ERF3B_HUMAN
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 03-AUG-2022, entry version 167.
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 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.
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.
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).
CC -!- FUNCTION: Involved in translation termination in response to the
CC termination codons UAA, UAG and UGA. May play a role as a potent
CC stimulator of the release factor activity of ETF1. Exhibits GTPase
CC activity, which is ribosome- and ETF1-dependent. May play a role in
CC cell cycle progression. 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 {ECO:0000269|PubMed:11524954, ECO:0000269|PubMed:15987998,
CC ECO:0000269|PubMed:17562865}.
CC -!- SUBUNIT: Interacts with ETF1 (By similarity). Component of the
CC transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with UPF1 and
CC PABPC1. {ECO:0000250, ECO:0000269|PubMed:18447585,
CC 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}.
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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 SMR; Q8IYD1; -.
DR BioGRID; 117221; 92.
DR CORUM; Q8IYD1; -.
DR IntAct; Q8IYD1; 35.
DR STRING; 9606.ENSP00000341247; -.
DR ChEMBL; CHEMBL4105974; -.
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; Q8IYD1; -.
DR PeptideAtlas; Q8IYD1; -.
DR PRIDE; Q8IYD1; -.
DR ProteomicsDB; 71156; -.
DR Antibodypedia; 26328; 195 antibodies from 25 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 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; ESWEHSK; -.
DR OrthoDB; 1150082at2759; -.
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; 12 hits in 707 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 192 other tissues.
DR Genevisible; Q8IYD1; HS.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003747; F:translation release factor activity; IBA:GO_Central.
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 Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00573; -.
DR InterPro; IPR009818; Ataxin-2_C.
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 Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF07145; PAM2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cytoplasm; GTP-binding;
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 210..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 287..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 349..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
FT SITE 350
FT /note="Interacts with GTP/GDP"
FT /evidence="ECO:0000250"
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
