ID PELO_HUMAN Reviewed; 385 AA. AC Q9BRX2; Q9GZS6; Q9Y306; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 2. DT 28-JAN-2026, entry version 186. DE RecName: Full=Protein pelota homolog {ECO:0000303|PubMed:11060452}; DE Short=hPelota {ECO:0000303|PubMed:27543824}; DE AltName: Full=Protein Dom34 homolog {ECO:0000303|PubMed:23667253}; GN Name=PELO {ECO:0000303|PubMed:11060452, ECO:0000312|HGNC:HGNC:8829}; GN ORFNames=CGI-17 {ECO:0000303|PubMed:10810093}; 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], TISSUE SPECIFICITY, AND VARIANT MET-221. RC TISSUE=Testis; RX PubMed=11060452; DOI=10.1159/000015667; RA Shamsadin R., Adham I.M., von Beust G., Engel W.; RT "Molecular cloning, expression and chromosome location of the human pelota RT gene PELO."; RL Cytogenet. Cell Genet. 90:75-78(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-221. RA Shamsadin R.; RT "Gene structure prediction and evidence of alternative splicing in the RT human pelota gene."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221. RC TISSUE=Brain, Skin, and Uterus; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-381, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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 [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21448132; DOI=10.1038/emboj.2011.93; RA Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V.; RT "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes RT and stalled elongation complexes."; RL EMBO J. 30:1804-1817(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP FUNCTION. RX PubMed=23667253; DOI=10.1074/jbc.m112.448977; RA Saito S., Hosoda N., Hoshino S.; RT "The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in RT mammalian cells."; RL J. Biol. Chem. 288:17832-17843(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY RP 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 [15] RP FUNCTION, AND MUTAGENESIS OF LYS-2 AND ARG-45. RX PubMed=27543824; DOI=10.1002/1873-3468.12366; RA Ikeuchi K., Yazaki E., Kudo K., Inada T.; RT "Conserved functions of human Pelota in mRNA quality control of nonstop RT mRNA."; RL FEBS Lett. 590:3254-3263(2016). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-162, AND IDENTIFICATION BY MASS RP 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 [17] RP FUNCTION, AND INTERACTION WITH PINK1; ABCE1 AND CNOT4. RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007; RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T., RA Montgomery S., Lu B.; RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links RT Co-translational Quality Control to PINK1-Directed Mitophagy."; RL Cell Metab. 28:130-144.e7(2018). RN [18] RP FUNCTION. RX PubMed=32006463; DOI=10.1016/j.molcel.2020.01.011; RA Zinoviev A., Ayupov R.K., Abaeva I.S., Hellen C.U.T., Pestova T.V.; RT "Extraction of mRNA from stalled ribosomes by the Ski complex."; RL Mol. Cell 77:1340-1349(2020). RN [19] RP STRUCTURE BY NMR OF 261-371. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C-terminal domain of the human pelota homolog RT (CGI-17)."; RL Submitted (NOV-2005) to the PDB data bank. RN [20] {ECO:0007744|PDB:5LZW, ECO:0007744|PDB:5LZX, ECO:0007744|PDB:5LZY, ECO:0007744|PDB:5LZZ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.47 ANGSTROMS) IN COMPLEX WITH HBS1L AND RP STALLED RIBOSOME, FUNCTION, AND IDENTIFICATION IN THE PELOTA-HBS1L COMPLEX. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). CC -!- FUNCTION: Component of the Pelota-HBS1L complex, a complex that CC recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway CC (PubMed:21448132, PubMed:23667253, PubMed:27543824, PubMed:27863242). CC In the Pelota-HBS1L complex, PELO recognizes ribosomes stalled at the CC 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA CC in the mRNA channel (PubMed:27543824, PubMed:27863242). Following mRNA CC extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L CC complex promotes recruitment of ABCE1, which drives the disassembly of CC stalled ribosomes, followed by degradation of damaged mRNAs as part of CC the NGD pathway (PubMed:21448132, PubMed:32006463). As part of the CC PINK1-regulated signaling, upon mitochondrial damage is recruited to CC the ribosome/mRNA-ribonucleoprotein complex associated to mitochondrial CC outer membrane thereby enabling the recruitment of autophagy receptors CC and induction of mitophagy (PubMed:29861391). CC {ECO:0000269|PubMed:21448132, ECO:0000269|PubMed:23667253, CC ECO:0000269|PubMed:27543824, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:32006463}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P33309}; CC -!- SUBUNIT: Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 CC complex, composed of PELO and HBS1L (PubMed:27863242). Interacts with CC PINK1 (PubMed:29861391). Interacts with ABCE1 (PubMed:29861391). CC Interacts with CNOT4 (PubMed:29861391). Interacts with GTPBP2 (By CC similarity). {ECO:0000250|UniProtKB:Q80X73, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29861391}. CC -!- INTERACTION: CC Q9BRX2; O95817: BAG3; NbExp=3; IntAct=EBI-1043580, EBI-747185; CC Q9BRX2; P63172: DYNLT1; NbExp=3; IntAct=EBI-1043580, EBI-1176455; CC Q9BRX2; O75821: EIF3G; NbExp=6; IntAct=EBI-1043580, EBI-366632; CC Q9BRX2; P11362-2: FGFR1; NbExp=3; IntAct=EBI-1043580, EBI-25852941; CC Q9BRX2; P21333-2: FLNA; NbExp=6; IntAct=EBI-1043580, EBI-9641086; CC Q9BRX2; O00165: HAX1; NbExp=7; IntAct=EBI-1043580, EBI-357001; CC Q9BRX2; Q9Y450: HBS1L; NbExp=7; IntAct=EBI-1043580, EBI-2868258; CC Q9BRX2; P04792: HSPB1; NbExp=4; IntAct=EBI-1043580, EBI-352682; CC Q9BRX2; P42858: HTT; NbExp=12; IntAct=EBI-1043580, EBI-466029; CC Q9BRX2; P05362: ICAM1; NbExp=3; IntAct=EBI-1043580, EBI-1035358; CC Q9BRX2; Q92993: KAT5; NbExp=3; IntAct=EBI-1043580, EBI-399080; CC Q9BRX2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1043580, EBI-10975473; CC Q9BRX2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-1043580, EBI-10176379; CC Q9BRX2; Q8TAP4-4: LMO3; NbExp=9; IntAct=EBI-1043580, EBI-11742507; CC Q9BRX2; P61968: LMO4; NbExp=3; IntAct=EBI-1043580, EBI-2798728; CC Q9BRX2; P31153: MAT2A; NbExp=3; IntAct=EBI-1043580, EBI-1050743; CC Q9BRX2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1043580, EBI-16439278; CC Q9BRX2; Q9HB07: MYG1; NbExp=3; IntAct=EBI-1043580, EBI-709754; CC Q9BRX2; P07196: NEFL; NbExp=3; IntAct=EBI-1043580, EBI-475646; CC Q9BRX2; P62937-2: PPIA; NbExp=3; IntAct=EBI-1043580, EBI-25884072; CC Q9BRX2; P17252: PRKCA; NbExp=3; IntAct=EBI-1043580, EBI-1383528; CC Q9BRX2; P60891: PRPS1; NbExp=3; IntAct=EBI-1043580, EBI-749195; CC Q9BRX2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1043580, EBI-9090795; CC Q9BRX2; P78539: SRPX; NbExp=6; IntAct=EBI-1043580, EBI-2371213; CC Q9BRX2; O76024: WFS1; NbExp=3; IntAct=EBI-1043580, EBI-720609; CC Q9BRX2; P61981: YWHAG; NbExp=3; IntAct=EBI-1043580, EBI-359832; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21448132}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11060452}. CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota CC subfamily. {ECO:0000305}. 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; AF139828; AAG22574.1; -; mRNA. DR EMBL; AF143952; AAG22575.1; -; Genomic_DNA. DR EMBL; AY117399; AAM89414.1; -; mRNA. DR EMBL; AF132951; AAD27726.1; -; mRNA. DR EMBL; AC026230; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005889; AAH05889.1; -; mRNA. DR EMBL; BC007249; AAH07249.1; -; mRNA. DR EMBL; BC007650; AAH07650.1; -; mRNA. DR EMBL; BC022789; AAH22789.1; -; mRNA. DR CCDS; CCDS3956.1; -. DR RefSeq; NP_057030.3; NM_015946.4. DR PDB; 1X52; NMR; -; A=261-371. DR PDB; 5EO3; X-ray; 2.60 A; A/B=265-385. DR PDB; 5LZW; EM; 3.53 A; ii=1-385. DR PDB; 5LZX; EM; 3.67 A; ii=1-385. DR PDB; 5LZY; EM; 3.99 A; ii=1-385. DR PDB; 5LZZ; EM; 3.47 A; ii=1-385. DR PDBsum; 1X52; -. DR PDBsum; 5EO3; -. DR PDBsum; 5LZW; -. DR PDBsum; 5LZX; -. DR PDBsum; 5LZY; -. DR PDBsum; 5LZZ; -. DR AlphaFoldDB; Q9BRX2; -. DR EMDB; EMD-4134; -. DR EMDB; EMD-4135; -. DR EMDB; EMD-4136; -. DR EMDB; EMD-4137; -. DR SMR; Q9BRX2; -. DR BioGRID; 119818; 190. DR ComplexPortal; CPX-26579; Pelota-HBS1L ribosome dissociation complex. DR FunCoup; Q9BRX2; 866. DR IntAct; Q9BRX2; 79. DR MINT; Q9BRX2; -. DR STRING; 9606.ENSP00000274311; -. DR GlyGen; Q9BRX2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BRX2; -. DR MetOSite; Q9BRX2; -. DR PhosphoSitePlus; Q9BRX2; -. DR BioMuta; PELO; -. DR DMDM; 322510057; -. DR jPOST; Q9BRX2; -. DR MassIVE; Q9BRX2; -. DR PaxDb; 9606-ENSP00000274311; -. DR PeptideAtlas; Q9BRX2; -. DR ProteomicsDB; 78846; -. DR Pumba; Q9BRX2; -. DR Antibodypedia; 23309; 157 antibodies from 25 providers. DR DNASU; 53918; -. DR Ensembl; ENST00000274311.3; ENSP00000274311.2; ENSG00000152684.12. DR GeneID; 53918; -. DR KEGG; hsa:53918; -. DR MANE-Select; ENST00000274311.3; ENSP00000274311.2; NM_015946.5; NP_057030.3. DR UCSC; uc003jos.5; human. DR AGR; HGNC:8829; -. DR ClinPGx; PA33174; -. DR CTD; 53918; -. DR DisGeNET; 53918; -. DR GeneCards; PELO; -. DR HGNC; HGNC:8829; PELO. DR HPA; ENSG00000152684; Low tissue specificity. DR MIM; 605757; gene. DR OpenTargets; ENSG00000152684; -. DR VEuPathDB; HostDB:ENSG00000152684; -. DR eggNOG; KOG2869; Eukaryota. DR GeneTree; ENSGT00390000016326; -. DR HOGENOM; CLU_023334_3_1_1; -. DR InParanoid; Q9BRX2; -. DR OMA; DDLWHLK; -. DR OrthoDB; 10249111at2759; -. DR PAN-GO; Q9BRX2; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q9BRX2; -. DR PathwayCommons; Q9BRX2; -. DR SignaLink; Q9BRX2; -. DR Agora; ENSG00000152684; -. DR BioGRID-ORCS; 53918; 618 hits in 1167 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR EvolutionaryTrace; Q9BRX2; -. DR GeneWiki; PELO; -. DR GenomeRNAi; 53918; -. DR Pharos; Q9BRX2; Tbio. DR PRO; PR:Q9BRX2; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9BRX2; protein. DR Bgee; ENSG00000152684; Expressed in vena cava and 197 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0170011; F:stalled ribosome sensor activity; IDA:UniProt. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl. DR GO; GO:0007492; P:endoderm development; IEA:Ensembl. DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl. DR GO; GO:0060231; P:mesenchymal to epithelial transition; IEA:Ensembl. DR GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central. DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:UniProtKB. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro. DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl. DR FunFam; 2.30.30.870:FF:000001; Protein pelota homolog; 1. DR FunFam; 3.30.1330.30:FF:000008; Protein pelota homolog; 1. DR FunFam; 3.30.420.60:FF:000002; Protein pelota homolog; 1. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.30.420.60; eRF1 domain 2; 1. DR Gene3D; 2.30.30.870; Pelota, domain A; 1. DR InterPro; IPR042226; eFR1_2_sf. DR InterPro; IPR005141; eRF1_2. DR InterPro; IPR005142; eRF1_3. DR InterPro; IPR005140; eRF1_Pelota-like_N. DR InterPro; IPR038069; Pelota/DOM34_N. DR InterPro; IPR058547; Pelota_N. DR InterPro; IPR029064; Ribosomal_eL30-like_sf. DR InterPro; IPR004405; TF_pelota. DR NCBIfam; TIGR00111; pelota; 1. DR PANTHER; PTHR10853; PELOTA; 1. DR PANTHER; PTHR10853:SF0; PROTEIN PELOTA HOMOLOG; 1. DR Pfam; PF03464; eRF1_2; 1. DR Pfam; PF03465; eRF1_3; 1. DR Pfam; PF26356; Pelota_N; 1. DR SMART; SM01194; eRF1_1; 1. DR SUPFAM; SSF159065; Dom34/Pelota N-terminal domain-like; 1. DR SUPFAM; SSF55315; L30e-like; 1. DR SUPFAM; SSF53137; Translational machinery components; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Isopeptide bond; KW Metal-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Translation regulation; Ubl conjugation. FT CHAIN 1..385 FT /note="Protein pelota homolog" FT /id="PRO_0000143188" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:21406692" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:21406692" FT CROSSLNK 162 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 221 FT /note="L -> M (in dbSNP:rs1499280)" FT /evidence="ECO:0000269|PubMed:10810093, FT ECO:0000269|PubMed:11060452, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.2" FT /id="VAR_019777" FT MUTAGEN 2 FT /note="K->A: Abolished ability to rescue stalled FT ribosomes." FT /evidence="ECO:0000269|PubMed:27543824" FT MUTAGEN 45 FT /note="R->A: Abolished ability to rescue stalled FT ribosomes." FT /evidence="ECO:0000269|PubMed:27543824" FT CONFLICT 135 FT /note="A -> D (in Ref. 1; AAG22574/AAG22575)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="E -> G (in Ref. 3; AAD27726)" FT /evidence="ECO:0000305" FT CONFLICT 263..264 FT /note="AS -> LA (in Ref. 3; AAD27726)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="F -> S (in Ref. 3; AAD27726)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="S -> Y (in Ref. 1; AAG22574/AAG22575)" FT /evidence="ECO:0000305" FT HELIX 273..287 FT /evidence="ECO:0007829|PDB:5EO3" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:5EO3" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:5EO3" FT HELIX 296..304 FT /evidence="ECO:0007829|PDB:5EO3" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:5EO3" FT HELIX 315..318 FT /evidence="ECO:0007829|PDB:5EO3" FT HELIX 323..338 FT /evidence="ECO:0007829|PDB:5EO3" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:5EO3" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:5EO3" FT HELIX 351..358 FT /evidence="ECO:0007829|PDB:5EO3" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:5EO3" FT STRAND 362..368 FT /evidence="ECO:0007829|PDB:5EO3" SQ SEQUENCE 385 AA; 43359 MW; 8A0D264202995B76 CRC64; MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT GVAAILRFPV PELSDQEGDS SSEED //