GSPT2

G1 to S phase transition 2
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3KUJ​
Identifiers
Symbols	GSPT2 ; ERF3B; GST2
External IDs	OMIM: 300418 MGI: 1316727 HomoloGene: 99786 GeneCards: GSPT2 Gene
Gene ontology Molecular function • translation release factor activity • GTPase activity • protein binding • GTP binding • poly(A) RNA binding Cellular component • cytosol • translation release factor complex Biological process • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • cytoplasmic translational termination • translation • translational termination • cell cycle • gene expression • cellular protein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23708	14853
Ensembl	ENSG00000189369	ENSMUSG00000071723
UniProt	Q8IYD1	Q149F3
RefSeq (mRNA)	NM_018094	NM_008179
RefSeq (protein)	NP_060564	NP_032205
Location (UCSC)	Chr X: 51.74 – 51.75 Mb	Chr X: 94.64 – 94.64 Mb
PubMed search

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

1. 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.
2. "Entrez Gene: GSPT2 G1 to S phase transition 2".
3. 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. (UNITED STATES) 274 (24): 16677–80. doi:10.1074/jbc.274.24.16677. ISSN 0021-9258. PMID 10358005.

Further reading

• 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. doi:10.1038/nature04209. PMID 16189514.
• 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.
• 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.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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.
• 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.
• 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.