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P07996 (TSP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombospondin-1
Gene names
Name:THBS1
Synonyms:TSP, TSP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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. 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. Interacts with ATF6 (via lumenal domain) By similarity. Ref.10 Ref.12 Ref.13 Ref.19 Ref.20 Ref.21

Subcellular location

Endoplasmic reticulum By similarity. Sarcoplasmic reticulum By similarity.

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 processCell adhesion
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Sarcoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Heparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from mutant phenotype PubMed 17413041. Source: BHF-UCL

behavioral response to pain

Inferred from sequence or structural similarity. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

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 growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to heat

Non-traceable author statement PubMed 9304800. Source: BHF-UCL

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response

Inferred from expression pattern PubMed 18674744. Source: BHF-UCL

endocardial cushion development

Inferred from electronic annotation. Source: Ensembl

engulfment of apoptotic cell

Inferred from direct assay PubMed 16882710. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

growth plate cartilage development

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from expression pattern PubMed 18674744. Source: BHF-UCL

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 cell-matrix adhesion

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 migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 17996481. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway

Traceable author statement PubMed 17879962. 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: Ensembl

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 coagulation

Inferred from direct assay PubMed 3997886. Source: BHF-UCL

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay PubMed 15700281. Source: BHF-UCL

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemotaxis

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 18726995. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay PubMed 18726995. 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 phosphorylation

Inferred from mutant phenotype PubMed 17413041. Source: BHF-UCL

positive regulation of protein kinase B signaling

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 endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucose

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 mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Traceable author statement PubMed 9304800. Source: BHF-UCL

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Inferred from electronic annotation. Source: UniProtKB-KW

sprouting angiogenesis

Inferred from mutant phenotype PubMed 17879962. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 2435757PubMed 3084490PubMed 6777381. Source: BHF-UCL

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

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 region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380PubMed 6777381. 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

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

platelet alpha granule lumen

Traceable author statement. Source: Reactome

sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

secretory granule

Inferred from direct assay PubMed 101549. Source: BHF-UCL

   Molecular_functioncalcium ion binding

Non-traceable author statement PubMed 9304800. Source: BHF-UCL

collagen V binding

Inferred from direct assay PubMed 6693501. 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

glycoprotein binding

Non-traceable author statement PubMed 6438154. 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

TGFB1P011372EBI-2530274,EBI-779636

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 11701152Thrombospondin-1
PRO_0000035842

Regions

Domain65 – 270206Laminin G-like
Domain316 – 37358VWFC
Domain379 – 42951TSP type-1 1
Domain435 – 49056TSP type-1 2
Domain492 – 54756TSP type-1 3
Domain547 – 58741EGF-like 1
Domain646 – 69045EGF-like 2
Repeat691 – 72636TSP type-3 1
Repeat727 – 76236TSP type-3 2
Repeat763 – 78523TSP type-3 3
Repeat786 – 82136TSP type-3 4
Repeat822 – 84423TSP type-3 5
Repeat845 – 88238TSP type-3 6
Repeat883 – 91836TSP type-3 7
Repeat919 – 95436TSP type-3 8
Domain958 – 1170213TSP C-terminal
Region47 – 9549Heparin-binding
Motif926 – 9283Cell attachment site Probable

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Probable
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3851C-linked (Man) Ref.11
CAR_000205
Glycosylation3941O-linked (Fuc...) Ref.11
CAR_000206
Glycosylation4381C-linked (Man) Ref.11
CAR_000207
Glycosylation4411C-linked (Man) Ref.11
CAR_000208
Glycosylation4501O-linked (Fuc...) Ref.11 Ref.19
CAR_000209
Glycosylation4981C-linked (Man) Ref.11
CAR_000210
Glycosylation5071O-linked (Fuc...) Ref.11 Ref.19
CAR_000211
Glycosylation7081N-linked (GlcNAc...) Potential
Glycosylation10671N-linked (GlcNAc...) Ref.14 Ref.15 Ref.17 Ref.20
Disulfide bond171 ↔ 232 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond270Interchain Probable
Disulfide bond274Interchain Probable
Disulfide bond391 ↔ 423 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond395 ↔ 428 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond406 ↔ 413 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond447 ↔ 484 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond451 ↔ 489 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond462 ↔ 474 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond504 ↔ 541 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond508 ↔ 546 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond519 ↔ 531 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond551 ↔ 562 By similarity
Disulfide bond556 ↔ 572 By similarity
Disulfide bond575 ↔ 586 By similarity
Disulfide bond592 ↔ 608 By similarity
Disulfide bond599 ↔ 617 By similarity
Disulfide bond620 ↔ 644 By similarity
Disulfide bond650 ↔ 663 By similarity
Disulfide bond657 ↔ 676 By similarity
Disulfide bond678 ↔ 689 By similarity
Disulfide bond705 ↔ 713 By similarity
Disulfide bond718 ↔ 738 By similarity
Disulfide bond754 ↔ 774 By similarity
Disulfide bond777 ↔ 797 By similarity
Disulfide bond813 ↔ 833 By similarity
Disulfide bond836 ↔ 856 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond874 ↔ 894 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond910 ↔ 930 Ref.13 Ref.19 Ref.20 Ref.21
Disulfide bond946 ↔ 1167 Ref.13 Ref.19 Ref.20 Ref.21

Natural variations

Natural variant241S → A.
Corresponds to variant rs41515347 [ dbSNP | Ensembl ].
VAR_052657
Natural variant5231T → A. Ref.2 Ref.3
Corresponds to variant rs2292305 [ dbSNP | Ensembl ].
VAR_028938
Natural variant7001N → S.
Corresponds to variant rs2228262 [ dbSNP | Ensembl ].
VAR_028939

Experimental info

Mutagenesis10671N → K: Loss of N-glycosylation site. Ref.20
Sequence conflict841A → T in CAA28370. Ref.1
Sequence conflict841A → T in AAA61178. Ref.8
Sequence conflict5461C → Y in BAF84328. Ref.3
Sequence conflict10081F → S in BAF84328. Ref.3

Secondary structure

............................................................................................................. 1170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07996 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 74749B2418E0943B

FASTA1,170129,383
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
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.
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.
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.
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, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-248.
+Additional computationally mapped references.

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.
PIRTSHUP1. A26155.
RefSeqNP_003237.2. NM_003246.2.
UniGeneHs.164226.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LSLX-ray1.90A434-546[»]
1UX6X-ray1.90A834-1170[»]
1Z78X-ray1.80A19-233[»]
1ZA4X-ray1.90A19-257[»]
2ERFX-ray1.45A25-233[»]
2ES3X-ray1.85A/B25-233[»]
2OUHX-ray2.40A/B19-257[»]
2OUJX-ray1.90A19-257[»]
3R6BX-ray2.40A434-547[»]
ProteinModelPortalP07996.
SMRP07996. Positions 25-233, 312-406, 434-1170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112915. 31 interactions.
DIPDIP-1037N.
IntActP07996. 12 interactions.
MINTMINT-6630675.
STRING9606.ENSP00000260356.

Chemistry

DrugBankDB00102. Becaplermin.

PTM databases

PhosphoSiteP07996.
UniCarbKBP07996.

Polymorphism databases

DMDM117949802.

2D gel databases

OGPP07996.

Proteomic databases

PaxDbP07996.
PeptideAtlasP07996.
PRIDEP07996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260356; ENSP00000260356; ENSG00000137801.
GeneID7057.
KEGGhsa:7057.
UCSCuc001zkh.3. human.

Organism-specific databases

CTD7057.
GeneCardsGC15P039873.
H-InvDBHIX0038125.
HGNCHGNC:11785. THBS1.
HPACAB033678.
MIM188060. gene.
neXtProtNX_P07996.
PharmGKBPA36497.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG018006.
InParanoidP07996.
KOK16857.
OMASPWDICS.
OrthoDBEOG76QFGD.
PhylomeDBP07996.
TreeFamTF324917.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP07996.
BgeeP07996.
CleanExHS_THBS1.
GenevestigatorP07996.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR000884. Thrombospondin_1_rpt.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]
PANTHERPTHR10199:SF53. PTHR10199:SF53. 1 hit.
PfamPF07645. 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]
SMARTSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
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]
ProtoNetSearch...

Other

ChiTaRSTHBS1. human.
EvolutionaryTraceP07996.
GeneWikiThrombospondin_1.
GenomeRNAi7057.
NextBio27597.
PMAP-CutDBP07996.
PROP07996.
SOURCESearch...

Entry information

Entry nameTSP1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM