GSPT2
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Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Eukaryotic peptide chain release factor GTP-binding subunit ERF3B is an enzyme that in humans is encoded by the GSPT2 gene.[1][2]
GSPT2 is closely related to GSPT1 (MIM 139259), a GTP-binding protein that plays an essential role at the G1- to S-phase transition of the cell cycle in yeast and human cells. GSPT1 is a positive regulator of translational accuracy and, in a binary complex with eRF1 (MIM 600285), functions as a polypeptide chain release factor.[supplied by OMIM][2]
Interactions
GSPT2 has been shown to interact with PABPC1.[3]
References
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- ^ Page Module:Citation/CS1/styles.css has no content.Hansen LL, Jakobsen CG, Justesen J (Jan 2000). "Assignment of the human peptide chain release factor 3 (GSPT2) to Xp11.23→p11.21 and of the distal marker DXS1039 by radiation hybrid mapping". Cytogenet Cell Genet. 86 (3–4): 250–1. doi:10.1159/000015353. PMID 10575220. S2CID 44348876.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: GSPT2 G1 to S phase transition 2".
- ^ Page Module:Citation/CS1/styles.css has no content.Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T (Jun 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). UNITED STATES: 16677–80. doi:10.1074/jbc.274.24.16677. ISSN 0021-9258. PMID 10358005.
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- Page Module:Citation/CS1/styles.css has no content.Chauvin C, Salhi S, Le Goff C, et al. (2005). "Involvement of Human Release Factors eRF3a and eRF3b in Translation Termination and Regulation of the Termination Complex Formation". Mol. Cell. Biol. 25 (14): 5801–11. doi:10.1128/MCB.25.14.5801-5811.2005. PMC 1168810. PMID 15987998.
- Page Module:Citation/CS1/styles.css has no content.Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Page Module:Citation/CS1/styles.css has no content.Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Page Module:Citation/CS1/styles.css has no content.Le Goff C, Zemlyanko O, Moskalenko S, et al. (2003). "Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo". Genes Cells. 7 (10): 1043–57. doi:10.1046/j.1365-2443.2002.00585.x. PMID 12354098.
- Page Module:Citation/CS1/styles.css has no content.Hoshino S, Imai M, Kobayashi T, et al. (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.Hoshino S, Imai M, Mizutani M, et al. (1998). "Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1". J. Biol. Chem. 273 (35): 22254–9. doi:10.1074/jbc.273.35.22254. PMID 9712840.
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