PABPC4

{{Short description|Protein-coding gene in the species Homo sapiens}}

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Polyadenylate-binding protein 4 (PABPC4) is a protein that in humans is encoded by the PABPC4 gene.{{cite journal | vauthors = Féral C, Mattéi MG, Pawlak A, Guellaën G | title = Chromosomal localization of three human poly(A)-binding protein genes and four related pseudogenes | journal = Hum Genet | volume = 105 | issue = 4 | pages = 347–53 | date = Nov 1999 | pmid = 10543404 | pmc = 1865476 | doi = 10.1007/s004399900148 }}{{cite web | title = Entrez Gene: PABPC4 poly(A) binding protein, cytoplasmic 4 (inducible form)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8761}}

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.

Interactions

PABPC4 has been shown to interact with PHLDA1.{{cite journal | vauthors = Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D | title = Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product | journal = Cell. Signal. | volume = 13 | issue = 5 | pages = 345–52 | date = May 2001 | pmid = 11369516 | doi = 10.1016/S0898-6568(01)00141-3 }}

References

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Further reading

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  • {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
  • {{cite journal | vauthors = Yang H, Duckett CS, Lindsten T | title = iPABP, an inducible poly(A)-binding protein detected in activated human T cells | journal = Mol. Cell. Biol. | volume = 15 | issue = 12 | pages = 6770–6 | year = 1996 | doi = 10.1128/mcb.15.12.6770 | pmid = 8524242 | pmc = 230930 }}
  • {{cite journal | vauthors = Houng AK, Maggini L, Clement CY, Reed GL | title = Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets | journal = Eur. J. Biochem. | volume = 243 | issue = 1–2 | pages = 209–18 | year = 1997 | pmid = 9030741 | doi = 10.1111/j.1432-1033.1997.0209a.x | doi-access = free }}
  • {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal | vauthors = Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T | title = 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 | journal = J. Biol. Chem. | volume = 274 | issue = 24 | pages = 16677–80 | year = 1999 | pmid = 10358005 | doi = 10.1074/jbc.274.24.16677 | doi-access = free }}
  • {{cite journal | vauthors = Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D | title = Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product | journal = Cell. Signal. | volume = 13 | issue = 5 | pages = 345–52 | year = 2001 | pmid = 11369516 | doi = 10.1016/S0898-6568(01)00141-3 }}
  • {{cite journal | vauthors = Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG | title = Regulation of Alternative Splicing by SRrp86 and Its Interacting Proteins | journal = Mol. Cell. Biol. | volume = 23 | issue = 21 | pages = 7437–47 | year = 2003 | pmid = 14559993 | pmc = 207616 | doi = 10.1128/MCB.23.21.7437-7447.2003 }}
  • {{cite journal | vauthors = Lehner B, Sanderson CM | title = A Protein Interaction Framework for Human mRNA Degradation | journal = Genome Res. | volume = 14 | issue = 7 | pages = 1315–23 | year = 2004 | pmid = 15231747 | pmc = 442147 | doi = 10.1101/gr.2122004 }}
  • {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional Proteomics Mapping of a Human Signaling Pathway | journal = Genome Res. | volume = 14 | issue = 7 | pages = 1324–32 | year = 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
  • {{cite journal |author23-link=Bernhard Landwehrmeyer| vauthors = 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 | title = A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease | journal = Mol. Cell | volume = 15 | issue = 6 | pages = 853–65 | year = 2004 | pmid = 15383276 | doi = 10.1016/j.molcel.2004.09.016 | doi-access = free }}
  • {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nat. Biotechnol. | volume = 23 | issue = 1 | pages = 94–101 | year = 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 | s2cid = 7200157 }}
  • {{cite journal | vauthors = Ong SE, Mittler G, Mann M | title = Identifying and quantifying in vivo methylation sites by heavy methyl SILAC | journal = Nat. Methods | volume = 1 | issue = 2 | pages = 119–26 | year = 2005 | pmid = 15782174 | doi = 10.1038/nmeth715 | s2cid = 6654604 }}
  • {{cite journal | vauthors = 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 | title = Large-scale mapping of human protein–protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}

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{{RNA-binding proteins}}

Category:Genes mutated in mice