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P35442

- TSP2_HUMAN

UniProt

P35442 - TSP2_HUMAN

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Protein
Thrombospondin-2
Gene
THBS2, TSP2
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
  3. protein binding Source: IntAct

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

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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 11721154Thrombospondin-2
PRO_0000035846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi151 – 1511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi266 – 266Interchain Inferred
Disulfide bondi270 – 270Interchain Inferred
Glycosylationi316 – 3161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi330 – 3301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi393 ↔ 425 By similarity
Disulfide bondi397 ↔ 430 By similarity
Disulfide bondi408 ↔ 415 By similarity
Disulfide bondi449 ↔ 486 By similarity
Disulfide bondi453 ↔ 491 By similarity
Glycosylationi457 – 4571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi464 ↔ 476 By similarity
Disulfide bondi506 ↔ 543 By similarity
Disulfide bondi510 ↔ 548 By similarity
Disulfide bondi521 ↔ 533 By similarity
Disulfide bondi553 ↔ 5642 Publications
Disulfide bondi558 ↔ 5742 Publications
Disulfide bondi577 ↔ 5882 Publications
Glycosylationi584 – 5841N-linked (GlcNAc...)1 Publication
Disulfide bondi594 ↔ 6102 Publications
Disulfide bondi601 ↔ 6192 Publications
Disulfide bondi622 ↔ 6462 Publications
Disulfide bondi652 ↔ 6652 Publications
Disulfide bondi659 ↔ 6782 Publications
Disulfide bondi680 ↔ 6912 Publications
Disulfide bondi707 ↔ 7152 Publications
Glycosylationi710 – 7101N-linked (GlcNAc...)1 Publication
Disulfide bondi720 ↔ 7402 Publications
Disulfide bondi756 ↔ 7762 Publications
Disulfide bondi779 ↔ 7992 Publications
Disulfide bondi815 ↔ 8352 Publications
Disulfide bondi838 ↔ 8582 Publications
Disulfide bondi876 ↔ 8962 Publications
Disulfide bondi912 ↔ 9322 Publications
Disulfide bondi948 ↔ 11692 Publications
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

ArrayExpressiP35442.
BgeeiP35442.
CleanExiHS_THBS2.
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.3 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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO8X-ray2.60A551-1172[»]
2RHPX-ray2.90A551-1172[»]
ProteinModelPortaliP35442.
SMRiP35442. Positions 25-226, 383-1172.

Miscellaneous databases

EvolutionaryTraceiP35442.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 232214Heparin-binding Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi928 – 9303Cell attachment site Reviewed prediction

Sequence similaritiesi

Belongs to the thrombospondin family.
Contains 2 EGF-like domains.
Contains 3 TSP type-1 domains.
Contains 8 TSP type-3 repeats.
Contains 1 VWFC domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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

MVWRLVLLAL WVWPSTQAGH QDKDTTFDLF SISNINRKTI GAKQFRGPDP     50
GVPAYRFVRF DYIPPVNADD LSKITKIMRQ KEGFFLTAQL KQDGKSRGTL 100
LALEGPGLSQ RQFEIVSNGP ADTLDLTYWI DGTRHVVSLE DVGLADSQWK 150
NVTVQVAGET YSLHVGCDLI DSFALDEPFY EHLQAEKSRM YVAKGSARES 200
HFRGLLQNVH LVFENSVEDI LSKKGCQQGQ GAEINAISEN TETLRLGPHV 250
TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND 300
NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC 350
HQITCPPATC ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TQCSVTCGSG 400
TQQRGRSCDV TSNTCLGPSI QTRACSLSKC DTRIRQDGGW SHWSPWSSCS 450
VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG RETKACQGAP CPIDGRWSPW 500
SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER QMCNKRSCPV 550
DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVPDI 600
CFSTSKVPRC VNTQPGFHCL PCPPRYRGNQ PVGVGLEAAK TEKQVCEPEN 650
PCKDKTHNCH KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW 700
PNLNLVCATN ATYHCIKDNC PHLPNSGQED FDKDGIGDAC DDDDDNDGVT 750
DEKDNCQLLF NPRQADYDKD EVGDRCDNCP YVHNPAQIDT DNNGEGDACS 800
VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL VHNPDQTDVD 850
NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NANQADHDRD GQGDACDPDD 900
DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN IPDIDDVCPE 950
NNAISETDFR NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV 1000
GFDEFGSVDF SGTFYVNTDR DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW 1050
EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN ALWHTGNTPG QVRTLWHDPR 1100
NIGWKDYTAY RWHLTHRPKT GYIRVLVHEG KQVMADSGPI YDQTYAGGRL 1150
GLFVFSQEMV YFSDLKYECR DI 1172
Length:1,172
Mass (Da):129,991
Last modified:November 25, 2008 - v2
Checksum:i415BF376F4669F6A
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → A in AAI50176. 1 Publication
Sequence conflicti171 – 1733DSF → GPV in AAA03703. 1 Publication
Sequence conflicti576 – 5761S → F in AAA03703. 1 Publication
Sequence conflicti1111 – 11111R → G in AAI46677. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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, 383-1172.
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 .
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.
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

ArrayExpressi P35442.
Bgeei P35442.
CleanExi HS_THBS2.
Genevestigatori P35442.

Family and domain databases

Gene3Di 2.60.120.200. 3 hits.
4.10.1080.10. 2 hits.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
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: September 3, 2014
This is version 150 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

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