P35442 (TSP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thrombospondin-2

Gene names

Name:	THBS2
Synonyms:	TSP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties. Ref.10
Subunit structure	Homotrimer; disulfide-linked. Interacts (via the TSP type I repeats) with CD36; the interaction conveys an antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG; the interaction blocks the antiangiogenic effect of THBS2 with CD36 By similarity. Can bind to fibrinogen, fibronectin, laminin and type V collagen. Ref.7 Ref.8 Ref.11
Tissue specificity	High expression in invertebral disk tissue. Ref.9
Involvement in disease	Genetic variations in THBS2 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain. Ref.9
Sequence similarities	Belongs to the thrombospondin family. Contains 3 EGF-like domains. Contains 1 TSP C-terminal (TSPC) domain. Contains 1 TSP N-terminal (TSPN) domain. Contains 3 TSP type-1 domains. Contains 8 TSP type-3 repeats. Contains 1 VWFC domain.

Ontologies

Keywords
Biological process	Cell adhesion
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of angiogenesis Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cacna2d1	P54290	2	EBI-2466249,EBI-2466294	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 1172

1154

Thrombospondin-2

PRO_0000035846

Regions

Domain

19 – 215

197

TSP N-terminal

Domain

318 – 375

58

VWFC

Domain

381 – 431

51

TSP type-1 1

Domain

437 – 492

56

TSP type-1 2

Domain

494 – 549

56

TSP type-1 3

Domain

549 – 589

41

EGF-like 1

Domain

590 – 647

58

EGF-like 2; calcium-binding Potential

Domain

648 – 692

45

EGF-like 3

Repeat

693 – 728

36

TSP type-3 1

Repeat

729 – 764

36

TSP type-3 2

Repeat

765 – 787

23

TSP type-3 3

Repeat

788 – 823

36

TSP type-3 4

Repeat

824 – 846

23

TSP type-3 5

Repeat

847 – 884

38

TSP type-3 6

Repeat

885 – 920

36

TSP type-3 7

Repeat

921 – 956

36

TSP type-3 8

Domain

960 – 1172

213

TSP C-terminal

Region

19 – 232

214

Heparin-binding Potential

Motif

928 – 930

3

Cell attachment site Potential

Amino acid modifications

Glycosylation

151

1

N-linked (GlcNAc...) Potential

Glycosylation

316

1

N-linked (GlcNAc...) Potential

Glycosylation

330

1

N-linked (GlcNAc...) Potential

Glycosylation

457

1

N-linked (GlcNAc...) Potential

Glycosylation

584

1

N-linked (GlcNAc...) Ref.11

Glycosylation

710

1

N-linked (GlcNAc...) Ref.11

Glycosylation

1069

1

N-linked (GlcNAc...) Ref.11

Disulfide bond

266

Interchain Probable

Disulfide bond

270

Interchain Probable

Disulfide bond

393 ↔ 425

By similarity

Disulfide bond

397 ↔ 430

By similarity

Disulfide bond

408 ↔ 415

By similarity

Disulfide bond

449 ↔ 486

By similarity

Disulfide bond

453 ↔ 491

By similarity

Disulfide bond

464 ↔ 476

By similarity

Disulfide bond

506 ↔ 543

By similarity

Disulfide bond

510 ↔ 548

By similarity

Disulfide bond

521 ↔ 533

By similarity

Disulfide bond

553 ↔ 564

Ref.8 Ref.11

Disulfide bond

558 ↔ 574

Ref.8 Ref.11

Disulfide bond

577 ↔ 588

Ref.8 Ref.11

Disulfide bond

594 ↔ 610

Ref.8 Ref.11

Disulfide bond

601 ↔ 619

Ref.8 Ref.11

Disulfide bond

622 ↔ 646

Ref.8 Ref.11

Disulfide bond

652 ↔ 665

Ref.8 Ref.11

Disulfide bond

659 ↔ 678

Ref.8 Ref.11

Disulfide bond

680 ↔ 691

Ref.8 Ref.11

Disulfide bond

707 ↔ 715

Ref.8 Ref.11

Disulfide bond

720 ↔ 740

Ref.8 Ref.11

Disulfide bond

756 ↔ 776

Ref.8 Ref.11

Disulfide bond

779 ↔ 799

Ref.8 Ref.11

Disulfide bond

815 ↔ 835

Ref.8 Ref.11

Disulfide bond

838 ↔ 858

Ref.8 Ref.11

Disulfide bond

876 ↔ 896

Ref.8 Ref.11

Disulfide bond

912 ↔ 932

Ref.8 Ref.11

Disulfide bond

948 ↔ 1169

Ref.8 Ref.11

Natural variations

Natural variant

133

1

T → S.
Corresponds to variant rs36088849 [ dbSNP | Ensembl ].

VAR_045842

Natural variant

375

1

L → F.
Corresponds to variant rs35404985 [ dbSNP | Ensembl ].

VAR_045843

Experimental info

Mutagenesis

702

1

N → S: Alters protein stability. Ref.12

Sequence conflict

2

1

V → A in AAI50176. Ref.5

Sequence conflict

171 – 173

3

DSF → GPV in AAA03703. Ref.1

Sequence conflict

576

1

S → F in AAA03703. Ref.1

Sequence conflict

1111

1

R → G in AAI46677. Ref.5

Secondary structure

1

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1172

Helix Strand Turn

Details...

Helix

552 – 555

4

Beta strand

564 – 566

3

Beta strand

572 – 574

3

Beta strand

585 – 587

3

Turn

593 – 596

4

Beta strand

605 – 607

3

Beta strand

610 – 612

3

Beta strand

614 – 619

6

Beta strand

626 – 628

3

Beta strand

632 – 636

5

Helix

637 – 640

4

Beta strand

646 – 648

3

Turn

651 – 655

5

Beta strand

663 – 667

5

Beta strand

673 – 680

8

Beta strand

684 – 693

10

Beta strand

697 – 700

4

Turn

706 – 710

5

Beta strand

712 – 714

3

Beta strand

734 – 736

3

Turn

738 – 740

3

Beta strand

746 – 749

4

Turn

751 – 753

3

Beta strand

767 – 772

6

Helix

774 – 776

3

Beta strand

793 – 795

3

Helix

797 – 799

3

Beta strand

805 – 808

4

Turn

810 – 812

3

Beta strand

829 – 831

3

Helix

833 – 835

3

Beta strand

851 – 854

4

Turn

856 – 858

3

Beta strand

866 – 869

4

Helix

871 – 873

3

Beta strand

890 – 892

3

Turn

894 – 896

3

Beta strand

903 – 905

3

Helix

907 – 909

3

Turn

911 – 914

4

Beta strand

926 – 928

3

Helix

930 – 932

3

Beta strand

939 – 941

3

Helix

943 – 945

3

Beta strand

960 – 968

9

Beta strand

971 – 973

3

Beta strand

979 – 982

4

Helix

983 – 985

3

Beta strand

987 – 990

4

Beta strand

995 – 1016

22

Beta strand

1024 – 1033

10

Beta strand

1036 – 1045

10

Beta strand

1053 – 1055

3

Beta strand

1061 – 1069

9

Helix

1076 – 1083

8

Beta strand

1084 – 1086

3

Turn

1089 – 1091

3

Beta strand

1092 – 1097

6

Beta strand

1110 – 1116

7

Turn

1118 – 1120

3

Beta strand

1122 – 1129

8

Beta strand

1132 – 1136

5

Beta strand

1148 – 1156

9

Beta strand

1159 – 1169

11

Sequences

	Sequence		Length	Mass (Da)
	P35442 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 415BF376F4669F6A	FASTA	1,172	129,991
	10 20 30 40 50 60 MVWRLVLLAL WVWPSTQAGH QDKDTTFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF 70 80 90 100 110 120 DYIPPVNADD LSKITKIMRQ KEGFFLTAQL KQDGKSRGTL LALEGPGLSQ RQFEIVSNGP 130 140 150 160 170 180 ADTLDLTYWI DGTRHVVSLE DVGLADSQWK NVTVQVAGET YSLHVGCDLI DSFALDEPFY 190 200 210 220 230 240 EHLQAEKSRM YVAKGSARES HFRGLLQNVH LVFENSVEDI LSKKGCQQGQ GAEINAISEN 250 260 270 280 290 300 TETLRLGPHV TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND 310 320 330 340 350 360 NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC HQITCPPATC 370 380 390 400 410 420 ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TQCSVTCGSG TQQRGRSCDV TSNTCLGPSI 430 440 450 460 470 480 QTRACSLSKC DTRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG 490 500 510 520 530 540 RETKACQGAP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER 550 560 570 580 590 600 QMCNKRSCPV DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVPDI 610 620 630 640 650 660 CFSTSKVPRC VNTQPGFHCL PCPPRYRGNQ PVGVGLEAAK TEKQVCEPEN PCKDKTHNCH 670 680 690 700 710 720 KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNLNLVCATN ATYHCIKDNC 730 740 750 760 770 780 PHLPNSGQED FDKDGIGDAC DDDDDNDGVT DEKDNCQLLF NPRQADYDKD EVGDRCDNCP 790 800 810 820 830 840 YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL 850 860 870 880 890 900 VHNPDQTDVD NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NANQADHDRD GQGDACDPDD 910 920 930 940 950 960 DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN IPDIDDVCPE NNAISETDFR 970 980 990 1000 1010 1020 NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR 1030 1040 1050 1060 1070 1080 DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN 1090 1100 1110 1120 1130 1140 ALWHTGNTPG QVRTLWHDPR NIGWKDYTAY RWHLTHRPKT GYIRVLVHEG KQVMADSGPI 1150 1160 1170 YDQTYAGGRL GLFVFSQEMV YFSDLKYECR DI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and characterization of the complete human thrombospondin 2 cDNA: potential regulatory role for the 3' untranslated region." Labell T.L., Byers P.H. Genomics 17:225-229(1993) [PubMed: 8406456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Thrombospondin II: partial cDNA sequence, chromosome location, and expression of a second member of the thrombospondin gene family in humans." Labell T.L., McGookey Milewicz D.J., Disteche C.M., Byers P.H. Genomics 12:421-429(1992) [PubMed: 1559694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 560-1172. Tissue: Fibroblast.
[7]	"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: 1371676] [Abstract] Cited for: INTERACTION WITH THBS1 AND THBS2.
[8]	"Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2." Misenheimer T.M., Hahr A.J., Harms A.C., Annis D.S., Mosher D.F. J. Biol. Chem. 276:45882-45887(2001) [PubMed: 11590138] [Abstract] Cited for: DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
[9]	"A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation." Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y., Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A., Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S. Am. J. Hum. Genet. 82:1122-1129(2008) [PubMed: 18455130] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO IDD, TISSUE SPECIFICITY.
[10]	"CD36-mediated activation of endothelial cell apoptosis by an N-terminal recombinant fragment of thrombospondin-2 inhibits breast cancer growth and metastasis in vivo." Koch M., Hussein F., Woeste A., Grundker C., Frontzek K., Emons G., Hawighorst T. Breast Cancer Res. Treat. 128:337-346(2011) [PubMed: 20714802] [Abstract] Cited for: FUNCTION.
[11]	"Structure of the calcium-rich signature domain of human thrombospondin-2." Carlson C.B., Bernstein D.A., Annis D.S., Misenheimer T.M., Hannah B.L., Mosher D.F., Keck J.L. Nat. Struct. Mol. Biol. 12:910-914(2005) [PubMed: 16186819] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 551-1172 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-584; ASN-710 AND ASN-1069.
[12]	"Influences of the N700S thrombospondin-1 polymorphism on protein structure and stability." Carlson C.B., Liu Y., Keck J.L., Mosher D.F. J. Biol. Chem. 283:20069-20076(2008) [PubMed: 18499674] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 551-1172, MUTAGENESIS OF ASN-702.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L12350 mRNA. Translation: AAA03703.1.
M81339 mRNA. No translation available.
AK292429 mRNA. Translation: BAF85118.1.
BX322234 Genomic DNA. Translation: CAI23645.1.
CH471051 Genomic DNA. Translation: EAW47455.1.
BC146676 mRNA. Translation: AAI46677.1.
BC150175 mRNA. Translation: AAI50176.1.

IPI

IPI00018769.

PIR

TSHUP2. A47379.

RefSeq

NP_003238.2. NM_003247.2.

UniGene

Hs.371147.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YO8	X-ray	2.60	A	551-1172	[»]
2RHP	X-ray	2.90	A	551-1172	[»]

ProteinModelPortal

P35442.

SMR

P35442. Positions 21-227, 316-377, 381-545, 551-1172.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35442. 1 interaction.

STRING

P35442.

Polymorphism databases

DMDM

215273908.

Proteomic databases

PRIDE

P35442.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366787; ENSP00000355751; ENSG00000186340.

GeneID

7058.

KEGG

hsa:7058.

Organism-specific databases

CTD

7058.

GeneCards

GC06M169615.

H-InvDB

HIX0025092.

HGNC

HGNC:11786. THBS2.

HPA

CAB017716.

MIM

188061. gene.
603932. phenotype.

neXtProt

NX_P35442.

PharmGKB

PA36498.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG15784.

HOGENOM

HBG358328.

HOVERGEN

HBG018006.

InParanoid

P35442.

OMA

TEKQVCE.

OrthoDB

EOG41JZBD.

PhylomeDB

P35442.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P35442.

Bgee

P35442.

CleanEx

HS_THBS2.

Genevestigator

P35442.

GermOnline

ENSG00000186340. Homo sapiens.

Family and domain databases

InterPro

IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR024731. EGF_dom_MSP1-like.
IPR003129. Laminin_G_thrombospondin_N.
IPR000884. Thrombospondin_1_rpt.
IPR015455. Thrombospondin_2.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 2 hits.

KO

K04659.

PANTHER

PTHR10199:SF10. THBS2. 1 hit.

Pfam

PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00090. TSP_1. 3 hits.
PF02412. TSP_3. 11 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]

SMART

SM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 2 hits.
SSF82895. TSP1. 3 hits.

PROSITE

PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

27601.

SOURCE

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Entry information

Entry name

TSP2_HUMAN

Accession

Primary (citable) accession number: P35442
Secondary accession number(s): A6H8N1, A7E232, Q5RI52

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.