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P07996

- TSP1_HUMAN

UniProt

P07996 - TSP1_HUMAN

Protein

Thrombospondin-1

Gene

THBS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
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    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. extracellular matrix binding Source: InterPro
    4. fibrinogen binding Source: BHF-UCL
    5. fibroblast growth factor binding Source: BHF-UCL
    6. fibronectin binding Source: BHF-UCL
    7. glycoprotein binding Source: BHF-UCL
    8. heparin binding Source: BHF-UCL
    9. identical protein binding Source: BHF-UCL
    10. integrin binding Source: BHF-UCL
    11. laminin binding Source: BHF-UCL
    12. low-density lipoprotein particle binding Source: BHF-UCL
    13. phosphatidylserine binding Source: UniProtKB
    14. protein binding Source: UniProtKB
    15. proteoglycan binding Source: BHF-UCL
    16. 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. inflammatory response Source: InterPro
    17. negative regulation of angiogenesis Source: UniProtKB
    18. negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II Source: BHF-UCL
    19. negative regulation of apoptotic process Source: UniProtKB
    20. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
    21. negative regulation of cell-matrix adhesion Source: BHF-UCL
    22. negative regulation of cGMP-mediated signaling Source: BHF-UCL
    23. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    24. negative regulation of dendritic cell antigen processing and presentation Source: BHF-UCL
    25. negative regulation of endothelial cell migration Source: BHF-UCL
    26. negative regulation of endothelial cell proliferation Source: BHF-UCL
    27. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    28. negative regulation of fibrinolysis Source: BHF-UCL
    29. negative regulation of fibroblast growth factor receptor signaling pathway Source: BHF-UCL
    30. negative regulation of focal adhesion assembly Source: BHF-UCL
    31. negative regulation of interleukin-12 production Source: BHF-UCL
    32. negative regulation of nitric oxide mediated signal transduction Source: BHF-UCL
    33. negative regulation of plasma membrane long-chain fatty acid transport Source: BHF-UCL
    34. negative regulation of plasminogen activation Source: BHF-UCL
    35. outflow tract morphogenesis Source: Ensembl
    36. peptide cross-linking Source: BHF-UCL
    37. platelet activation Source: Reactome
    38. platelet degranulation Source: Reactome
    39. positive regulation of angiogenesis Source: BHF-UCL
    40. positive regulation of blood coagulation Source: BHF-UCL
    41. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    42. positive regulation of cell migration Source: BHF-UCL
    43. positive regulation of cell-substrate adhesion Source: Ensembl
    44. positive regulation of chemotaxis Source: BHF-UCL
    45. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    46. positive regulation of endothelial cell migration Source: BHF-UCL
    47. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    48. positive regulation of fibroblast migration Source: BHF-UCL
    49. positive regulation of macrophage activation Source: BHF-UCL
    50. positive regulation of macrophage chemotaxis Source: BHF-UCL
    51. positive regulation of phosphorylation Source: BHF-UCL
    52. positive regulation of protein kinase B signaling Source: UniProtKB
    53. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    54. positive regulation of transforming growth factor beta1 production Source: BHF-UCL
    55. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    56. positive regulation of translation Source: BHF-UCL
    57. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
    58. response to calcium ion Source: BHF-UCL
    59. response to drug Source: UniProtKB
    60. response to endoplasmic reticulum stress Source: UniProtKB
    61. response to glucose Source: BHF-UCL
    62. response to hypoxia Source: BHF-UCL
    63. response to magnesium ion Source: BHF-UCL
    64. response to mechanical stimulus Source: Ensembl
    65. response to progesterone Source: BHF-UCL
    66. response to testosterone Source: Ensembl
    67. response to unfolded protein Source: UniProtKB-KW
    68. sprouting angiogenesis Source: BHF-UCL

    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: BHF-UCL
    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

    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

    ArrayExpressiP07996.
    BgeeiP07996.
    CleanExiHS_THBS1.
    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. 31 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.
    HOVERGENiHBG018006.
    InParanoidiP07996.
    KOiK16857.
    OMAiSPWDICS.
    OrthoDBiEOG76QFGD.
    PhylomeDBiP07996.
    TreeFamiTF324917.

    Family and domain databases

    Gene3Di2.60.120.200. 3 hits.
    4.10.1080.10. 2 hits.
    InterProiIPR008985. 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.
    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

    MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK     50
    GPDPSSPAFR IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT 100
    RGTLLALERK DHSGQVFSVV SNGKAGTLDL SLTVQGKQHV VSVEEALLAT 150
    GQWKSITLFV QEDRAQLYID CEKMENAELD VPIQSVFTRD LASIARLRIA 200
    KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL TLDNNVVNGS 250
    SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK 300
    VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK 350
    VSCPIMPCSN ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ 400
    QRGRSCDSLN NRCEGSSVQT RTCHIQECDK RFKQDGGWSH WSPWSSCSVT 450
    CGDGVITRIR LCNSPSPQMN GKPCEGEARE TKACKKDACP INGGWGPWSP 500
    WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI CNKQDCPIDG 550
    CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF 600
    NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEHATAN KQVCKPRNPC 650
    TDGTHDCNKN AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN 700
    ENLVCVANAT YHCKKDNCPN LPNSGQEDYD KDGIGDACDD DDDNDKIPDD 750
    RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN HNPDQADTDN NGEGDACAAD 800
    IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH NPDQLDSDSD 850
    RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN 900
    DGIPDDKDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV 950
    DISETDFRRF QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY 1000
    DEFNAVDFSG TFFINTERDD DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT 1050
    NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL WHTGNTPGQV RTLWHDPRHI 1100
    GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD KTYAGGRLGL 1150
    FVFSQEMVFF SDLKYECRDP 1170
    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.
    PIRiA26155. TSHUP1.
    RefSeqiNP_003237.2. NM_003246.2.
    UniGeneiHs.164226.

    Genome annotation databases

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

    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.
    PIRi A26155. TSHUP1.
    RefSeqi NP_003237.2. NM_003246.2.
    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. 31 interactions.
    DIPi DIP-1037N.
    IntActi P07996. 12 interactions.
    MINTi MINT-6630675.
    STRINGi 9606.ENSP00000260356.

    Chemistry

    DrugBanki DB00102. Becaplermin.

    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.

    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.
    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

    ArrayExpressi P07996.
    Bgeei P07996.
    CleanExi HS_THBS1.
    Genevestigatori P07996.

    Family and domain databases

    Gene3Di 2.60.120.200. 3 hits.
    4.10.1080.10. 2 hits.
    InterProi IPR008985. 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.
    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

    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 1, 2014
    This is version 188 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