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P07996

- TSP1_HUMAN

UniProt

P07996 - TSP1_HUMAN

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Protein

Thrombospondin-1

Gene

THBS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. calcium ion binding Source: BHF-UCL
  2. collagen V binding Source: BHF-UCL
  3. fibrinogen binding Source: BHF-UCL
  4. fibroblast growth factor binding Source: BHF-UCL
  5. fibronectin binding Source: BHF-UCL
  6. glycoprotein binding Source: BHF-UCL
  7. heparin binding Source: BHF-UCL
  8. identical protein binding Source: BHF-UCL
  9. integrin binding Source: BHF-UCL
  10. laminin binding Source: BHF-UCL
  11. low-density lipoprotein particle binding Source: BHF-UCL
  12. phosphatidylserine binding Source: UniProtKB
  13. proteoglycan binding Source: BHF-UCL
  14. transforming growth factor beta binding Source: BHF-UCL

GO - Biological processi

  1. activation of MAPK activity Source: BHF-UCL
  2. behavioral response to pain Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. cell adhesion Source: BHF-UCL
  5. cell cycle arrest Source: BHF-UCL
  6. cell migration Source: BHF-UCL
  7. cellular response to growth factor stimulus Source: Ensembl
  8. cellular response to heat Source: BHF-UCL
  9. cellular response to tumor necrosis factor Source: Ensembl
  10. chronic inflammatory response Source: BHF-UCL
  11. endocardial cushion development Source: Ensembl
  12. engulfment of apoptotic cell Source: BHF-UCL
  13. extracellular matrix organization Source: Reactome
  14. growth plate cartilage development Source: Ensembl
  15. immune response Source: BHF-UCL
  16. negative regulation of angiogenesis Source: UniProtKB
  17. negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II Source: BHF-UCL
  18. negative regulation of apoptotic process Source: UniProtKB
  19. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  20. negative regulation of cell-matrix adhesion Source: BHF-UCL
  21. negative regulation of cGMP-mediated signaling Source: BHF-UCL
  22. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  23. negative regulation of dendritic cell antigen processing and presentation Source: BHF-UCL
  24. negative regulation of endothelial cell migration Source: BHF-UCL
  25. negative regulation of endothelial cell proliferation Source: BHF-UCL
  26. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  27. negative regulation of fibrinolysis Source: BHF-UCL
  28. negative regulation of fibroblast growth factor receptor signaling pathway Source: BHF-UCL
  29. negative regulation of focal adhesion assembly Source: BHF-UCL
  30. negative regulation of interleukin-12 production Source: BHF-UCL
  31. negative regulation of nitric oxide mediated signal transduction Source: BHF-UCL
  32. negative regulation of plasma membrane long-chain fatty acid transport Source: BHF-UCL
  33. negative regulation of plasminogen activation Source: BHF-UCL
  34. outflow tract morphogenesis Source: Ensembl
  35. peptide cross-linking Source: BHF-UCL
  36. platelet activation Source: Reactome
  37. platelet degranulation Source: Reactome
  38. positive regulation of angiogenesis Source: BHF-UCL
  39. positive regulation of blood coagulation Source: BHF-UCL
  40. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  41. positive regulation of cell migration Source: BHF-UCL
  42. positive regulation of cell-substrate adhesion Source: Ensembl
  43. positive regulation of chemotaxis Source: BHF-UCL
  44. positive regulation of endothelial cell apoptotic process Source: UniProtKB
  45. positive regulation of endothelial cell migration Source: BHF-UCL
  46. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  47. positive regulation of fibroblast migration Source: BHF-UCL
  48. positive regulation of macrophage activation Source: BHF-UCL
  49. positive regulation of macrophage chemotaxis Source: BHF-UCL
  50. positive regulation of phosphorylation Source: BHF-UCL
  51. positive regulation of protein kinase B signaling Source: UniProtKB
  52. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  53. positive regulation of transforming growth factor beta1 production Source: BHF-UCL
  54. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  55. positive regulation of translation Source: BHF-UCL
  56. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  57. response to calcium ion Source: BHF-UCL
  58. response to drug Source: UniProtKB
  59. response to endoplasmic reticulum stress Source: UniProtKB
  60. response to glucose Source: BHF-UCL
  61. response to hypoxia Source: BHF-UCL
  62. response to magnesium ion Source: BHF-UCL
  63. response to mechanical stimulus Source: Ensembl
  64. response to progesterone Source: BHF-UCL
  65. response to testosterone Source: Ensembl
  66. response to unfolded protein Source: UniProtKB-KW
  67. sprouting angiogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Unfolded protein response

Keywords - Ligandi

Calcium, Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombospondin-1
Gene namesi
Name:THBS1
Synonyms:TSP, TSP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11785. THBS1.

Subcellular locationi

Endoplasmic reticulum By similarity. Sarcoplasmic reticulum By similarity

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. endoplasmic reticulum Source: UniProtKB
  3. external side of plasma membrane Source: BHF-UCL
  4. extracellular matrix Source: UniProtKB
  5. extracellular region Source: Reactome
  6. extracellular space Source: BHF-UCL
  7. extracellular vesicular exosome Source: UniProtKB
  8. fibrinogen complex Source: BHF-UCL
  9. platelet alpha granule Source: BHF-UCL
  10. platelet alpha granule lumen Source: Reactome
  11. sarcoplasmic reticulum Source: UniProtKB
  12. secretory granule Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1067 – 10671N → K: Loss of N-glycosylation site. 1 Publication

Organism-specific databases

PharmGKBiPA36497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 11701152Thrombospondin-1PRO_0000035842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi171 ↔ 232
Glycosylationi248 – 2481N-linked (GlcNAc...)3 Publications
Disulfide bondi270 – 270InterchainCurated
Disulfide bondi274 – 274InterchainCurated
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi385 – 3851C-linked (Man)CAR_000205
Disulfide bondi391 ↔ 423
Glycosylationi394 – 3941O-linked (Fuc...)1 PublicationCAR_000206
Disulfide bondi395 ↔ 428
Disulfide bondi406 ↔ 413
Glycosylationi438 – 4381C-linked (Man)CAR_000207
Glycosylationi441 – 4411C-linked (Man)CAR_000208
Disulfide bondi447 ↔ 484
Glycosylationi450 – 4501O-linked (Fuc...)2 PublicationsCAR_000209
Disulfide bondi451 ↔ 489
Disulfide bondi462 ↔ 474
Glycosylationi498 – 4981C-linked (Man)CAR_000210
Disulfide bondi504 ↔ 541
Glycosylationi507 – 5071O-linked (Fuc...)2 PublicationsCAR_000211
Disulfide bondi508 ↔ 546
Disulfide bondi519 ↔ 531
Disulfide bondi551 ↔ 562By similarity
Disulfide bondi556 ↔ 572By similarity
Disulfide bondi575 ↔ 586By similarity
Disulfide bondi592 ↔ 608By similarity
Disulfide bondi599 ↔ 617By similarity
Disulfide bondi620 ↔ 644By similarity
Disulfide bondi650 ↔ 663By similarity
Disulfide bondi657 ↔ 676By similarity
Disulfide bondi678 ↔ 689By similarity
Disulfide bondi705 ↔ 713By similarity
Glycosylationi708 – 7081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi718 ↔ 738By similarity
Disulfide bondi754 ↔ 774By similarity
Disulfide bondi777 ↔ 797By similarity
Disulfide bondi813 ↔ 833By similarity
Disulfide bondi836 ↔ 856
Disulfide bondi874 ↔ 894
Disulfide bondi910 ↔ 930
Disulfide bondi946 ↔ 1167
Glycosylationi1067 – 10671N-linked (GlcNAc...)4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP07996.
PaxDbiP07996.
PeptideAtlasiP07996.
PRIDEiP07996.

2D gel databases

OGPiP07996.

PTM databases

PhosphoSiteiP07996.
UniCarbKBiP07996.

Miscellaneous databases

PMAP-CutDBP07996.

Expressioni

Gene expression databases

BgeeiP07996.
CleanExiHS_THBS1.
ExpressionAtlasiP07996. baseline and differential.
GenevestigatoriP07996.

Organism-specific databases

HPAiCAB033678.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PCOLCEQ151133EBI-2530274,EBI-8869614
TGFB1P011372EBI-2530274,EBI-779636

Protein-protein interaction databases

BioGridi112915. 32 interactions.
DIPiDIP-1037N.
IntActiP07996. 12 interactions.
MINTiMINT-6630675.
STRINGi9606.ENSP00000260356.

Structurei

Secondary structure

1
1170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323
Helixi33 – 375
Turni38 – 414
Beta strandi44 – 496
Beta strandi58 – 625
Helixi64 – 663
Helixi72 – 8514
Beta strandi87 – 9610
Beta strandi101 – 1099
Beta strandi115 – 1228
Turni123 – 1264
Beta strandi127 – 1348
Beta strandi137 – 1459
Beta strandi150 – 16112
Beta strandi164 – 1696
Turni170 – 1723
Beta strandi173 – 1786
Helixi183 – 1853
Helixi191 – 1944
Beta strandi195 – 2006
Turni203 – 2053
Beta strandi210 – 2189
Helixi223 – 2286
Turni229 – 2313
Beta strandi450 – 45910
Beta strandi478 – 4858
Beta strandi507 – 5093
Beta strandi511 – 5166
Beta strandi535 – 5417
Turni838 – 8403
Beta strandi849 – 8524
Turni854 – 8563
Beta strandi865 – 8673
Helixi869 – 8713
Beta strandi888 – 8903
Helixi892 – 8943
Beta strandi901 – 9033
Helixi905 – 9073
Turni909 – 9124
Beta strandi924 – 9263
Helixi928 – 9303
Beta strandi937 – 9393
Turni941 – 9433
Beta strandi961 – 9655
Beta strandi986 – 9883
Beta strandi995 – 101420
Beta strandi1022 – 103110
Beta strandi1034 – 104310
Beta strandi1051 – 10533
Beta strandi1059 – 10679
Helixi1074 – 10818
Beta strandi1082 – 10843
Turni1087 – 10893
Beta strandi1090 – 10956
Beta strandi1107 – 11159
Turni1116 – 11194
Beta strandi1120 – 11278
Beta strandi1130 – 11345
Beta strandi1146 – 11549
Beta strandi1156 – 116712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LSLX-ray1.90A434-546[»]
1UX6X-ray1.90A834-1170[»]
1Z78X-ray1.80A19-233[»]
1ZA4X-ray1.90A19-233[»]
2ERFX-ray1.45A25-233[»]
2ES3X-ray1.85A/B25-233[»]
2OUHX-ray2.40A/B19-257[»]
2OUJX-ray1.90A19-257[»]
3R6BX-ray2.40A434-547[»]
ProteinModelPortaliP07996.
SMRiP07996. Positions 25-233, 434-1170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07996.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 270206Laminin G-likeAdd
BLAST
Domaini316 – 37358VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini379 – 42951TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini435 – 49056TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini492 – 54756TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini547 – 58741EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini646 – 69045EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati691 – 72636TSP type-3 1Add
BLAST
Repeati727 – 76236TSP type-3 2Add
BLAST
Repeati763 – 78523TSP type-3 3Add
BLAST
Repeati786 – 82136TSP type-3 4Add
BLAST
Repeati822 – 84423TSP type-3 5Add
BLAST
Repeati845 – 88238TSP type-3 6Add
BLAST
Repeati883 – 91836TSP type-3 7Add
BLAST
Repeati919 – 95436TSP type-3 8Add
BLAST
Domaini958 – 1170213TSP C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 9549Heparin-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi926 – 9283Cell attachment siteCurated

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 3 TSP type-1 domains.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOVERGENiHBG018006.
InParanoidiP07996.
KOiK16857.
OMAiSPWDICS.
OrthoDBiEOG76QFGD.
PhylomeDBiP07996.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
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.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_C.
[Graphical view]
PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
PfamiPF07645. 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]
SMARTiSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEiPS01186. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P07996-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK
60 70 80 90 100
GPDPSSPAFR IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT
110 120 130 140 150
RGTLLALERK DHSGQVFSVV SNGKAGTLDL SLTVQGKQHV VSVEEALLAT
160 170 180 190 200
GQWKSITLFV QEDRAQLYID CEKMENAELD VPIQSVFTRD LASIARLRIA
210 220 230 240 250
KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL TLDNNVVNGS
260 270 280 290 300
SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK
310 320 330 340 350
VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK
360 370 380 390 400
VSCPIMPCSN ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ
410 420 430 440 450
QRGRSCDSLN NRCEGSSVQT RTCHIQECDK RFKQDGGWSH WSPWSSCSVT
460 470 480 490 500
CGDGVITRIR LCNSPSPQMN GKPCEGEARE TKACKKDACP INGGWGPWSP
510 520 530 540 550
WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI CNKQDCPIDG
560 570 580 590 600
CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF
610 620 630 640 650
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC
660 670 680 690 700
TDGTHDCNKN AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN
710 720 730 740 750
ENLVCVANAT YHCKKDNCPN LPNSGQEDYD KDGIGDACDD DDDNDKIPDD
760 770 780 790 800
RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN HNPDQADTDN NGEGDACAAD
810 820 830 840 850
IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH NPDQLDSDSD
860 870 880 890 900
RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
910 920 930 940 950
DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV
960 970 980 990 1000
DISETDFRRF QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY
1010 1020 1030 1040 1050
DEFNAVDFSG TFFINTERDD DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT
1060 1070 1080 1090 1100
NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL WHTGNTPGQV RTLWHDPRHI
1110 1120 1130 1140 1150
GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD KTYAGGRLGL
1160 1170
FVFSQEMVFF SDLKYECRDP
Length:1,170
Mass (Da):129,383
Last modified:October 31, 2006 - v2
Checksum:i74749B2418E0943B
GO
Isoform 2 (identifier: P07996-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-101: Missing.

Note: No experimental confirmation available.

Show »
Length:1,085
Mass (Da):120,148
Checksum:i3670FD07DED233DD
GO

Sequence cautioni

The sequence BAD93149.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → S in BAG65509. (PubMed:14702039)Curated
Sequence conflicti84 – 841A → T in CAA28370. (PubMed:2430973)Curated
Sequence conflicti84 – 841A → T in AAA61178. (PubMed:2544587)Curated
Sequence conflicti431 – 4311R → I in BAG65509. (PubMed:14702039)Curated
Sequence conflicti451 – 4511C → R in BAG65509. (PubMed:14702039)Curated
Sequence conflicti546 – 5461C → Y in BAF84328. (PubMed:14702039)Curated
Sequence conflicti812 – 8121N → D in BAG65509. (PubMed:14702039)Curated
Sequence conflicti1008 – 10081F → S in BAF84328. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241S → A.
Corresponds to variant rs41515347 [ dbSNP | Ensembl ].
VAR_052657
Natural varianti523 – 5231T → A.2 Publications
Corresponds to variant rs2292305 [ dbSNP | Ensembl ].
VAR_028938
Natural varianti700 – 7001N → S.1 Publication
Corresponds to variant rs2228262 [ dbSNP | Ensembl ].
VAR_028939

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei17 – 10185Missing in isoform 2. 1 PublicationVSP_055757Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04665 mRNA. Translation: CAA28370.1.
X14787 mRNA. Translation: CAA32889.1.
AK291639 mRNA. Translation: BAF84328.1.
AK304754 mRNA. Translation: BAG65509.1.
AB209912 mRNA. Translation: BAD93149.1. Different initiation.
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.
CCDSiCCDS32194.1. [P07996-1]
PIRiA26155. TSHUP1.
RefSeqiNP_003237.2. NM_003246.2. [P07996-1]
UniGeneiHs.164226.

Genome annotation databases

EnsembliENST00000260356; ENSP00000260356; ENSG00000137801. [P07996-1]
GeneIDi7057.
KEGGihsa:7057.
UCSCiuc001zkh.3. human. [P07996-1]

Polymorphism databases

DMDMi117949802.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04665 mRNA. Translation: CAA28370.1 .
X14787 mRNA. Translation: CAA32889.1 .
AK291639 mRNA. Translation: BAF84328.1 .
AK304754 mRNA. Translation: BAG65509.1 .
AB209912 mRNA. Translation: BAD93149.1 . Different initiation.
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 .
CCDSi CCDS32194.1. [P07996-1 ]
PIRi A26155. TSHUP1.
RefSeqi NP_003237.2. NM_003246.2. [P07996-1 ]
UniGenei Hs.164226.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 19-233 [» ]
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 [» ]
ProteinModelPortali P07996.
SMRi P07996. Positions 25-233, 434-1170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112915. 32 interactions.
DIPi DIP-1037N.
IntActi P07996. 12 interactions.
MINTi MINT-6630675.
STRINGi 9606.ENSP00000260356.

PTM databases

PhosphoSitei P07996.
UniCarbKBi P07996.

Polymorphism databases

DMDMi 117949802.

2D gel databases

OGPi P07996.

Proteomic databases

MaxQBi P07996.
PaxDbi P07996.
PeptideAtlasi P07996.
PRIDEi P07996.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260356 ; ENSP00000260356 ; ENSG00000137801 . [P07996-1 ]
GeneIDi 7057.
KEGGi hsa:7057.
UCSCi uc001zkh.3. human. [P07996-1 ]

Organism-specific databases

CTDi 7057.
GeneCardsi GC15P039873.
H-InvDB HIX0038125.
HGNCi HGNC:11785. THBS1.
HPAi CAB033678.
MIMi 188060. gene.
neXtProti NX_P07996.
PharmGKBi PA36497.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00550000074507.
HOVERGENi HBG018006.
InParanoidi P07996.
KOi K16857.
OMAi SPWDICS.
OrthoDBi EOG76QFGD.
PhylomeDBi P07996.
TreeFami TF324917.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

ChiTaRSi THBS1. human.
EvolutionaryTracei P07996.
GeneWikii Thrombospondin_1.
GenomeRNAii 7057.
NextBioi 27597.
PMAP-CutDB P07996.
PROi P07996.
SOURCEi Search...

Gene expression databases

Bgeei P07996.
CleanExi HS_THBS1.
ExpressionAtlasi P07996. baseline and differential.
Genevestigatori P07996.

Family and domain databases

Gene3Di 2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProi IPR013320. ConA-like_dom.
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.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_C.
[Graphical view ]
PANTHERi PTHR10199:SF78. PTHR10199:SF78. 1 hit.
Pfami 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 ]
SMARTi SM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
SUPFAMi SSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2), VARIANT ALA-523.
    Tissue: Placenta and Uterus.
  4. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-700.
    Tissue: Aortic endothelium.
  5. "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].
  6. "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] (ISOFORM 1).
    Tissue: Testis.
  7. "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 (ISOFORM 1).
  8. "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 (ISOFORM 1).
  9. "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.
  10. "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 (ISOFORM 1).
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiTSP1_HUMAN
AccessioniPrimary (citable) accession number: P07996
Secondary accession number(s): A8K6H4
, B4E3J7, B9EGH6, Q15667, Q59E99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 31, 2006
Last modified: October 29, 2014
This is version 189 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3