RENT1_HUMAN
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 03-AUG-2022, entry version 216.
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 + H(+) + phosphate; 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 + H(+) + phosphate; 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:11163187, PubMed:11073994, PubMed:11113196, 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).
CC {ECO:0000250|UniProtKB:Q9EPU0, ECO:0000269|PubMed:11073994,
CC ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187,
CC ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12554878,
CC ECO:0000269|PubMed:15721257, ECO:0000269|PubMed:16086026,
CC ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:18362360, ECO:0000269|PubMed:18447585,
CC ECO:0000269|PubMed:19150429, ECO:0000269|PubMed:19417104,
CC ECO:0000269|PubMed:19556969, ECO:0000269|PubMed:19864460,
CC ECO:0000269|PubMed:21419344, ECO:0000269|PubMed:24726324,
CC ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:26000482,
CC ECO:0000269|PubMed:26841701, 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; P15170: GSPT1; NbExp=2; IntAct=EBI-373471, EBI-948993;
CC Q92900; Q8IYD1: GSPT2; NbExp=3; 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=3; IntAct=EBI-373471, EBI-719830;
CC Q92900; O95793: STAU1; NbExp=5; IntAct=EBI-373471, EBI-358174;
CC Q92900; O14746: TERT; NbExp=3; IntAct=EBI-373471, EBI-1772203;
CC Q92900; Q9HAU5: UPF2; NbExp=29; IntAct=EBI-373471, EBI-372073;
CC Q92900; Q9H1J1: UPF3A; NbExp=4; IntAct=EBI-373471, EBI-521530;
CC Q92900; Q9BZI7: UPF3B; NbExp=10; 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};
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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_001297549.1. [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 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 AlphaFoldDB; Q92900; -.
DR SMR; Q92900; -.
DR BioGRID; 111908; 475.
DR CORUM; Q92900; -.
DR DIP; DIP-29875N; -.
DR IntAct; Q92900; 184.
DR MINT; Q92900; -.
DR STRING; 9606.ENSP00000470142; -.
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 EPD; Q92900; -.
DR jPOST; Q92900; -.
DR MassIVE; Q92900; -.
DR MaxQB; Q92900; -.
DR PaxDb; Q92900; -.
DR PeptideAtlas; Q92900; -.
DR PRIDE; Q92900; -.
DR ProteomicsDB; 75581; -. [Q92900-1]
DR ProteomicsDB; 75582; -. [Q92900-2]
DR Antibodypedia; 15175; 353 antibodies from 37 providers.
DR DNASU; 5976; -.
DR Ensembl; ENST00000262803.10; ENSP00000262803.5; ENSG00000005007.13. [Q92900-2]
DR Ensembl; ENST00000599848.5; ENSP00000470142.1; ENSG00000005007.13. [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 CTD; 5976; -.
DR DisGeNET; 5976; -.
DR GeneCards; UPF1; -.
DR HGNC; HGNC:9962; UPF1.
DR HPA; ENSG00000005007; Low tissue specificity.
DR MIM; 601430; gene.
DR neXtProt; NX_Q92900; -.
DR OpenTargets; ENSG00000005007; -.
DR PharmGKB; PA34328; -.
DR VEuPathDB; HostDB:ENSG00000005007; -.
DR eggNOG; KOG1802; Eukaryota.
DR GeneTree; ENSGT00940000157413; -.
DR HOGENOM; CLU_001666_4_3_1; -.
DR InParanoid; Q92900; -.
DR OMA; HHDSIGY; -.
DR OrthoDB; 62494at2759; -.
DR PhylomeDB; Q92900; -.
DR TreeFam; TF300554; -.
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 BioGRID-ORCS; 5976; 776 hits in 1097 CRISPR screens.
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 177 other tissues.
DR ExpressionAtlas; Q92900; baseline and differential.
DR Genevisible; Q92900; HS.
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:InterPro.
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; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA: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:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; 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: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; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; PTHR10887; 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; SSF52540; 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 Reference proteome; Repeat; RNA-binding; Zinc; 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 1037..1058
FT /note="Polar residues"
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 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:2WJV"
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
