ECO:0000305"
CONFLICT 84
/note="A -> T (in Ref. 1; CAA28370 and 9; AAA61178)"
/evidence="ECO:0000305"
CONFLICT 431
/note="R -> I (in Ref. 3; BAG65509)"
/evidence="ECO:0000305"
CONFLICT 451
/note="C -> R (in Ref. 3; BAG65509)"
/evidence="ECO:0000305"
CONFLICT 546
/note="C -> Y (in Ref. 3; BAF84328)"
/evidence="ECO:0000305"
CONFLICT 812
/note="N -> D (in Ref. 3; BAG65509)"
/evidence="ECO:0000305"
CONFLICT 1008
/note="F -> S (in Ref. 3; BAF84328)"
/evidence="ECO:0000305"
STRAND 30..32
/evidence="ECO:0000244|PDB:2ERF"
HELIX 33..37
/evidence="ECO:0000244|PDB:2ERF"
TURN 38..41
/evidence="ECO:0000244|PDB:2ERF"
STRAND 44..49
/evidence="ECO:0000244|PDB:2ERF"
STRAND 58..62
/evidence="ECO:0000244|PDB:2ERF"
HELIX 64..66
/evidence="ECO:0000244|PDB:2ERF"
HELIX 72..85
/evidence="ECO:0000244|PDB:2ERF"
STRAND 87..96
/evidence="ECO:0000244|PDB:2ERF"
STRAND 101..109
/evidence="ECO:0000244|PDB:2ERF"
STRAND 115..122
/evidence="ECO:0000244|PDB:2ERF"
TURN 123..126
/evidence="ECO:0000244|PDB:2ERF"
STRAND 127..134
/evidence="ECO:0000244|PDB:2ERF"
STRAND 137..145
/evidence="ECO:0000244|PDB:2ERF"
STRAND 150..161
/evidence="ECO:0000244|PDB:2ERF"
STRAND 164..169
/evidence="ECO:0000244|PDB:2ERF"
TURN 170..172
/evidence="ECO:0000244|PDB:2ERF"
STRAND 173..178
/evidence="ECO:0000244|PDB:2ERF"
HELIX 183..185
/evidence="ECO:0000244|PDB:2ERF"
HELIX 191..194
/evidence="ECO:0000244|PDB:2ERF"
STRAND 195..200
/evidence="ECO:0000244|PDB:2ERF"
TURN 203..205
/evidence="ECO:0000244|PDB:2ERF"
STRAND 210..218
/evidence="ECO:0000244|PDB:2ERF"
HELIX 223..228
/evidence="ECO:0000244|PDB:2ERF"
TURN 229..231
/evidence="ECO:0000244|PDB:2OUH"
STRAND 394..403
/evidence="ECO:0000244|PDB:5FOE"
TURN 408..410
/evidence="ECO:0000244|PDB:5FOE"
STRAND 417..424
/evidence="ECO:0000244|PDB:5FOE"
STRAND 450..459
/evidence="ECO:0000244|PDB:1LSL"
STRAND 478..485
/evidence="ECO:0000244|PDB:1LSL"
STRAND 507..509
/evidence="ECO:0000244|PDB:1LSL"
STRAND 511..516
/evidence="ECO:0000244|PDB:1LSL"
STRAND 535..541
/evidence="ECO:0000244|PDB:1LSL"
TURN 838..840
/evidence="ECO:0000244|PDB:1UX6"
STRAND 849..852
/evidence="ECO:0000244|PDB:1UX6"
TURN 854..856
/evidence="ECO:0000244|PDB:1UX6"
STRAND 865..867
/evidence="ECO:0000244|PDB:1UX6"
HELIX 869..871
/evidence="ECO:0000244|PDB:1UX6"
STRAND 888..890
/evidence="ECO:0000244|PDB:1UX6"
HELIX 892..894
/evidence="ECO:0000244|PDB:1UX6"
STRAND 901..903
/evidence="ECO:0000244|PDB:1UX6"
HELIX 905..907
/evidence="ECO:0000244|PDB:1UX6"
TURN 909..912
/evidence="ECO:0000244|PDB:1UX6"
STRAND 924..926
/evidence="ECO:0000244|PDB:1UX6"
HELIX 928..930
/evidence="ECO:0000244|PDB:1UX6"
STRAND 937..939
/evidence="ECO:0000244|PDB:1UX6"
TURN 941..943
/evidence="ECO:0000244|PDB:1UX6"
STRAND 961..965
/evidence="ECO:0000244|PDB:1UX6"
STRAND 986..988
/evidence="ECO:0000244|PDB:1UX6"
STRAND 995..1014
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1022..1031
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1034..1043
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1051..1053
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1059..1067
/evidence="ECO:0000244|PDB:1UX6"
HELIX 1074..1081
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1082..1084
/evidence="ECO:0000244|PDB:1UX6"
TURN 1087..1089
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1090..1095
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1107..1115
/evidence="ECO:0000244|PDB:1UX6"
TURN 1116..1119
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1120..1127
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1130..1134
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1146..1154
/evidence="ECO:0000244|PDB:1UX6"
STRAND 1156..1167
/evidence="ECO:0000244|PDB:1UX6"
SEQUENCE 1170 AA; 129383 MW; 74749B2418E0943B CRC64;
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


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LF-MA41371 anti-Thrombospondin 1 , Mouse monoclonal to Thrombospondin 1, Isotype IgG1, Host Mouse 50 ug
orb82126 Human Thrombospondin protein Thrombospondin, Human is a purified platelets_hemostasis antigen. For research use only. 25
EIAAB34629 Ammonium transporter Rh type C,C15orf6,CDRC2,Homo sapiens,Human,PDRC2,Rh family type C glycoprotein,Rh glycoprotein kidney,Rh type C glycoprotein,RHCG,Rhesus blood group family type C glycoprotein,RHG
20-272-190593 Thrombospondin - Mouse monoclonal [TSP - B7] to Thrombospondin; Megakaryocyte colony-stimulating factor; Myeloproliferative leukemia virus oncogene ligand; C-mpl ligand; ML; Megakaryocyte growth and d 0.1 ml
20-272-192237 Thrombospondin - Mouse monoclonal [A6.1] to Thrombospondin; Megakaryocyte colony-stimulating factor; Myeloproliferative leukemia virus oncogene ligand; C-mpl ligand; ML; Megakaryocyte growth and devel 0.25 ml
E0674b ELISA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674b ELISA kit Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674b CLIA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674m CLIA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA kit Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
EIAAB34597 Ammonium transporter Rh type A,Erythrocyte membrane glycoprotein Rh50,Mouse,Mus musculus,Rh family type A glycoprotein,Rh type A glycoprotein,Rh50,Rhag,Rhesus blood group family type A glycoprotein
EIAAB34594 Ammonium transporter Rh type A,Bos taurus,Bovine,Erythrocyte membrane glycoprotein Rh50,Rh family type A glycoprotein,Rh type A glycoprotein,RH50,RHAG,Rhesus blood group family type A glycoprotein
EIAAB34596 Ammonium transporter Rh type A,Erythrocyte membrane glycoprotein Rh50,Rat,Rattus norvegicus,Rh family type A glycoprotein,Rh type A glycoprotein,Rh50,Rhag,Rhesus blood group family type A glycoprotein
EIAAB43501 5t4,5T4 oncofetal trophoblast glycoprotein,5T4 oncotrophoblast glycoprotein,Mouse,Mus musculus,Tpbg,Trophoblast glycoprotein
EIAAB43500 5t4,5T4 oncofetal trophoblast glycoprotein,5T4 oncotrophoblast glycoprotein,Rat,Rattus norvegicus,Tpbg,Trophoblast glycoprotein
EIAAB34595 Ammonium transporter Rh type A,Erythrocyte membrane glycoprotein Rh50,Erythrocyte plasma membrane 50 kDa glycoprotein,Homo sapiens,Human,Rh family type A glycoprotein,Rh type A glycoprotein,RH50,Rh50A
EIAAB43502 5T4,5T4 oncofetal antigen,5T4 oncofetal trophoblast glycoprotein,5T4 oncotrophoblast glycoprotein,Homo sapiens,Human,M6P1,TPBG,Trophoblast glycoprotein
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
Pathways :
WP1970: Glycoprotein VI platelet signaling

Related Genes :
[THBS1 TSP TSP1] Thrombospondin-1 (Glycoprotein G)
[Thbs1 Tsp1] Thrombospondin-1 (Glycoprotein G)
[CD36 GP3B GP4] Platelet glycoprotein 4 (Fatty acid translocase) (FAT) (Glycoprotein IIIb) (GPIIIB) (Leukocyte differentiation antigen CD36) (PAS IV) (PAS-4) (Platelet collagen receptor) (Platelet glycoprotein IV) (GPIV) (Thrombospondin receptor) (CD antigen CD36)
[THBS1 TSP-1 TSP1] Thrombospondin-1 (Glycoprotein G)
[THSD7A KIAA0960] Thrombospondin type-1 domain-containing protein 7A [Cleaved into: Thrombospondin type-1 domain-containing protein 7A, soluble form]
[Adamts2] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[Adamts1] A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-)
[Adamts1] A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-)
[ADAMTS4 KIAA0688 UNQ769/PRO1563] A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (ADMP-1) (Aggrecanase-1)
[TSPEAR C21orf29] Thrombospondin-type laminin G domain and EAR repeat-containing protein (TSP-EAR)
[ADAMTSL4 TSRC1 PP1396 UNQ2803/PRO34012] ADAMTS-like protein 4 (ADAMTSL-4) (Thrombospondin repeat-containing protein 1)
[thsd7aa thsd7a si:dkey-12h3.1] Thrombospondin type-1 domain-containing protein 7A
[gon-1 F25H8.3] A disintegrin and metalloproteinase with thrombospondin motifs gon-1 (ADAMTS gon-1) (EC 3.4.24.-) (Abnormal gonad development protein 1)
[ADAMTS5 ADAMTS11 ADMP2] A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (A disintegrin and metalloproteinase with thrombospondin motifs 11) (ADAM-TS 11) (ADAMTS-11) (ADMP-2) (Aggrecanase-2)
[ADAMTS1 KIAA1346 METH1] A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-) (METH-1)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[ADAMTS2 PCINP PCPNI] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[Thsd7a Gm837 Kiaa0960] Thrombospondin type-1 domain-containing protein 7A [Cleaved into: Thrombospondin type-1 domain-containing protein 7A, soluble form]
[Rspo1] R-spondin-1 (Cysteine-rich and single thrombospondin domain-containing protein 3) (Cristin-3) (mCristin-3) (Roof plate-specific spondin-1)
[ADAMTS2 NPI] A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
[RSPO3 PWTSR THSD2] R-spondin-3 (Protein with TSP type-1 repeat) (hPWTSR) (Roof plate-specific spondin-3) (hRspo3) (Thrombospondin type-1 domain-containing protein 2)
[Rspo3] R-spondin-3 (Cabriolet) (Cysteine-rich and single thrombospondin domain-containing protein 1) (Cristin-1) (Nucleopondin) (Roof plate-specific spondin-3)
[ADAMTS13 C9orf8 UNQ6102/PRO20085] A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease)
[COMP] Cartilage oligomeric matrix protein (COMP) (Thrombospondin-5) (TSP5)
[Adamts4] A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (Aggrecanase-1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ADAMTS14] A disintegrin and metalloproteinase with thrombospondin motifs 14 (ADAM-TS 14) (ADAM-TS14) (ADAMTS-14) (EC 3.4.24.-)
[ADAMTS18 ADAMTS21] A disintegrin and metalloproteinase with thrombospondin motifs 18 (ADAM-TS 18) (ADAM-TS18) (ADAMTS-18) (EC 3.4.24.-)
[ADAMTS12 UNQ1918/PRO4389] A disintegrin and metalloproteinase with thrombospondin motifs 12 (ADAM-TS 12) (ADAM-TS12) (ADAMTS-12) (EC 3.4.24.-)
[Adamts20] A disintegrin and metalloproteinase with thrombospondin motifs 20 (ADAM-TS 20) (ADAM-TS20) (ADAMTS-20) (EC 3.4.24.-)

Bibliography :