{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q92900","secondaryAccessions":["O00239","O43343","Q86Z25","Q92842"],"uniProtkbId":"RENT1_HUMAN","entryAudit":{"firstPublicDate":"2001-10-18","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-10-18","entryVersion":235,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9962"}],"value":"Regulator of nonsense transcripts 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30218034"}],"value":"5.6.2.3"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"}],"value":"5.6.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9EPU0"}],"value":"ATP-dependent helicase RENT1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Double-stranded nucleic acid 5'-3' helicase UPF1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9962"}],"value":"Nonsense mRNA reducing factor 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9962"}],"value":"NORF1"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9064659"}],"value":"Up-frameshift suppressor 1 homolog"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9064659"}],"value":"hUpf1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9962"}],"value":"UPF1"},"synonyms":[{"value":"KIAA0221"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9962"}],"value":"RENT1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9EPU0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11544179"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16086026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18066079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18172165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18447585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19417104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21145460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23275559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24726324"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25220460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30218034"}],"value":"RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and which modulates the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). ATP-dependent 5'-3' helicase active on RNA:DNA substrates with a 5'-RNA extension (PubMed:18066079, PubMed:21419344, PubMed:23275559, PubMed:26138914). ATP-dependent 5'-3' helicase active on RNA:RNA substrates with a 5'-RNA extension (PubMed:26138914). ATP-dependent 5'-3' helicase active on DNA:DNA substrates with a 5'-DNA extension (PubMed:10999600, PubMed:26138914, PubMed:30218034). 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 (PubMed:11544179, PubMed:25220460). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). 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 (PubMed:21419344). 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 (PubMed:12554878). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (PubMed:18447585). Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (PubMed:16086026, PubMed:18172165). 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 (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (PubMed:21145460). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (By similarity). Has ssDNA-stimulated ATPase activity (poly(dT) and poly(dA) are most stimulatory) (PubMed:10999600). Binds RNA; addition of ATP decreases RNA-binding (PubMed:10999600, PubMed:18066079, PubMed:21419344)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"n ATP + n H2O + wound RNA = n ADP + n phosphate + unwound RNA.","ecNumber":"5.6.2.5","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30218034"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21145460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30218034"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"}],"value":"Binds 1 Mg(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556969"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556969"}],"value":"Binds 3 Zn(2+) per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18066079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23275559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"}],"value":"The helicase domain is maintained in an inactive state by intramolecular interactions with its N- and C-terminal domains (PubMed:23275559). UPF2 and UPF3B together stimulate both the ATPase and 5'-3' RNA:DNA helicase activities of this protein (PubMed:18066079). UPF2 alone stimulates the ATPase and 5'-3' RNA:DNA helicase activities of UPF1 missing the CH-rich domain (PubMed:21419344, PubMed:26138914). The N-terminal CH-rich domain inhibits the 5'-3' helicase activity (PubMed:18066079, PubMed:21419344, PubMed:26138914). The C-terminal SQ domain also inhibits the 5'-3' helicase activity (PubMed:23275559)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"}],"value":"Optimum pH is 5.0 for ATPase, active from pH 4.0 to 7.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9EPU0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10999600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11073994"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11113196"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11546874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12554878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15721257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16086026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16452507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17932509"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18066079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18362360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18447585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19150429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19417104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19556969"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19864460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23275559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24726324"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25220460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26000482"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26841701"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27974568"}],"value":"Monomeric in solution (PubMed:10999600, PubMed:26138914). Forms a trimeric UPF complex where UPF2 bridges UPF1 and UPF3B; UPF2 contacts the N-terminal CH-rich domain of UPF1 and the N-terminus of UPF3B (PubMed:18066079). The trimeric UPF complex interacts with the EJC core complex (PubMed:18066079). 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). Part of a complex composed of SMG1, DHX34 and UPF1; within the complex DHX34 acts as a scaffolding protein to facilitate SMG1 phosphorylation of UPF1 (PubMed:26841701). Interacts with UPF2 via the CH-rich domain (PubMed:11073994, PubMed:11113196, PubMed:11163187, PubMed:19556969, PubMed:23275559). 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). Interacts with CPSF6 (PubMed:19864460). Interacts with MOV10; the interaction is direct and RNA-dependent (PubMed:24726324). Interacts with SHFL; the interaction increases in the presence of RNA (PubMed:27974568). Interacts with UPF2 and DDX4; interactions are mediated by TDRD6 (PubMed:25220460). Interacts with DHX34 and PABPC1/PABP1; the interactions are RNA-independent (PubMed:25220460). Interacts with RBM46 (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29382845"}],"value":"(Microbial infection) Interacts with human T-cell leukemia virus 1/HTLV-1 protein Tax; this interaction inhibits the host nonsense-mediated mRNA decay (NMD)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q96AP0","geneName":"ACD","intActId":"EBI-717666"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"P55265","geneName":"ADAR","intActId":"EBI-2462104"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9NPI6","geneName":"DCP1A","intActId":"EBI-374238"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q8IU60","geneName":"DCP2","intActId":"EBI-521577"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9NZB2","geneName":"FAM120A","intActId":"EBI-1171960"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"P15170","geneName":"GSPT1","intActId":"EBI-948993"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q8IYD1","geneName":"GSPT2","intActId":"EBI-3869637"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9UN81","geneName":"L1RE1","intActId":"EBI-722458"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9NPJ4","geneName":"PNRC2","intActId":"EBI-726549"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q14493","geneName":"SLBP","intActId":"EBI-2696402"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q92540","geneName":"SMG7","intActId":"EBI-719830"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"O95793","geneName":"STAU1","intActId":"EBI-358174"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q7Z422","geneName":"SZRD1","intActId":"EBI-2874567"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"O14746","geneName":"TERT","intActId":"EBI-1772203"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9HAU5","geneName":"UPF2","intActId":"EBI-372073"},"numberOfExperiments":30,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9H1J1","geneName":"UPF3A","intActId":"EBI-521530"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q9BZI7","geneName":"UPF3B","intActId":"EBI-372780"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900","intActId":"EBI-373471"},"interactantTwo":{"uniProtKBAccession":"Q08491","geneName":"SKI7","intActId":"EBI-1389"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q92900-2","intActId":"EBI-373492"},"interactantTwo":{"uniProtKBAccession":"Q14152","geneName":"EIF3A","intActId":"EBI-366617"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900-2","intActId":"EBI-373492"},"interactantTwo":{"uniProtKBAccession":"Q9UPR3","geneName":"SMG5","intActId":"EBI-3400861"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900-2","intActId":"EBI-373492"},"interactantTwo":{"uniProtKBAccession":"Q86US8","geneName":"SMG6","intActId":"EBI-3232100"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q92900-2","intActId":"EBI-373492"},"interactantTwo":{"uniProtKBAccession":"Q9HAU5","geneName":"UPF2","intActId":"EBI-372073"},"numberOfExperiments":9,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9EPU0"}],"value":"Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm. Localized in the chromatoid bodies of round spermatids (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9064659"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"value":"Cytoplasm, P-body","id":"SL-0230"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11163187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18362360"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9EPU0"}],"value":"Cytoplasm, perinuclear region","id":"SL-0198"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q92900-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q92900-2"],"sequenceIds":["VSP_003393"],"isoformSequenceStatus":"Described"}]},{"texts":[{"value":"Ubiquitous"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18066079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21419344"}],"value":"The CH-rich domain contacts UPF2 and inhibits both the ATPase and 5'-3' RNA:DNA helicase activities of this protein (PubMed:18066079, PubMed:26138914). It increases RNA-binding by the helicase domain (PubMed:21419344). The isolated CH-rich domain has no RNA-binding or ATPase activity (PubMed:18066079). Comparison with a yeast structure that includes the CH-rich domain suggests the CH-rich domain docks RNA into the protein, increasing RNA binding and thus decreasing ATPase activity (Probable). The CH-rich domain probably binds to the same region of UPF1 as UPF2 (Probable). Deletion of the CH-rich domain increases ATPase activity and 5'-3' helicase activity dramatically (PubMed:18066079, PubMed:21419344)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26138914"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30218034"}],"value":"Helicase activity (of the isolated helicase domain (HD) or the HD plus the CH-rich domain) is slow but highly processive, capable of translocating on ssDNA, may be able to unwind over 10 kb of dsDNA, and translocates through protein-bound sequences, allowing it to remodel ribonucleoprotein complexes"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21419344"}],"value":"The two helicase domains face each other and sandwich ATP at one end of the molecule; they form an interface which binds extended RNA at the other end of protein"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11544179"}],"value":"The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23275559"}],"value":"The SQ domain (serine-glutamine clusters) inhibits the 5'-3' RNA:DNA helicase, ATPase and RNA-binding activities of this protein; deletion of the SQ domain increases helicase activity about 6-fold (PubMed:23275559). Protein phosphorylation does not prevent the SQ domain from inhibiting the helicase activity (PubMed:23275559)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11331269"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11544179"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14636577"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16452507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19150429"}],"value":"Phosphorylated by SMG1; required for formation of mRNA surveillance complexes"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the DNA2/NAM7 helicase family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA19664.2","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1129,"modifier":"EXACT"}},"description":"Regulator of nonsense transcripts 1","featureId":"PRO_0000080716"},{"type":"Domain","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Upf1 CH-rich","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01341"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18066079"}]},{"type":"Domain","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"UPF1-type SF1B helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01433"}]},{"type":"Domain","location":{"start":{"value":710,"modifier":"EXACT"},"end":{"value":922,"modifier":"EXACT"}},"description":"UPF1-type SF1B helicase 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