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P35442

- TSP2_HUMAN

UniProt

P35442 - TSP2_HUMAN

Protein

Thrombospondin-2

Gene

THBS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    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

    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

    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

    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.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 – 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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 151 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