Эчтәлеккә күчү

SLC4A1

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/SLC4A1 latin yazuında])
SLC4A1
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген SLC4A1[d][1]
Молекуляр функция гомодимеризация белка[d][2], protein-membrane adaptor activity[d][3], chloride transmembrane transporter activity[d][4][4], transporter activity[d][5], anion transmembrane transporter activity[d][6][4], bicarbonate transmembrane transporter activity[d][7], связывание с белками плазмы[d][8][9][10][…], ankyrin binding[d][2], inorganic anion exchanger activity[d][5][5][11], sodium:bicarbonate symporter activity[d][5], inorganic anion exchanger activity[d][4][7], bicarbonate transmembrane transporter activity[d][4][7], hemoglobin binding[d][4] һәм ankyrin binding[d][2][4]
Күзәнәк компоненты мембрана өлеше[d][12][4][4], blood microparticle[d][13], мембрана[d][4][4][4], cortical cytoskeleton[d][4][8], күзәнәк мембранасы[d][4][4][4], күзәнәк мембранасы өлеше[d][14][11][15], basolateral plasma membrane[d][4][4][16][…], экзосома[d][17], Z discdkac[d][4], күзәнәк мембранасы өлеше[d][6][7][2][…], экзосома[d][18], blood microparticle[d][19] һәм cytoplasmic side of plasma membrane[d][4]
Биологик процесс anion transport[d][6][4][16], bicarbonate transport[d][5][11], cellular ion homeostasis[d][20], chloride transport[d][4][4], ion transport[d][4], regulation of intracellular pH[d][21], anion transmembrane transport[d][4], chloride transmembrane transport[d][4], sodium ion transmembrane transport[d][5], перенос[d][5][5], bicarbonate transport[d][4][7][21], гликолиз[d][4], cвёртывание крови[d][4], bicarbonate transport[d][4][4][7][…], plasma membrane phospholipid scrambling[d][4], negative regulation of urine volume[d][4], pH elevation[d][4], erythrocyte development[d][4] һәм protein localization to plasma membrane[d][4]
Изображение Gene Atlas

SLC4A1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[22][23]

  1. 1,0 1,1 UniProt
  2. 2,0 2,1 2,2 2,3 V. Bennett, Stenbuck P. J. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes // Nature / M. SkipperNPG, Springer Science+Business Media, 1979. — ISSN 1476-4687; 0028-0836doi:10.1038/280468A0PMID:379653
  3. Y Matsuoka, X Li, V Bennett Adducin: structure, function and regulation // Cell Mol Life SciBirkhäuser, Springer Science+Business Media, 2000. — ISSN 1420-9071; 1420-682Xdoi:10.1007/PL00000731PMID:10950304
  4. 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 4,16 4,17 4,18 4,19 4,20 4,21 4,22 4,23 4,24 4,25 4,26 4,27 4,28 4,29 4,30 4,31 4,32 4,33 4,34 4,35 GOA
  5. 5,0 5,1 5,2 5,3 5,4 5,5 5,6 5,7 GOA
  6. 6,0 6,1 6,2 L Hsu, M Morrison A new variant of the anion transport protein in human erythrocytes // Biochemistry / A. SchepartzACS, 1985. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI00334A003PMID:4027230
  7. 7,0 7,1 7,2 7,3 7,4 7,5 Calmettes C., Casey J. A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — 13 p. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M113.511865PMID:24121512
  8. 8,0 8,1 Mohandas N., An X., Baines A. J. et al. Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins // Biochemistry / A. SchepartzACS, 2006. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI060015VPMID:16669616
  9. Nuiplot N., Junking M., Duangtum N. et al. Transmembrane protein 139 (TMEM139) interacts with human kidney isoform of anion exchanger 1 (kAE1) // Biochem. Biophys. Res. Commun.Academic Press, Elsevier BV, 2015. — ISSN 0006-291X; 1090-2104doi:10.1016/J.BBRC.2015.05.128PMID:26049106
  10. Zhou A., Fiona E Karet Frankl Physical and functional links between anion exchanger-1 and sodium pump // Journal of the American Society of Nephrology / J. BriggsAmerican Society of Nephrology, 2015. — ISSN 1046-6673; 1533-3450doi:10.1681/ASN.2013101063PMID:25012180
  11. 11,0 11,1 11,2 Calmettes C., Casey J. A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — 13 p. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M113.511865PMID:24121512
  12. D. Kang, K. Okubo, N. Hamasaki et al. A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1992. — ISSN 0021-9258; 1083-351X; 1067-8816PMID:1527044
  13. Bastos-Amador P., González E., Conde-Vancells J. et al. Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability // Journal of ProteomicsElsevier BV, 2012. — ISSN 1874-3919; 0165-022Xdoi:10.1016/J.JPROT.2012.03.054PMID:22516433
  14. L Hsu, M Morrison A new variant of the anion transport protein in human erythrocytes // Biochemistry / A. SchepartzACS, 1985. — ISSN 0006-2960; 1520-4995; 1943-295Xdoi:10.1021/BI00334A003PMID:4027230
  15. V. Bennett, Stenbuck P. J. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes // Nature / M. SkipperNPG, Springer Science+Business Media, 1979. — ISSN 1476-4687; 0028-0836doi:10.1038/280468A0PMID:379653
  16. 16,0 16,1 Karet F. E., Reimann F. A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells // J. Biol. Chem. / L. M. GieraschBaltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816doi:10.1074/JBC.M400188200PMID:14734552
  17. Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. BriggsAmerican Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450doi:10.1681/ASN.2008040406PMID:19056867
  18. Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. BriggsAmerican Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450doi:10.1681/ASN.2008040406PMID:19056867
  19. Bastos-Amador P., González E., Conde-Vancells J. et al. Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability // Journal of ProteomicsElsevier BV, 2012. — ISSN 1874-3919; 0165-022Xdoi:10.1016/J.JPROT.2012.03.054PMID:22516433
  20. Southgate C. D., Chishti A. H., B Mitchell et al. Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton // Nature Genetics / M. Axton, T. FaialNPG, 1996. — ISSN 1061-4036; 1546-1718doi:10.1038/NG1096-227PMID:8841202
  21. 21,0 21,1 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
  22. HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  23. UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
  • 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.)