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Protein

Thrombospondin-1

Gene

THBS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 similarity2 Publications

GO - Molecular functioni

  • calcium ion binding Source: BHF-UCL
  • collagen V binding Source: BHF-UCL
  • fibrinogen binding Source: BHF-UCL
  • fibroblast growth factor binding Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • glycoprotein binding Source: BHF-UCL
  • heparin binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • integrin binding Source: BHF-UCL
  • laminin binding Source: BHF-UCL
  • low-density lipoprotein particle binding Source: BHF-UCL
  • phosphatidylserine binding Source: UniProtKB
  • proteoglycan binding Source: BHF-UCL
  • transforming growth factor beta binding Source: BHF-UCL

GO - Biological processi

  • activation of MAPK activity Source: BHF-UCL
  • behavioral response to pain Source: UniProtKB
  • cell adhesion Source: BHF-UCL
  • cell cycle arrest Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cellular response to growth factor stimulus Source: Ensembl
  • cellular response to heat Source: BHF-UCL
  • cellular response to tumor necrosis factor Source: Ensembl
  • chronic inflammatory response Source: BHF-UCL
  • engulfment of apoptotic cell Source: BHF-UCL
  • extracellular matrix organization Source: Reactome
  • immune response Source: BHF-UCL
  • inflammatory response Source: CACAO
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II Source: BHF-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • negative regulation of cell-matrix adhesion Source: BHF-UCL
  • negative regulation of cGMP-mediated signaling Source: BHF-UCL
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of dendritic cell antigen processing and presentation Source: BHF-UCL
  • negative regulation of endothelial cell chemotaxis Source: MGI
  • negative regulation of endothelial cell migration Source: BHF-UCL
  • negative regulation of endothelial cell proliferation Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of fibrinolysis Source: BHF-UCL
  • negative regulation of fibroblast growth factor receptor signaling pathway Source: BHF-UCL
  • negative regulation of focal adhesion assembly Source: BHF-UCL
  • negative regulation of interleukin-12 production Source: BHF-UCL
  • negative regulation of nitric oxide mediated signal transduction Source: BHF-UCL
  • negative regulation of plasma membrane long-chain fatty acid transport Source: BHF-UCL
  • negative regulation of plasminogen activation Source: BHF-UCL
  • peptide cross-linking Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of blood coagulation Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of chemotaxis Source: BHF-UCL
  • positive regulation of endothelial cell apoptotic process Source: UniProtKB
  • positive regulation of endothelial cell migration Source: BHF-UCL
  • positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • positive regulation of fibroblast migration Source: BHF-UCL
  • positive regulation of macrophage activation Source: BHF-UCL
  • positive regulation of macrophage chemotaxis Source: BHF-UCL
  • positive regulation of phosphorylation Source: BHF-UCL
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of transforming growth factor beta1 production Source: BHF-UCL
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • positive regulation of translation Source: BHF-UCL
  • positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  • protein O-linked fucosylation Source: Reactome
  • regulation of cGMP metabolic process Source: MGI
  • response to calcium ion Source: BHF-UCL
  • response to drug Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
  • response to glucose Source: BHF-UCL
  • response to hypoxia Source: BHF-UCL
  • response to magnesium ion Source: BHF-UCL
  • response to mechanical stimulus Source: Ensembl
  • response to progesterone Source: BHF-UCL
  • response to testosterone Source: Ensembl
  • response to unfolded protein Source: UniProtKB-KW
  • 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

BioCyciZFISH:ENSG00000137801-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-186797. Signaling by PDGF.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.
SIGNORiP07996.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombospondin-1
Gene namesi
Name:THBS1
Synonyms:TSP, TSP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11785. THBS1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • external side of plasma membrane Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • fibrinogen complex Source: BHF-UCL
  • platelet alpha granule Source: BHF-UCL
  • platelet alpha granule lumen Source: Reactome
  • sarcoplasmic reticulum Source: UniProtKB
  • secretory granule Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1067N → K: Loss of N-glycosylation site. 1 Publication1

Organism-specific databases

DisGeNETi7057.
OpenTargetsiENSG00000137801.
PharmGKBiPA36497.

Polymorphism and mutation databases

BioMutaiTHBS1.
DMDMi117949802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000003584219 – 1170Thrombospondin-1Add BLAST1152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi171 ↔ 232Combined sources2 Publications
Glycosylationi248N-linked (GlcNAc...)3 Publications1
Disulfide bondi270InterchainCurated
Disulfide bondi274InterchainCurated
Glycosylationi360N-linked (GlcNAc...)Sequence analysis1
GlycosylationiCAR_000205385C-linked (Man)1 Publication1
Disulfide bondi391 ↔ 423
GlycosylationiCAR_000206394O-linked (Fuc...)1 Publication1
Disulfide bondi395 ↔ 428
Disulfide bondi406 ↔ 413
GlycosylationiCAR_000207438C-linked (Man)1 Publication1
GlycosylationiCAR_000208441C-linked (Man)1 Publication1
Disulfide bondi447 ↔ 484Combined sources1 Publication
GlycosylationiCAR_000209450O-linked (Fuc...)2 Publications1
Disulfide bondi451 ↔ 489Combined sources1 Publication
Disulfide bondi462 ↔ 474Combined sources1 Publication
GlycosylationiCAR_000210498C-linked (Man)1 Publication1
Disulfide bondi504 ↔ 541Combined sources1 Publication
GlycosylationiCAR_000211507O-linked (Fuc...)2 Publications1
Disulfide bondi508 ↔ 546Combined sources1 Publication
Disulfide bondi519 ↔ 531Combined sources1 Publication
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
Glycosylationi708N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi718 ↔ 738By similarity
Disulfide bondi754 ↔ 774By similarity
Disulfide bondi777 ↔ 797By similarity
Disulfide bondi813 ↔ 833By similarity
Disulfide bondi836 ↔ 856Combined sources1 Publication
Disulfide bondi874 ↔ 894Combined sources1 Publication
Disulfide bondi910 ↔ 930Combined sources1 Publication
Disulfide bondi946 ↔ 1167Combined sources1 Publication
Glycosylationi1067N-linked (GlcNAc...)4 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP07996.
MaxQBiP07996.
PaxDbiP07996.
PeptideAtlasiP07996.
PRIDEiP07996.

2D gel databases

OGPiP07996.

PTM databases

iPTMnetiP07996.
PhosphoSitePlusiP07996.
UniCarbKBiP07996.

Miscellaneous databases

PMAP-CutDBP07996.

Expressioni

Gene expression databases

BgeeiENSG00000137801.
CleanExiHS_THBS1.
ExpressionAtlasiP07996. baseline and differential.
GenevisibleiP07996. HS.

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
FN1P027512EBI-2530274,EBI-1220319
PCOLCEQ151133EBI-2530274,EBI-8869614
TGFB1P011372EBI-2530274,EBI-779636

GO - Molecular functioni

  • collagen V binding Source: BHF-UCL
  • fibrinogen binding Source: BHF-UCL
  • fibroblast growth factor binding Source: BHF-UCL
  • fibronectin binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • integrin binding Source: BHF-UCL
  • laminin binding Source: BHF-UCL
  • transforming growth factor beta binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112915. 33 interactors.
DIPiDIP-1037N.
IntActiP07996. 14 interactors.
MINTiMINT-6630675.
STRINGi9606.ENSP00000260356.

Structurei

Secondary structure

11170
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Helixi33 – 37Combined sources5
Turni38 – 41Combined sources4
Beta strandi44 – 49Combined sources6
Beta strandi58 – 62Combined sources5
Helixi64 – 66Combined sources3
Helixi72 – 85Combined sources14
Beta strandi87 – 96Combined sources10
Beta strandi101 – 109Combined sources9
Beta strandi115 – 122Combined sources8
Turni123 – 126Combined sources4
Beta strandi127 – 134Combined sources8
Beta strandi137 – 145Combined sources9
Beta strandi150 – 161Combined sources12
Beta strandi164 – 169Combined sources6
Turni170 – 172Combined sources3
Beta strandi173 – 178Combined sources6
Helixi183 – 185Combined sources3
Helixi191 – 194Combined sources4
Beta strandi195 – 200Combined sources6
Turni203 – 205Combined sources3
Beta strandi210 – 218Combined sources9
Helixi223 – 228Combined sources6
Turni229 – 231Combined sources3
Beta strandi394 – 403Combined sources10
Turni408 – 410Combined sources3
Beta strandi417 – 424Combined sources8
Beta strandi450 – 459Combined sources10
Beta strandi478 – 485Combined sources8
Beta strandi507 – 509Combined sources3
Beta strandi511 – 516Combined sources6
Beta strandi535 – 541Combined sources7
Turni838 – 840Combined sources3
Beta strandi849 – 852Combined sources4
Turni854 – 856Combined sources3
Beta strandi865 – 867Combined sources3
Helixi869 – 871Combined sources3
Beta strandi888 – 890Combined sources3
Helixi892 – 894Combined sources3
Beta strandi901 – 903Combined sources3
Helixi905 – 907Combined sources3
Turni909 – 912Combined sources4
Beta strandi924 – 926Combined sources3
Helixi928 – 930Combined sources3
Beta strandi937 – 939Combined sources3
Turni941 – 943Combined sources3
Beta strandi961 – 965Combined sources5
Beta strandi986 – 988Combined sources3
Beta strandi995 – 1014Combined sources20
Beta strandi1022 – 1031Combined sources10
Beta strandi1034 – 1043Combined sources10
Beta strandi1051 – 1053Combined sources3
Beta strandi1059 – 1067Combined sources9
Helixi1074 – 1081Combined sources8
Beta strandi1082 – 1084Combined sources3
Turni1087 – 1089Combined sources3
Beta strandi1090 – 1095Combined sources6
Beta strandi1107 – 1115Combined sources9
Turni1116 – 1119Combined sources4
Beta strandi1120 – 1127Combined sources8
Beta strandi1130 – 1134Combined sources5
Beta strandi1146 – 1154Combined sources9
Beta strandi1156 – 1167Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FOEX-ray1.98A/B378-429[»]
ProteinModelPortaliP07996.
SMRiP07996.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07996.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini65 – 270Laminin G-likeAdd BLAST206
Domaini316 – 373VWFCPROSITE-ProRule annotationAdd BLAST58
Domaini379 – 429TSP type-1 1PROSITE-ProRule annotationAdd BLAST51
Domaini435 – 490TSP type-1 2PROSITE-ProRule annotationAdd BLAST56
Domaini492 – 547TSP type-1 3PROSITE-ProRule annotationAdd BLAST56
Domaini547 – 587EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini646 – 690EGF-like 2PROSITE-ProRule annotationAdd BLAST45
Repeati691 – 726TSP type-3 1Add BLAST36
Repeati727 – 762TSP type-3 2Add BLAST36
Repeati763 – 785TSP type-3 3Add BLAST23
Repeati786 – 821TSP type-3 4Add BLAST36
Repeati822 – 844TSP type-3 5Add BLAST23
Repeati845 – 882TSP type-3 6Add BLAST38
Repeati883 – 918TSP type-3 7Add BLAST36
Repeati919 – 954TSP type-3 8Add BLAST36
Domaini958 – 1170TSP C-terminalPROSITE-ProRule annotationAdd BLAST213

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 95Heparin-bindingAdd BLAST49

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi926 – 928Cell attachment siteCurated3

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

eggNOGiENOG410IFQQ. Eukaryota.
ENOG410XQKE. LUCA.
GeneTreeiENSGT00850000132273.
HOGENOMiHOG000007542.
HOVERGENiHBG018006.
InParanoidiP07996.
KOiK16857.
OMAiTPQFGGK.
OrthoDBiEOG091G00TV.
PhylomeDBiP07996.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR000884. TSP1_rpt.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_dom.
[Graphical view]
PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
PfamiPF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4A → S in BAG65509 (PubMed:14702039).Curated1
Sequence conflicti84A → T in CAA28370 (PubMed:2430973).Curated1
Sequence conflicti84A → T in AAA61178 (PubMed:2544587).Curated1
Sequence conflicti431R → I in BAG65509 (PubMed:14702039).Curated1
Sequence conflicti451C → R in BAG65509 (PubMed:14702039).Curated1
Sequence conflicti546C → Y in BAF84328 (PubMed:14702039).Curated1
Sequence conflicti812N → D in BAG65509 (PubMed:14702039).Curated1
Sequence conflicti1008F → S in BAF84328 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05265724S → A.Corresponds to variant rs41515347dbSNPEnsembl.1
Natural variantiVAR_028938523T → A.2 PublicationsCorresponds to variant rs2292305dbSNPEnsembl.1
Natural variantiVAR_028939700N → S.1 PublicationCorresponds to variant rs2228262dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05575717 – 101Missing in isoform 2. 1 PublicationAdd BLAST85

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_003246.3. [P07996-1]
UniGeneiHs.164226.
Hs.732539.

Genome annotation databases

EnsembliENST00000260356; ENSP00000260356; ENSG00000137801. [P07996-1]
GeneIDi7057.
KEGGihsa:7057.
UCSCiuc001zkh.4. human. [P07996-1]

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:
EMBLi
GenBanki
DDBJi
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_003246.3. [P07996-1]
UniGeneiHs.164226.
Hs.732539.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FOEX-ray1.98A/B378-429[»]
ProteinModelPortaliP07996.
SMRiP07996.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112915. 33 interactors.
DIPiDIP-1037N.
IntActiP07996. 14 interactors.
MINTiMINT-6630675.
STRINGi9606.ENSP00000260356.

PTM databases

iPTMnetiP07996.
PhosphoSitePlusiP07996.
UniCarbKBiP07996.

Polymorphism and mutation databases

BioMutaiTHBS1.
DMDMi117949802.

2D gel databases

OGPiP07996.

Proteomic databases

EPDiP07996.
MaxQBiP07996.
PaxDbiP07996.
PeptideAtlasiP07996.
PRIDEiP07996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260356; ENSP00000260356; ENSG00000137801. [P07996-1]
GeneIDi7057.
KEGGihsa:7057.
UCSCiuc001zkh.4. human. [P07996-1]

Organism-specific databases

CTDi7057.
DisGeNETi7057.
GeneCardsiTHBS1.
H-InvDBHIX0038125.
HGNCiHGNC:11785. THBS1.
HPAiCAB033678.
MIMi188060. gene.
neXtProtiNX_P07996.
OpenTargetsiENSG00000137801.
PharmGKBiPA36497.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFQQ. Eukaryota.
ENOG410XQKE. LUCA.
GeneTreeiENSGT00850000132273.
HOGENOMiHOG000007542.
HOVERGENiHBG018006.
InParanoidiP07996.
KOiK16857.
OMAiTPQFGGK.
OrthoDBiEOG091G00TV.
PhylomeDBiP07996.
TreeFamiTF324917.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137801-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-186797. Signaling by PDGF.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.
SIGNORiP07996.

Miscellaneous databases

ChiTaRSiTHBS1. human.
EvolutionaryTraceiP07996.
GeneWikiiThrombospondin_1.
GenomeRNAii7057.
PMAP-CutDBP07996.
PROiP07996.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137801.
CleanExiHS_THBS1.
ExpressionAtlasiP07996. baseline and differential.
GenevisibleiP07996. HS.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR000884. TSP1_rpt.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_dom.
[Graphical view]
PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
PfamiPF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 211 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.