ID RENT1_HUMAN Reviewed; 1129 AA. AC Q92900; O00239; O43343; Q86Z25; Q92842; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 18-OCT-2001, sequence version 2. DT 28-JAN-2026, entry version 233. DE RecName: Full=Regulator of nonsense transcripts 1 {ECO:0000312|HGNC:HGNC:9962}; DE EC=3.6.4.12 {ECO:0000269|PubMed:10999600, ECO:0000269|PubMed:30218034}; DE EC=3.6.4.13 {ECO:0000305|PubMed:10999600}; DE AltName: Full=ATP-dependent helicase RENT1 {ECO:0000250|UniProtKB:Q9EPU0}; DE AltName: Full=Nonsense mRNA reducing factor 1 {ECO:0000312|HGNC:HGNC:9962}; DE Short=NORF1 {ECO:0000312|HGNC:HGNC:9962}; DE AltName: Full=Up-frameshift suppressor 1 homolog; DE Short=hUpf1; GN Name=UPF1 {ECO:0000312|HGNC:HGNC:9962}; GN Synonyms=KIAA0221, RENT1 {ECO:0000312|HGNC:HGNC:9962}; 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 2). RC TISSUE=Heart; RX PubMed=8855285; DOI=10.1073/pnas.93.20.10928; RA Perlick H.A., Medghalchi S.M., Spencer F.A., Kendzior R.J. Jr., Dietz H.C.; RT "Mammalian orthologues of a yeast regulator of nonsense transcript RT stability."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10928-10932(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION. RX PubMed=9064659; DOI=10.1093/nar/25.4.814; RA Applequist S.E., Selg M., Raman C., Jaeck H.-M.; RT "Cloning and characterization of HUPF1, a human homolog of the RT Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein."; RL Nucleic Acids Res. 25:814-821(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-69. RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10454541; DOI=10.1128/mcb.19.9.5943; RA Page M.F., Carr B., Anders K.R., Grimson A., Anderson P.; RT "SMG-2 is a phosphorylated protein required for mRNA surveillance in RT Caenorhabditis elegans and related to Upf1p of yeast."; RL Mol. Cell. Biol. 19:5943-5951(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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 [7] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF2; UPF3A AND RP UPF3B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-843. RX PubMed=11163187; DOI=10.1016/s0092-8674(00)00214-2; RA Lykke-Andersen J., Shu M.-D., Steitz J.A.; RT "Human Upf proteins target an mRNA for nonsense-mediated decay when bound RT downstream of a termination codon."; RL Cell 103:1121-1131(2000). RN [8] RP INTERACTION WITH UPF2. RX PubMed=11073994; DOI=10.1128/mcb.20.23.8944-8957.2000; RA Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.; RT "Novel Upf2p orthologues suggest a functional link between translation RT initiation and nonsense surveillance complexes."; RL Mol. Cell. Biol. 20:8944-8957(2000). RN [9] RP FUNCTION, ENZYME ACTIVITY, CATALYTIC ACTIVITY, RNA-BINDING, AND MUTAGENESIS RP OF 647-ASP-GLU-648. RX PubMed=10999600; DOI=10.1017/s1355838200000546; RA Bhattacharya A., Czaplinski K., Trifillis P., He F., Jacobson A., RA Peltz S.W.; RT "Characterization of the biochemical properties of the human Upf1 gene RT product that is involved in nonsense-mediated mRNA decay."; RL RNA 6:1226-1235(2000). RN [10] RP FUNCTION, PHOSPHORYLATION AT SER-1089 AND SER-1107, AND MUTAGENESIS OF RP SER-1089; SER-1107 AND GLN-1108. RX PubMed=11544179; DOI=10.1101/gad.913001; RA Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.; RT "Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, RT associates with components of the mRNA surveillance complex and is involved RT in the regulation of nonsense-mediated mRNA decay."; RL Genes Dev. 15:2215-2228(2001). RN [11] RP PHOSPHORYLATION. RX PubMed=11331269; DOI=10.1074/jbc.c100144200; RA Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.; RT "Cloning of a novel phosphatidylinositol kinase-related kinase: RT characterization of the human SMG-1 RNA surveillance protein."; RL J. Biol. Chem. 276:22709-22714(2001). RN [12] RP INTERACTION WITH UPF2, AND SUBCELLULAR LOCATION. RX PubMed=11113196; DOI=10.1128/mcb.21.1.209-223.2001; RA Serin G., Gersappe A., Black J.D., Aronoff R., Maquat L.E.; RT "Identification and characterization of human orthologues to Saccharomyces RT cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)."; RL Mol. Cell. Biol. 21:209-223(2001). RN [13] RP IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, AND ASSOCIATION WITH THE RP EJC COMPLEX. RX PubMed=11546874; DOI=10.1126/science.1062786; RA Lykke-Andersen J., Shu M.-D., Steitz J.A.; RT "Communication of the position of exon-exon junctions to the mRNA RT surveillance machinery by the protein RNPS1."; RL Science 293:1836-1839(2001). RN [14] RP PHOSPHORYLATION. RX PubMed=14636577; DOI=10.1016/s1097-2765(03)00443-x; RA Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., RA Hachiya T., Hentze M.W., Anderson P., Ohno S.; RT "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes RT containing hSMG-5 and hSMG-7."; RL Mol. Cell 12:1187-1200(2003). RN [15] RP FUNCTION, AND INTERACTION WITH EST1A. RX PubMed=12554878; DOI=10.1261/rna.2137903; RA Chiu S.-Y., Serin G., Ohara O., Maquat L.E.; RT "Characterization of human Smg5/7a: a protein with similarities to RT Caenorhabditis elegans SMG5 and SMG7 that functions in the RT dephosphorylation of Upf1."; RL RNA 9:77-87(2003). RN [16] RP INTERACTION WITH SMG7. RX PubMed=15721257; DOI=10.1016/j.molcel.2005.01.010; RA Fukuhara N., Ebert J., Unterholzner L., Lindner D., Izaurralde E., RA Conti E.; RT "SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay RT pathway."; RL Mol. Cell 17:537-547(2005). RN [17] RP FUNCTION, INTERACTION WITH SLBP, AND MUTAGENESIS OF LYS-509 AND ARG-843. RX PubMed=16086026; DOI=10.1038/nsmb972; RA Kaygun H., Marzluff W.F.; RT "Regulated degradation of replication-dependent histone mRNAs requires both RT ATR and Upf1."; RL Nat. Struct. Mol. Biol. 12:794-800(2005). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [19] RP IDENTIFICATION IN THE SURF COMPLEX, PHOSPHORYLATION AT SER-1089 AND RP SER-1107, AND MUTAGENESIS OF CYS-126; LYS-509; SER-1084; SER-1089; SER-1107 RP AND SER-1127. RX PubMed=16452507; DOI=10.1101/gad.1389006; RA Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R., Hoshino S., RA Ohno M., Dreyfuss G., Ohno S.; RT "Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon RT junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA RT decay."; RL Genes Dev. 20:355-367(2006). RN [20] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [22] RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY. RX PubMed=18172165; DOI=10.1101/gad.1622708; RA Mullen T.E., Marzluff W.F.; RT "Degradation of histone mRNA requires oligouridylation followed by RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to RT 5'."; RL Genes Dev. 22:50-65(2008). RN [23] RP FUNCTION, AND INTERACTION WITH GSPT2. RX PubMed=18447585; DOI=10.1371/journal.pbio.0060111; RA Singh G., Rebbapragada I., Lykke-Andersen J.; RT "A competition between stimulators and antagonists of Upf complex RT recruitment governs human nonsense-mediated mRNA decay."; RL PLoS Biol. 6:E111-E111(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION BY RP 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 [25] RP INTERACTION WITH ADAR, AND SUBCELLULAR LOCATION. RX PubMed=18362360; DOI=10.1073/pnas.0710576105; RA Agranat L., Raitskin O., Sperling J., Sperling R.; RT "The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact RT in the cell nucleus."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [27] RP FUNCTION, ASSOCIATION WITH THE SMG1C COMPLEX, AND MUTAGENESIS OF CYS-126. 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 [28] RP INTERACTION WITH CPSF6. RX PubMed=19864460; DOI=10.1091/mbc.e09-05-0389; RA Ruepp M.D., Aringhieri C., Vivarelli S., Cardinale S., Paro S., RA Schuemperli D., Barabino S.M.; RT "Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA RT export."; RL Mol. Biol. Cell 20:5211-5223(2009). RN [29] RP SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PNRC2, AND RP MUTAGENESIS OF 506-GLY--GLY-508. RX PubMed=19150429; DOI=10.1016/j.molcel.2008.11.022; RA Cho H., Kim K.M., Kim Y.K.; RT "Human proline-rich nuclear receptor coregulatory protein 2 mediates an RT interaction between mRNA surveillance machinery and decapping complex."; RL Mol. Cell 33:75-86(2009). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, 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 [31] RP FUNCTION IN MRNP DISASSEMBLY. RX PubMed=21145460; DOI=10.1016/j.cell.2010.11.043; RA Franks T.M., Singh G., Lykke-Andersen J.; RT "Upf1 ATPase-dependent mRNP disassembly is required for completion of RT nonsense- mediated mRNA decay."; RL Cell 143:938-950(2010). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; SER-1110 AND SER-1127, RP AND 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 [33] 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 [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1110, AND RP 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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565; SER-956 AND SER-1107, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [36] RP FUNCTION, INTERACTION WITH DHX34; PABPC1 AND UPF2, AND MUTAGENESIS OF RP CYS-126; 181-LEU--TYR-184; 204-VAL--VAL-205; GLY-506; GLY-508 AND LYS-509. RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020; RA Hug N., Caceres J.F.; RT "The RNA helicase DHX34 activates NMD by promoting a transition from the RT surveillance to the decay-inducing complex."; RL Cell Rep. 8:1845-1856(2014). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-31, AND 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 [38] RP FUNCTION, AND INTERACTION WITH MOV10. RX PubMed=24726324; DOI=10.1016/j.molcel.2014.03.017; RA Gregersen L.H., Schueler M., Munschauer M., Mastrobuoni G., Chen W., RA Kempa S., Dieterich C., Landthaler M.; RT "MOV10 Is a 5' to 3' RNA helicase contributing to UPF1 mRNA target RT degradation by translocation along 3' UTRs."; RL Mol. Cell 54:573-585(2014). RN [39] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1019, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [40] RP INTERACTION WITH ZC3H12A, AND MUTAGENESIS OF 647-ASP-GLU-648. RX PubMed=26000482; DOI=10.1016/j.cell.2015.04.029; RA Mino T., Murakawa Y., Fukao A., Vandenbon A., Wessels H.H., Ori D., RA Uehata T., Tartey S., Akira S., Suzuki Y., Vinuesa C.G., Ohler U., RA Standley D.M., Landthaler M., Fujiwara T., Takeuchi O.; RT "Regnase-1 and Roquin regulate a common element in inflammatory mRNAs by RT spatiotemporally distinct mechanisms."; RL Cell 161:1058-1073(2015). RN [41] RP IDENTIFICATION IN A COMPLEX WITH DHX34 AND SMG1, INTERACTION WITH DHX34 AND RP SMG1, AND MUTAGENESIS OF CYS-126. RX PubMed=26841701; DOI=10.1038/ncomms10585; RA Melero R., Hug N., Lopez-Perrote A., Yamashita A., Caceres J.F., Llorca O.; RT "The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1 RT phosphorylation."; RL Nat. Commun. 7:10585-10585(2016). RN [42] RP INTERACTION WITH SHFL. RX PubMed=27974568; DOI=10.1128/jvi.01606-16; RA Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K., RA Zoon K.C.; RT "IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity RT against Dengue Virus, Interacts with MOV10."; RL J. Virol. 91:0-0(2017). RN [43] RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN TAX. RX PubMed=29382845; DOI=10.1038/s41467-017-02793-6; RA Fiorini F., Robin J.P., Kanaan J., Borowiak M., Croquette V., Le Hir H., RA Jalinot P., Mocquet V.; RT "HTLV-1 Tax plugs and freezes UPF1 helicase leading to nonsense-mediated RT mRNA decay inhibition."; RL Nat. Commun. 9:431-431(2018). RN [44] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30218034; DOI=10.1038/s41467-018-06313-y; RA Kanaan J., Raj S., Decourty L., Saveanu C., Croquette V., Le Hir H.; RT "UPF1-like helicase grip on nucleic acids dictates processivity."; RL Nat. Commun. 9:3752-3752(2018). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 295-914, AND MUTAGENESIS OF RP LYS-509; 610-LYS--ARG-612; ARG-615; 647-ASP-GLU-648; GLN-676; ARG-714 AND RP ARG-876. RX PubMed=17159905; DOI=10.1038/sj.emboj.7601464; RA Cheng Z., Muhlrad D., Lim M.K., Parker R., Song H.; RT "Structural and functional insights into the human Upf1 helicase core."; RL EMBO J. 26:253-264(2007). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-914 IN COMPLEX WITH UPF2. RX PubMed=19556969; DOI=10.1038/emboj.2009.175; RA Clerici M., Mourao A., Gutsche I., Gehring N.H., Hentze M.W., Kulozik A., RA Kadlec J., Sattler M., Cusack S.; RT "Unusual bipartite mode of interaction between the nonsense-mediated decay RT factors, UPF1 and UPF2."; RL EMBO J. 28:2293-2306(2009). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 295-925 IN COMPLEX WITH ATP ANALOG RP AND RNA, AND FUNCTION. RX PubMed=21419344; DOI=10.1016/j.molcel.2011.02.010; RA Chakrabarti S., Jayachandran U., Bonneau F., Fiorini F., Basquin C., RA Domcke S., Le Hir H., Conti E.; RT "Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its RT regulation by Upf2."; RL Mol. Cell 41:693-703(2011). CC -!- FUNCTION: RNA-dependent helicase required for nonsense-mediated decay CC (NMD) of aberrant mRNAs containing premature stop codons and modulates CC the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, CC PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). Is CC recruited to mRNAs upon translation termination and undergoes a cycle CC of phosphorylation and dephosphorylation; its phosphorylation appears CC to be a key step in NMD (PubMed:11544179, PubMed:25220460). Recruited CC by release factors to stalled ribosomes together with the SMG1C protein CC kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex CC (PubMed:19417104). In EJC-dependent NMD, the SURF complex associates CC with the exon junction complex (EJC) (located 50-55 or more nucleotides CC downstream from the termination codon) through UPF2 and allows the CC formation of an UPF1-UPF2-UPF3 surveillance complex which is believed CC to activate NMD (PubMed:21419344). Phosphorylated UPF1 is recognized by CC EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the CC mRNA degradation machinery involving exonucleolytic and endonucleolytic CC pathways, and to serve as adapters to protein phosphatase 2A (PP2A), CC thereby triggering UPF1 dephosphorylation and allowing the recycling of CC NMD factors (PubMed:12554878). UPF1 can also activate NMD without UPF2 CC or UPF3, and in the absence of the NMD-enhancing downstream EJC CC indicative for alternative NMD pathways (PubMed:18447585). Plays a role CC in replication-dependent histone mRNA degradation at the end of phase CC S; the function is independent of UPF2 (PubMed:16086026, CC PubMed:18172165). For the recognition of premature termination codons CC (PTC) and initiation of NMD a competitive interaction between UPF1 and CC PABPC1 with the ribosome-bound release factors is proposed CC (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is CC required for disassembly of mRNPs undergoing NMD (PubMed:21145460). CC Together with UPF2 and dependent on TDRD6, mediates the degradation of CC mRNA harboring long 3'UTR by inducing the NMD machinery (By CC similarity). Also capable of unwinding double-stranded DNA and CC translocating on single-stranded DNA (PubMed:30218034). CC {ECO:0000250|UniProtKB:Q9EPU0, ECO:0000269|PubMed:11163187, CC ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:12554878, CC ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:18172165, CC ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19417104, CC ECO:0000269|PubMed:21145460, ECO:0000269|PubMed:21419344, CC ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:25220460, CC ECO:0000269|PubMed:30218034}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC Evidence={ECO:0000269|PubMed:30218034}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:30218034}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000305|PubMed:10999600}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000305|PubMed:10999600}; CC -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP) CC complex (PubMed:21419344). Associates with the exon junction complex CC (EJC) (PubMed:11546874, PubMed:16452507). Associates with the SGM1C CC complex; is phosphorylated by the complex kinase component SGM1 CC (PubMed:19417104). Part of a complex composed of SMG1, DHX34 and UPF1; CC within the complex DHX34 acts as a scaffolding protein to facilitate CC SMG1 phosphorylation of UPF1 (PubMed:26841701). Interacts with UPF2 CC (PubMed:11073994, PubMed:11113196, PubMed:11163187, PubMed:19556969). CC Interacts with UPF3A and UPF3B (PubMed:11163187). Interacts with EST1A CC (PubMed:12554878). Interacts with SLBP (PubMed:16086026). Interacts CC (when hyperphosphorylated) with PNRC2 (PubMed:19150429). Interacts with CC AGO1 and AGO2 (PubMed:17932509). Interacts with GSPT2 CC (PubMed:18447585). Interacts with isoform 1 and isoform 5 of ADAR/ADAR1 CC (PubMed:18362360). Interacts with SMG7 (PubMed:15721257). Interacts CC with ZC3H12A; this interaction occurs in a mRNA translationally CC active- and termination-dependent manner and is essential for ZC3H12A- CC mediated degradation of target mRNAs (PubMed:26000482). Interacts with CC CPSF6 (PubMed:19864460). Interacts with MOV10; the interaction is CC direct and RNA-dependent (PubMed:24726324). Interacts with SHFL; the CC interaction increases in the presence of RNA (PubMed:27974568). CC Interacts with UPF2 and DDX4; interactions are mediated by TDRD6 CC (PubMed:25220460). Interacts with DHX34 and PABPC1/PABP1; the CC interactions are RNA-independent (PubMed:25220460). Interacts with CC RBM46 (By similarity). {ECO:0000250|UniProtKB:Q9EPU0, CC ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, CC ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:11546874, CC ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:15721257, CC ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16452507, CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18362360, CC ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19150429, CC ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:19556969, CC ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:21419344, CC ECO:0000269|PubMed:24726324, ECO:0000269|PubMed:25220460, CC ECO:0000269|PubMed:26000482, ECO:0000269|PubMed:26841701, CC ECO:0000269|PubMed:27974568}. CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia CC virus 1/HTLV-1 protein Tax; this interaction inhibits the host CC nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:29382845}. CC -!- INTERACTION: CC Q92900; Q96AP0: ACD; NbExp=3; IntAct=EBI-373471, EBI-717666; CC Q92900; P55265: ADAR; NbExp=3; IntAct=EBI-373471, EBI-2462104; CC Q92900; Q9NPI6: DCP1A; NbExp=13; IntAct=EBI-373471, EBI-374238; CC Q92900; Q8IU60: DCP2; NbExp=3; IntAct=EBI-373471, EBI-521577; CC Q92900; Q9NZB2: FAM120A; NbExp=3; IntAct=EBI-373471, EBI-1171960; CC Q92900; P15170: GSPT1; NbExp=3; IntAct=EBI-373471, EBI-948993; CC Q92900; Q8IYD1: GSPT2; NbExp=4; IntAct=EBI-373471, EBI-3869637; CC Q92900; Q9UN81: L1RE1; NbExp=6; IntAct=EBI-373471, EBI-722458; CC Q92900; Q9NPJ4: PNRC2; NbExp=9; IntAct=EBI-373471, EBI-726549; CC Q92900; Q14493: SLBP; NbExp=3; IntAct=EBI-373471, EBI-2696402; CC Q92900; Q92540: SMG7; NbExp=4; IntAct=EBI-373471, EBI-719830; CC Q92900; O95793: STAU1; NbExp=6; IntAct=EBI-373471, EBI-358174; CC Q92900; Q7Z422: SZRD1; NbExp=2; IntAct=EBI-373471, EBI-2874567; CC Q92900; O14746: TERT; NbExp=3; IntAct=EBI-373471, EBI-1772203; CC Q92900; Q9HAU5: UPF2; NbExp=30; IntAct=EBI-373471, EBI-372073; CC Q92900; Q9H1J1: UPF3A; NbExp=4; IntAct=EBI-373471, EBI-521530; CC Q92900; Q9BZI7: UPF3B; NbExp=11; IntAct=EBI-373471, EBI-372780; CC Q92900; Q08491: SKI7; Xeno; NbExp=2; IntAct=EBI-373471, EBI-1389; CC Q92900-2; Q14152: EIF3A; NbExp=5; IntAct=EBI-373492, EBI-366617; CC Q92900-2; Q9UPR3: SMG5; NbExp=2; IntAct=EBI-373492, EBI-3400861; CC Q92900-2; Q86US8: SMG6; NbExp=2; IntAct=EBI-373492, EBI-3232100; CC Q92900-2; Q9HAU5: UPF2; NbExp=9; IntAct=EBI-373492, EBI-372073; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11163187}. CC Cytoplasm, P-body. Nucleus {ECO:0000269|PubMed:11163187, CC ECO:0000269|PubMed:18362360}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:Q9EPU0}. Note=Hyperphosphorylated form is CC targeted to the P-body, while unphosphorylated protein is distributed CC throughout the cytoplasm. Localized in the chromatoid bodies of round CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q9EPU0}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92900-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92900-2; Sequence=VSP_003393; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases CC from the PI3/PI4-kinase family. {ECO:0000269|PubMed:11544179}. CC -!- PTM: Phosphorylated by SMG1; required for formation of mRNA CC surveillance complexes. {ECO:0000269|PubMed:11331269, CC ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:14636577, CC ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:19150429}. CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA19664.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U65533; AAC50771.1; -; mRNA. DR EMBL; U59323; AAC51140.1; -; mRNA. DR EMBL; D86988; BAA19664.2; ALT_INIT; mRNA. DR EMBL; AF074016; AAC26788.1; -; mRNA. DR EMBL; AC003972; AAB94785.1; -; Genomic_DNA. DR EMBL; BC039817; AAH39817.1; -; mRNA. DR CCDS; CCDS12386.1; -. [Q92900-2] DR CCDS; CCDS74315.1; -. [Q92900-1] DR RefSeq; NP_001284478.1; NM_001297549.2. [Q92900-1] DR RefSeq; NP_002902.2; NM_002911.3. [Q92900-2] DR PDB; 2GJK; X-ray; 2.60 A; A=295-925. DR PDB; 2GK6; X-ray; 2.40 A; A/B=295-925. DR PDB; 2GK7; X-ray; 2.80 A; A=295-925. DR PDB; 2IYK; X-ray; 2.95 A; A/B=115-272. DR PDB; 2WJV; X-ray; 2.85 A; A/B=115-925. DR PDB; 2WJY; X-ray; 2.50 A; A=115-925. DR PDB; 2XZO; X-ray; 2.40 A; A=295-925. DR PDB; 2XZP; X-ray; 2.72 A; A=295-925. DR PDB; 6EJ5; X-ray; 3.34 A; A=295-925. DR PDB; 6Z3R; EM; 2.97 A; E=1085-1095. DR PDB; 8RXB; X-ray; 2.60 A; A/D/E/I/L/P=115-287. DR PDBsum; 2GJK; -. DR PDBsum; 2GK6; -. DR PDBsum; 2GK7; -. DR PDBsum; 2IYK; -. DR PDBsum; 2WJV; -. DR PDBsum; 2WJY; -. DR PDBsum; 2XZO; -. DR PDBsum; 2XZP; -. DR PDBsum; 6EJ5; -. DR PDBsum; 6Z3R; -. DR PDBsum; 8RXB; -. DR AlphaFoldDB; Q92900; -. DR EMDB; EMD-11063; -. DR EMDB; EMD-19450; -. DR EMDB; EMD-19451; -. DR EMDB; EMD-2664; -. DR EMDB; EMD-2666; -. DR EMDB; EMD-3065; -. DR EMDB; EMD-3066; -. DR SMR; Q92900; -. DR BioGRID; 111908; 611. DR CORUM; Q92900; -. DR DIP; DIP-29875N; -. DR FunCoup; Q92900; 4495. DR IntAct; Q92900; 297. DR MINT; Q92900; -. DR STRING; 9606.ENSP00000470142; -. DR GlyCosmos; Q92900; 1 site, 1 glycan. DR GlyGen; Q92900; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92900; -. DR MetOSite; Q92900; -. DR PhosphoSitePlus; Q92900; -. DR SwissPalm; Q92900; -. DR BioMuta; UPF1; -. DR DMDM; 17380291; -. DR jPOST; Q92900; -. DR MassIVE; Q92900; -. DR PaxDb; 9606-ENSP00000470142; -. DR PeptideAtlas; Q92900; -. DR ProteomicsDB; 75581; -. [Q92900-1] DR ProteomicsDB; 75582; -. [Q92900-2] DR Pumba; Q92900; -. DR Antibodypedia; 15175; 351 antibodies from 38 providers. DR DNASU; 5976; -. DR Ensembl; ENST00000262803.10; ENSP00000262803.5; ENSG00000005007.15. [Q92900-2] DR Ensembl; ENST00000599848.5; ENSP00000470142.1; ENSG00000005007.15. [Q92900-1] DR GeneID; 5976; -. DR KEGG; hsa:5976; -. DR MANE-Select; ENST00000262803.10; ENSP00000262803.5; NM_002911.4; NP_002902.2. [Q92900-2] DR UCSC; uc002nkf.4; human. [Q92900-1] DR AGR; HGNC:9962; -. DR ClinPGx; PA34328; -. DR CTD; 5976; -. DR DisGeNET; 5976; -. DR GeneCards; UPF1; -. DR HGNC; HGNC:9962; UPF1. DR HPA; ENSG00000005007; Low tissue specificity. DR MalaCards; UPF1; -. DR MIM; 601430; gene. DR OpenTargets; ENSG00000005007; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000005007; -. DR eggNOG; KOG1802; Eukaryota. DR GeneTree; ENSGT00940000157413; -. DR HOGENOM; CLU_001666_4_3_1; -. DR InParanoid; Q92900; -. DR OMA; QYMQMNG; -. DR OrthoDB; 6513042at2759; -. DR PAN-GO; Q92900; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q92900; -. DR BRENDA; 3.6.4.13; 2681. DR PathwayCommons; Q92900; -. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q92900; -. DR SIGNOR; Q92900; -. DR Agora; ENSG00000005007; -. DR BioGRID-ORCS; 5976; 794 hits in 1183 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; UPF1; human. DR EvolutionaryTrace; Q92900; -. DR GeneWiki; UPF1; -. DR GenomeRNAi; 5976; -. DR Pharos; Q92900; Tbio. DR PRO; PR:Q92900; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q92900; protein. DR Bgee; ENSG00000005007; Expressed in right hemisphere of cerebellum and 179 other cell types or tissues. DR ExpressionAtlas; Q92900; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:HGNC-UCL. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:HGNC-UCL. DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB. DR GO; GO:0004386; F:helicase activity; NAS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB. DR GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB. DR GO; GO:0071347; P:cellular response to interleukin-1; TAS:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; TAS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IDA:HGNC-UCL. DR GO; GO:0006260; P:DNA replication; IMP:HGNC-UCL. DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:HGNC-UCL. DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB. DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB. DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IEA:Ensembl. DR GO; GO:0060816; P:random inactivation of X chromosome; IEA:Ensembl. DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL. DR GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB. DR GO; GO:0032201; P:telomere maintenance via semi-conservative replication; IDA:BHF-UCL. DR CDD; cd21407; 1B_UPF1-like; 1. DR CDD; cd18039; DEXXQc_UPF1; 1. DR CDD; cd18808; SF1_C_Upf1; 1. DR CDD; cd21400; ZBD_UPF1-like; 1. DR DisProt; DP01921; -. DR DisProt; DP03233; -. [Q92900-2] DR FunFam; 2.40.30.230:FF:000001; Regulator of nonsense transcripts 1; 1. DR FunFam; 3.40.50.300:FF:000097; Regulator of nonsense transcripts 1; 1. DR Gene3D; 2.40.30.230; -; 1. DR Gene3D; 6.10.140.1240; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR IDEAL; IID00325; -. DR InterPro; IPR045055; DNA2/NAM7-like. DR InterPro; IPR041679; DNA2/NAM7-like_C. DR InterPro; IPR041677; DNA2/NAM7_AAA_11. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR047187; SF1_C_Upf1. DR InterPro; IPR040812; UPF1_1B_dom. DR InterPro; IPR018999; UPF1_CH/ZBD. DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1. DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1. DR Pfam; PF13086; AAA_11; 1. DR Pfam; PF13087; AAA_12; 1. DR Pfam; PF04851; ResIII; 1. DR Pfam; PF18141; UPF1_1B_dom; 1. DR Pfam; PF09416; UPF1_Zn_bind; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51997; UPF1_CH_RICH; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Helicase; KW Host-virus interaction; Hydrolase; Metal-binding; Methylation; KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; RNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1..1129 FT /note="Regulator of nonsense transcripts 1" FT /id="PRO_0000080716" FT DOMAIN 115..272 FT /note="Upf1 CH-rich" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT REGION 1..415 FT /note="Sufficient for interaction with RENT2" FT REGION 39..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 123..155 FT /note="C3H" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT REGION 137..165 FT /note="CC/SHH/C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT REGION 183..213 FT /note="C4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT REGION 1009..1058 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1073..1096 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1110..1129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1089..1090 FT /note="[ST]-Q motif 1" FT MOTIF 1107..1108 FT /note="[ST]-Q motif 2" FT COMPBIAS 52..69 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1025..1034 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1041..1058 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1073..1086 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 126 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 213 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01341" FT BINDING 486 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:21419344" FT BINDING 506..510 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:2GJK" FT BINDING 676 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:21419344" FT BINDING 713 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:21419344" FT BINDING 844 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:21419344" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 565 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 956 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1019 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1089 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507" FT MOD_RES 1107 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507, ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 353..363 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10454541, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8855285, FT ECO:0000303|PubMed:9064659" FT /id="VSP_003393" FT VARIANT 69 FT /note="A -> S (in dbSNP:rs17339451)" FT /evidence="ECO:0000269|PubMed:9039502" FT /id="VAR_056207" FT MUTAGEN 126 FT /note="C->S: Abolishes ability to interact with UPF2/RENT2 FT and copurifies with greater amounts of SMG1, SMG8 and SMG9. FT Increases interaction with DHX34. No effect on interaction FT with SMG1-DHX34-UPF1 complex." FT /evidence="ECO:0000269|PubMed:16452507, FT ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:25220460, FT ECO:0000269|PubMed:26841701" FT MUTAGEN 181..184 FT /note="LECY->VRVD: Abolishes interaction with UPF2. FT Decreases interaction with DHX34." FT /evidence="ECO:0000269|PubMed:25220460" FT MUTAGEN 204..205 FT /note="VV->DI: Abolishes interaction with UPF2. No effect FT on interaction with DHX34." FT /evidence="ECO:0000269|PubMed:25220460" FT MUTAGEN 506..508 FT /note="GTG->RTE: Prevents dephosphorylation and targets the FT protein to the P-body." FT /evidence="ECO:0000269|PubMed:19150429" FT MUTAGEN 506 FT /note="G->R: Decreases interaction with DHX34; when FT associated with E-508." FT /evidence="ECO:0000269|PubMed:25220460" FT MUTAGEN 508 FT /note="G->E: Decreases interaction with DHX34; when FT associated with R-506." FT /evidence="ECO:0000269|PubMed:25220460" FT MUTAGEN 509 FT /note="K->A: Inhibits histone mRNA degradation, ATPase FT activity and ATP binding. No effect on interaction with FT DHX34." FT /evidence="ECO:0000269|PubMed:16086026, FT ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:17159905, FT ECO:0000269|PubMed:25220460" FT MUTAGEN 610..611 FT /note="KR->AA: Impairs RNA binding." FT MUTAGEN 615 FT /note="R->A: Impairs RNA binding." FT /evidence="ECO:0000269|PubMed:17159905" FT MUTAGEN 647..648 FT /note="DE->AA: Loss of ATPase activity and helicase FT activity." FT /evidence="ECO:0000269|PubMed:10999600, FT ECO:0000269|PubMed:17159905" FT MUTAGEN 647..648 FT /note="DE->AA: Loss of ATPase activity and helicase FT activity. Inhibits ZC3H12A-mediated IL6 mRNA degradation." FT /evidence="ECO:0000269|PubMed:10999600, FT ECO:0000269|PubMed:17159905, ECO:0000269|PubMed:26000482" FT MUTAGEN 676 FT /note="Q->A: Impairs ATPase activity, no effect on ATP FT binding." FT /evidence="ECO:0000269|PubMed:17159905" FT MUTAGEN 714 FT /note="R->A: Impairs ATPase activity and ATP binding." FT /evidence="ECO:0000269|PubMed:17159905" FT MUTAGEN 843 FT /note="R->A: Inhibits histone mRNA degradation." FT /evidence="ECO:0000269|PubMed:11163187, FT ECO:0000269|PubMed:16086026" FT MUTAGEN 843 FT /note="R->C: Abolishes NMD." FT /evidence="ECO:0000269|PubMed:11163187, FT ECO:0000269|PubMed:16086026" FT MUTAGEN 876 FT /note="R->A: Impairs ATPase activity and ATP binding." FT /evidence="ECO:0000269|PubMed:17159905" FT MUTAGEN 1084 FT /note="S->A: Impairs association with UPF2, SMG1 and SMG7 FT and impairs phosphorylation; when associated with A-1089, FT A-1107 and A-1127." FT /evidence="ECO:0000269|PubMed:16452507" FT MUTAGEN 1089 FT /note="S->A: Impairs association with UPF2, SMG1 and SMG7 FT and impairs phosphorylation; when associated with A-1084, FT A-1107 and A-1127." FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507" FT MUTAGEN 1089 FT /note="S->A: Still phosphorylated but with less FT efficiency." FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507" FT MUTAGEN 1107 FT /note="S->A: Impairs association with UPF2, SMG1 and SMG7 FT and impairs phosphorylation; when associated with A-1084, FT A-1089 and A-1127." FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507" FT MUTAGEN 1107 FT /note="S->A: Impairs phosphorylation." FT /evidence="ECO:0000269|PubMed:11544179, FT ECO:0000269|PubMed:16452507" FT MUTAGEN 1108 FT /note="Q->N: Impairs phosphorylation." FT /evidence="ECO:0000269|PubMed:11544179" FT MUTAGEN 1127 FT /note="S->A: Impairs association with UPF2, SMG1 and SMG7 FT and impairs phosphorylation; when associated with A-1084, FT A-1089 and A-1107." FT /evidence="ECO:0000269|PubMed:16452507" FT CONFLICT 61 FT /note="G -> S (in Ref. 2; AAC51140)" FT /evidence="ECO:0000305" FT CONFLICT 466 FT /note="I -> T (in Ref. 2; AAC51140)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="G -> A (in Ref. 1; AAC50771)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="G -> D (in Ref. 1; AAC50771)" FT /evidence="ECO:0000305" FT CONFLICT 557 FT /note="A -> P (in Ref. 1; AAC50771)" FT /evidence="ECO:0000305" FT CONFLICT 901..902 FT /note="NY -> IF (in Ref. 1; AAC50771)" FT /evidence="ECO:0000305" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:2WJY" FT TURN 138..141 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 142..146 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 155..163 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:2WJV" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:8RXB" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:2WJY" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:2WJV" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:8RXB" FT TURN 210..213 FT /evidence="ECO:0007829|PDB:2WJY" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:2WJV" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:2IYK" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:2WJV" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:2WJY" FT TURN 240..242 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 248..253 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 259..269 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 299..321 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:2GK6" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:2XZO" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:2GJK" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:2XZP" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 379..382 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 385..393 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:2GK7" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 410..412 FT /evidence="ECO:0007829|PDB:2GJK" FT STRAND 418..425 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 429..443 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:6EJ5" FT HELIX 450..456 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 484..493 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 497..502 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 509..522 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 523..525 FT /evidence="ECO:0007829|PDB:2GK6" FT STRAND 528..534 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 535..547 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 552..554 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 558..560 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 568..570 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 572..577 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 582..591 FT /evidence="ECO:0007829|PDB:2XZO" FT TURN 593..595 FT /evidence="ECO:0007829|PDB:2WJY" FT HELIX 600..620 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 622..627 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 630..632 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 634..636 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 642..646 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 649..651 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 654..661 FT /evidence="ECO:0007829|PDB:2XZO" FT TURN 662..664 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 665..672 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:6EJ5" FT HELIX 684..688 FT /evidence="ECO:0007829|PDB:2XZO" FT TURN 689..692 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 695..702 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 717..727 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 733..736 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 739..741 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 751..754 FT /evidence="ECO:0007829|PDB:2GK7" FT STRAND 757..761 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 766..768 FT /evidence="ECO:0007829|PDB:2GJK" FT STRAND 770..773 FT /evidence="ECO:0007829|PDB:2WJY" FT STRAND 775..777 FT /evidence="ECO:0007829|PDB:2GJK" FT HELIX 778..794 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 798..800 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 801..806 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 808..819 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 826..830 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 832..836 FT /evidence="ECO:0007829|PDB:2XZO" FT TURN 837..842 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 845..851 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 857..859 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 862..865 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 867..874 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 875..885 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 887..890 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 894..905 FT /evidence="ECO:0007829|PDB:2XZO" FT STRAND 909..912 FT /evidence="ECO:0007829|PDB:2XZO" FT HELIX 914..916 FT /evidence="ECO:0007829|PDB:2XZO" SQ SEQUENCE 1129 AA; 124345 MW; 6CCA6FE42B15BA28 CRC64; MSVEAYGPSS QTLTFLDTEE AELLGADTQG SEFEFTDFTL PSQTQTPPGG PGGPGGGGAG GPGGAGAGAA AGQLDAQVGP EGILQNGAVD DSVAKTSQLL AELNFEEDEE DTYYTKDLPI HACSYCGIHD PACVVYCNTS KKWFCNGRGN TSGSHIVNHL VRAKCKEVTL HKDGPLGETV LECYNCGCRN VFLLGFIPAK ADSVVVLLCR QPCASQSSLK DINWDSSQWQ PLIQDRCFLS WLVKIPSEQE QLRARQITAQ QINKLEELWK ENPSATLEDL EKPGVDEEPQ HVLLRYEDAY QYQNIFGPLV KLEADYDKKL KESQTQDNIT VRWDLGLNKK RIAYFTLPKT DSGNEDLVII WLRDMRLMQG DEICLRYKGD LAPLWKGIGH VIKVPDNYGD EIAIELRSSV GAPVEVTHNF QVDFVWKSTS FDRMQSALKT FAVDETSVSG YIYHKLLGHE VEDVIIKCQL PKRFTAQGLP DLNHSQVYAV KTVLQRPLSL IQGPPGTGKT VTSATIVYHL ARQGNGPVLV CAPSNIAVDQ LTEKIHQTGL KVVRLCAKSR EAIDSPVSFL ALHNQIRNMD SMPELQKLQQ LKDETGELSS ADEKRYRALK RTAERELLMN ADVICCTCVG AGDPRLAKMQ FRSILIDEST QATEPECMVP VVLGAKQLIL VGDHCQLGPV VMCKKAAKAG LSQSLFERLV VLGIRPIRLQ VQYRMHPALS AFPSNIFYEG SLQNGVTAAD RVKKGFDFQW PQPDKPMFFY VTQGQEEIAS SGTSYLNRTE AANVEKITTK LLKAGAKPDQ IGIITPYEGQ RSYLVQYMQF SGSLHTKLYQ EVEIASVDAF QGREKDFIIL SCVRANEHQG IGFLNDPRRL NVALTRARYG VIIVGNPKAL SKQPLWNHLL NYYKEQKVLV EGPLNNLRES LMQFSKPRKL VNTINPGARF MTTAMYDARE AIIPGSVYDR SSQGRPSSMY FQTHDQIGMI SAGPSHVAAM NIPIPFNLVM PPMPPPGYFG QANGPAAGRG TPKGKTGRGG RQKNRFGLPG PSQTNLPNSQ ASQDVASQPF SQGALTQGYI SMSQPSQMSQ PGLSQPELSQ DSYLGDEFKS QIDVALSQDS TYQGERAYQH GGVTGLSQY //