P07996 (TSP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thrombospondin-1

Gene names

Name:	THBS1
Synonyms:	TSP, TSP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1170 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.12 Ref.20
Subunit structure	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. Ref.10 Ref.12 Ref.13 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the thrombospondin family. Contains 2 EGF-like domains. Contains 1 laminin G-like domain. Contains 1 TSP C-terminal (TSPC) domain. Contains 3 TSP type-1 domains. Contains 8 TSP type-3 repeats. Contains 1 VWFC domain.

Ontologies

Keywords
Biological process	Cell adhesion
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from mutant phenotype PubMed 17413041. Source: BHF-UCL cell adhesion Non-traceable author statement PubMed 9304800. Source: BHF-UCL cell cycle arrest Inferred from direct assay PubMed 17596205. Source: BHF-UCL cell migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL cellular response to heat Non-traceable author statement PubMed 9304800. Source: BHF-UCL chronic inflammatory response Inferred from expression pattern PubMed 18674744. Source: BHF-UCL endocardial cushion development Inferred from electronic annotation. Source: Compara engulfment of apoptotic cell Inferred from direct assay PubMed 16882710. Source: BHF-UCL growth plate cartilage development Inferred from electronic annotation. Source: Compara immune response Inferred from expression pattern PubMed 18674744. Source: BHF-UCL induction of apoptosis Inferred from direct assay PubMed 18726995. Source: UniProtKB negative regulation of angiogenesis Inferred from direct assay PubMed 18726995. Source: UniProtKB negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II Inferred from direct assay PubMed 16882710. Source: BHF-UCL negative regulation of apoptotic process Inferred from direct assay PubMed 18653767. Source: UniProtKB negative regulation of blood vessel endothelial cell migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL negative regulation of cGMP-mediated signaling Inferred from direct assay PubMed 17416590. Source: BHF-UCL negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 18653767. Source: UniProtKB negative regulation of dendritic cell antigen processing and presentation Inferred from direct assay PubMed 16882710. Source: BHF-UCL negative regulation of endothelial cell proliferation Inferred from direct assay PubMed 17996481. Source: BHF-UCL negative regulation of fibrinolysis Inferred from direct assay PubMed 6438154. Source: BHF-UCL negative regulation of fibroblast growth factor receptor signaling pathway Inferred from direct assay PubMed 17996481. Source: BHF-UCL negative regulation of focal adhesion assembly Traceable author statement PubMed 9304800. Source: BHF-UCL negative regulation of interleukin-12 production Inferred from direct assay PubMed 16882710. Source: BHF-UCL negative regulation of nitric oxide mediated signal transduction Inferred from direct assay PubMed 17416590. Source: BHF-UCL negative regulation of plasma membrane long-chain fatty acid transport Inferred from direct assay PubMed 17416590. Source: BHF-UCL negative regulation of plasminogen activation Inferred from direct assay PubMed 6438154. Source: BHF-UCL outflow tract morphogenesis Inferred from electronic annotation. Source: Compara peptide cross-linking Inferred from direct assay PubMed 3997886. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of angiogenesis Inferred from mutant phenotype PubMed 17413041PubMed 17879962. Source: BHF-UCL positive regulation of blood vessel endothelial cell migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara positive regulation of eukaryotic cell surface binding Inferred from direct assay PubMed 2435757. Source: BHF-UCL positive regulation of fibroblast migration Inferred from direct assay PubMed 18555217. Source: BHF-UCL positive regulation of macrophage activation Inferred from direct assay PubMed 18757424. Source: BHF-UCL positive regulation of macrophage chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from direct assay PubMed 18653767. Source: UniProtKB positive regulation of reactive oxygen species metabolic process Inferred from direct assay PubMed 18757424. Source: BHF-UCL positive regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 18555217. Source: BHF-UCL positive regulation of transforming growth factor beta1 production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of translation Inferred from direct assay PubMed 15700281. Source: BHF-UCL positive regulation of tumor necrosis factor biosynthetic process Inferred from direct assay PubMed 18726995. Source: UniProtKB response to calcium ion Inferred from direct assay PubMed 18757424PubMed 6777381. Source: BHF-UCL response to drug Inferred from expression pattern PubMed 19738618. Source: UniProtKB response to glucose stimulus Inferred from direct assay PubMed 18096704. Source: BHF-UCL response to hypoxia Non-traceable author statement PubMed 9304800. Source: BHF-UCL response to magnesium ion Inferred from direct assay PubMed 6777381. Source: BHF-UCL response to progesterone stimulus Traceable author statement PubMed 9304800. Source: BHF-UCL sprouting angiogenesis Inferred from mutant phenotype PubMed 17879962. Source: BHF-UCL
Cellular_component	external side of plasma membrane Inferred from direct assay PubMed 6777381. Source: BHF-UCL extracellular matrix Traceable author statement PubMed 9304800. Source: BHF-UCL extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB fibrinogen complex Inferred from direct assay PubMed 3997886. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Non-traceable author statement PubMed 9304800. Source: BHF-UCL collagen V binding Inferred from direct assay PubMed 6693501. Source: BHF-UCL eukaryotic cell surface binding Inferred from direct assay PubMed 3084490PubMed 6777381. Source: BHF-UCL fibrinogen binding Inferred from direct assay PubMed 6693501. Source: BHF-UCL fibroblast growth factor binding Inferred from direct assay PubMed 17996481. Source: BHF-UCL fibronectin binding Inferred from direct assay PubMed 6693501. Source: BHF-UCL heparin binding Inferred from direct assay PubMed 101549. Source: BHF-UCL identical protein binding Non-traceable author statement PubMed 9304800. Source: BHF-UCL integrin binding Inferred from mutant phenotype PubMed 17413041PubMed 18757424. Source: BHF-UCL laminin binding Inferred from direct assay PubMed 6693501. Source: BHF-UCL low-density lipoprotein particle binding Inferred from direct assay PubMed 6693501. Source: BHF-UCL phosphatidylserine binding Inferred from direct assay PubMed 18940719. Source: UniProtKB proteoglycan binding Traceable author statement PubMed 9304800. Source: BHF-UCL transforming growth factor beta binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TGFB1	P01137	2	EBI-2530274,EBI-779636

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Chain

19 – 1170

1152

Thrombospondin-1

PRO_0000035842

Regions

Domain

65 – 270

206

Laminin G-like

Domain

316 – 373

58

VWFC

Domain

379 – 429

51

TSP type-1 1

Domain

435 – 490

56

TSP type-1 2

Domain

492 – 547

56

TSP type-1 3

Domain

547 – 587

41

EGF-like 1

Domain

646 – 690

45

EGF-like 2

Repeat

691 – 726

36

TSP type-3 1

Repeat

727 – 762

36

TSP type-3 2

Repeat

763 – 785

23

TSP type-3 3

Repeat

786 – 821

36

TSP type-3 4

Repeat

822 – 844

23

TSP type-3 5

Repeat

845 – 882

38

TSP type-3 6

Repeat

883 – 918

36

TSP type-3 7

Repeat

919 – 954

36

TSP type-3 8

Domain

958 – 1170

213

TSP C-terminal

Region

47 – 95

49

Heparin-binding

Motif

926 – 928

3

Cell attachment site Probable

Amino acid modifications

Glycosylation

248

1

N-linked (GlcNAc...) Probable

Glycosylation

360

1

N-linked (GlcNAc...) Potential

Glycosylation

385

1

C-linked (Man) Ref.11

CAR_000205

Glycosylation

394

1

O-linked (Fuc...) Ref.11

CAR_000206

Glycosylation

438

1

C-linked (Man) Ref.11

CAR_000207

Glycosylation

441

1

C-linked (Man) Ref.11

CAR_000208

Glycosylation

450

1

O-linked (Fuc...) Ref.11 Ref.19

CAR_000209

Glycosylation

498

1

C-linked (Man) Ref.11

CAR_000210

Glycosylation

507

1

O-linked (Fuc...) Ref.11 Ref.19

CAR_000211

Glycosylation

708

1

N-linked (GlcNAc...) Potential

Glycosylation

1067

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.17 Ref.20

Disulfide bond

171 ↔ 232

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

270

Interchain Probable

Disulfide bond

274

Interchain Probable

Disulfide bond

391 ↔ 423

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

395 ↔ 428

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

406 ↔ 413

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

447 ↔ 484

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

451 ↔ 489

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

462 ↔ 474

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

504 ↔ 541

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

508 ↔ 546

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

519 ↔ 531

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

551 ↔ 562

By similarity

Disulfide bond

556 ↔ 572

By similarity

Disulfide bond

575 ↔ 586

By similarity

Disulfide bond

592 ↔ 608

By similarity

Disulfide bond

599 ↔ 617

By similarity

Disulfide bond

620 ↔ 644

By similarity

Disulfide bond

650 ↔ 663

By similarity

Disulfide bond

657 ↔ 676

By similarity

Disulfide bond

678 ↔ 689

By similarity

Disulfide bond

705 ↔ 713

By similarity

Disulfide bond

718 ↔ 738

By similarity

Disulfide bond

754 ↔ 774

By similarity

Disulfide bond

777 ↔ 797

By similarity

Disulfide bond

813 ↔ 833

By similarity

Disulfide bond

836 ↔ 856

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

874 ↔ 894

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

910 ↔ 930

Ref.13 Ref.19 Ref.20 Ref.21

Disulfide bond

946 ↔ 1167

Ref.13 Ref.19 Ref.20 Ref.21

Natural variations

Natural variant

24

1

S → A.
Corresponds to variant rs41515347 [ dbSNP | Ensembl ].

VAR_052657

Natural variant

523

1

T → A. Ref.2 Ref.3
Corresponds to variant rs2292305 [ dbSNP | Ensembl ].

VAR_028938

Natural variant

700

1

N → S.
Corresponds to variant rs2228262 [ dbSNP | Ensembl ].

VAR_028939

Experimental info

Mutagenesis

1067

1

N → K: Loss of N-glycosylation site. Ref.20

Sequence conflict

84

1

A → T in CAA28370. Ref.1

Sequence conflict

84

1

A → T in AAA61178. Ref.8

Sequence conflict

546

1

C → Y in BAF84328. Ref.3

Sequence conflict

1008

1

F → S in BAF84328. Ref.3

Secondary structure

1

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1170

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Helix

33 – 37

5

Turn

38 – 41

4

Beta strand

44 – 49

6

Beta strand

58 – 62

5

Helix

64 – 66

3

Helix

72 – 85

14

Beta strand

87 – 96

10

Beta strand

101 – 109

9

Beta strand

115 – 122

8

Turn

123 – 126

4

Beta strand

127 – 134

8

Beta strand

137 – 145

9

Beta strand

150 – 161

12

Beta strand

164 – 169

6

Turn

170 – 172

3

Beta strand

173 – 178

6

Helix

183 – 185

3

Helix

191 – 194

4

Beta strand

195 – 200

6

Turn

203 – 205

3

Beta strand

210 – 218

9

Helix

223 – 228

6

Turn

229 – 231

3

Beta strand

450 – 459

10

Beta strand

478 – 485

8

Beta strand

507 – 509

3

Beta strand

511 – 516

6

Beta strand

535 – 541

7

Turn

838 – 840

3

Beta strand

849 – 852

4

Turn

854 – 856

3

Beta strand

865 – 867

3

Helix

869 – 871

3

Beta strand

888 – 890

3

Helix

892 – 894

3

Beta strand

901 – 903

3

Helix

905 – 907

3

Turn

909 – 912

4

Beta strand

924 – 926

3

Helix

928 – 930

3

Beta strand

937 – 939

3

Turn

941 – 943

3

Beta strand

961 – 965

5

Beta strand

986 – 988

3

Beta strand

995 – 1014

20

Beta strand

1022 – 1031

10

Beta strand

1034 – 1043

10

Beta strand

1051 – 1053

3

Beta strand

1059 – 1067

9

Helix

1074 – 1081

8

Beta strand

1082 – 1084

3

Turn

1087 – 1089

3

Beta strand

1090 – 1095

6

Beta strand

1107 – 1115

9

Turn

1116 – 1119

4

Beta strand

1120 – 1127

8

Beta strand

1130 – 1134

5

Beta strand

1146 – 1154

9

Beta strand

1156 – 1167

12

Sequences

	Sequence		Length	Mass (Da)
	P07996 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 74749B2418E0943B	FASTA	1,170	129,383
	10 20 30 40 50 60 MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK GPDPSSPAFR 70 80 90 100 110 120 IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLALERK DHSGQVFSVV 130 140 150 160 170 180 SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD 190 200 210 220 230 240 VPIQSVFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL 250 260 270 280 290 300 TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK 310 320 330 340 350 360 VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN 370 380 390 400 410 420 ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ QRGRSCDSLN NRCEGSSVQT 430 440 450 460 470 480 RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE 490 500 510 520 530 540 TKACKKDACP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI 550 560 570 580 590 600 CNKQDCPIDG CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF 610 620 630 640 650 660 NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC TDGTHDCNKN 670 680 690 700 710 720 AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN 730 740 750 760 770 780 LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN 790 800 810 820 830 840 HNPDQADTDN NGEGDACAAD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH 850 860 870 880 890 900 NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN 910 920 930 940 950 960 DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV DISETDFRRF 970 980 990 1000 1010 1020 QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD 1030 1040 1050 1060 1070 1080 DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL 1090 1100 1110 1120 1130 1140 WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD 1150 1160 1170 KTYAGGRLGL FVFSQEMVFF SDLKYECRDP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins." Lawler J., Hynes R.O. J. Cell Biol. 103:1635-1648(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endothelial cell.
[2]	"Complete thrombospondin mRNA sequence includes potential regulatory sites in the 3' untranslated region." Hennessy S.W., Frazier B.A., Kim D.D., Deckwerth T.L., Baumgartel D.M., Rotwein P., Frazier W.A. J. Cell Biol. 108:729-736(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-523.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-523. Tissue: Placenta.
[4]	"Analysis of the DNA sequence and duplication history of human chromosome 15." 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. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	"Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins." Kobayashi S., Eden-Mccutchan F., Framson P., Bornstein P. Biochemistry 25:8418-8425(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-397.
[7]	"Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin." Dixit V.M., Hennessy S.W., Grant G.A., Rotwein P., Frazier W.A. Proc. Natl. Acad. Sci. U.S.A. 83:5449-5453(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-374.
[8]	"Characterization of the promoter region of the human thrombospondin gene. DNA sequences within the first intron increase transcription." Laherty C.D., Gierman T.M., Dixit V.M. J. Biol. Chem. 264:11222-11227(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
[9]	"Expression of thrombospondin in chronic inflammation: neutrophils from synovial fluids synthesize a novel 3.9 kb TSP mRNA." la Fleur M., Jobin C., Gauthier J., Kreis C.G. Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1170.
[10]	"Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding." Asch A.S., Silbiger S., Heimer E., Nachman R.L. Biochem. Biophys. Res. Commun. 182:1208-1217(1992) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD36.
[11]	"C-mannosylation and O-fucosylation of the thrombospondin type 1 module." Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J. J. Biol. Chem. 276:6485-6498(2001) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498 AND THR-507. Tissue: Platelet.
[12]	"Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1." Simantov R., Febbraio M., Crombie R., Asch A.S., Nachman R.L., Silverstein R.L. J. Clin. Invest. 107:45-52(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HRG, FUNCTION.
[13]	"Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1." Huwiler K.G., Vestling M.M., Annis D.S., Mosher D.F. Biochemistry 41:14329-14339(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
[14]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248 AND ASN-1067, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, MASS SPECTROMETRY. Tissue: Saliva.
[16]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication." Tan K., Duquette M., Liu J.-H., Dong Y., Zhang R., Joachimiak A., Lawler J., Wang J.-H. J. Cell Biol. 159:373-382(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 434-546, DISULFIDE BONDS, GLYCOSYLATION AT THR-450 AND THR-507.
[20]	"Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats." Kvansakul M., Adams J.C., Hohenester E. EMBO J. 23:1223-1233(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 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, FUNCTION.
[21]	"The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin." Tan K., Duquette M., Liu J.-H., Zhang R., Joachimiak A., Wang J.-H., Lawler J. Structure 14:33-42(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-233 IN COMPLEX WITH SYNTHETIC PENTAMERIC HEPARIN, DISULFIDE BOND.
[22]	"Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain." Tan K., Duquette M., Liu J.-H., Shanmugasundaram K., Joachimiak A., Gallagher J.T., Rigby A.C., Wang J.-H., Lawler J. J. Biol. Chem. 283:3932-3941(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-257 IN COMPLEXES WITH HEPARIN, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-248.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04665 mRNA. Translation: CAA28370.1.
X14787 mRNA. Translation: CAA32889.1.
AK291639 mRNA. Translation: BAF84328.1.
AC037198 Genomic DNA. No translation available.
BC136469 mRNA. Translation: AAI36470.1.
BC136470 mRNA. Translation: AAI36471.1.
M25631 mRNA. Translation: AAA36741.1.
M14326 mRNA. Translation: AAA61237.1. Sequence problems.
J04835 Genomic DNA. Translation: AAA61178.1.
M99425 mRNA. Translation: AAB59366.1.

IPI

IPI00296099.

PIR

TSHUP1. A26155.

RefSeq

NP_003237.2. NM_003246.2.

UniGene

Hs.164226.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LSL	X-ray	1.90	A	434-546	[»]
1UX6	X-ray	1.90	A	834-1170	[»]
1Z78	X-ray	1.80	A	19-233	[»]
1ZA4	X-ray	1.90	A	19-257	[»]
2ERF	X-ray	1.45	A	25-233	[»]
2ES3	X-ray	1.85	A/B	25-233	[»]
2OUH	X-ray	2.40	A/B	19-257	[»]
2OUJ	X-ray	1.90	A	19-257	[»]
3R6B	X-ray	2.40	A	434-547	[»]

ProteinModelPortal

P07996.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1037N.

IntAct

P07996. 10 interactions.

MINT

MINT-6630675.

STRING

9606.ENSP00000260356.

PTM databases

GlycoSuiteDB

P07996.

PhosphoSite

P07996.

Polymorphism databases

DMDM

117949802.

2D gel databases

OGP

P07996.

Proteomic databases

PaxDb

P07996.

PeptideAtlas

P07996.

PRIDE

P07996.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260356; ENSP00000260356; ENSG00000137801.

GeneID

7057.

KEGG

hsa:7057.

UCSC

uc001zkh.3. human.

Organism-specific databases

CTD

7057.

GeneCards

GC15P039873.

H-InvDB

HIX0038125.

HGNC

HGNC:11785. THBS1.

HPA

CAB033678.

MIM

188060. gene.

neXtProt

NX_P07996.

PharmGKB

PA36497.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG018006.

InParanoid

P07996.

KO

K16857.

OMA

SPWDICS.

OrthoDB

EOG466VK5.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P07996.

Bgee

P07996.

CleanEx

HS_THBS1.

Genevestigator

P07996.

GermOnline

ENSG00000137801. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 3 hits.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
IPR000884. Thrombospondin_1_rpt.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF07645. EGF_CA. 1 hit.
PF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]

SMART

SM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 2 hits.
SSF82895. TSP1. 3 hits.

PROSITE

PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50025. LAM_G_DOMAIN. False negative.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

THBS1. human.

DrugBank

DB00102. Becaplermin.

EvolutionaryTrace

P07996.

GenomeRNAi

7057.

NextBio

27597.

PMAP-CutDB

P07996.

SOURCE

Search...

Entry information

Entry name

TSP1_HUMAN

Accession

Primary (citable) accession number: P07996
Secondary accession number(s): A8K6H4, B9EGH6, Q15667

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 31, 2006
Last modified:	May 29, 2013
This is version 174 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.