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Regulator of nonsense transcripts 1 (EC 3.6.4.-) (ATP-dependent helicase RENT1) (Nonsense mRNA reducing factor 1) (NORF1) (Up-frameshift suppressor 1 homolog) (hUpf1)

 RENT1_HUMAN             Reviewed;        1129 AA.
Q92900; O00239; O43343; Q86Z25; Q92842;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
28-MAR-2018, entry version 184.
RecName: Full=Regulator of nonsense transcripts 1;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase RENT1;
AltName: Full=Nonsense mRNA reducing factor 1;
Short=NORF1;
AltName: Full=Up-frameshift suppressor 1 homolog;
Short=hUpf1;
Name=UPF1; Synonyms=KIAA0221, RENT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=8855285; DOI=10.1073/pnas.93.20.10928;
Perlick H.A., Medghalchi S.M., Spencer F.A., Kendzior R.J. Jr.,
Dietz H.C.;
"Mammalian orthologues of a yeast regulator of nonsense transcript
stability.";
Proc. Natl. Acad. Sci. U.S.A. 93:10928-10932(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
PubMed=9064659; DOI=10.1093/nar/25.4.814;
Applequist S.E., Selg M., Raman C., Jaeck H.-M.;
"Cloning and characterization of HUPF1, a human homolog of the
Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein.";
Nucleic Acids Res. 25:814-821(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-69.
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10454541; DOI=10.1128/MCB.19.9.5943;
Page M.F., Carr B., Anders K.R., Grimson A., Anderson P.;
"SMG-2 is a phosphorylated protein required for mRNA surveillance in
Caenorhabditis elegans and related to Upf1p of yeast.";
Mol. Cell. Biol. 19:5943-5951(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF2; UPF3A
AND UPF3B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-843.
PubMed=11163187; DOI=10.1016/S0092-8674(00)00214-2;
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Human Upf proteins target an mRNA for nonsense-mediated decay when
bound downstream of a termination codon.";
Cell 103:1121-1131(2000).
[8]
INTERACTION WITH UPF2.
PubMed=11073994; DOI=10.1128/MCB.20.23.8944-8957.2000;
Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
"Novel Upf2p orthologues suggest a functional link between translation
initiation and nonsense surveillance complexes.";
Mol. Cell. Biol. 20:8944-8957(2000).
[9]
ENZYME ACTIVITY, RNA-BINDING, AND MUTAGENESIS OF 647-ASP-GLU-648.
PubMed=10999600; DOI=10.1017/S1355838200000546;
Bhattacharya A., Czaplinski K., Trifillis P., He F., Jacobson A.,
Peltz S.W.;
"Characterization of the biochemical properties of the human Upf1 gene
product that is involved in nonsense-mediated mRNA decay.";
RNA 6:1226-1235(2000).
[10]
PHOSPHORYLATION AT SER-1089 AND SER-1107, AND MUTAGENESIS OF SER-1089;
SER-1107 AND GLN-1108.
PubMed=11544179; DOI=10.1101/gad.913001;
Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.;
"Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein
kinase, associates with components of the mRNA surveillance complex
and is involved in the regulation of nonsense-mediated mRNA decay.";
Genes Dev. 15:2215-2228(2001).
[11]
PHOSPHORYLATION.
PubMed=11331269; DOI=10.1074/jbc.C100144200;
Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.;
"Cloning of a novel phosphatidylinositol kinase-related kinase:
characterization of the human SMG-1 RNA surveillance protein.";
J. Biol. Chem. 276:22709-22714(2001).
[12]
INTERACTION WITH UPF2, AND SUBCELLULAR LOCATION.
PubMed=11113196; DOI=10.1128/MCB.21.1.209-223.2001;
Serin G., Gersappe A., Black J.D., Aronoff R., Maquat L.E.;
"Identification and characterization of human orthologues to
Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis
elegans SMG-4).";
Mol. Cell. Biol. 21:209-223(2001).
[13]
IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, AND ASSOCIATION WITH
THE EJC COMPLEX.
PubMed=11546874; DOI=10.1126/science.1062786;
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Communication of the position of exon-exon junctions to the mRNA
surveillance machinery by the protein RNPS1.";
Science 293:1836-1839(2001).
[14]
PHOSPHORYLATION.
PubMed=14636577; DOI=10.1016/S1097-2765(03)00443-X;
Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R.,
Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S.;
"Phosphorylation of hUPF1 induces formation of mRNA surveillance
complexes containing hSMG-5 and hSMG-7.";
Mol. Cell 12:1187-1200(2003).
[15]
INTERACTION WITH EST1A.
PubMed=12554878; DOI=10.1261/rna.2137903;
Chiu S.-Y., Serin G., Ohara O., Maquat L.E.;
"Characterization of human Smg5/7a: a protein with similarities to
Caenorhabditis elegans SMG5 and SMG7 that functions in the
dephosphorylation of Upf1.";
RNA 9:77-87(2003).
[16]
INTERACTION WITH SMG7.
PubMed=15721257; DOI=10.1016/j.molcel.2005.01.010;
Fukuhara N., Ebert J., Unterholzner L., Lindner D., Izaurralde E.,
Conti E.;
"SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay
pathway.";
Mol. Cell 17:537-547(2005).
[17]
FUNCTION, INTERACTION WITH SLBP, AND MUTAGENESIS OF LYS-509 AND
ARG-843.
PubMed=16086026; DOI=10.1038/nsmb972;
Kaygun H., Marzluff W.F.;
"Regulated degradation of replication-dependent histone mRNAs requires
both ATR and Upf1.";
Nat. Struct. Mol. Biol. 12:794-800(2005).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
IDENTIFICATION IN THE SURF COMPLEX, PHOSPHORYLATION AT SER-1089 AND
SER-1107, AND MUTAGENESIS OF CYS-126; LYS-509; SER-1084; SER-1089;
SER-1107 AND SER-1127.
PubMed=16452507; DOI=10.1101/gad.1389006;
Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R.,
Hoshino S., Ohno M., Dreyfuss G., Ohno S.;
"Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon
junction complex triggers Upf1 phosphorylation and nonsense-mediated
mRNA decay.";
Genes Dev. 20:355-367(2006).
[20]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[22]
FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[23]
INTERACTION WITH GSPT2.
PubMed=18447585; DOI=10.1371/journal.pbio.0060111;
Singh G., Rebbapragada I., Lykke-Andersen J.;
"A competition between stimulators and antagonists of Upf complex
recruitment governs human nonsense-mediated mRNA decay.";
PLoS Biol. 6:E111-E111(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
INTERACTION WITH ADAR, AND SUBCELLULAR LOCATION.
PubMed=18362360; DOI=10.1073/pnas.0710576105;
Agranat L., Raitskin O., Sperling J., Sperling R.;
"The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1
interact in the cell nucleus.";
Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
ASSOCIATION WITH THE SMG1C COMPLEX, AND MUTAGENESIS OF CYS-126.
PubMed=19417104; DOI=10.1101/gad.1767209;
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B.,
Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T.,
Kurata R., Hirano H., Anderson P., Ohno S.;
"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
remodeling of the mRNA surveillance complex during nonsense-mediated
mRNA decay.";
Genes Dev. 23:1091-1105(2009).
[28]
SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PNRC2, AND
MUTAGENESIS OF 506-GLY--GLY-508.
PubMed=19150429; DOI=10.1016/j.molcel.2008.11.022;
Cho H., Kim K.M., Kim Y.K.;
"Human proline-rich nuclear receptor coregulatory protein 2 mediates
an interaction between mRNA surveillance machinery and decapping
complex.";
Mol. Cell 33:75-86(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
FUNCTION IN MRNP DISASSEMBLY.
PubMed=21145460; DOI=10.1016/j.cell.2010.11.043;
Franks T.M., Singh G., Lykke-Andersen J.;
"Upf1 ATPase-dependent mRNP disassembly is required for completion of
nonsense- mediated mRNA decay.";
Cell 143:938-950(2010).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; SER-1110 AND
SER-1127, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1110, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565; SER-956 AND
SER-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-31, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1019, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[37]
INTERACTION WITH ZC3H12A, AND MUTAGENESIS OF 647-ASP-GLU-648.
PubMed=26000482; DOI=10.1016/j.cell.2015.04.029;
Mino T., Murakawa Y., Fukao A., Vandenbon A., Wessels H.H., Ori D.,
Uehata T., Tartey S., Akira S., Suzuki Y., Vinuesa C.G., Ohler U.,
Standley D.M., Landthaler M., Fujiwara T., Takeuchi O.;
"Regnase-1 and Roquin regulate a common element in inflammatory mRNAs
by spatiotemporally distinct mechanisms.";
Cell 161:1058-1073(2015).
[38]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 295-914, AND MUTAGENESIS OF
LYS-509; 610-LYS--ARG-612; ARG-615; 647-ASP-GLU-648; GLN-676; ARG-714
AND ARG-876.
PubMed=17159905; DOI=10.1038/sj.emboj.7601464;
Cheng Z., Muhlrad D., Lim M.K., Parker R., Song H.;
"Structural and functional insights into the human Upf1 helicase
core.";
EMBO J. 26:253-264(2007).
[39]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-914 IN COMPLEX WITH UPF2.
PubMed=19556969; DOI=10.1038/emboj.2009.175;
Clerici M., Mourao A., Gutsche I., Gehring N.H., Hentze M.W.,
Kulozik A., Kadlec J., Sattler M., Cusack S.;
"Unusual bipartite mode of interaction between the nonsense-mediated
decay factors, UPF1 and UPF2.";
EMBO J. 28:2293-2306(2009).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 295-925 IN COMPLEX WITH ATP
ANALOG AND RNA, AND FUNCTION.
PubMed=21419344; DOI=10.1016/j.molcel.2011.02.010;
Chakrabarti S., Jayachandran U., Bonneau F., Fiorini F., Basquin C.,
Domcke S., Le Hir H., Conti E.;
"Molecular mechanisms for the RNA-dependent ATPase activity of Upf1
and its regulation by Upf2.";
Mol. Cell 41:693-703(2011).
-!- FUNCTION: RNA-dependent helicase and ATPase required for nonsense-
mediated decay (NMD) of mRNAs containing premature stop codons. Is
recruited to mRNAs upon translation termination and undergoes a
cycle of phosphorylation and dephosphorylation; its
phosphorylation appears to be a key step in NMD. Recruited by
release factors to stalled ribosomes together with the SMG1C
protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-
eRF3) complex. In EJC-dependent NMD, the SURF complex associates
with the exon junction complex (EJC) (located 50-55 or more
nucleotides downstream from the termination codon) through UPF2
and allows the formation of an UPF1-UPF2-UPF3 surveillance complex
which is believed to activate NMD. Phosphorylated UPF1 is
recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to
provide a link to the mRNA degradation machinery involving
exonucleolytic and endonucleolytic pathways, and to serve as
adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1
dephosphorylation and allowing the recycling of NMD factors. UPF1
can also activate NMD without UPF2 or UPF3, and in the absence of
the NMD-enhancing downstream EJC indicative for alternative NMD
pathways. Plays a role in replication-dependent histone mRNA
degradation at the end of phase S; the function is independent of
UPF2. For the recognition of premature termination codons (PTC)
and initiation of NMD a competitive interaction between UPF1 and
PABPC1 with the ribosome-bound release factors is proposed. The
ATPase activity of UPF1 is required for disassembly of mRNPs
undergoing NMD. Essential for embryonic viability.
{ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:16086026,
ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21145460,
ECO:0000269|PubMed:21419344}.
-!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein
(mRNP) complex (PubMed:21419344). Associates with the exon
junction complex (EJC) (PubMed:11546874, PubMed:16452507).
Associates with the SGM1C complex; is phosphorylated by the
complex kinase component SGM1 (PubMed:19417104). Interacts with
UPF2 (PubMed:11163187, PubMed:11073994, PubMed:11113196,
PubMed:19556969). Interacts with UPF3A and UPF3B
(PubMed:11163187). Interacts with EST1A (PubMed:12554878).
Interacts with SLBP (PubMed:16086026). Interacts (when
hyperphosphorylated) with PNRC2 (PubMed:19150429). Interacts with
AGO1 and AGO2 (PubMed:17932509). Interacts with GSPT2
(PubMed:18447585). Interacts with isoform 1 and isoform 5 of
ADAR/ADAR1 (PubMed:18362360). Interacts with SMG7
(PubMed:15721257). Interacts with ZC3H12A; this interaction occurs
in a mRNA translationally active- and termination-dependent manner
and is essential for ZC3H12A-mediated degradation of target mRNAs
(PubMed:26000482). {ECO:0000269|PubMed:11073994,
ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187,
ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12554878,
ECO:0000269|PubMed:15721257, ECO:0000269|PubMed:16086026,
ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:17932509,
ECO:0000269|PubMed:18362360, ECO:0000269|PubMed:18447585,
ECO:0000269|PubMed:19150429, ECO:0000269|PubMed:19417104,
ECO:0000269|PubMed:19556969, ECO:0000269|PubMed:21419344,
ECO:0000269|PubMed:26000482}.
-!- INTERACTION:
Q96AP0:ACD; NbExp=3; IntAct=EBI-373471, EBI-717666;
P55265:ADAR; NbExp=3; IntAct=EBI-373471, EBI-2462104;
Q9NPI6:DCP1A; NbExp=13; IntAct=EBI-373471, EBI-374238;
Q8IU60:DCP2; NbExp=3; IntAct=EBI-373471, EBI-521577;
Q14152:EIF3A; NbExp=5; IntAct=EBI-373492, EBI-366617;
P15170:GSPT1; NbExp=2; IntAct=EBI-373471, EBI-948993;
Q8IYD1:GSPT2; NbExp=3; IntAct=EBI-373471, EBI-3869637;
Q9UN81:L1RE1; NbExp=6; IntAct=EBI-373471, EBI-722458;
Q9NPJ4:PNRC2; NbExp=9; IntAct=EBI-373471, EBI-726549;
Q08491:SKI7 (xeno); NbExp=2; IntAct=EBI-373471, EBI-1389;
Q14493:SLBP; NbExp=3; IntAct=EBI-373471, EBI-2696402;
Q9UPR3:SMG5; NbExp=2; IntAct=EBI-373492, EBI-3400861;
Q86US8:SMG6; NbExp=2; IntAct=EBI-373492, EBI-3232100;
Q92540:SMG7; NbExp=3; IntAct=EBI-373471, EBI-719830;
O95793:STAU1; NbExp=5; IntAct=EBI-373471, EBI-358174;
O14746:TERT; NbExp=3; IntAct=EBI-373471, EBI-1772203;
Q9HAU5:UPF2; NbExp=29; IntAct=EBI-373471, EBI-372073;
Q9H1J1:UPF3A; NbExp=4; IntAct=EBI-373471, EBI-521530;
Q9BZI7:UPF3B; NbExp=10; IntAct=EBI-373471, EBI-372780;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. Nucleus.
Note=Hyperphosphorylated form is targeted to the P-body, while
unphosphorylated protein is distributed throughout the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92900-1; Sequence=Displayed;
Name=2;
IsoId=Q92900-2; Sequence=VSP_003393;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for
kinases from the PI3/PI4-kinase family.
-!- PTM: Phosphorylated by SMG1; required for formation of mRNA
surveillance complexes. {ECO:0000269|PubMed:11331269,
ECO:0000269|PubMed:11544179, ECO:0000269|PubMed:14636577,
ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:19150429}.
-!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA19664.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U65533; AAC50771.1; -; mRNA.
EMBL; U59323; AAC51140.1; -; mRNA.
EMBL; D86988; BAA19664.2; ALT_INIT; mRNA.
EMBL; AF074016; AAC26788.1; -; mRNA.
EMBL; AC003972; AAB94785.1; -; Genomic_DNA.
EMBL; BC039817; AAH39817.1; -; mRNA.
CCDS; CCDS12386.1; -. [Q92900-2]
CCDS; CCDS74315.1; -. [Q92900-1]
RefSeq; NP_001284478.1; NM_001297549.1. [Q92900-1]
RefSeq; NP_002902.2; NM_002911.3. [Q92900-2]
UniGene; Hs.515266; -.
PDB; 2GJK; X-ray; 2.60 A; A=295-925.
PDB; 2GK6; X-ray; 2.40 A; A/B=295-925.
PDB; 2GK7; X-ray; 2.80 A; A=295-925.
PDB; 2IYK; X-ray; 2.95 A; A/B=115-272.
PDB; 2WJV; X-ray; 2.85 A; A/B=115-925.
PDB; 2WJY; X-ray; 2.50 A; A=115-925.
PDB; 2XZO; X-ray; 2.40 A; A=295-925.
PDB; 2XZP; X-ray; 2.72 A; A=295-925.
PDB; 6EJ5; X-ray; 3.34 A; A=295-925.
PDBsum; 2GJK; -.
PDBsum; 2GK6; -.
PDBsum; 2GK7; -.
PDBsum; 2IYK; -.
PDBsum; 2WJV; -.
PDBsum; 2WJY; -.
PDBsum; 2XZO; -.
PDBsum; 2XZP; -.
PDBsum; 6EJ5; -.
ProteinModelPortal; Q92900; -.
SMR; Q92900; -.
BioGrid; 111908; 176.
CORUM; Q92900; -.
DIP; DIP-29875N; -.
IntAct; Q92900; 121.
MINT; Q92900; -.
STRING; 9606.ENSP00000262803; -.
iPTMnet; Q92900; -.
PhosphoSitePlus; Q92900; -.
SwissPalm; Q92900; -.
BioMuta; UPF1; -.
DMDM; 17380291; -.
EPD; Q92900; -.
MaxQB; Q92900; -.
PaxDb; Q92900; -.
PeptideAtlas; Q92900; -.
PRIDE; Q92900; -.
Ensembl; ENST00000262803; ENSP00000262803; ENSG00000005007. [Q92900-2]
Ensembl; ENST00000599848; ENSP00000470142; ENSG00000005007. [Q92900-1]
GeneID; 5976; -.
KEGG; hsa:5976; -.
UCSC; uc002nkf.4; human. [Q92900-1]
CTD; 5976; -.
DisGeNET; 5976; -.
EuPathDB; HostDB:ENSG00000005007.12; -.
GeneCards; UPF1; -.
HGNC; HGNC:9962; UPF1.
HPA; HPA019587; -.
HPA; HPA020857; -.
MIM; 601430; gene.
neXtProt; NX_Q92900; -.
OpenTargets; ENSG00000005007; -.
PharmGKB; PA34328; -.
eggNOG; KOG1802; Eukaryota.
eggNOG; COG1112; LUCA.
GeneTree; ENSGT00800000124068; -.
HOGENOM; HOG000205990; -.
HOVERGEN; HBG061556; -.
InParanoid; Q92900; -.
KO; K14326; -.
OMA; QPCAAQN; -.
OrthoDB; EOG091G01B6; -.
PhylomeDB; Q92900; -.
TreeFam; TF300554; -.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNOR; Q92900; -.
ChiTaRS; UPF1; human.
EvolutionaryTrace; Q92900; -.
GeneWiki; UPF1; -.
GenomeRNAi; 5976; -.
PRO; PR:Q92900; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000005007; -.
CleanEx; HS_UPF1; -.
ExpressionAtlas; Q92900; baseline and differential.
Genevisible; Q92900; HS.
GO; GO:0000785; C:chromatin; IDA:HGNC.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:HGNC.
GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IMP:UniProtKB.
GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IDA:HGNC.
GO; GO:0006260; P:DNA replication; IMP:HGNC.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:HGNC.
GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IMP:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IMP:UniProtKB.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
GO; GO:0032201; P:telomere maintenance via semi-conservative replication; IDA:BHF-UCL.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR018999; RNA-helicase_UPF1_UPF2-interct.
Pfam; PF04851; ResIII; 1.
Pfam; PF09416; UPF1_Zn_bind; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Helicase; Hydrolase; Metal-binding; Methylation;
Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding;
Zinc; Zinc-finger.
CHAIN 1 1129 Regulator of nonsense transcripts 1.
/FTId=PRO_0000080716.
ZN_FING 121 272 UPF1-type.
NP_BIND 506 510 ATP.
REGION 1 415 Sufficient for interaction with RENT2.
MOTIF 1089 1090 [ST]-Q motif 1.
MOTIF 1107 1108 [ST]-Q motif 2.
COMPBIAS 47 80 Ala/Gly/Pro-rich.
COMPBIAS 1042 1129 Gln/Ser-rich.
BINDING 486 486 ATP.
BINDING 676 676 ATP.
BINDING 713 713 ATP.
BINDING 844 844 ATP.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 956 956 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1019 1019 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1089 1089 Phosphoserine.
{ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MOD_RES 1110 1110 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1127 1127 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 353 363 Missing (in isoform 2).
{ECO:0000303|PubMed:10454541,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8855285,
ECO:0000303|PubMed:9064659}.
/FTId=VSP_003393.
VARIANT 69 69 A -> S (in dbSNP:rs17339451).
{ECO:0000269|PubMed:9039502}.
/FTId=VAR_056207.
MUTAGEN 126 126 C->S: Abolishes ability to interact with
UPF2/RENT2 and copurifies with greater
amounts of SMG1, SMG8 and SMG9.
{ECO:0000269|PubMed:16452507,
ECO:0000269|PubMed:19417104}.
MUTAGEN 506 508 GTG->RTE: Prevents dephosphorylation and
targets the protein to the P-body.
{ECO:0000269|PubMed:19150429}.
MUTAGEN 509 509 K->A: Inhibits histone mRNA degradation,
ATPase activity and ATP binding.
{ECO:0000269|PubMed:16086026,
ECO:0000269|PubMed:16452507,
ECO:0000269|PubMed:17159905}.
MUTAGEN 610 611 KR->AA: Impairs RNA binding.
MUTAGEN 615 615 R->A: Impairs RNA binding.
{ECO:0000269|PubMed:17159905}.
MUTAGEN 647 648 DE->AA: Loss of ATPase activity and
helicase activity.
{ECO:0000269|PubMed:10999600,
ECO:0000269|PubMed:17159905}.
MUTAGEN 647 648 DE->AA: Loss of ATPase activity and
helicase activity. Inhibits ZC3H12A-
mediated IL6 mRNA degradation.
{ECO:0000269|PubMed:10999600,
ECO:0000269|PubMed:17159905,
ECO:0000269|PubMed:26000482}.
MUTAGEN 676 676 Q->A: Impairs ATPase activity, no effect
on ATP binding.
{ECO:0000269|PubMed:17159905}.
MUTAGEN 714 714 R->A: Impairs ATPase activity and ATP
binding. {ECO:0000269|PubMed:17159905}.
MUTAGEN 843 843 R->A: Inhibits histone mRNA degradation.
{ECO:0000269|PubMed:11163187,
ECO:0000269|PubMed:16086026}.
MUTAGEN 843 843 R->C: Abolishes NMD.
{ECO:0000269|PubMed:11163187,
ECO:0000269|PubMed:16086026}.
MUTAGEN 876 876 R->A: Impairs ATPase activity and ATP
binding. {ECO:0000269|PubMed:17159905}.
MUTAGEN 1084 1084 S->A: Impairs association with UPF2, SMG1
and SMG7 and impairs phosphorylation;
when associated with A-1089, A-1107 and
A-1127. {ECO:0000269|PubMed:16452507}.
MUTAGEN 1089 1089 S->A: Impairs association with UPF2, SMG1
and SMG7 and impairs phosphorylation;
when associated with A-1084, A-1107 and
A-1127. {ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MUTAGEN 1089 1089 S->A: Still phosphorylated but with less
efficiency. {ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MUTAGEN 1107 1107 S->A: Impairs association with UPF2, SMG1
and SMG7 and impairs phosphorylation;
when associated with A-1084, A-1089 and
A-1127. {ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MUTAGEN 1107 1107 S->A: Impairs phosphorylation.
{ECO:0000269|PubMed:11544179,
ECO:0000269|PubMed:16452507}.
MUTAGEN 1108 1108 Q->N: Impairs phosphorylation.
{ECO:0000269|PubMed:11544179}.
MUTAGEN 1127 1127 S->A: Impairs association with UPF2, SMG1
and SMG7 and impairs phosphorylation;
when associated with A-1084, A-1089 and
A-1107. {ECO:0000269|PubMed:16452507}.
CONFLICT 61 61 G -> S (in Ref. 2; AAC51140).
{ECO:0000305}.
CONFLICT 466 466 I -> T (in Ref. 2; AAC51140).
{ECO:0000305}.
CONFLICT 478 478 G -> A (in Ref. 1; AAC50771).
{ECO:0000305}.
CONFLICT 524 524 G -> D (in Ref. 1; AAC50771).
{ECO:0000305}.
CONFLICT 557 557 A -> P (in Ref. 1; AAC50771).
{ECO:0000305}.
CONFLICT 901 902 NY -> IF (in Ref. 1; AAC50771).
{ECO:0000305}.
TURN 124 126 {ECO:0000244|PDB:2WJY}.
HELIX 131 133 {ECO:0000244|PDB:2WJY}.
STRAND 134 137 {ECO:0000244|PDB:2WJY}.
TURN 138 141 {ECO:0000244|PDB:2WJY}.
STRAND 142 146 {ECO:0000244|PDB:2WJY}.
STRAND 151 153 {ECO:0000244|PDB:2WJY}.
HELIX 155 163 {ECO:0000244|PDB:2WJY}.
STRAND 168 170 {ECO:0000244|PDB:2WJY}.
STRAND 174 176 {ECO:0000244|PDB:2WJV}.
TURN 184 186 {ECO:0000244|PDB:2WJY}.
TURN 191 193 {ECO:0000244|PDB:2WJY}.
STRAND 195 197 {ECO:0000244|PDB:2WJY}.
STRAND 200 202 {ECO:0000244|PDB:2WJV}.
STRAND 204 209 {ECO:0000244|PDB:2WJV}.
TURN 210 213 {ECO:0000244|PDB:2WJY}.
TURN 216 218 {ECO:0000244|PDB:2WJV}.
TURN 220 222 {ECO:0000244|PDB:2IYK}.
HELIX 226 228 {ECO:0000244|PDB:2WJV}.
STRAND 230 233 {ECO:0000244|PDB:2WJY}.
STRAND 235 238 {ECO:0000244|PDB:2WJY}.
TURN 240 242 {ECO:0000244|PDB:2WJY}.
HELIX 248 253 {ECO:0000244|PDB:2WJY}.
HELIX 259 269 {ECO:0000244|PDB:2WJY}.
HELIX 299 321 {ECO:0000244|PDB:2XZO}.
STRAND 326 329 {ECO:0000244|PDB:2GK6}.
STRAND 332 335 {ECO:0000244|PDB:2XZO}.
TURN 337 339 {ECO:0000244|PDB:2GJK}.
STRAND 341 345 {ECO:0000244|PDB:2XZO}.
HELIX 364 366 {ECO:0000244|PDB:2XZP}.
STRAND 372 377 {ECO:0000244|PDB:2XZO}.
STRAND 379 382 {ECO:0000244|PDB:2XZO}.
STRAND 385 393 {ECO:0000244|PDB:2XZO}.
STRAND 396 398 {ECO:0000244|PDB:2GK7}.
STRAND 402 407 {ECO:0000244|PDB:2XZO}.
STRAND 410 412 {ECO:0000244|PDB:2GJK}.
STRAND 418 425 {ECO:0000244|PDB:2XZO}.
HELIX 429 443 {ECO:0000244|PDB:2XZO}.
HELIX 450 456 {ECO:0000244|PDB:2XZO}.
HELIX 484 493 {ECO:0000244|PDB:2XZO}.
STRAND 497 502 {ECO:0000244|PDB:2XZO}.
HELIX 509 522 {ECO:0000244|PDB:2XZO}.
STRAND 523 525 {ECO:0000244|PDB:2GK6}.
STRAND 528 534 {ECO:0000244|PDB:2XZO}.
HELIX 535 547 {ECO:0000244|PDB:2XZO}.
STRAND 552 554 {ECO:0000244|PDB:2XZO}.
HELIX 558 560 {ECO:0000244|PDB:2XZO}.
HELIX 568 570 {ECO:0000244|PDB:2XZO}.
HELIX 572 577 {ECO:0000244|PDB:2XZO}.
HELIX 582 591 {ECO:0000244|PDB:2XZO}.
TURN 593 595 {ECO:0000244|PDB:2WJY}.
HELIX 600 620 {ECO:0000244|PDB:2XZO}.
STRAND 622 627 {ECO:0000244|PDB:2XZO}.
HELIX 630 632 {ECO:0000244|PDB:2XZO}.
HELIX 634 636 {ECO:0000244|PDB:2XZO}.
STRAND 642 646 {ECO:0000244|PDB:2XZO}.
HELIX 649 651 {ECO:0000244|PDB:2XZO}.
HELIX 654 661 {ECO:0000244|PDB:2XZO}.
TURN 662 664 {ECO:0000244|PDB:2XZO}.
STRAND 665 672 {ECO:0000244|PDB:2XZO}.
HELIX 684 688 {ECO:0000244|PDB:2XZO}.
TURN 689 692 {ECO:0000244|PDB:2XZO}.
HELIX 695 702 {ECO:0000244|PDB:2XZO}.
HELIX 717 727 {ECO:0000244|PDB:2XZO}.
STRAND 733 736 {ECO:0000244|PDB:2XZO}.
HELIX 739 741 {ECO:0000244|PDB:2XZO}.
STRAND 751 754 {ECO:0000244|PDB:2GK7}.
STRAND 757 761 {ECO:0000244|PDB:2XZO}.
STRAND 766 768 {ECO:0000244|PDB:2GJK}.
STRAND 770 773 {ECO:0000244|PDB:2WJY}.
STRAND 775 777 {ECO:0000244|PDB:2GJK}.
HELIX 778 794 {ECO:0000244|PDB:2XZO}.
HELIX 798 800 {ECO:0000244|PDB:2XZO}.
STRAND 801 806 {ECO:0000244|PDB:2XZO}.
HELIX 808 819 {ECO:0000244|PDB:2XZO}.
HELIX 826 830 {ECO:0000244|PDB:2XZO}.
STRAND 832 836 {ECO:0000244|PDB:2XZO}.
TURN 837 842 {ECO:0000244|PDB:2XZO}.
STRAND 845 851 {ECO:0000244|PDB:2XZO}.
STRAND 857 859 {ECO:0000244|PDB:2XZO}.
HELIX 862 865 {ECO:0000244|PDB:2XZO}.
HELIX 867 874 {ECO:0000244|PDB:2XZO}.
STRAND 875 885 {ECO:0000244|PDB:2XZO}.
HELIX 887 890 {ECO:0000244|PDB:2XZO}.
HELIX 894 905 {ECO:0000244|PDB:2XZO}.
STRAND 909 912 {ECO:0000244|PDB:2XZO}.
HELIX 914 916 {ECO:0000244|PDB:2XZO}.
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


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OBT1801 Regulator of Nonsense Transcripts 1 (RENT1) encoded within exons 5 & 6, Nonsense mRNA reducing factor 1 (NORF1), Human Up_Frameshift Suppressor 1 homolog ( HUPF1), delta helicase, Goat anti_Human, Mou 0.1 mg.
OBT1801 Regulator of Nonsense Transcripts 1 (RENT1) encoded within exons 5 & 6, Nonsense mRNA reducing factor 1 (NORF1), Human Up_Frameshift Suppressor 1 homolog ( HUPF1), delta helicase, Goat anti_Human, Mou 0.1 mg.
OBT1802 Regulator of Nonsense Transcripts 1 (RENT1) encoded within exons 19 & 20, Nonsense mRNA reducing factor 1 (NORF1), Human Up_Frameshift Suppressor 1 homolog ( HUPF1), delta helicase, Goat anti_Human, M 0.1 mg.
OBT1803 Regulator of Nonsense Transcripts 1 (RENT1) portion of the C_terminus, Nonsense mRNA reducing factor 1 (NORF1), Human Up_Frameshift Suppressor 1 homolog ( HUPF1), delta helicase, Goat anti_Human, Mous 0.1 mg.
OBT1803 Regulator of Nonsense Transcripts 1 (RENT1) portion of the C_terminus, Nonsense mRNA reducing factor 1 (NORF1), Human Up_Frameshift Suppressor 1 homolog ( HUPF1), delta helicase, Goat anti_Human, Mous 0.1 mg.
EIAAB34256 Homo sapiens,Human,hUpf3B,hUpf3p-X,Nonsense mRNA reducing factor 3B,Regulator of nonsense transcripts 3B,RENT3B,UPF3B,UPF3X,Up-frameshift suppressor 3 homolog B,Up-frameshift suppressor 3 homolog on c
EIAAB34255 Homo sapiens,Human,hUpf3,Nonsense mRNA reducing factor 3A,Regulator of nonsense transcripts 3A,RENT3A,UPF3,UPF3A,Up-frameshift suppressor 3 homolog A
EIAAB34270 Homo sapiens,Human,hUpf2,KIAA1408,Nonsense mRNA reducing factor 2,Regulator of nonsense transcripts 2,RENT2,UPF2,Up-frameshift suppressor 2 homolog
201-20-6268 UPF3A{UPF3 regulator of nonsense transcripts homolog A (yeast)}rabbit.pAb 0.2ml
GWB-B573B2 Anti- UPF3B (UPF3 regulator of nonsense transcripts homolog B (yeast)) Antibody
UPF3A UPF3A Gene UPF3 regulator of nonsense transcripts homolog A (yeast)
UPF3B UPF3B Gene UPF3 regulator of nonsense transcripts homolog B (yeast)
ARP36350_P050 UPF1(UPF1 regulator of nonsense transcripts homolog (yeast)) 50 µg
FZD2_RAT Human ELISA Kit FOR Regulator of nonsense transcripts 3B 96T
TSN1_MOUSE Human ELISA Kit FOR Regulator of nonsense transcripts 3B 96T
WAPL_MOUSE Human ELISA Kit FOR Regulator of nonsense transcripts 3A 96T
E0105b Human ELISA Kit FOR Regulator of nonsense transcripts 3B 96T
E3034h Human Regulator Of Nonsense Transcripts 1 ELISA Ki 96T
E3035h Human Regulator Of Nonsense Transcripts 2 ELISA Ki 96T
E3036h Human Regulator Of Nonsense Transcripts 3A ELISA K 96T
E0739m Human ELISA Kit FOR Regulator of nonsense transcripts 3A 96T
RENT1_HUMAN Human ELISA Kit FOR Regulator of nonsense transcripts 1 96T


 

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