PABPC4
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Polyadenylate-binding protein 4 (PABPC4) is a protein that in humans is encoded by the PABPC4 gene.[1][2]
Function
Poly(A)-binding proteins (PABPs) bind to the poly(A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.[2]
Interactions
PABPC4 has been shown to interact with PHLDA1.[3]
References
Page Template:Reflist/styles.css has no content.
- ^ Page Module:Citation/CS1/styles.css has no content.Féral C, Mattéi MG, Pawlak A, Guellaën G (Nov 1999). "Chromosomal localization of three human poly(A)-binding protein genes and four related pseudogenes". Hum Genet. 105 (4): 347–53. doi:10.1007/s004399900148. PMC 1865476. PMID 10543404.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: PABPC4 poly(A) binding protein, cytoplasmic 4 (inducible form)".
- ^ Page Module:Citation/CS1/styles.css has no content.Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (May 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Page Module:Citation/CS1/styles.css has no content.Yang H, Duckett CS, Lindsten T (1996). "iPABP, an inducible poly(A)-binding protein detected in activated human T cells". Mol. Cell. Biol. 15 (12): 6770–6. doi:10.1128/mcb.15.12.6770. PMC 230930. PMID 8524242.
- Page Module:Citation/CS1/styles.css has no content.Houng AK, Maggini L, Clement CY, Reed GL (1997). "Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets". Eur. J. Biochem. 243 (1–2): 209–18. doi:10.1111/j.1432-1033.1997.0209a.x. PMID 9030741.
- Page Module:Citation/CS1/styles.css has no content.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Page Module:Citation/CS1/styles.css has no content.Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T (1999). "The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein". J. Biol. Chem. 274 (24): 16677–80. doi:10.1074/jbc.274.24.16677. PMID 10358005.
- Page Module:Citation/CS1/styles.css has no content.Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product". Cell. Signal. 13 (5): 345–52. doi:10.1016/S0898-6568(01)00141-3. PMID 11369516.
- Page Module:Citation/CS1/styles.css has no content.Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (2003). "Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins". Mol. Cell. Biol. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
- Page Module:Citation/CS1/styles.css has no content.Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
- Page Module:Citation/CS1/styles.css has no content.Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Page Module:Citation/CS1/styles.css has no content.Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, Droege A, Lindenberg KS, Knoblich M, Haenig C, Herbst M, Suopanki J, Scherzinger E, Abraham C, Bauer B, Hasenbank R, Fritzsche A, Ludewig AH, Büssow K, Buessow K, Coleman SH, Gutekunst CA, Landwehrmeyer BG, Lehrach H, Wanker EE (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
- Page Module:Citation/CS1/styles.css has no content.Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
- Page Module:Citation/CS1/styles.css has no content.Ong SE, Mittler G, Mann M (2005). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nat. Methods. 1 (2): 119–26. doi:10.1038/nmeth715. PMID 15782174. S2CID 6654604.
- Page Module:Citation/CS1/styles.css has no content.Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1) 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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