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Тромбоспондин 1 англ Thrombospondin 1 білок який кодується геном THBS1 розташованим у людей на короткому плечі 15 ї хром

Тромбоспондин-1

Тромбоспондин-1

Тромбоспондин-1 (англ. Thrombospondin 1) – білок, який кодується геном THBS1, розташованим у людей на короткому плечі 15-ї хромосоми. Довжина поліпептидного ланцюга білка становить 1 170 амінокислот, а молекулярна маса — 129 383.

Тромбоспондин-1
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Наявні структури
PDBПошук ортологів: PDBe RCSB
Ідентифікатори
Символи THBS1, THBS, THBS-1, TSP, TSP-1, TSP1, thrombospondin 1
Зовнішні ІД OMIM: 188060 MGI: 98737 HomoloGene: 31142 GeneCards: THBS1
Шаблон експресії
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Більше даних
Ортологи
Види Людина Миша
Entrez
7057
21825
Ensembl
ENSG00000137801
ENSMUSG00000040152
UniProt
P07996
P35441
RefSeq (мРНК)
NM_003246
NM_011580
NM_001313914
RefSeq (білок)
NP_003237
н/д
Локус (UCSC) Хр. 15: 39.58 – 39.6 Mb Хр. 2: 117.94 – 117.96 Mb
PubMed search
Вікідані
Див./Ред. для людейДив./Ред. для мишей
Послідовність амінокислот
1020304050
MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVK
GPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKT
RGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLAT
GQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIA
KGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGS
SPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRK
VTEENKELANELRRPPLCYHNGVQYRNNEEWTVDSCTECHCQNSVTICKK
VSCPIMPCSNATVPDGECCPRCWPSDSADDGWSPWSEWTSCSTSCGNGIQ
QRGRSCDSLNNRCEGSSVQTRTCHIQECDKRFKQDGGWSHWSPWSSCSVT
CGDGVITRIRLCNSPSPQMNGKPCEGEARETKACKKDACPINGGWGPWSP
WDICSVTCGGGVQKRSRLCNNPTPQFGGKDCVGDVTENQICNKQDCPIDG
CLSNPCFAGVKCTSYPDGSWKCGACPPGYSGNGIQCTDVDECKEVPDACF
NHNGEHRCENTDPGYNCLPCPPRFTGSQPFGQGVEHATANKQVCKPRNPC
TDGTHDCNKNAKCNYLGHYSDPMYRCECKPGYAGNGIICGEDTDLDGWPN
ENLVCVANATYHCKKDNCPNLPNSGQEDYDKDGIGDACDDDDDNDKIPDD
RDNCPFHYNPAQYDYDRDDVGDRCDNCPYNHNPDQADTDNNGEGDACAAD
IDGDGILNERDNCQYVYNVDQRDTDMDGVGDQCDNCPLEHNPDQLDSDSD
RIGDTCDNNQDIDEDGHQNNLDNCPYVPNANQADHDKDGKGDACDHDDDN
DGIPDDKDNCRLVPNPDQKDSDGDGRGDACKDDFDHDSVPDIDDICPENV
DISETDFRRFQMIPLDPKGTSQNDPNWVVRHQGKELVQTVNCDPGLAVGY
DEFNAVDFSGTFFINTERDDDYAGFVFGYQSSSRFYVVMWKQVTQSYWDT
NPTRAQGYSGLSVKVVNSTTGPGEHLRNALWHTGNTPGQVRTLWHDPRHI
GWKDFTAYRWRLSHRPKTGFIRVVMYEGKKIMADSGPIYDKTYAGGRLGL
FVFSQEMVFFSDLKYECRDP

Задіяний у таких біологічних процесах як клітинна адгезія, відповідь на порушення конформації білку. Білок має сайт для зв'язування з іоном кальцію, з молекулою гепарину. Локалізований у ендоплазматичному ретикулумі, саркоплазматичному ретикулумі.

Література

  • Lawler J., Hynes R.O. (1986). The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J. Cell Biol. 103: 1635—1648. PMID 2430973 DOI:10.1083/jcb.103.5.1635
  • The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
  • Kobayashi S., Eden-Mccutchan F., Framson P., Bornstein P. (1986). Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones: homology to malarial circumsporozoite proteins. Biochemistry. 25: 8418—8425. PMID 3030396 DOI:10.1021/bi00374a014
  • Dixit V.M., Hennessy S.W., Grant G.A., Rotwein P., Frazier W.A. (1986). Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin. Proc. Natl. Acad. Sci. U.S.A. 83: 5449—5453. PMID 3461443 DOI:10.1073/pnas.83.15.5449
  • Asch A.S., Silbiger S., Heimer E., Nachman R.L. (1992). Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding. Biochem. Biophys. Res. Commun. 182: 1208—1217. PMID 1371676 DOI:10.1016/0006-291X(92)91860-S
  • Huwiler K.G., Vestling M.M., Annis D.S., Mosher D.F. (2002). Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1. Biochemistry. 41: 14329—14339. PMID 12450399 DOI:10.1021/bi026463u

Примітки

  1. Human PubMed Reference:.
  2. Mouse PubMed Reference:.
  3. HUGO Gene Nomenclature Commitee, HGNC:11785 (англ.) . Процитовано 30 січня 2017.
  4. UniProt, P07996 (англ.) . Процитовано 30 січня 2017.

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Trombospondin 1 angl Thrombospondin 1 bilok yakij koduyetsya genom THBS1 roztashovanim u lyudej na korotkomu plechi 15 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 1 170 aminokislot a molekulyarna masa 129 383 Trombospondin 1Nayavni strukturiPDBPoshuk ortologiv PDBe RCSBSpisok kodiv PDB1LSL 1UX6 1Z78 1ZA4 2ERF 2ES3 2OUH 2OUJ 3R6B 5FOEIdentifikatoriSimvoliTHBS1 THBS THBS 1 TSP TSP 1 TSP1 thrombospondin 1Zovnishni ID OMIM 188060 MGI 98737 HomoloGene 31142 GeneCards THBS1Ontologiya genaMolekulyarna funkciya calcium ion binding heparin binding extracellular matrix binding fibroblast growth factor binding phosphatidylserine binding proteoglycan binding collagen V binding fibrinogen binding low density lipoprotein particle binding integrin binding laminin binding fibronectin binding identical protein binding transforming growth factor beta binding GO 0001948 GO 0016582 protein binding extracellular matrix structural constituentKlitinna komponenta endoplasmic reticulum lumen platelet alpha granule cell surface endoplazmatichnij retikulum ekzosoma GO 0005578 Pozaklitinna matricya secretory granule platelet alpha granule lumen Fibrinogen sarcoplasmic reticulum external side of plasma membrane citoplazma mizhklitinnij prostir extracellular region collagen containing extracellular matrixBiologichnij proces positive regulation of transforming growth factor beta receptor signaling pathway cellular response to heat negative regulation of fibrinolysis protein O linked fucosylation response to progesterone response to magnesium ion positive regulation of translation negative regulation of endothelial cell migration negative regulation of cell matrix adhesion negative regulation of long chain fatty acid import across plasma membrane positive regulation of reactive oxygen species metabolic process positive regulation of blood coagulation positive regulation of blood vessel endothelial cell migration positive regulation of macrophage chemotaxis positive regulation of protein kinase B signaling negative regulation of plasminogen activation negative regulation of blood vessel endothelial cell migration negative regulation of extrinsic apoptotic signaling pathway response to endoplasmic reticulum stress positive regulation of endothelial cell apoptotic process response to unfolded protein positive regulation of chemotaxis negative regulation of cGMP mediated signaling positive regulation of phosphorylation inflammatory response negative regulation of focal adhesion assembly chronic inflammatory response negative regulation of nitric oxide mediated signal transduction engulfment of apoptotic cell extracellular matrix organization positive regulation of macrophage activation sprouting angiogenesis negative regulation of apoptotic process response to glucose positive regulation of angiogenesis response to calcium ion positive regulation of transforming growth factor beta1 production adgeziya klitin behavioral response to pain GO 0046730 GO 0046737 GO 0046738 GO 0046736 imunna vidpovid negative regulation of interleukin 12 production positive regulation of extrinsic apoptotic signaling pathway via death domain receptors negative regulation of cysteine type endopeptidase activity involved in apoptotic process response to hypoxia positive regulation of cell migration platelet degranulation negative regulation of endothelial cell chemotaxis negative regulation of endothelial cell proliferation positive regulation of endothelial cell migration negative regulation of fibroblast growth factor receptor signaling pathway GO 0051357 GO 0051358 GO 0051359 peptide cross linking negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II negative regulation of dendritic cell antigen processing and presentation negative regulation of angiogenesis cell migration positive regulation of fibroblast migration response to testosterone cellular response to tumor necrosis factor cellular response to growth factor stimulus positive regulation of transforming growth factor beta production response to mechanical stimulus positive regulation of cell population proliferation positive regulation of smooth muscle cell proliferation regulation of megakaryocyte differentiation negative regulation of cell migration involved in sprouting angiogenesis negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis negative regulation of sprouting angiogenesisDzherela Amigo QuickGOShablon ekspresiyiBilshe danihOrtologiVidi Lyudina MishaEntrez7057 21825Ensembl ENSG00000137801 ENSMUSG00000040152UniProt P07996 P35441RefSeq mRNK NM 003246NM 011580 NM 001313914RefSeq bilok NP 003237n dLokus UCSC Hr 15 39 58 39 6 MbHr 2 117 94 117 96 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishejPoslidovnist aminokislot1020304050MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRKVTEENKELANELRRPPLCYHNGVQYRNNEEWTVDSCTECHCQNSVTICKKVSCPIMPCSNATVPDGECCPRCWPSDSADDGWSPWSEWTSCSTSCGNGIQQRGRSCDSLNNRCEGSSVQTRTCHIQECDKRFKQDGGWSHWSPWSSCSVTCGDGVITRIRLCNSPSPQMNGKPCEGEARETKACKKDACPINGGWGPWSPWDICSVTCGGGVQKRSRLCNNPTPQFGGKDCVGDVTENQICNKQDCPIDGCLSNPCFAGVKCTSYPDGSWKCGACPPGYSGNGIQCTDVDECKEVPDACFNHNGEHRCENTDPGYNCLPCPPRFTGSQPFGQGVEHATANKQVCKPRNPCTDGTHDCNKNAKCNYLGHYSDPMYRCECKPGYAGNGIICGEDTDLDGWPNENLVCVANATYHCKKDNCPNLPNSGQEDYDKDGIGDACDDDDDNDKIPDDRDNCPFHYNPAQYDYDRDDVGDRCDNCPYNHNPDQADTDNNGEGDACAADIDGDGILNERDNCQYVYNVDQRDTDMDGVGDQCDNCPLEHNPDQLDSDSDRIGDTCDNNQDIDEDGHQNNLDNCPYVPNANQADHDKDGKGDACDHDDDNDGIPDDKDNCRLVPNPDQKDSDGDGRGDACKDDFDHDSVPDIDDICPENVDISETDFRRFQMIPLDPKGTSQNDPNWVVRHQGKELVQTVNCDPGLAVGYDEFNAVDFSGTFFINTERDDDYAGFVFGYQSSSRFYVVMWKQVTQSYWDTNPTRAQGYSGLSVKVVNSTTGPGEHLRNALWHTGNTPGQVRTLWHDPRHIGWKDFTAYRWRLSHRPKTGFIRVVMYEGKKIMADSGPIYDKTYAGGRLGLFVFSQEMVFFSDLKYECRDPA Alanin C Cisteyin D Asparaginova kislota E Glutaminova kislota F Fenilalanin G Glicin H Gistidin I Izolejcin K Lizin L Lejcin M Metionin N Asparagin P Prolin Q Glutamin R Arginin S Serin T Treonin V Valin W Triptofan Y Tirozin Zadiyanij u takih biologichnih procesah yak klitinna adgeziya vidpovid na porushennya konformaciyi bilku Bilok maye sajt dlya zv yazuvannya z ionom kalciyu z molekuloyu geparinu Lokalizovanij u endoplazmatichnomu retikulumi sarkoplazmatichnomu retikulumi LiteraturaLawler J Hynes R O 1986 The structure of human thrombospondin an adhesive glycoprotein with multiple calcium binding sites and homologies with several different proteins J Cell Biol 103 1635 1648 PMID 2430973 DOI 10 1083 jcb 103 5 1635 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 2121 2127 2004 PMID 15489334 DOI 10 1101 gr 2596504 Kobayashi S Eden Mccutchan F Framson P Bornstein P 1986 Partial amino acid sequence of human thrombospondin as determined by analysis of cDNA clones homology to malarial circumsporozoite proteins Biochemistry 25 8418 8425 PMID 3030396 DOI 10 1021 bi00374a014 Dixit V M Hennessy S W Grant G A Rotwein P Frazier W A 1986 Characterization of a cDNA encoding the heparin and collagen binding domains of human thrombospondin Proc Natl Acad Sci U S A 83 5449 5453 PMID 3461443 DOI 10 1073 pnas 83 15 5449 Asch A S Silbiger S Heimer E Nachman R L 1992 Thrombospondin sequence motif CSVTCG is responsible for CD36 binding Biochem Biophys Res Commun 182 1208 1217 PMID 1371676 DOI 10 1016 0006 291X 92 91860 S Huwiler K G Vestling M M Annis D S Mosher D F 2002 Biophysical characterization including disulfide bond assignments of the anti angiogenic type 1 domains of human thrombospondin 1 Biochemistry 41 14329 14339 PMID 12450399 DOI 10 1021 bi026463uPrimitkiHuman PubMed Reference Mouse PubMed Reference HUGO Gene Nomenclature Commitee HGNC 11785 angl Procitovano 30 sichnya 2017 UniProt P07996 angl Procitovano 30 sichnya 2017 Div takozhHromosoma 15Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi

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