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P35442 (TSP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombospondin-2
Gene names
Name:THBS2
Synonyms:TSP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the thrombospondin family.

Contains 2 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 3 TSP type-1 domains.

Contains 8 TSP type-3 repeats.

Contains 1 VWFC domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cacna2d1P542902EBI-2466249,EBI-2466294From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11721154Thrombospondin-2
PRO_0000035846

Regions

Domain19 – 215197Laminin G-like
Domain318 – 37558VWFC
Domain381 – 43151TSP type-1 1
Domain437 – 49256TSP type-1 2
Domain494 – 54956TSP type-1 3
Domain549 – 58941EGF-like 1
Domain648 – 69245EGF-like 2
Repeat693 – 72836TSP type-3 1
Repeat729 – 76436TSP type-3 2
Repeat765 – 78723TSP type-3 3
Repeat788 – 82336TSP type-3 4
Repeat824 – 84623TSP type-3 5
Repeat847 – 88438TSP type-3 6
Repeat885 – 92036TSP type-3 7
Repeat921 – 95636TSP type-3 8
Domain960 – 1172213TSP C-terminal
Region19 – 232214Heparin-binding Potential
Motif928 – 9303Cell attachment site Potential

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Ref.11
Glycosylation7101N-linked (GlcNAc...) Ref.11
Glycosylation10691N-linked (GlcNAc...) Ref.11
Disulfide bond266Interchain Probable
Disulfide bond270Interchain Probable
Disulfide bond393 ↔ 425 By similarity
Disulfide bond397 ↔ 430 By similarity
Disulfide bond408 ↔ 415 By similarity
Disulfide bond449 ↔ 486 By similarity
Disulfide bond453 ↔ 491 By similarity
Disulfide bond464 ↔ 476 By similarity
Disulfide bond506 ↔ 543 By similarity
Disulfide bond510 ↔ 548 By similarity
Disulfide bond521 ↔ 533 By similarity
Disulfide bond553 ↔ 564 Ref.8 Ref.11
Disulfide bond558 ↔ 574 Ref.8 Ref.11
Disulfide bond577 ↔ 588 Ref.8 Ref.11
Disulfide bond594 ↔ 610 Ref.8 Ref.11
Disulfide bond601 ↔ 619 Ref.8 Ref.11
Disulfide bond622 ↔ 646 Ref.8 Ref.11
Disulfide bond652 ↔ 665 Ref.8 Ref.11
Disulfide bond659 ↔ 678 Ref.8 Ref.11
Disulfide bond680 ↔ 691 Ref.8 Ref.11
Disulfide bond707 ↔ 715 Ref.8 Ref.11
Disulfide bond720 ↔ 740 Ref.8 Ref.11
Disulfide bond756 ↔ 776 Ref.8 Ref.11
Disulfide bond779 ↔ 799 Ref.8 Ref.11
Disulfide bond815 ↔ 835 Ref.8 Ref.11
Disulfide bond838 ↔ 858 Ref.8 Ref.11
Disulfide bond876 ↔ 896 Ref.8 Ref.11
Disulfide bond912 ↔ 932 Ref.8 Ref.11
Disulfide bond948 ↔ 1169 Ref.8 Ref.11

Natural variations

Natural variant1331T → S.
Corresponds to variant rs36088849 [ dbSNP | Ensembl ].
VAR_045842
Natural variant3751L → F.
Corresponds to variant rs35404985 [ dbSNP | Ensembl ].
VAR_045843

Experimental info

Mutagenesis7021N → S: Alters protein stability. Ref.12
Sequence conflict21V → A in AAI50176. Ref.5
Sequence conflict171 – 1733DSF → GPV in AAA03703. Ref.1
Sequence conflict5761S → F in AAA03703. Ref.1
Sequence conflict11111R → G in AAI46677. Ref.5

Secondary structure

................................................................................................................................. 1172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35442 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 415BF376F4669F6A

FASTA1,172129,991
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 551-1172, MUTAGENESIS OF ASN-702.
+Additional computationally mapped references.

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.
CCDSCCDS34574.1.
PIRTSHUP2. A47379.
RefSeqNP_003238.2. NM_003247.3.
UniGeneHs.371147.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO8X-ray2.60A551-1172[»]
2RHPX-ray2.90A551-1172[»]
ProteinModelPortalP35442.
SMRP35442. Positions 25-226, 383-1172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112916. 4 interactions.
IntActP35442. 1 interaction.
STRING9606.ENSP00000355751.

PTM databases

PhosphoSiteP35442.

Polymorphism databases

DMDM215273908.

Proteomic databases

MaxQBP35442.
PaxDbP35442.
PRIDEP35442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366787; ENSP00000355751; ENSG00000186340.
GeneID7058.
KEGGhsa:7058.
UCSCuc003qwt.3. human.

Organism-specific databases

CTD7058.
GeneCardsGC06M169615.
H-InvDBHIX0025092.
HIX0165050.
HGNCHGNC:11786. THBS2.
HPACAB017716.
MIM188061. gene.
603932. phenotype.
neXtProtNX_P35442.
PharmGKBPA36498.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007542.
HOVERGENHBG018006.
InParanoidP35442.
KOK04659.
OMATEKQVCE.
OrthoDBEOG76QFGD.
PhylomeDBP35442.
TreeFamTF324917.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP35442.
BgeeP35442.
CleanExHS_THBS2.
GenevestigatorP35442.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR024731. EGF_dom_MSP1-like.
IPR001791. Laminin_G.
IPR015455. Thrombospondin-2.
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]
PANTHERPTHR10199:SF10. PTHR10199:SF10. 1 hit.
PfamPF12947. EGF_3. 1 hit.
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]
SMARTSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTHBS2. human.
EvolutionaryTraceP35442.
GeneWikiTHBS2.
GenomeRNAi7058.
NextBio27601.
PMAP-CutDBQ5RI52.
PROP35442.
SOURCESearch...

Entry information

Entry nameTSP2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM