TCAP (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[14][15]

TCAP
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген TCAP[d][1]
Молекуляр функция protein-macromolecule adaptor activity[d][2], transmembrane transporter binding[d][3], titin Z domain binding[d][4], titin binding[d][4][2][5], BMP binding[d][6], связывание с белками плазмы[d][7][8][9][…], FATZ binding[d][2], structural constituent of muscle[d][10][5], structural constituent of muscle[d][10][5][11], protein-macromolecule adaptor activity[d][2][11], titin binding[d][5][2][4][…] һәм titin Z domain binding[d][4][11]
Күзәнәк компоненты цитоплазма[12], цитозоль[d][12], I band[d][12][12], саркомер[d][12], Z discdkac[d][12][6][5] һәм Z discdkac[d][12][6][5][…]
Биологик процесс somitogenesis[d][12], response to muscle stretch[d][6], sarcomerogenesis[d][5], cardiac muscle contraction[d][13][2], adult heart development[d][5][12], otic vesicle formation[d][12], skeletal muscle contraction[d][5], cardiac muscle hypertrophy[d][2], cardiac muscle tissue morphogenesis[d][5], skeletal muscle thin filament assembly[d][5], detection of muscle stretch[d][13], cardiac myofibril assembly[d][5], cardiac muscle hypertrophy in response to stress[d][13], detection of mechanical stimulus[d][6], muscle filament sliding[d][12], sarcomere organization[d][6][5], skeletal muscle myosin thick filament assembly[d][5], protein-containing complex assembly[d][5], skeletal muscle contraction[d][5][11], skeletal muscle thin filament assembly[d][5][11], skeletal muscle myosin thick filament assembly[d][5][11], detection of muscle stretch[d][13][11], sarcomerogenesis[d][5][11], cardiac myofibril assembly[d][5][11], cardiac muscle tissue morphogenesis[d][5][11] һәм cardiac muscle contraction[d][2][13][11]
Изображение Gene Atlas

Искәрмәләр

үзгәртү
  1. 1,0 1,1 UniProt
  2. 2,0 2,1 2,2 2,3 2,4 2,5 2,6 2,7 Knöll R., Arimura T. Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy // J. Am. Coll. Cardiol. / V. F. CarullaElsevier BV, American College of Cardiology, 2004. — ISSN 0735-1097; 1558-3597doi:10.1016/J.JACC.2004.08.058PMID:15582318
  3. T Furukawa, Y Ono, H Tsuchiya et al. Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system // Journal of Molecular Biology / P. WrightElsevier BV, 2001. — ISSN 0022-2836; 1089-8638doi:10.1006/JMBI.2001.5053PMID:11697903
  4. 4,0 4,1 4,2 4,3 Arimura T. Titin mutations as the molecular basis for dilated cardiomyopathy // Biochem. Biophys. Res. Commun.Academic Press, Elsevier BV, 2002. — ISSN 0006-291X; 1090-2104doi:10.1006/BBRC.2002.6448PMID:11846417
  5. 5,00 5,01 5,02 5,03 5,04 5,05 5,06 5,07 5,08 5,09 5,10 5,11 5,12 5,13 5,14 5,15 5,16 5,17 5,18 5,19 5,20 B Herrmann, H Sorimachi The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity // J. Cell Biol. / J. NunnariRockefeller University Press, 1998. — 15 p. — ISSN 0021-9525; 1540-8140doi:10.1083/JCB.143.4.1013PMID:9817758
  6. 6,0 6,1 6,2 6,3 6,4 6,5 Arimura T. Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy // American Journal of Physiology: Heart and circulatory physiology — 2007. — ISSN 0363-6135; 1522-1539doi:10.1152/AJPHEART.00311.2007PMID:17921333
  7. Frey N., Olson E. N. Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2002. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M200712200PMID:11842093
  8. Pallavicini A., Valle G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle // 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.M007493200PMID:10984498
  9. Giacomello E., Barone V., Rossi D. et al. Molecular interactions with obscurin are involved in the localization of muscle-specific small ankyrin1 isoforms to subcompartments of the sarcoplasmic reticulum // Exp. Cell. Res.Academic Press, Elsevier BV, 2006. — ISSN 0014-4827; 1090-2422doi:10.1016/J.YEXCR.2006.07.027PMID:16962094
  10. 10,0 10,1 S. Toppo, A. Pallavicini, N. Tiso Telethonin, a novel sarcomeric protein of heart and skeletal muscle // FEBS LettersElsevier BV, 1997. — ISSN 0014-5793; 1873-3468doi:10.1016/S0014-5793(97)01108-3PMID:9350988
  11. 11,00 11,01 11,02 11,03 11,04 11,05 11,06 11,07 11,08 11,09 11,10 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform.OUP, 2011. — ISSN 1467-5463; 1477-4054doi:10.1093/BIB/BBR042PMID:21873635
  12. 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 12,10 GOA
  13. 13,0 13,1 13,2 13,3 13,4 Bang M., Knöll R., Schork N. J. The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy // CellCell Press, Elsevier BV, 2002. — ISSN 0092-8674; 1097-4172doi:10.1016/S0092-8674(02)01226-6PMID:12507422
  14. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  15. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

үзгәртү
  • 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.)