DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation weight by comassie molecular weight estimation by coomasie staining weight by comassie Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250961X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250952X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250959X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250958X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250960X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250954X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250957X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250953X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250956X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. Nature structural & molecular biology 2012 imex curation Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Melero R., Buchwald G., Castaño R., Raabe M., Gil D., Lázaro M., Urlaub H., Conti E., Llorca O. DIP original experiment: DIP-250955X Nature structural & molecular biology 2012 IMEx The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end. casc3_human Protein CASC3 CASC3 MLN51 Cancer susceptibility candidate gene 3 protein Metastatic lymph node gene 51 protein Protein barentsz protein protein human Homo sapiens Human MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS DIP protein O15234 original sequence version: 129 DIP protein O15234 original sequence version: 130 DIP protein O15234 original sequence version: 94 DIP protein O15234 original sequence version: 106 DIP protein O15234 original sequence version: 114 642A4C01C8DD3BE0 rent1_human Regulator of nonsense transcripts 1 UPF1 RENT1 KIAA0221 ATP-dependent helicase RENT1 Nonsense mRNA reducing factor 1 Up-frameshift suppressor 1 homolog protein protein human Homo sapiens Human MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPGPSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY DIP protein Q92900 original sequence version: 137 DIP protein Q92900 original sequence version: 76 DIP protein Q92900 original sequence version: 101 DIP protein Q92900 original sequence version: 102 DIP protein Q92900 original sequence version: 135 DIP protein Q92900-1 original sequence version: 123 DIP protein Q92900 original sequence version: 132 6CCA6FE42B15BA28 mgn_human Protein mago nashi homolog MAGOH MAGOHA protein protein human Homo sapiens Human MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI DIP protein P61326 original sequence version: 113 DIP protein P61326 original sequence version: 114 DIP protein P61326 original sequence version: 78 DIP protein P61326 original sequence version: 91 DIP protein P61326 original sequence version: 100 FFAD0B075E045875 if4a3_human Eukaryotic initiation factor 4A-III KIAA0111 EIF4A3 DDX48 Eukaryotic translation initiation factor 4A isoform 3 ATP-dependent RNA helicase eIF4A-3 ATP-dependent RNA helicase DDX48 DEAD box protein 48 Eukaryotic initiation factor 4A-like NUK-34 Nuclear matrix protein 265 protein protein human Homo sapiens Human MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI DIP protein P38919 original sequence version: 160 DIP protein P38919 original sequence version: 161 DIP protein P38919 original sequence version: 124 DIP protein P38919 original sequence version: 137 DIP protein P38919 original sequence version: 157 DIP protein P38919 original sequence version: 146 DIP protein P38919 original sequence version: 151 3A21888CA96CA5EA q9bzi7-2 Regulator of nonsense transcripts 3B UPF3B RENT3B UPF3X Nonsense mRNA reducing factor 3B Up-frameshift suppressor 3 homolog B Up-frameshift suppressor 3 homolog on chromosome X protein protein human Homo sapiens Human MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNRLCPPDDSTKSGDSAAERKQESGISHRKEGGEE DIP protein Q9BZI7-2 original sequence version: 109 DIP protein Q9BZI7-2 original sequence version: 75 DIP protein Q9BZI7-2 original sequence version: 87 DIP protein Q9BZI7-2 original sequence version: 96 rent2_human Regulator of nonsense transcripts 2 Nonsense mRNA reducing factor 2 Up-frameshift suppressor 2 homolog UPF2 KIAA1408 RENT2 protein protein human Homo sapiens Human MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKVKAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR DIP protein Q9HAU5 original sequence version: 113 DIP protein Q9HAU5-1 original sequence version: 115 DIP protein Q9HAU5 original sequence version: 81 DIP protein Q9HAU5 original sequence version: 82 DIP protein Q9HAU5-1 original sequence version: 82 DIP protein Q9HAU5 original sequence version: 94 DIP protein Q9HAU5-1 original sequence version: 103 95F3C57D2854BB44 q9y5s9-1 RNA-binding protein 8A RBM8A Binder of OVCA1-1 RBM8 RNA-binding motif protein 8A RNA-binding protein Y14 Ribonucleoprotein RBM8A HSPC114 MDS014 BOV-1a protein protein human Homo sapiens Human MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR DIP protein Q9Y5S9-1 original sequence version: 158 DIP protein Q9Y5S9-1 original sequence version: 159 DIP protein Q9Y5S9 original sequence version: 121 DIP protein Q9Y5S9-1 original sequence version: 134 DIP protein Q9Y5S9-1 original sequence version: 143 DIP protein Q9Y5S9 original sequence version: 148 70BBD03CDDFEECFE casc3-eif4a3-11 2 17 unspecified role unspecified role unspecified role unspecified role RRM domain Region 66-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association casc3-eif4a3-12 5 17 unspecified role unspecified role unspecified role unspecified role RRM domain Region 66-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association casc3-eif4a3-13 8 17 unspecified role unspecified role unspecified role unspecified role RRM domain Region 66-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association upf1-upf2-14 6 15 unspecified role unspecified role unspecified role unspecified role RRM domain Region 42-143 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association upf2-upf3b-1 9 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction upf1-upf2-15 3 15 unspecified role unspecified role unspecified role unspecified role RRM domain Region 42-143 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association casc3-eif4a3-14 7 17 unspecified role unspecified role unspecified role unspecified role RRM domain Region 66-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association casc3-eif4a3-15 4 17 unspecified role unspecified role unspecified role unspecified role RRM domain Region 66-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association upf2-upf3b-2 10 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction casc3-eif4a3-16 1 11 unspecified role unspecified role unspecified role unspecified role Region 137-286 Region 137-286 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 115-914 Region 115-914 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association