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Database: UniProt
Entry: P62495
LinkDB: P62495
Original site: P62495 
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   29-SEP-2021, entry version 170.
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=3; 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   BMRB; P62495; -.
DR   SMR; P62495; -.
DR   BioGRID; 108408; 76.
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; 198 antibodies.
DR   DNASU; 2107; -.
DR   Ensembl; ENST00000360541; ENSP00000353741; ENSG00000120705. [P62495-1]
DR   Ensembl; ENST00000499810; ENSP00000421288; ENSG00000120705. [P62495-2]
DR   GeneID; 2107; -.
DR   KEGG; hsa:2107; -.
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; GPGTEKM; -.
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   BioGRID-ORCS; 2107; 707 hits in 1011 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 bone marrow and 248 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; IBA:GO_Central.
DR   GO; GO:0018444; C:translation release factor complex; IBA:GO_Central.
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:MGI.
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
//
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