ERF1_HUMAN
ID ERF1_HUMAN Reviewed; 437 AA.
AC P62495; B2R6B4; D3DQC1; P46055; Q5M7Z7; Q96CG1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=eRF1;
DE AltName: Full=Protein Cl1;
DE AltName: Full=TB3-1;
GN Name=ETF1; Synonyms=ERF1, RF1, SUP45L1;
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] (ISOFORM 1).
RX PubMed=1537561; DOI=10.1016/0378-1119(92)90655-9;
RA Grenett H.E., Fuller G.M., Bounelis P.;
RT "Identification of a human cDNA with high homology to yeast omnipotent
RT suppressor 45.";
RL Gene 110:239-243(1992).
RN [2]
RP SEQUENCE REVISION, AND FUNCTION.
RX PubMed=7990965; DOI=10.1038/372701a0;
RA Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G.,
RA Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L.;
RT "A highly conserved eukaryotic protein family possessing properties of
RT polypeptide chain release factor.";
RL Nature 372:701-703(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9003791; DOI=10.1002/j.1460-2075.1996.tb01107.x;
RA Andjelkovic N., Zolnierowicz S., van Hoof C., Goris J., Hemmings B.A.;
RT "The catalytic subunit of protein phosphatase 2A associates with the
RT translation termination factor eRF1.";
RL EMBO J. 15:7156-7167(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10413110; DOI=10.1016/s0014-5793(99)00795-4;
RA Guenet L., Toutain B., Guilleret I., Chauvel B., Deaven L.L.,
RA Longmire J.L., Le Gall L.Y., David V., Le Treut A.;
RT "Human release factor eRF1: structural organisation of the unique
RT functional gene on chromosome 5 and of the three processed pseudogenes.";
RL FEBS Lett. 454:131-136(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Testis;
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 [10]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP METHYLATION AT GLN-185.
RX PubMed=18539146; DOI=10.1016/j.febslet.2008.05.045;
RA Figaro S., Scrima N., Buckingham R.H., Heurgue-Hamard V.;
RT "HemK2 protein, encoded on human chromosome 21, methylates translation
RT termination factor eRF1.";
RL FEBS Lett. 582:2352-2356(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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 [14]
RP METHYLATION AT GLN-185, AND MUTAGENESIS OF GLN-185.
RX PubMed=20606008; DOI=10.1128/mcb.00218-10;
RA Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R.,
RA Xu G.L.;
RT "Deficiency in a glutamine-specific methyltransferase for release factor
RT causes mouse embryonic lethality.";
RL Mol. Cell. Biol. 30:4245-4253(2010).
RN [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP FUNCTION, INTERACTION WITH JMJD4, SUBCELLULAR LOCATION, HYDROXYLATION AT
RP LYS-63, MUTAGENESIS OF LYS-63, AND MOTIF NIKS.
RX PubMed=24486019; DOI=10.1016/j.molcel.2013.12.028;
RA Feng T., Yamamoto A., Wilkins S.E., Sokolova E., Yates L.A., Muenzel M.,
RA Singh P., Hopkinson R.J., Fischer R., Cockman M.E., Shelley J.,
RA Trudgian D.C., Schoedel J., McCullagh J.S., Ge W., Kessler B.M.,
RA Gilbert R.J., Frolova L.Y., Alkalaeva E., Ratcliffe P.J., Schofield C.J.,
RA Coleman M.L.;
RT "Optimal translational termination requires C4 lysyl hydroxylation of
RT eRF1.";
RL Mol. Cell 53:645-654(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP METHYLATION AT GLN-185, AND MUTAGENESIS OF GLN-185.
RX PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA Kusevic D., Kudithipudi S., Jeltsch A.;
RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT identification of novel substrates.";
RL J. Biol. Chem. 291:6124-6133(2016).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-404, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP FUNCTION.
RX PubMed=30682371; DOI=10.1016/j.cell.2018.12.030;
RA Wang X., Xuan Y., Han Y., Ding X., Ye K., Yang F., Gao P., Goff S.P.,
RA Gao G.;
RT "Regulation of HIV-1 Gag-Pol Expression by Shiftless, an Inhibitor of
RT Programmed -1 Ribosomal Frameshifting.";
RL Cell 176:625.E14-635.E14(2019).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10676813; DOI=10.1016/s0092-8674(00)80667-4;
RA Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F.,
RA Hemmings B.A., Barford D.;
RT "The crystal structure of human eukaryotic release factor eRF1 -- mechanism
RT of stop codon recognition and peptidyl-tRNA hydrolysis.";
RL Cell 100:311-321(2000).
RN [25]
RP STRUCTURE BY NMR OF 140-277.
RX PubMed=17651434; DOI=10.1111/j.1742-4658.2007.05949.x;
RA Ivanova E.V., Kolosov P.M., Birdsall B., Kelly G., Pastore A.,
RA Kisselev L.L., Polshakov V.I.;
RT "Eukaryotic class 1 translation termination factor eRF1 -- the NMR
RT structure and dynamics of the middle domain involved in triggering
RT ribosome-dependent peptidyl-tRNA hydrolysis.";
RL FEBS J. 274:4223-4237(2007).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA
CC (PubMed:7990965, PubMed:24486019). Component of the transient SURF
CC complex which recruits UPF1 to stalled ribosomes in the context of
CC nonsense-mediated decay (NMD) of mRNAs containing premature stop
CC codons. Required for SHFL-mediated translation termination which
CC inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from
CC viruses and cellular genes (PubMed:30682371).
CC {ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:24486019,
CC ECO:0000269|PubMed:30682371, ECO:0000269|PubMed:7990965}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP
CC (PubMed:19417104). Component of the transient SURF (SMG1-UPF1-eRF1-
CC eRF3) complex (PubMed:19417104). Interacts with JMJD4
CC (PubMed:24486019). The ETF1-GSPT1 complex interacts with JMJD4
CC (PubMed:24486019). {ECO:0000269|PubMed:19417104,
CC ECO:0000269|PubMed:24486019}.
CC -!- INTERACTION:
CC P62495; P15170: GSPT1; NbExp=4; IntAct=EBI-750990, EBI-948993;
CC P62495; Q8IYD1: GSPT2; NbExp=2; IntAct=EBI-750990, EBI-3869637;
CC P62495; Q14145: KEAP1; NbExp=8; IntAct=EBI-750990, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24486019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62495-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62495-2; Sequence=VSP_056189;
CC -!- PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000269|PubMed:18539146,
CC ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}.
CC -!- PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational
CC termination efficiency. {ECO:0000269|PubMed:24486019}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; M75715; AAA36665.1; ALT_SEQ; mRNA.
DR EMBL; X81625; CAA57281.1; -; mRNA.
DR EMBL; U90176; AAB49726.1; -; mRNA.
DR EMBL; AF095901; AAD43966.1; -; Genomic_DNA.
DR EMBL; BT007374; AAP36038.1; -; mRNA.
DR EMBL; AK312510; BAG35411.1; -; mRNA.
DR EMBL; AC011385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62130.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62131.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62132.1; -; Genomic_DNA.
DR EMBL; BC088358; AAH88358.1; -; mRNA.
DR EMBL; BC014269; AAH14269.1; -; mRNA.
DR CCDS; CCDS4207.1; -. [P62495-1]
DR CCDS; CCDS75313.1; -. [P62495-2]
DR PIR; S50853; S50853.
DR RefSeq; NP_001243231.1; NM_001256302.1. [P62495-2]
DR RefSeq; NP_001278903.1; NM_001291974.1. [P62495-2]
DR RefSeq; NP_001278904.1; NM_001291975.1. [P62495-2]
DR RefSeq; NP_004721.1; NM_004730.3. [P62495-1]
DR RefSeq; XP_005271978.1; XM_005271921.1.
DR PDB; 1DT9; X-ray; 2.70 A; A=1-437.
DR PDB; 2HST; NMR; -; A=140-275.
DR PDB; 2KTU; NMR; -; A=276-437.
DR PDB; 2KTV; NMR; -; A=276-437.
DR PDB; 2LGT; NMR; -; A=1-142.
DR PDB; 2LLX; NMR; -; A=1-142.
DR PDB; 2MQ6; NMR; -; A=1-142.
DR PDB; 2MQ9; NMR; -; A=1-142.
DR PDB; 3E1Y; X-ray; 3.80 A; A/B/C/D=1-437.
DR PDB; 3J5Y; EM; 9.70 A; A=7-420.
DR PDB; 3JAG; EM; 3.65 A; ii=6-421.
DR PDB; 3JAH; EM; 3.45 A; ii=6-421.
DR PDB; 3JAI; EM; 3.65 A; ii=6-421.
DR PDB; 4D5N; EM; 9.00 A; A=5-437.
DR PDB; 4D61; EM; 9.00 A; h=5-437.
DR PDB; 5A8L; EM; 3.80 A; Q=7-437.
DR PDB; 5LZT; EM; 3.65 A; ii=1-437.
DR PDB; 5LZU; EM; 3.75 A; ii=1-437.
DR PDB; 5LZV; EM; 3.35 A; ii=1-437.
DR PDB; 6D90; EM; 3.20 A; jj=1-437.
DR PDB; 6IP8; EM; 3.90 A; zw=7-437.
DR PDB; 6XA1; EM; 2.80 A; j=11-421.
DR PDB; 6ZME; EM; 3.00 A; CH=1-437.
DR PDBsum; 1DT9; -.
DR PDBsum; 2HST; -.
DR PDBsum; 2KTU; -.
DR PDBsum; 2KTV; -.
DR PDBsum; 2LGT; -.
DR PDBsum; 2LLX; -.
DR PDBsum; 2MQ6; -.
DR PDBsum; 2MQ9; -.
DR PDBsum; 3E1Y; -.
DR PDBsum; 3J5Y; -.
DR PDBsum; 3JAG; -.
DR PDBsum; 3JAH; -.
DR PDBsum; 3JAI; -.
DR PDBsum; 4D5N; -.
DR PDBsum; 4D61; -.
DR PDBsum; 5A8L; -.
DR PDBsum; 5LZT; -.
DR PDBsum; 5LZU; -.
DR PDBsum; 5LZV; -.
DR PDBsum; 6D90; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6ZME; -.
DR AlphaFoldDB; P62495; -.
DR BMRB; P62495; -.
DR SMR; P62495; -.
DR BioGRID; 108408; 102.
DR ComplexPortal; CPX-2721; Translation release factor ERF1-ERF3 complex.
DR CORUM; P62495; -.
DR IntAct; P62495; 41.
DR MINT; P62495; -.
DR STRING; 9606.ENSP00000353741; -.
DR GlyGen; P62495; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62495; -.
DR MetOSite; P62495; -.
DR PhosphoSitePlus; P62495; -.
DR SwissPalm; P62495; -.
DR BioMuta; ETF1; -.
DR DMDM; 50402099; -.
DR EPD; P62495; -.
DR jPOST; P62495; -.
DR MassIVE; P62495; -.
DR MaxQB; P62495; -.
DR PaxDb; P62495; -.
DR PeptideAtlas; P62495; -.
DR PRIDE; P62495; -.
DR ProteomicsDB; 57403; -. [P62495-1]
DR ProteomicsDB; 76184; -.
DR Antibodypedia; 26674; 207 antibodies from 28 providers.
DR DNASU; 2107; -.
DR Ensembl; ENST00000360541.10; ENSP00000353741.5; ENSG00000120705.13. [P62495-1]
DR Ensembl; ENST00000499810.6; ENSP00000421288.1; ENSG00000120705.13. [P62495-2]
DR GeneID; 2107; -.
DR KEGG; hsa:2107; -.
DR MANE-Select; ENST00000360541.10; ENSP00000353741.5; NM_004730.4; NP_004721.1.
DR UCSC; uc003ldc.6; human. [P62495-1]
DR CTD; 2107; -.
DR DisGeNET; 2107; -.
DR GeneCards; ETF1; -.
DR HGNC; HGNC:3477; ETF1.
DR HPA; ENSG00000120705; Low tissue specificity.
DR MIM; 600285; gene.
DR neXtProt; NX_P62495; -.
DR OpenTargets; ENSG00000120705; -.
DR PharmGKB; PA27893; -.
DR VEuPathDB; HostDB:ENSG00000120705; -.
DR eggNOG; KOG0688; Eukaryota.
DR GeneTree; ENSGT00390000009004; -.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; P62495; -.
DR OMA; RCHGENT; -.
DR OrthoDB; 592406at2759; -.
DR PhylomeDB; P62495; -.
DR TreeFam; TF105672; -.
DR PathwayCommons; P62495; -.
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; P62495; -.
DR BioGRID-ORCS; 2107; 716 hits in 1074 CRISPR screens.
DR ChiTaRS; ETF1; human.
DR EvolutionaryTrace; P62495; -.
DR GeneWiki; Eukaryotic_release_factors; -.
DR GenomeRNAi; 2107; -.
DR Pharos; P62495; Tbio.
DR PRO; PR:P62495; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P62495; protein.
DR Bgee; ENSG00000120705; Expressed in islet of Langerhans and 204 other tissues.
DR ExpressionAtlas; P62495; baseline and differential.
DR Genevisible; P62495; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0018444; C:translation release factor complex; IPI:ComplexPortal.
DR GO; GO:0043022; F:ribosome binding; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IMP:UniProtKB.
DR GO; GO:0003747; F:translation release factor activity; IDA:MGI.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central.
DR GO; GO:0008079; F:translation termination factor activity; IMP:UniProtKB.
DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006479; P:protein methylation; IDA:MGI.
DR GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
DR GO; GO:0006415; P:translational termination; IDA:ComplexPortal.
DR DisProt; DP00310; -.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR Gene3D; 3.30.960.10; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR024049; eRF1_1_sf.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR PANTHER; PTHR10113; PTHR10113; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF55481; SSF55481; 1.
DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Hydroxylation; Isopeptide bond; Methylation;
KW Nonsense-mediated mRNA decay; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT CHAIN 2..437
FT /note="Eukaryotic peptide chain release factor subunit 1"
FT /id="PRO_0000143138"
FT MOTIF 61..64
FT /note="NIKS motif; plays an important role in translational
FT termination"
FT /evidence="ECO:0000305|PubMed:24486019"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT MOD_RES 63
FT /note="4-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:24486019"
FT MOD_RES 185
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:18539146,
FT ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_056189"
FT MUTAGEN 63
FT /note="K->A,R: Loss of hydroxylation."
FT /evidence="ECO:0000269|PubMed:24486019"
FT MUTAGEN 185
FT /note="Q->R,I,N: Abolishes methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:20606008,
FT ECO:0000269|PubMed:26797129"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2LLX"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2MQ6"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2HST"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 198..203
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 244..249
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 278..295
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:2KTU"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2KTU"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:2KTU"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:2KTU"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2KTU"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2KTU"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:2KTU"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1DT9"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:1DT9"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:1DT9"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2KTU"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2KTU"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2KTU"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:2KTU"
SQ SEQUENCE 437 AA; 49031 MW; CECC50D100E59D19 CRC64;
MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS
NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI
NTSLYLCDNK FHTEALTALL SDDSKFGFIV IDGSGALFGT LQGNTREVLH KFTVDLPKKH
GRGGQSALRF ARLRMEKRHN YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD
MFDQRLQSKV LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK
YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ EKDKSHFTDK
ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ
GMEYQGGDDE FFDLDDY
