ID ELP2_YEAST Reviewed; 788 AA. AC P42935; D6VUY2; E9P8V1; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 205. DE RecName: Full=Elongator complex protein 2; DE AltName: Full=Gamma-toxin target 2; GN Name=ELP2; Synonyms=TOT2; OrderedLocusNames=YGR200C; ORFNames=G7725; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8904340; RX DOI=10.1002/(sici)1097-0061(19960315)12:3%3c273::aid-yea898%3e3.0.co;2-1; RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., RA Rodrigues-Pousada C.; RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine RT phosphohydrolase, and five new ORFs."; RL Yeast 12:273-280(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; DOI=10.1038/387s081; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=10024884; DOI=10.1016/s1097-2765(00)80179-3; RA Otero G., Fellows J., Li Y., de Bizemont T., Dirac A.M., Gustafsson C.M., RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.; RT "Elongator, a multisubunit component of a novel RNA polymerase II RT holoenzyme for transcriptional elongation."; RL Mol. Cell 3:109-118(1999). RN [6] RP FUNCTION OF THE ELONGATOR COMPLEX IN ZYMOCIN SENSITIVITY. RX PubMed=11296232; DOI=10.1093/emboj/20.8.1993; RA Frohloff F., Fichtner L., Jablonowski D., Breunig K.D., Schaffrath R.; RT "Saccharomyces cerevisiae Elongator mutations confer resistance to the RT Kluyveromyces lactis zymocin."; RL EMBO J. 20:1993-2003(2001). RN [7] RP IDENTIFICATION IN THE ELONGATOR COMPLEX. RX PubMed=11435442; DOI=10.1074/jbc.m105303200; RA Winkler G.S., Petrakis T.G., Ethelberg S., Tokunaga M., RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.; RT "RNA polymerase II elongator holoenzyme is composed of two discrete RT subcomplexes."; RL J. Biol. Chem. 276:32743-32749(2001). RN [8] RP IDENTIFICATION IN THE ELONGATOR COMPLEX. RX PubMed=11689709; DOI=10.1128/mcb.21.23.8203-8212.2001; RA Krogan N.J., Greenblatt J.F.; RT "Characterization of a six-subunit holo-elongator complex required for the RT regulated expression of a group of genes in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 21:8203-8212(2001). RN [9] RP INTERACTION WITH IKI3. RX PubMed=12139626; DOI=10.1046/j.1365-2958.2002.03055.x; RA Fichtner L., Frohloff F., Jablonowski D., Stark M.J.R., Schaffrath R.; RT "Protein interactions within Saccharomyces cerevisiae Elongator, a complex RT essential for Kluyveromyces lactis zymocicity."; RL Mol. Microbiol. 45:817-826(2002). RN [10] RP DISPUTED FUNCTION IN HISTONE ACETYLATION. RX PubMed=11904415; DOI=10.1073/pnas.022042899; RA Winkler G.S., Kristjuhan A., Erdjument-Bromage H., Tempst P., RA Svejstrup J.Q.; RT "Elongator is a histone H3 and H4 acetyltransferase important for normal RT histone acetylation levels in vivo."; RL Proc. Natl. Acad. Sci. U.S.A. 99:3517-3522(2002). RN [11] RP FUNCTION OF THE ELONGATOR COMPLEX IN PICHIA INOSITOVORA TOXIN SENSITIVITY. RX PubMed=13680368; DOI=10.1007/s00438-003-0920-5; RA Klassen R., Meinhardt F.; RT "Structural and functional analysis of the killer element pPin1-3 from RT Pichia inositovora."; RL Mol. Genet. Genomics 270:190-199(2003). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [13] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [14] RP FUNCTION. RX PubMed=15138274; DOI=10.1074/jbc.m403361200; RA Petrakis T.G., Wittschieben B.O., Svejstrup J.Q.; RT "Molecular architecture, structure-function relationship, and importance of RT the Elp3 subunit for the RNA binding of holo-elongator."; RL J. Biol. Chem. 279:32087-32092(2004). RN [15] RP FUNCTION IN EXOCYTOSIS REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=15780940; DOI=10.1016/j.molcel.2005.02.018; RA Rahl P.B., Chen C.Z., Collins R.N.; RT "Elp1p, the yeast homolog of the FD disease syndrome protein, negatively RT regulates exocytosis independently of transcriptional elongation."; RL Mol. Cell 17:841-853(2005). RN [16] RP FUNCTION IN TRNA MODIFICATION. RX PubMed=15769872; DOI=10.1261/rna.7247705; RA Huang B., Johansson M.J.O., Bystroem A.S.; RT "An early step in wobble uridine tRNA modification requires the Elongator RT complex."; RL RNA 11:424-436(2005). RN [17] RP INTERACTION WITH KTI11. RX PubMed=18627462; DOI=10.1111/j.1365-2958.2008.06350.x; RA Baer C., Zabel R., Liu S., Stark M.J., Schaffrath R.; RT "A versatile partner of eukaryotic protein complexes that is involved in RT multiple biological processes: Kti11/Dph3."; RL Mol. Microbiol. 69:1221-1233(2008). RN [18] RP FUNCTION. RX PubMed=18755837; DOI=10.1261/rna.1184108; RA Huang B., Lu J., Bystroem A.S.; RT "A genome-wide screen identifies genes required for formation of the wobble RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces RT cerevisiae."; RL RNA 14:2183-2194(2008). RN [19] RP SUBUNIT. RX PubMed=22343726; DOI=10.1038/nsmb.2234; RA Glatt S., Letoquart J., Faux C., Taylor N.M., Seraphin B., Muller C.W.; RT "The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase."; RL Nat. Struct. Mol. Biol. 19:314-320(2012). RN [20] RP PHOSPHORYLATION AT SER-492. RX PubMed=25569479; DOI=10.1371/journal.pgen.1004931; RA Abdel-Fattah W., Jablonowski D., Di Santo R., Thuering K.L., Scheidt V., RA Hammermeister A., Ten Have S., Helm M., Schaffrath R., Stark M.J.; RT "Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA RT modification in yeast."; RL PLoS Genet. 11:e1004931-e1004931(2015). RN [21] RP REVIEW. RX PubMed=29332244; DOI=10.1007/s00018-018-2747-6; RA Dalwadi U., Yip C.K.; RT "Structural insights into the function of Elongator."; RL Cell. Mol. Life Sci. 75:1613-1622(2018). RN [22] {ECO:0007744|PDB:4XFV} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), FUNCTION, IDENTIFICATION IN THE RP ELONGATOR ELP123 SUBCOMPLEX, DOMAIN, AND MUTAGENESIS OF 1-MET--ALA-14; RP ARG-626; ARG-628; ARG-654 AND ARG-675. RX PubMed=25960406; DOI=10.1016/j.str.2015.03.018; RA Dong C., Lin Z., Diao W., Li D., Chu X., Wang Z., Zhou H., Xie Z., Shen Y., RA Long J.; RT "The Elp2 subunit is essential for elongator complex assembly and RT functional regulation."; RL Structure 23:1078-1086(2015). RN [23] RP INTERACTION WITH KTI11, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=27694803; DOI=10.1038/nchembio.2190; RA Lin Z., Dong M., Zhang Y., Lee E.A., Lin H.; RT "Cbr1 is a Dph3 reductase required for the tRNA wobble uridine RT modification."; RL Nat. Chem. Biol. 12:995-997(2016). RN [24] RP STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS), AND IDENTIFICATION IN THE RP ELONGATOR COMPLEX. RX PubMed=27974378; DOI=10.15252/embr.201643353; RA Dauden M.I., Kosinski J., Kolaj-Robin O., Desfosses A., Ori A., Faux C., RA Hoffmann N.A., Onuma O.F., Breunig K.D., Beck M., Sachse C., Seraphin B., RA Glatt S., Mueller C.W.; RT "Architecture of the yeast Elongator complex."; RL EMBO Rep. 18:264-279(2017). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS), STRUCTURE BY ELECTRON MICROSCOPY, RP AND IDENTIFICATION IN THE ELONGATOR COMPLEX. RX PubMed=27872205; DOI=10.15252/embr.201642548; RA Setiaputra D.T., Cheng D.T., Lu S., Hansen J.M., Dalwadi U., Lam C.H., RA To J.L., Dong M.Q., Yip C.K.; RT "Molecular architecture of the yeast Elongator complex reveals an RT unexpected asymmetric subunit arrangement."; RL EMBO Rep. 18:280-291(2017). RN [26] {ECO:0007744|PDB:6QK7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF THE ELONGATOR ELP123 RP SUBCOMPLEX, AND FUNCTION. RX PubMed=31309145; DOI=10.1126/sciadv.aaw2326; RA Dauden M.I., Jaciuk M., Weis F., Lin T.Y., Kleindienst C., Abbassi N.E.H., RA Khatter H., Krutyholowa R., Breunig K.D., Kosinski J., Mueller C.W., RA Glatt S.; RT "Molecular basis of tRNA recognition by the Elongator complex."; RL Sci. Adv. 5:eaaw2326-eaaw2326(2019). CC -!- FUNCTION: Component of the elongator complex, a multiprotein complex CC which is required for multiple tRNA modifications, including mcm5U (5- CC methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2- CC thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:15769872, CC PubMed:18755837, PubMed:31309145). The elongator complex catalyzes CC formation of carboxymethyluridine in the wobble base at position 34 in CC tRNAs (PubMed:29332244). It functions as a gamma-toxin target (TOT); CC disruption of the complex confers resistance to Kluyveromyces lactis CC toxin zymocin (pGKL1 killer toxin) (PubMed:11296232). May also be CC involved in sensitivity to Pichia inositovora toxin (PubMed:13680368). CC ELP2 binds to microtubules (PubMed:25960406). Independently, ELP2 may CC be involved in polarized exocytosis (PubMed:15138274, PubMed:15780940). CC {ECO:0000269|PubMed:11296232, ECO:0000269|PubMed:13680368, CC ECO:0000269|PubMed:15138274, ECO:0000269|PubMed:15769872, CC ECO:0000269|PubMed:15780940, ECO:0000269|PubMed:18755837, CC ECO:0000269|PubMed:25960406, ECO:0000269|PubMed:31309145, CC ECO:0000303|PubMed:29332244}. CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA CC biosynthesis. {ECO:0000269|PubMed:15769872, CC ECO:0000269|PubMed:18755837}. CC -!- SUBUNIT: Component of the elongator complex which consists of CC ELP1/IKI3, ELP2, ELP3, ELP4, ELP5/IKI1 and ELP6 (PubMed:11435442, CC PubMed:11689709, PubMed:27872205, PubMed:27974378). The elongator CC complex is composed of two copies of the Elp123 subcomplex (composed of CC ELP1/IKI3, ELP2 and ELP3) and two copies of the Elp456 subcomplex CC (composed of ELP4, ELP5/IKI1 and ELP6) (PubMed:25960406, CC PubMed:27872205, PubMed:27974378). The Elp123 subcomplex forms a two- CC lobed scaffold, which binds the Elp456 subcomplex asymmetrically CC (PubMed:27872205, PubMed:27974378). In the complex, ELP2 interacts with CC ELP1/IKI3 (PubMed:12139626). In each lobe, ELP2 is tightly sandwiched CC between ELP1/IKI3 and ELP3 (PubMed:31309145). The Elp123 subcomplex CC binds tRNA through ELP1/IKI3 and ELP3 and can bind 2 tRNAs CC simultaneously (PubMed:31309145). tRNA-binding induces conformational CC rearrangements which precisely position the targeted anticodon base in CC the active site (PubMed:31309145). The Elp456 subcomplex binds tRNA and CC has ATPase activity (PubMed:22343726). Interacts with KTI11/DPH3 CC (PubMed:18627462, PubMed:27694803). {ECO:0000269|PubMed:11435442, CC ECO:0000269|PubMed:11689709, ECO:0000269|PubMed:12139626, CC ECO:0000269|PubMed:22343726, ECO:0000269|PubMed:25960406, CC ECO:0000269|PubMed:27694803, ECO:0000269|PubMed:27872205, CC ECO:0000269|PubMed:27974378, ECO:0000269|PubMed:31309145}. CC -!- INTERACTION: CC P42935; Q02908: ELP3; NbExp=8; IntAct=EBI-23459, EBI-33957; CC P42935; Q02884: ELP4; NbExp=7; IntAct=EBI-23459, EBI-35277; CC P42935; Q04868: ELP6; NbExp=3; IntAct=EBI-23459, EBI-27653; CC P42935; P38874: IKI1; NbExp=6; IntAct=EBI-23459, EBI-9061; CC P42935; Q06706: IKI3; NbExp=12; IntAct=EBI-23459, EBI-9068; CC P42935; Q3E840: KTI11; NbExp=3; IntAct=EBI-23459, EBI-2055307; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is CC required for elongator complex assembly and association with CC microtubules. {ECO:0000269|PubMed:25960406}. CC -!- MISCELLANEOUS: Present with 6090 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat ELP2 family. {ECO:0000305}. CC -!- CAUTION: The elongator complex was originally thought to play a role in CC transcription elongation. However, it is no longer thought to play a CC direct role in this process and its primary function is thought to be CC in tRNA modification. {ECO:0000305|PubMed:10024884, CC ECO:0000305|PubMed:11689709, ECO:0000305|PubMed:11904415, CC ECO:0000305|PubMed:15138274, ECO:0000305|PubMed:29332244}. 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; Z49133; CAA88993.1; -; Genomic_DNA. DR EMBL; Z72985; CAA97227.1; -; Genomic_DNA. DR EMBL; AY558100; AAS56426.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08293.1; -; Genomic_DNA. DR PIR; S53923; S53923. DR RefSeq; NP_011716.3; NM_001181329.3. DR PDB; 4XFV; X-ray; 3.20 A; A=1-788. DR PDB; 5M2N; X-ray; 2.81 A; A=1-788. DR PDB; 6QK7; EM; 3.30 A; B=1-788. DR PDB; 8ASV; EM; 4.35 A; B=1-788. DR PDB; 8ASW; EM; 3.96 A; B=1-788. DR AlphaFoldDB; P42935; -. DR EMDB; EMD-15622; -. DR EMDB; EMD-15623; -. DR EMDB; EMD-4571; -. DR SMR; P42935; -. DR BioGRID; 33453; 596. DR ComplexPortal; CPX-779; Elongator holoenzyme complex. DR DIP; DIP-2386N; -. DR FunCoup; P42935; 1307. DR IntAct; P42935; 76. DR MINT; P42935; -. DR STRING; 4932.YGR200C; -. DR iPTMnet; P42935; -. DR PaxDb; 4932-YGR200C; -. DR PeptideAtlas; P42935; -. DR DNASU; 853114; -. DR EnsemblFungi; YGR200C_mRNA; YGR200C; YGR200C. DR GeneID; 853114; -. DR KEGG; sce:YGR200C; -. DR AGR; SGD:S000003432; -. DR SGD; S000003432; ELP2. DR VEuPathDB; FungiDB:YGR200C; -. DR eggNOG; KOG1063; Eukaryota. DR HOGENOM; CLU_006430_0_0_1; -. DR InParanoid; P42935; -. DR OMA; ENFRHIS; -. DR OrthoDB; 27911at2759; -. DR BioCyc; MetaCyc:G3O-30885-MONOMER; -. DR BioCyc; YEAST:G3O-30885-MONOMER; -. DR UniPathway; UPA00988; -. DR BioGRID-ORCS; 853114; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P42935; -. DR PRO; PR:P42935; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P42935; protein. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0008017; F:microtubule binding; IDA:SGD. DR GO; GO:0032447; P:protein urmylation; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006417; P:regulation of translation; NAS:ComplexPortal. DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD. DR CDD; cd00200; WD40; 1. DR FunFam; 2.130.10.10:FF:001142; Elongator complex protein 2; 1. DR FunFam; 2.130.10.10:FF:001393; Elongator complex protein 2; 1. DR FunFam; 2.130.10.10:FF:001077; Elongator protein 2; 1. DR FunFam; 2.130.10.10:FF:000835; RNA polymerase II Elongator subunit; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4. DR InterPro; IPR037289; Elp2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR44111; ELONGATOR COMPLEX PROTEIN 2; 1. DR PANTHER; PTHR44111:SF1; ELONGATOR COMPLEX PROTEIN 2; 1. DR Pfam; PF00400; WD40; 8. DR SMART; SM00320; WD40; 11. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 3. DR PDBsum; 4XFV; -. DR PDBsum; 5M2N; -. DR PDBsum; 6QK7; -. DR PDBsum; 8ASV; -. DR PDBsum; 8ASW; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Repeat; Transport; tRNA processing; WD repeat. FT CHAIN 1..788 FT /note="Elongator complex protein 2" FT /id="PRO_0000051474" FT REPEAT 13..51 FT /note="WD 1" FT /evidence="ECO:0000255" FT REPEAT 57..96 FT /note="WD 2" FT /evidence="ECO:0000255" FT REPEAT 102..139 FT /note="WD 3" FT /evidence="ECO:0000255" FT REPEAT 200..243 FT /note="WD 4" FT /evidence="ECO:0000255" FT REPEAT 279..318 FT /note="WD 5" FT /evidence="ECO:0000255" FT REPEAT 336..377 FT /note="WD 6" FT /evidence="ECO:0000255" FT REPEAT 383..422 FT /note="WD 7" FT /evidence="ECO:0000255" FT REPEAT 437..475 FT /note="WD 8" FT /evidence="ECO:0000255" FT REPEAT 556..600 FT /note="WD 9" FT /evidence="ECO:0000255" FT REPEAT 604..643 FT /note="WD 10" FT /evidence="ECO:0000255" FT REPEAT 651..692 FT /note="WD 11" FT /evidence="ECO:0000255" FT REPEAT 699..742 FT /note="WD 12" FT /evidence="ECO:0000255" FT REPEAT 750..788 FT /note="WD 13" FT /evidence="ECO:0000255" FT REGION 490..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 507..517 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:25569479" FT MUTAGEN 1..14 FT /note="Missing: Abolishes interaction with ELP1/IKI3 and FT ELP3." FT /evidence="ECO:0000269|PubMed:25960406" FT MUTAGEN 626 FT /note="R->A: Dramatically reduced interaction with FT microtubules but no effect on interaction with ELP1/IKI3 or FT ELP3; when associated with A-628, A-654 and A-675." FT /evidence="ECO:0000269|PubMed:25960406" FT MUTAGEN 628 FT /note="R->A: Dramatically reduced interaction with FT microtubules but no effect on interaction with ELP1/IKI3 or FT ELP3; when associated with A-626, A-654 and A-675." FT /evidence="ECO:0000269|PubMed:25960406" FT MUTAGEN 654 FT /note="R->A: Dramatically reduced interaction with FT microtubules but no effect on interaction with ELP1/IKI3 or FT ELP3; when associated with A-626, A-628 and A-675." FT /evidence="ECO:0000269|PubMed:25960406" FT MUTAGEN 675 FT /note="Missing: Dramatically reduced interaction with FT microtubules but no effect on interaction with ELP1/IKI3 or FT ELP3; when associated with A-626, A-628 and A-654." FT /evidence="ECO:0000269|PubMed:25960406" FT CONFLICT 579 FT /note="S -> P (in Ref. 4; AAS56426)" FT /evidence="ECO:0000305" FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:5M2N" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 69..78 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 83..92 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 124..131 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 138..145 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 153..162 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 165..185 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 188..198 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:4XFV" FT STRAND 218..225 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 228..239 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 267..278 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 280..289 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 303..310 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 317..324 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 344..349 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 352..358 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 364..373 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:4XFV" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 398..404 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 405..407 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 408..414 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 429..438 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 442..457 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 460..466 FT /evidence="ECO:0007829|PDB:5M2N" FT HELIX 469..474 FT /evidence="ECO:0007829|PDB:5M2N" FT HELIX 475..479 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 498..501 FT /evidence="ECO:0007829|PDB:6QK7" FT HELIX 539..544 FT /evidence="ECO:0007829|PDB:5M2N" FT HELIX 547..549 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 550..555 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 561..566 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 572..577 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 586..591 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 592..594 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 597..603 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 609..614 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 618..625 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:4XFV" FT STRAND 630..636 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 637..640 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 641..651 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 656..661 FT /evidence="ECO:0007829|PDB:5M2N" FT HELIX 664..666 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 668..674 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 677..685 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 687..699 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 704..709 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 714..716 FT /evidence="ECO:0007829|PDB:6QK7" FT STRAND 717..724 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 729..735 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 738..744 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 747..749 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 755..760 FT /evidence="ECO:0007829|PDB:5M2N" FT STRAND 768..775 FT /evidence="ECO:0007829|PDB:5M2N" FT TURN 776..778 FT /evidence="ECO:0007829|PDB:4XFV" FT STRAND 780..786 FT /evidence="ECO:0007829|PDB:5M2N" SQ SEQUENCE 788 AA; 89411 MW; 5371908FE2E6EC0D CRC64; MVECITPEAI FIGANKQTQV SDIHKVKKIV AFGAGKTIAL WDPIEPNNKG VYATLKGHEA EVTCVRFVPD SDFMVSASED HHVKIWKFTD YSHLQCIQTI QHYSKTIVAL SALPSLISVG CADGTISIWR QNIQNDEFGL AHEFTIKKGF FYPLCLSLSK VEEKKYLLAI GGTNVNVFIA SFILSDSGIE KCRVVAELEG HEDWVKSLAF RHQETPGDYL LCSGSQDRYI RLWRIRINDL IDDSEEDSKK LTLLSNKQYK FQIDDELRVG INFEALIMGH DDWISSLQWH ESRLQLLAAT ADTSLMVWEP DETSGIWVCS LRLGEMSSKG ASTATGSSGG FWSCLWFTHE RMDFFLTNGK TGSWRMWATK DNIICDQRLG ISGATKDVTD IAWSPSGEYL LATSLDQTTR LFAPWIYDAS GRKREIATWH EFSRPQIHGY DMICVETVTD TRFVSGGDEK ILRSFDLPKG VAGMLQKFVG IQFEEKSEMP DSATVPVLGL SNKAGEDDAN EDDEEEEGGN KETPDITDPL SLLECPPMED QLQRHLLWPE VEKLYGHGFE ITCLDISPDQ KLIASACRSN NVQNAVIRIF STENWLEIKP ALPFHSLTIT RLKFSKDGKF LLSVCRDRKW ALWERNMEDN TFELRFKNEK PHTRIIWDAD WAPLEFGNVF VTASRDKTVK VWRHQKEPAD DYVLEASIKH TKAVTAISIH DSMIREKILI SVGLENGEIY LYSYTLGKFE LITQLNEDIT PADKITRLRW SHLKRNGKLF LGVGSSDLST RIYSLAYE //