PABPC4

PABPC4
Identifiers
Aliases	PABPC4 , APP-1, APP1, PABP4, iPABP, poly(A) binding protein cytoplasmic 4
External IDs	OMIM: 603407; MGI: 2385206; HomoloGene: 37855; GeneCards: PABPC4; OMA:PABPC4 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p34.3 Start 39,560,709 bp [1] End 39,576,790 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D2.2 Start 123,156,144 bp [2] End 123,192,718 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas gastrocnemius muscle muscle of thigh secondary oocyte glutes skeletal muscle tissue vastus lateralis muscle body of tongue triceps brachii muscle left ovary Top expressed in bone marrow epiblast muscle of thigh skeletal muscle tissue tail of embryo quadriceps femoris muscle morula yolk sac genital tubercle primary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function poly(C) RNA binding protein binding poly(A) binding nucleic acid binding poly(U) RNA binding RNA binding mRNA binding mRNA 3'-UTR binding Cellular component cytoplasmic stress granule nucleus cytoplasm cytosol ribonucleoprotein complex Biological process RNA processing RNA catabolic process blood coagulation protein biosynthesis regulation of mRNA stability myeloid cell development Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8761 230721 Ensembl ENSG00000090621 ENSMUSG00000011257 UniProt Q13310 n/a RefSeq (mRNA) NM_003819 NM_001135653 NM_001135654 NM_130881 NM_148917 NM_001356377 RefSeq (protein) NP_001129125 NP_001129126 NP_003810 n/a Location (UCSC) Chr 1: 39.56 – 39.58 Mb Chr 4: 123.16 – 123.19 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Polyadenylate-binding protein 4 (PABPC4) is a protein that in humans is encoded by the PABPC4 gene. ^{[5] [6]}

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. ^[6]

Interactions

PABPC4 has been shown to interact with PHLDA1. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000090621 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000011257 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: PABPC4 poly(A) binding protein, cytoplasmic 4 (inducible form)".
7. 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

• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.