PLAUR

PLAUR
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген Рецептор урокиназы[d][1]
Молекуляр функция protein domain specific binding[d][2], связывание с белками плазмы[d][3][4][5][…], urokinase plasminogen activator receptor activity[d][6][7][8][…], enzyme binding[d][9][10], signaling receptor binding[d][2], urokinase plasminogen activator receptor activity[d][11][12][13] һәм signaling receptor activity[d][14][11][12]
Күзәнәк компоненты мембрана өлеше[d][11], cell projection[d][13], endoplasmic reticulum lumen[d][13], endoplasmic reticulum membrane[d][13], мембрана[d][13], фокальные контакты[d][15], күзәнәк мембранасы өлеше[d][13], күзәнәк тышындагы өлкә[d][13], межклеточные контакты[d][13], anchored component of membrane[d][13], экзосома[d][16], extrinsic component of membrane[d][17], күзәнәк мембранасы[d][8][18][8][…], specific granule membrane[d][13], күзәнәк өслеге[d][10], күзәнәк мембранасы[d][13][14][13][…] һәм фокальные контакты[d][19]
Биологик процесс positive regulation of protein phosphorylation[d][20], negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway[d][20], фибринолиз[d][13], negative regulation of intrinsic apoptotic signaling pathway[d][20], urokinase plasminogen activator signaling pathway[d][8][8], негативная регуляция апоптоза[d][20], cвёртывание крови[d][17][12], attachment of GPI anchor to protein[d][8], хемотаксис[d][14], positive regulation of release of cytochrome c from mitochondria[d][20], positive regulation of DNA binding[d][20], positive regulation of epidermal growth factor receptor signaling pathway[d][20], regulation of proteolysis[d][11][13], передача сигнала[d][14], neutrophil degranulation[d][13] һәм urokinase plasminogen activator signaling pathway[d][13]
Изображение Gene Atlas

PLAUR (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]

Искәрмәләр

  1. 1,0 1,1 UniProt
  2. 2,0 2,1 Kreiling J. L., Byrd J. C., Deisz R. J. et al. Binding of urokinase-type plasminogen activator receptor (uPAR) to the mannose 6-phosphate/insulin-like growth factor II receptor: contrasting interactions of full-length and soluble forms of uPAR // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M302249200PMID:12665524
  3. F Mahdi, Z Shariat-Madar, Todd R. F. et al. Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells // BloodAmerican Society of Hematology, Elsevier, 2001. — ISSN 0006-4971; 1528-0020doi:10.1182/BLOOD.V97.8.2342PMID:11290596
  4. Zhu Y., Bujo H., Yamazaki H. et al. LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration // Circ. Res.Lippincott Williams & Wilkins, 2004. — ISSN 0009-7330; 1524-4571doi:10.1161/01.RES.0000120862.79154.0FPMID:14764453
  5. Robaglia-Schlupp A., Szepetowski P., Massacrier A. et al. Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR // Human Molecular GeneticsOUP, 2008. — ISSN 0964-6906; 1460-2083doi:10.1093/HMG/DDN256PMID:18718938
  6. Roldan A. L., Cubellis M. V., Masucci M. T. et al. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis // EMBO J.NPG, 1990. — ISSN 0261-4189; 1460-2075doi:10.1002/(ISSN)1460-2075PMID:1689240
  7. C Pyke, J Eriksen, H Solberg et al. An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator // FEBS LettersElsevier, 1993. — ISSN 0014-5793; 1873-3468doi:10.1016/0014-5793(93)81763-PPMID:8392005
  8. 8,0 8,1 8,2 8,3 8,4 8,5 GOA
  9. Magdolen V. Proteolytic regulation of the urokinase receptor/CD87 on monocytic cells by neutrophil elastase and cathepsin G // J. Immunol.Baltimore: 2004. — ISSN 0022-1767; 1550-6606doi:10.4049/JIMMUNOL.172.1.540PMID:14688365
  10. 10,0 10,1 Jin H., Song Y. P., Boel G. et al. Group A streptococcal surface GAPDH, SDH, recognizes uPAR/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells // Journal of Molecular Biology / P. WrightElsevier, 2005. — ISSN 0022-2836; 1089-8638doi:10.1016/J.JMB.2005.04.063PMID:15922359
  11. 11,0 11,1 11,2 11,3 Roldan A. L., Cubellis M. V., Masucci M. T. et al. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis // EMBO J.NPG, 1990. — ISSN 0261-4189; 1460-2075doi:10.1002/(ISSN)1460-2075PMID:1689240
  12. 12,0 12,1 12,2 C Pyke, J Eriksen, H Solberg et al. An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator // FEBS LettersElsevier, 1993. — ISSN 0014-5793; 1873-3468doi:10.1016/0014-5793(93)81763-PPMID:8392005
  13. 13,00 13,01 13,02 13,03 13,04 13,05 13,06 13,07 13,08 13,09 13,10 13,11 13,12 13,13 13,14 13,15 GOA
  14. 14,0 14,1 14,2 14,3 A Shevelev, V Tkachuk The chemotactic action of urokinase on smooth muscle cells is dependent on its kringle domain. Characterization of interactions and contribution to chemotaxis // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M909080199PMID:10749881
  15. Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol.NPG, 2011. — ISSN 1465-7392; 1476-4679doi:10.1038/NCB2216PMID:21423176
  16. Farina A., Lane L., Lescuyer P. et al. Proteomic analysis of podocyte exosome-enriched fraction from normal human urine // Journal of ProteomicsElsevier, 2013. — ISSN 1874-3919; 0165-022Xdoi:10.1016/J.JPROT.2013.01.012PMID:23376485
  17. 17,0 17,1 JR C., JG P., Kottra J et al. The structure of the urokinase-type plasminogen activator receptor gene // BloodAmerican Society of Hematology, Elsevier, 1994. — 6 p. — ISSN 0006-4971; 1528-0020PMID:8049431
  18. A Shevelev, V Tkachuk The chemotactic action of urokinase on smooth muscle cells is dependent on its kringle domain. Characterization of interactions and contribution to chemotaxis // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M909080199PMID:10749881
  19. Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol.NPG, 2011. — ISSN 1465-7392; 1476-4679doi:10.1038/NCB2216PMID:21423176
  20. 20,0 20,1 20,2 20,3 20,4 20,5 20,6 Gondi C. S., Rao J. S., Kotipatruni R. R. Apoptosis induced by knockdown of uPAR and MMP-9 is mediated by inactivation of EGFR/STAT3 signaling in medulloblastoma, Apoptosis Induced by Knockdown of uPAR and MMP-9 is Mediated by Inactivation of EGFR/STAT3 Signaling in Medulloblastoma // PLOS ONE / PLOS ONE EditorsPLoS, 2012. — ISSN 1932-6203doi:10.1371/JOURNAL.PONE.0044798PMID:22984561
  21. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  22. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)

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