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Reviewed, UniProtKB/Swiss-Prot P07996 (TSP1_HUMAN)

Last modified February 9, 2010. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Thrombospondin-1
Gene names
Name: THBS1
Synonyms: TSP, TSP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ref.17

Subunit structure

Homotrimer; disulfide-linked. Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Ref.17 Ref.11 Ref.16 Ref.18

Sequence similarities

Belongs to the thrombospondin family.

Contains 3 EGF-like domains.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 1 TSP N-terminal (TSPN) domain.

Contains 3 TSP type-1 domains.

Contains 8 TSP type-3 repeats.

Contains 1 VWFC domain.

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Ontologies

Keywords
   Biological processCell adhesion
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Heparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processactivation of MAPK activity

Inferred from mutant phenotype. Source: UniProtKB

anti-apoptosis

Traceable author statement. Source: UniProtKB

apoptosis

Inferred from expression pattern. Source: UniProtKB

cell adhesion

Non-traceable author statement. Source: UniProtKB

cell cycle arrest

Inferred from direct assay. Source: UniProtKB

cell migration

Inferred from direct assay. Source: UniProtKB

cellular response to heat

Non-traceable author statement. Source: UniProtKB

chronic inflammatory response

Inferred from expression pattern. Source: UniProtKB

engulfment of apoptotic cell

Inferred from direct assay. Source: UniProtKB

immune response

Inferred from expression pattern. Source: UniProtKB

negative regulation of angiogenesis

Inferred from direct assay. Source: UniProtKB

negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II

Inferred from direct assay. Source: UniProtKB

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay. Source: UniProtKB

negative regulation of cGMP-mediated signaling

Inferred from direct assay. Source: UniProtKB

negative regulation of dendritic cell antigen processing and presentation

Inferred from direct assay. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from direct assay. Source: UniProtKB

negative regulation of fibrinolysis

Inferred from direct assay. Source: UniProtKB

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

negative regulation of focal adhesion assembly

Traceable author statement. Source: UniProtKB

negative regulation of interleukin-12 production

Inferred from direct assay. Source: UniProtKB

negative regulation of nitric oxide mediated signal transduction

Inferred from direct assay. Source: UniProtKB

negative regulation of plasma membrane long-chain fatty acid transport

Inferred from direct assay. Source: UniProtKB

negative regulation of plasminogen activation

Inferred from direct assay. Source: UniProtKB

peptide cross-linking

Inferred from direct assay. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of blood coagulation

Inferred from direct assay. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay. Source: UniProtKB

positive regulation of fibroblast migration

Inferred from direct assay. Source: UniProtKB

positive regulation of macrophage activation

Inferred from direct assay. Source: UniProtKB

positive regulation of macrophage chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of oxygen and reactive oxygen species metabolic process

Inferred from direct assay. Source: UniProtKB

positive regulation of phosphorylation

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

positive regulation of transforming growth factor-beta1 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translation

Inferred from direct assay. Source: UniProtKB

response to calcium ion

Inferred from direct assay. Source: UniProtKB

response to glucose stimulus

Inferred from direct assay. Source: UniProtKB

response to hypoxia

Non-traceable author statement. Source: UniProtKB

response to magnesium ion

Inferred from direct assay. Source: UniProtKB

response to progesterone stimulus

Traceable author statement. Source: UniProtKB

sprouting angiogenesis

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentexternal side of plasma membrane

Inferred from direct assay. Source: UniProtKB

extracellular matrix

Traceable author statement. Source: UniProtKB

fibrinogen complex

Inferred from direct assay. Source: UniProtKB

platelet alpha granule lumen

Inferred from Experiment. Source: Reactome

   Molecular functioncalcium ion binding

Non-traceable author statement. Source: UniProtKB

collagen V binding

Inferred from direct assay. Source: UniProtKB

eukaryotic cell surface binding

Inferred from direct assay. Source: UniProtKB

fibrinogen binding

Inferred from direct assay. Source: UniProtKB

fibroblast growth factor 2 binding

Inferred from direct assay. Source: UniProtKB

fibronectin binding

Inferred from direct assay. Source: UniProtKB

heparin binding

Inferred from direct assay. Source: UniProtKB

identical protein binding

Non-traceable author statement. Source: UniProtKB

integrin binding

Inferred from mutant phenotype. Source: UniProtKB

laminin binding

Inferred from direct assay. Source: UniProtKB

low-density lipoprotein binding

Inferred from direct assay. Source: UniProtKB

proteoglycan binding

Traceable author statement. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta binding

Traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 11701152Thrombospondin-1
PRO_0000035842

Regions

Domain24 – 221198TSP N-terminal
Domain316 – 37358VWFC
Domain379 – 42951TSP type-1 1
Domain435 – 49056TSP type-1 2
Domain492 – 54756TSP type-1 3
Domain549 – 58739EGF-like 1
Domain588 – 64558EGF-like 2; calcium-binding Potential
Domain646 – 69045EGF-like 3
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.10
CAR_000205
Glycosylation3941O-linked (Fuc...) Ref.10
CAR_000206
Glycosylation4381C-linked (Man) Ref.10
CAR_000207
Glycosylation4411C-linked (Man) Ref.10
CAR_000208
Glycosylation4501O-linked (Fuc...) Ref.16 Ref.10
CAR_000209
Glycosylation4981C-linked (Man) Ref.10
CAR_000210
Glycosylation5071O-linked (Fuc...) Ref.16 Ref.10
CAR_000211
Glycosylation7081N-linked (GlcNAc...) Potential
Glycosylation10671N-linked (GlcNAc...) Ref.17 Ref.12 Ref.13 Ref.15
Disulfide bond171 ↔ 232 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond270Interchain Probable
Disulfide bond274Interchain Probable
Disulfide bond391 ↔ 423 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond395 ↔ 428 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond406 ↔ 413 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond447 ↔ 484 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond451 ↔ 489 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond462 ↔ 474 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond504 ↔ 541 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond508 ↔ 546 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond519 ↔ 531 Ref.17 Ref.11 Ref.16 Ref.18
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.17 Ref.11 Ref.16 Ref.18
Disulfide bond874 ↔ 894 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond910 ↔ 930 Ref.17 Ref.11 Ref.16 Ref.18
Disulfide bond946 ↔ 1167 Ref.17 Ref.11 Ref.16 Ref.18

Natural variations

Natural variant241S → A: dbSNP rs41515347.
VAR_052657
Natural variant5231T → A: dbSNP rs2292305. Ref.2 Ref.3
VAR_028938
Natural variant7001N → S: dbSNP rs2228262.
VAR_028939

Experimental info

Mutagenesis10671N → K: Loss of N-glycosylation site. Ref.17
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

1 ............................................................................................................ 1170
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07996-1 [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

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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: 2430973] [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: 2918029] [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: 14702039] [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: 16572171] [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: 15489334] [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: 3030396] [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: 3461443] [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: 2544587] [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]"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: 11067851] [Abstract]
Cited for: GLYCOSYLATION AT TRP-385; SER-394; TRP-438; TRP-441; THR-450; TRP-498 AND THR-507.
Tissue: Platelet.
[11]"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: 12450399] [Abstract]
Cited for: DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
[12]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248 AND ASN-1067, MASS SPECTROMETRY.
Tissue: Plasma.
[13]"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: 16740002] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, MASS SPECTROMETRY.
Tissue: Saliva.
[14]"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: 16263699] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-248, MASS SPECTROMETRY.
Tissue: Platelet.
[15]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067, MASS SPECTROMETRY.
Tissue: Liver.
[16]"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: 12391027] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 434-546, DISULFIDE BONDS, GLYCOSYLATION AT THR-450 AND THR-507.
[17]"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: 15014436] [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.
[18]"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: 16407063] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 19-233 IN COMPLEX WITH SYNTHETIC PENTAMERIC HEPARIN, DISULFIDE BOND.
[19]"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: 18065761] [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.

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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.
IPIIPI00296099.
PIRTSHUP1. A26155.
RefSeqNP_003237.2.
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[»]
SMRP07996. Positions 311-373, 549-1169.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1037N.
STRINGP07996.

PTM databases

GlycoSuiteDBP07996.

2-D gel databases

OGPP07996.

Proteomic databases

PeptideAtlasP07996.
PRIDEP07996.

Genome annotation databases

EnsemblENST00000260356; ENSP00000260356; ENSG00000137801; Homo sapiens. [Genome view]
GeneID7057.
KEGGhsa:7057.
NMPDRfig|9606.3.peg.10483.
UCSCuc001zkh.1. human.

Organism-specific databases

CTD7057.
GeneCardsGC15P037660.
HGNCHGNC:11785. THBS1.
MIM188060. gene.
PharmGKBPA36497.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP07996.
InParanoidP07996.
OMAEHNPDQL.
OrthoDBEOG9PG8KV.
PhylomeDBP07996.

Enzyme and pathway databases

Pathway_Interaction_DBsyndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP07996.
BgeeP07996.
CleanExHS_THBS1.
GenevestigatorP07996.
GermOnlineENSG00000137801. Homo sapiens.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR013091. EGF_Ca_bd_2.
IPR003129. Laminin_G_thrombospondin_N.
IPR000884. Thrombospondin_1_rpt.
IPR008085. Thrombospondin_1_rpt_sub.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF07645. EGF_CA. 1 hit.
PF00090. TSP_1. 3 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSPR01705. TSP1REPEAT.
SMARTSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. False negative.
PS01186. 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 Resources

DrugBankDB00102. Becaplermin.
NextBio27597.
PMAP-CutDBP07996.
SOURCESearch...

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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: February 9, 2010
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents