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P35442

- TSP2_HUMAN

UniProt

P35442 - TSP2_HUMAN

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Protein

Thrombospondin-2

Gene

THBS2

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

Functioni

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. heparin binding Source: ProtInc

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. negative regulation of angiogenesis Source: UniProtKB
  3. positive regulation of synapse assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_16888. Signaling by PDGF.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombospondin-2
Gene namesi
Name:THBS2
Synonyms:TSP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11786. THBS2.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. extracellular region Source: Reactome
  3. platelet alpha granule Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi702 – 7021N → S: Alters protein stability. 1 Publication

Organism-specific databases

MIMi603932. phenotype.
PharmGKBiPA36498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 11721154Thrombospondin-2PRO_0000035846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi266 – 266InterchainCurated
Disulfide bondi270 – 270InterchainCurated
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi393 ↔ 425By similarity
Disulfide bondi397 ↔ 430By similarity
Disulfide bondi408 ↔ 415By similarity
Disulfide bondi449 ↔ 486By similarity
Disulfide bondi453 ↔ 491By similarity
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi464 ↔ 476By similarity
Disulfide bondi506 ↔ 543By similarity
Disulfide bondi510 ↔ 548By similarity
Disulfide bondi521 ↔ 533By similarity
Disulfide bondi553 ↔ 564
Disulfide bondi558 ↔ 574
Disulfide bondi577 ↔ 588
Glycosylationi584 – 5841N-linked (GlcNAc...)1 Publication
Disulfide bondi594 ↔ 610
Disulfide bondi601 ↔ 619
Disulfide bondi622 ↔ 646
Disulfide bondi652 ↔ 665
Disulfide bondi659 ↔ 678
Disulfide bondi680 ↔ 691
Disulfide bondi707 ↔ 715
Glycosylationi710 – 7101N-linked (GlcNAc...)1 Publication
Disulfide bondi720 ↔ 740
Disulfide bondi756 ↔ 776
Disulfide bondi779 ↔ 799
Disulfide bondi815 ↔ 835
Disulfide bondi838 ↔ 858
Disulfide bondi876 ↔ 896
Disulfide bondi912 ↔ 932
Disulfide bondi948 ↔ 1169
Glycosylationi1069 – 10691N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP35442.
PaxDbiP35442.
PRIDEiP35442.

PTM databases

PhosphoSiteiP35442.

Miscellaneous databases

PMAP-CutDBQ5RI52.

Expressioni

Tissue specificityi

High expression in invertebral disk tissue.1 Publication

Gene expression databases

BgeeiP35442.
CleanExiHS_THBS2.
ExpressionAtlasiP35442. baseline and differential.
GenevestigatoriP35442.

Organism-specific databases

HPAiCAB017716.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cacna2d1P542902EBI-2466249,EBI-2466294From a different organism.

Protein-protein interaction databases

BioGridi112916. 4 interactions.
IntActiP35442. 1 interaction.
STRINGi9606.ENSP00000355751.

Structurei

Secondary structure

1
1172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi552 – 5554Combined sources
Beta strandi564 – 5663Combined sources
Beta strandi572 – 5743Combined sources
Beta strandi585 – 5873Combined sources
Turni593 – 5964Combined sources
Beta strandi605 – 6073Combined sources
Beta strandi610 – 6123Combined sources
Beta strandi614 – 6196Combined sources
Beta strandi626 – 6283Combined sources
Beta strandi632 – 6365Combined sources
Helixi637 – 6404Combined sources
Beta strandi646 – 6483Combined sources
Turni651 – 6555Combined sources
Beta strandi663 – 6675Combined sources
Beta strandi673 – 6808Combined sources
Beta strandi684 – 69310Combined sources
Beta strandi697 – 7004Combined sources
Turni706 – 7105Combined sources
Beta strandi712 – 7143Combined sources
Beta strandi734 – 7363Combined sources
Turni738 – 7403Combined sources
Beta strandi746 – 7494Combined sources
Turni751 – 7533Combined sources
Turni755 – 7584Combined sources
Beta strandi767 – 7726Combined sources
Helixi774 – 7763Combined sources
Beta strandi793 – 7953Combined sources
Helixi797 – 7993Combined sources
Beta strandi805 – 8084Combined sources
Turni810 – 8123Combined sources
Beta strandi829 – 8313Combined sources
Helixi833 – 8353Combined sources
Beta strandi851 – 8544Combined sources
Turni856 – 8583Combined sources
Beta strandi866 – 8694Combined sources
Helixi871 – 8733Combined sources
Beta strandi890 – 8923Combined sources
Turni894 – 8963Combined sources
Beta strandi903 – 9053Combined sources
Helixi907 – 9093Combined sources
Turni911 – 9144Combined sources
Beta strandi926 – 9283Combined sources
Helixi930 – 9323Combined sources
Beta strandi939 – 9413Combined sources
Helixi943 – 9453Combined sources
Beta strandi960 – 9689Combined sources
Beta strandi971 – 9733Combined sources
Beta strandi979 – 9824Combined sources
Helixi983 – 9853Combined sources
Beta strandi987 – 9904Combined sources
Beta strandi995 – 101622Combined sources
Beta strandi1024 – 103310Combined sources
Beta strandi1036 – 104510Combined sources
Beta strandi1053 – 10553Combined sources
Beta strandi1061 – 10699Combined sources
Helixi1076 – 10838Combined sources
Beta strandi1084 – 10863Combined sources
Turni1089 – 10913Combined sources
Beta strandi1092 – 10976Combined sources
Beta strandi1110 – 11167Combined sources
Turni1118 – 11203Combined sources
Beta strandi1122 – 11298Combined sources
Beta strandi1132 – 11365Combined sources
Beta strandi1139 – 11413Combined sources
Beta strandi1148 – 11569Combined sources
Beta strandi1159 – 116911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO8X-ray2.60A551-1172[»]
2RHPX-ray2.90A551-1172[»]
ProteinModelPortaliP35442.
SMRiP35442. Positions 25-226, 383-492, 494-1172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35442.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 215197Laminin G-likeAdd
BLAST
Domaini318 – 37558VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini381 – 43151TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini437 – 49256TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini494 – 54956TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini549 – 58941EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini648 – 69245EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati693 – 72836TSP type-3 1Add
BLAST
Repeati729 – 76436TSP type-3 2Add
BLAST
Repeati765 – 78723TSP type-3 3Add
BLAST
Repeati788 – 82336TSP type-3 4Add
BLAST
Repeati824 – 84623TSP type-3 5Add
BLAST
Repeati847 – 88438TSP type-3 6Add
BLAST
Repeati885 – 92036TSP type-3 7Add
BLAST
Repeati921 – 95636TSP type-3 8Add
BLAST
Domaini960 – 1172213TSP C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 232214Heparin-bindingSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi928 – 9303Cell attachment siteSequence Analysis

Sequence similaritiesi

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

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074507.
HOGENOMiHOG000007542.
HOVERGENiHBG018006.
InParanoidiP35442.
KOiK04659.
OMAiTEKQVCE.
OrthoDBiEOG76QFGD.
PhylomeDBiP35442.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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]
PANTHERiPTHR10199:SF10. PTHR10199:SF10. 1 hit.
PfamiPF12947. 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]
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]

Sequencei

Sequence statusi: Complete.

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

P35442-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVWRLVLLAL WVWPSTQAGH QDKDTTFDLF SISNINRKTI GAKQFRGPDP
60 70 80 90 100
GVPAYRFVRF DYIPPVNADD LSKITKIMRQ KEGFFLTAQL KQDGKSRGTL
110 120 130 140 150
LALEGPGLSQ RQFEIVSNGP ADTLDLTYWI DGTRHVVSLE DVGLADSQWK
160 170 180 190 200
NVTVQVAGET YSLHVGCDLI DSFALDEPFY EHLQAEKSRM YVAKGSARES
210 220 230 240 250
HFRGLLQNVH LVFENSVEDI LSKKGCQQGQ GAEINAISEN TETLRLGPHV
260 270 280 290 300
TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND
310 320 330 340 350
NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC
360 370 380 390 400
HQITCPPATC ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TQCSVTCGSG
410 420 430 440 450
TQQRGRSCDV TSNTCLGPSI QTRACSLSKC DTRIRQDGGW SHWSPWSSCS
460 470 480 490 500
VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG RETKACQGAP CPIDGRWSPW
510 520 530 540 550
SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER QMCNKRSCPV
560 570 580 590 600
DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVPDI
610 620 630 640 650
CFSTSKVPRC VNTQPGFHCL PCPPRYRGNQ PVGVGLEAAK TEKQVCEPEN
660 670 680 690 700
PCKDKTHNCH KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW
710 720 730 740 750
PNLNLVCATN ATYHCIKDNC PHLPNSGQED FDKDGIGDAC DDDDDNDGVT
760 770 780 790 800
DEKDNCQLLF NPRQADYDKD EVGDRCDNCP YVHNPAQIDT DNNGEGDACS
810 820 830 840 850
VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL VHNPDQTDVD
860 870 880 890 900
NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NANQADHDRD GQGDACDPDD
910 920 930 940 950
DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN IPDIDDVCPE
960 970 980 990 1000
NNAISETDFR NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV
1010 1020 1030 1040 1050
GFDEFGSVDF SGTFYVNTDR DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW
1060 1070 1080 1090 1100
EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN ALWHTGNTPG QVRTLWHDPR
1110 1120 1130 1140 1150
NIGWKDYTAY RWHLTHRPKT GYIRVLVHEG KQVMADSGPI YDQTYAGGRL
1160 1170
GLFVFSQEMV YFSDLKYECR DI
Length:1,172
Mass (Da):129,991
Last modified:November 25, 2008 - v2
Checksum:i415BF376F4669F6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → A in AAI50176. (PubMed:15489334)Curated
Sequence conflicti171 – 1733DSF → GPV in AAA03703. (PubMed:8406456)Curated
Sequence conflicti576 – 5761S → F in AAA03703. (PubMed:8406456)Curated
Sequence conflicti1111 – 11111R → G in AAI46677. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331T → S.
Corresponds to variant rs36088849 [ dbSNP | Ensembl ].
VAR_045842
Natural varianti375 – 3751L → F.
Corresponds to variant rs35404985 [ dbSNP | Ensembl ].
VAR_045843

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34574.1.
PIRiA47379. TSHUP2.
RefSeqiNP_003238.2. NM_003247.3.
UniGeneiHs.371147.

Genome annotation databases

EnsembliENST00000366787; ENSP00000355751; ENSG00000186340.
ENST00000617924; ENSP00000482784; ENSG00000186340.
GeneIDi7058.
KEGGihsa:7058.
UCSCiuc003qwt.3. human.

Polymorphism databases

DMDMi215273908.

Keywords - Coding sequence diversityi

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
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 .
CCDSi CCDS34574.1.
PIRi A47379. TSHUP2.
RefSeqi NP_003238.2. NM_003247.3.
UniGenei Hs.371147.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YO8 X-ray 2.60 A 551-1172 [» ]
2RHP X-ray 2.90 A 551-1172 [» ]
ProteinModelPortali P35442.
SMRi P35442. Positions 25-226, 383-492, 494-1172.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112916. 4 interactions.
IntActi P35442. 1 interaction.
STRINGi 9606.ENSP00000355751.

PTM databases

PhosphoSitei P35442.

Polymorphism databases

DMDMi 215273908.

Proteomic databases

MaxQBi P35442.
PaxDbi P35442.
PRIDEi P35442.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366787 ; ENSP00000355751 ; ENSG00000186340 .
ENST00000617924 ; ENSP00000482784 ; ENSG00000186340 .
GeneIDi 7058.
KEGGi hsa:7058.
UCSCi uc003qwt.3. human.

Organism-specific databases

CTDi 7058.
GeneCardsi GC06M169615.
H-InvDB HIX0025092.
HIX0165050.
HGNCi HGNC:11786. THBS2.
HPAi CAB017716.
MIMi 188061. gene.
603932. phenotype.
neXtProti NX_P35442.
PharmGKBi PA36498.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00550000074507.
HOGENOMi HOG000007542.
HOVERGENi HBG018006.
InParanoidi P35442.
KOi K04659.
OMAi TEKQVCE.
OrthoDBi EOG76QFGD.
PhylomeDBi P35442.
TreeFami TF324917.

Enzyme and pathway databases

Reactomei REACT_16888. Signaling by PDGF.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

ChiTaRSi THBS2. human.
EvolutionaryTracei P35442.
GeneWikii THBS2.
GenomeRNAii 7058.
NextBioi 27601.
PMAP-CutDB Q5RI52.
PROi P35442.
SOURCEi Search...

Gene expression databases

Bgeei P35442.
CleanExi HS_THBS2.
ExpressionAtlasi P35442. baseline and differential.
Genevestigatori P35442.

Family and domain databases

Gene3Di 2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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 ]
PANTHERi PTHR10199:SF10. PTHR10199:SF10. 1 hit.
Pfami PF12947. 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 ]
SMARTi SM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
SUPFAMi SSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEi PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiTSP2_HUMAN
AccessioniPrimary (citable) accession number: P35442
Secondary accession number(s): A6H8N1, A7E232, Q5RI52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 153 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 6
    Human chromosome 6: 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