ID ERF3B_HUMAN Reviewed; 628 AA. AC Q8IYD1; Q9H909; Q9NVY0; Q9NY44; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 27-MAR-2024, entry version 176. DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit ERF3B; DE Short=Eukaryotic peptide chain release factor subunit 3b; DE Short=eRF3b; DE EC=3.6.5.- {ECO:0000305|PubMed:15987998}; DE AltName: Full=G1 to S phase transition protein 2 homolog; GN Name=GSPT2; Synonyms=ERF3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=11524954; RA Jakobsen C.G., Segaard T.M., Jean-Jean O., Frolova L., Justesen J.; RT "Identification of a novel termination release factor eRF3b expressing the RT eRF3 activity in vitro and in vivo."; RL Mol. Biol. (Mosk.) 35:672-681(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-23. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15987998; DOI=10.1128/mcb.25.14.5801-5811.2005; RA Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., Jean-Jean O.; RT "Involvement of human release factors eRF3a and eRF3b in translation RT termination and regulation of the termination complex formation."; RL Mol. Cell. Biol. 25:5801-5811(2005). RN [7] RP TISSUE SPECIFICITY. RX PubMed=16721809; DOI=10.1002/ijc.22027; RA Groene J., Mansmann U., Meister R., Staub E., Roepcke S., Heinze M., RA Klaman I., Bruemmendorf T., Hermann K., Loddenkemper C., Pilarsky C., RA Mann B., Adams H.-P., Buhr H.J., Rosenthal A.; RT "Transcriptional census of 36 microdissected colorectal cancers yields a RT gene signature to distinguish UICC II and III."; RL Int. J. Cancer 119:1829-1836(2006). RN [8] RP FUNCTION. RX PubMed=17562865; DOI=10.1128/mcb.00035-07; RA Chauvin C., Salhi S., Jean-Jean O.; RT "Human eukaryotic release factor 3a depletion causes cell cycle arrest at RT G1 phase through inhibition of the mTOR pathway."; RL Mol. Cell. Biol. 27:5619-5629(2007). RN [9] RP INTERACTION WITH UPF1 AND PABPC1, AND MUTAGENESIS OF LEU-52; ASN-55; ALA-56 RP AND PHE-59. RX PubMed=18447585; DOI=10.1371/journal.pbio.0060111; RA Singh G., Rebbapragada I., Lykke-Andersen J.; RT "A competition between stimulators and antagonists of Upf complex RT recruitment governs human nonsense-mediated mRNA decay."; RL PLoS Biol. 6:E111-E111(2008). RN [10] RP IDENTIFICATION IN THE SURF COMPLEX, AND FUNCTION. RX PubMed=19417104; DOI=10.1101/gad.1767209; RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., RA Anderson P., Ohno S.; RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA RT decay."; RL Genes Dev. 23:1091-1105(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] {ECO:0007744|PDB:3KUJ} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 59-73. RX PubMed=20418951; DOI=10.1371/journal.pone.0010169; RA Kozlov G., Gehring K.; RT "Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding RT protein."; RL PLoS ONE 5:E10169-E10169(2010). CC -!- FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a CC ternary complex that mediates translation termination in response to CC the termination codons UAA, UAG and UGA (PubMed:15987998, CC PubMed:11524954, PubMed:17562865). GSPT2/ERF3B mediates ETF1/ERF1 CC delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop CC codon in the ribosomal A-site (PubMed:15987998). GTP hydrolysis by CC GSPT2/ERF3B induces a conformational change that leads to its CC dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site CC (PubMed:15987998). Component of the transient SURF complex which CC recruits UPF1 to stalled ribosomes in the context of nonsense-mediated CC decay (NMD) of mRNAs containing premature stop codons CC (PubMed:19417104). {ECO:0000269|PubMed:11524954, CC ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:17562865, CC ECO:0000269|PubMed:19417104}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000305|PubMed:15987998}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000305|PubMed:15987998}; CC -!- SUBUNIT: Component of the eRF1-eRF3-GTP ternary complex, composed of CC ETF1/ERF1 and ERF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP CC (PubMed:15987998). Component of the transient SURF (SMG1-UPF1-eRF1- CC eRF3) complex (PubMed:19417104). Interacts with UPF1 and PABPC1 CC (PubMed:18447585). {ECO:0000269|PubMed:15987998, CC ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19417104}. CC -!- INTERACTION: CC Q8IYD1; P62495: ETF1; NbExp=2; IntAct=EBI-3869637, EBI-750990; CC Q8IYD1; P11940: PABPC1; NbExp=8; IntAct=EBI-3869637, EBI-81531; CC Q8IYD1; Q92900: UPF1; NbExp=3; IntAct=EBI-3869637, EBI-373471; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Highly expressed in IUCC stage II colorectal cancer CC (CRC). {ECO:0000269|PubMed:16721809}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. ERF3 subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU01059}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ251548; CAB91089.1; -; mRNA. DR EMBL; AK001303; BAA91612.1; -; mRNA. DR EMBL; AL929101; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471230; EAW62898.1; -; Genomic_DNA. DR EMBL; BC036077; AAH36077.1; -; mRNA. DR CCDS; CCDS14336.1; -. DR RefSeq; NP_060564.2; NM_018094.4. DR PDB; 3KUJ; X-ray; 1.40 A; B=59-73. DR PDBsum; 3KUJ; -. DR AlphaFoldDB; Q8IYD1; -. DR BMRB; Q8IYD1; -. DR EMDB; EMD-2813; -. DR SMR; Q8IYD1; -. DR BioGRID; 117221; 107. DR CORUM; Q8IYD1; -. DR IntAct; Q8IYD1; 36. DR STRING; 9606.ENSP00000341247; -. DR ChEMBL; CHEMBL4105974; -. DR GlyGen; Q8IYD1; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8IYD1; -. DR PhosphoSitePlus; Q8IYD1; -. DR SwissPalm; Q8IYD1; -. DR BioMuta; GSPT2; -. DR DMDM; 182647413; -. DR EPD; Q8IYD1; -. DR jPOST; Q8IYD1; -. DR MassIVE; Q8IYD1; -. DR MaxQB; Q8IYD1; -. DR PaxDb; 9606-ENSP00000341247; -. DR PeptideAtlas; Q8IYD1; -. DR ProteomicsDB; 71156; -. DR Pumba; Q8IYD1; -. DR Antibodypedia; 26328; 218 antibodies from 24 providers. DR DNASU; 23708; -. DR Ensembl; ENST00000340438.6; ENSP00000341247.4; ENSG00000189369.9. DR GeneID; 23708; -. DR KEGG; hsa:23708; -. DR MANE-Select; ENST00000340438.6; ENSP00000341247.4; NM_018094.5; NP_060564.2. DR UCSC; uc004dpl.4; human. DR AGR; HGNC:4622; -. DR CTD; 23708; -. DR DisGeNET; 23708; -. DR GeneCards; GSPT2; -. DR HGNC; HGNC:4622; GSPT2. DR HPA; ENSG00000189369; Low tissue specificity. DR MalaCards; GSPT2; -. DR MIM; 300418; gene. DR neXtProt; NX_Q8IYD1; -. DR OpenTargets; ENSG00000189369; -. DR PharmGKB; PA29013; -. DR VEuPathDB; HostDB:ENSG00000189369; -. DR eggNOG; KOG0459; Eukaryota. DR GeneTree; ENSGT00940000163245; -. DR HOGENOM; CLU_007265_3_8_1; -. DR InParanoid; Q8IYD1; -. DR OMA; NDETCTG; -. DR OrthoDB; 5477300at2759; -. DR PhylomeDB; Q8IYD1; -. DR TreeFam; TF300566; -. DR PathwayCommons; Q8IYD1; -. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q8IYD1; -. DR BioGRID-ORCS; 23708; 13 hits in 783 CRISPR screens. DR ChiTaRS; GSPT2; human. DR EvolutionaryTrace; Q8IYD1; -. DR GeneWiki; GSPT2; -. DR GenomeRNAi; 23708; -. DR Pharos; Q8IYD1; Tchem. DR PRO; PR:Q8IYD1; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8IYD1; Protein. DR Bgee; ENSG00000189369; Expressed in sperm and 193 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0018444; C:translation release factor complex; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003747; F:translation release factor activity; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR GO; GO:0006415; P:translational termination; IDA:UniProtKB. DR CDD; cd01883; EF1_alpha; 1. DR CDD; cd03704; eRF3_C_III; 1. DR CDD; cd04089; eRF3_II; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR IDEAL; IID00573; -. DR InterPro; IPR009818; Ataxin-2_C. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR PANTHER; PTHR23115:SF119; EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT ERF3B; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR Pfam; PF07145; PAM2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. DR Genevisible; Q8IYD1; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cytoplasm; GTP-binding; Hydrolase; KW Nonsense-mediated mRNA decay; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..628 FT /note="Eukaryotic peptide chain release factor GTP-binding FT subunit ERF3B" FT /id="PRO_0000327256" FT DOMAIN 201..425 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 72..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 146..195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 210..217 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 266..270 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 287..290 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 349..352 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 391..393 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT COMPBIAS 81..95 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 176..190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 213..218 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT BINDING 349..352 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT BINDING 391..393 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT VARIANT 23 FT /note="P -> T (in dbSNP:rs17855593)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_042431" FT MUTAGEN 52 FT /note="L->K: Impairs interaction with UPF1 and PABPC1; when FT associated with A-55, K-56 and A-59." FT /evidence="ECO:0000269|PubMed:18447585" FT MUTAGEN 55 FT /note="N->A: Impairs interaction with UPF1 and PABPC1; when FT associated with K-52, K-56 and A-59." FT /evidence="ECO:0000269|PubMed:18447585" FT MUTAGEN 56 FT /note="A->K: Impairs interaction with UPF1 and PABPC1; when FT associated with K52, A-55, and A-59." FT /evidence="ECO:0000269|PubMed:18447585" FT MUTAGEN 59 FT /note="F->A: Impairs interaction with UPF1 and PABPC1; when FT associated with K-52, A-55 and K-56." FT /evidence="ECO:0000269|PubMed:18447585" FT CONFLICT 25 FT /note="S -> L (in Ref. 2; BAA91612)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="V -> A (in Ref. 2; BAA91612)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="S -> G (in Ref. 2; BAA91612)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="P -> H (in Ref. 5; AAH36077)" FT /evidence="ECO:0000305" FT CONFLICT 625 FT /note="P -> Q (in Ref. 5; AAH36077)" FT /evidence="ECO:0000305" SQ SEQUENCE 628 AA; 68883 MW; 909FCDEF04EC89C9 CRC64; MDSGSSSSDS APDCWDQVDM ESPGSAPSGD GVSSAVAEAQ REPLSSAFSR KLNVNAKPFV PNVHAAEFVP SFLRGPTQPP TLPAGSGSND ETCTGAGYPQ GKRMGRGAPV EPSREEPLVS LEGSNSAVTM ELSEPVVENG EVEMALEESW EHSKEVSEAE PGGGSSGDSG PPEESGQEMM EEKEEIRKSK SVIVPSGAPK KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER EAKEKNRETW YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK MDDPTVNWSI ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANIKE QSDFCPWYTG LPFIPYLDNL PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT ETDFVAPGEN LKIRLKGIEE EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN AVLHIHTCIE EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF PQMGRFTLRD EGKTIAIGKV LKLVPEKD //