ID RENT2_HUMAN Reviewed; 1272 AA. AC Q9HAU5; A6NLJ5; D3DRS0; Q14BM1; Q5W0J4; Q8N8U1; Q9H1J2; Q9NWL1; Q9P2D9; AC Q9Y4M9; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 192. DE RecName: Full=Regulator of nonsense transcripts 2 {ECO:0000312|HGNC:HGNC:17854}; DE AltName: Full=Up-frameshift suppressor 2 homolog {ECO:0000250|UniProtKB:P38798}; DE Short=hUpf2; GN Name=UPF2 {ECO:0000312|HGNC:HGNC:17854}; GN Synonyms=KIAA1408, RENT2 {ECO:0000312|HGNC:HGNC:17854}; 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], INTERACTION WITH UPF1; EIF4A1 AND EIF1, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Heart; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, RP INTERACTION WITH UPF1; UPF3A AND UPF3B, AND SUBCELLULAR LOCATION. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UPF1; UPF3A AND UPF3B, AND RP SUBCELLULAR LOCATION. RC TISSUE=Cervix carcinoma; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 1023-1272. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-1272. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP INTERACTION WITH SMG1. 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 IDENTIFICATION IN A POST-SPLICING MRNP 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 [12] RP 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 [13] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND IDENTIFICATION IN A COMPLEX RP WITH UPF3B AND RNPS1. RX PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012; RA Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., RA Kulozik A.E.; RT "Exon-junction complex components specify distinct routes of nonsense- RT mediated mRNA decay with differential cofactor requirements."; RL Mol. Cell 20:65-75(2005). RN [14] RP SUBUNIT, AND MUTAGENESIS OF GLU-858. 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 [15] RP FUNCTION, AND RECONSTITUTION OF THE EJC CORE-UPF COMPLEX. RX PubMed=18066079; DOI=10.1038/nsmb1330; RA Chamieh H., Ballut L., Bonneau F., Le Hir H.; RT "NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and RT stimulate its RNA helicase activity."; RL Nat. Struct. Mol. Biol. 15:85-93(2008). RN [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1088, AND IDENTIFICATION BY RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1088, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [19] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 768-1015 IN COMPLEX WITH UPF3B RP RNP-LIKE DOMAIN, RNA-BINDING, AND MUTAGENESIS OF 796-ARG-ARG-797; ASP-847; RP 851-GLU-ASP-852; ARG-854; GLU-858; TYR-894 AND TYR-932. RX PubMed=15004547; DOI=10.1038/nsmb741; RA Kadlec J., Izaurralde E., Cusack S.; RT "The structural basis for the interaction between nonsense-mediated mRNA RT decay factors UPF2 and UPF3."; RL Nat. Struct. Mol. Biol. 11:330-337(2004). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1105-1198 IN COMPLEX WITH UPF1, RP AND MUTAGENESIS OF PHE-1113; MET-1120; MET-1121; GLU-1123; MET-1169; RP PHE-1171; MET-1173; LEU-1174 AND ARG-1176. 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). CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing CC premature stop codons by associating with the nuclear exon junction CC complex (EJC). Recruited by UPF3B associated with the EJC core at the CC cytoplasmic side of the nuclear envelope and the subsequent formation CC of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to CC release factors at the stalled ribosome) is believed to activate NMD. CC In cooperation with UPF3B stimulates both ATPase and RNA helicase CC activities of UPF1. Binds spliced mRNA. {ECO:0000269|PubMed:11163187, CC ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:18066079}. CC -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP) CC complex. Associates with the exon junction complex (EJC). Interacts CC with SMG1, EST1A, UPF1, UPF3A, UPF3B, EIF4A1 and EIF1. CC {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, CC ECO:0000269|PubMed:11163187, ECO:0000269|PubMed:11544179, CC ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12554878, CC ECO:0000269|PubMed:15004547, ECO:0000269|PubMed:16209946, CC ECO:0000269|PubMed:16452507, ECO:0000269|PubMed:19556969}. CC -!- INTERACTION: CC Q9HAU5; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-372073, EBI-1053259; CC Q9HAU5; Q96Q15: SMG1; NbExp=7; IntAct=EBI-372073, EBI-1049832; CC Q9HAU5; Q92900: UPF1; NbExp=29; IntAct=EBI-372073, EBI-373471; CC Q9HAU5; Q92900-2: UPF1; NbExp=9; IntAct=EBI-372073, EBI-373492; CC Q9HAU5; Q9H1J1: UPF3A; NbExp=5; IntAct=EBI-372073, EBI-521530; CC Q9HAU5; Q9BZI7: UPF3B; NbExp=8; IntAct=EBI-372073, EBI-372780; CC Q9HAU5; Q9BZI7-2: UPF3B; NbExp=7; IntAct=EBI-372073, EBI-15674130; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, CC ECO:0000269|PubMed:11163187}. Cytoplasm {ECO:0000250|UniProtKB:A2AT37}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11073994}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92646.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04721.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF301013; AAG33225.1; -; mRNA. DR EMBL; AY013249; AAG48509.1; -; mRNA. DR EMBL; AF318574; AAG60689.1; -; mRNA. DR EMBL; AB037829; BAA92646.1; ALT_INIT; mRNA. DR EMBL; AK000764; BAA91369.1; -; mRNA. DR EMBL; AK096191; BAC04721.1; ALT_SEQ; mRNA. DR EMBL; AC073160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138898; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645617; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86329.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86330.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86332.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86333.1; -; Genomic_DNA. DR EMBL; BC114964; AAI14965.1; -; mRNA. DR EMBL; BC115737; AAI15738.1; -; mRNA. DR EMBL; AL080198; CAB45771.1; -; mRNA. DR CCDS; CCDS7086.1; -. DR PIR; T12507; T12507. DR RefSeq; NP_056357.1; NM_015542.3. DR RefSeq; NP_542166.1; NM_080599.2. DR PDB; 1UW4; X-ray; 1.95 A; B/D=768-1015. DR PDB; 2WJV; X-ray; 2.85 A; D/E=1105-1198. DR PDB; 4CEK; X-ray; 2.35 A; A=455-757. DR PDB; 4CEM; X-ray; 2.60 A; A/B=121-486. DR PDB; 7NWU; X-ray; 2.60 A; B/D/F/H=767-1017. DR PDB; 7QG6; X-ray; 2.95 A; B/D/F/H=761-1054. DR PDBsum; 1UW4; -. DR PDBsum; 2WJV; -. DR PDBsum; 4CEK; -. DR PDBsum; 4CEM; -. DR PDBsum; 7NWU; -. DR PDBsum; 7QG6; -. DR AlphaFoldDB; Q9HAU5; -. DR EMDB; EMD-2665; -. DR EMDB; EMD-2666; -. DR SMR; Q9HAU5; -. DR BioGRID; 117490; 179. DR CORUM; Q9HAU5; -. DR DIP; DIP-31148N; -. DR IntAct; Q9HAU5; 45. DR MINT; Q9HAU5; -. DR STRING; 9606.ENSP00000348708; -. DR MoonDB; Q9HAU5; Predicted. DR CarbonylDB; Q9HAU5; -. DR GlyGen; Q9HAU5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9HAU5; -. DR MetOSite; Q9HAU5; -. DR PhosphoSitePlus; Q9HAU5; -. DR SwissPalm; Q9HAU5; -. DR BioMuta; UPF2; -. DR DMDM; 60390647; -. DR EPD; Q9HAU5; -. DR jPOST; Q9HAU5; -. DR MassIVE; Q9HAU5; -. DR MaxQB; Q9HAU5; -. DR PaxDb; 9606-ENSP00000348708; -. DR PeptideAtlas; Q9HAU5; -. DR Pumba; Q9HAU5; -. DR Antibodypedia; 24600; 195 antibodies from 26 providers. DR DNASU; 26019; -. DR Ensembl; ENST00000356352.6; ENSP00000348708.2; ENSG00000151461.20. DR Ensembl; ENST00000357604.10; ENSP00000350221.5; ENSG00000151461.20. DR Ensembl; ENST00000397053.6; ENSP00000380244.2; ENSG00000151461.20. DR GeneID; 26019; -. DR KEGG; hsa:26019; -. DR MANE-Select; ENST00000357604.10; ENSP00000350221.5; NM_015542.4; NP_056357.1. DR UCSC; uc001ila.3; human. DR AGR; HGNC:17854; -. DR CTD; 26019; -. DR DisGeNET; 26019; -. DR GeneCards; UPF2; -. DR HGNC; HGNC:17854; UPF2. DR HPA; ENSG00000151461; Low tissue specificity. DR MIM; 605529; gene. DR neXtProt; NX_Q9HAU5; -. DR OpenTargets; ENSG00000151461; -. DR PharmGKB; PA134945630; -. DR VEuPathDB; HostDB:ENSG00000151461; -. DR eggNOG; KOG2051; Eukaryota. DR GeneTree; ENSGT00530000064318; -. DR HOGENOM; CLU_002633_2_1_1; -. DR InParanoid; Q9HAU5; -. DR OMA; DFQHHQI; -. DR OrthoDB; 276824at2759; -. DR PhylomeDB; Q9HAU5; -. DR TreeFam; TF300543; -. DR PathwayCommons; Q9HAU5; -. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q9HAU5; -. DR SIGNOR; Q9HAU5; -. DR BioGRID-ORCS; 26019; 779 hits in 1178 CRISPR screens. DR ChiTaRS; UPF2; human. DR EvolutionaryTrace; Q9HAU5; -. DR GeneWiki; UPF2; -. DR GenomeRNAi; 26019; -. DR Pharos; Q9HAU5; Tbio. DR PRO; PR:Q9HAU5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9HAU5; Protein. DR Bgee; ENSG00000151461; Expressed in sural nerve and 218 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005844; C:polysome; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:HGNC-UCL. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB. DR DisProt; DP00949; -. DR Gene3D; 1.25.40.180; -; 3. DR Gene3D; 4.10.80.160; -; 1. DR Gene3D; 6.10.250.770; -; 1. DR IDEAL; IID00252; -. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR003890; MIF4G-like_typ-3. DR InterPro; IPR039762; Nmd2/UPF2. DR InterPro; IPR007193; Upf2/Nmd2_C. DR PANTHER; PTHR12839; NONSENSE-MEDIATED MRNA DECAY PROTEIN 2 UP-FRAMESHIFT SUPPRESSOR 2; 1. DR PANTHER; PTHR12839:SF7; REGULATOR OF NONSENSE TRANSCRIPTS 2; 1. DR Pfam; PF02854; MIF4G; 3. DR Pfam; PF04050; Upf2; 1. DR SMART; SM00543; MIF4G; 3. DR SUPFAM; SSF48371; ARM repeat; 3. DR Genevisible; Q9HAU5; HS. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; KW Phosphoprotein; Reference proteome; Repeat; RNA-binding. FT CHAIN 1..1272 FT /note="Regulator of nonsense transcripts 2" FT /id="PRO_0000097248" FT DOMAIN 168..431 FT /note="MIF4G 1" FT DOMAIN 569..758 FT /note="MIF4G 2" FT DOMAIN 773..986 FT /note="MIF4G 3" FT REGION 1..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 94..133 FT /note="Sufficient for interaction with UPF1" FT REGION 370..389 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 423..445 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 490..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 711..928 FT /note="Sufficient for interaction with UPF3A and UPF3B" FT REGION 757..1272 FT /note="Sufficient for interaction with EIF4A1 and EIF1" FT /evidence="ECO:0000269|PubMed:11073994" FT REGION 839..859 FT /note="Binds to UPF3B" FT REGION 1018..1098 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1084..1272 FT /note="Sufficient for interaction with UPF1 C-terminus" FT REGION 1105..1198 FT /note="Necessary for interaction with UPF1" FT REGION 1105..1129 FT /note="Interaction with UPF1" FT REGION 1167..1207 FT /note="Interaction with UPF1" FT REGION 1220..1272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 54..134 FT /evidence="ECO:0000255" FT COILED 487..559 FT /evidence="ECO:0000255" FT COMPBIAS 1025..1078 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1079..1097 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1088 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VARIANT 496 FT /note="N -> S (in dbSNP:rs7079388)" FT /id="VAR_024345" FT MUTAGEN 796..797 FT /note="RK->EE: Strongly impairs RNA-binding." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 847 FT /note="D->K: Does not abolish interaction with UPF3B." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 851..852 FT /note="ED->KR: Does not abolish interaction with UPF3B. FT Does not abolish interaction with UPF3B; when associated FT with D-854." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 854 FT /note="R->D: Does not abolish interaction with UPF3B; when FT associated with K-851 and R-852." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 858 FT /note="E->R: Abolishes interaction with UPF3B and FT association with SMG1 and RBM8A; reduces phosphorylation of FT UPF1." FT /evidence="ECO:0000269|PubMed:15004547, FT ECO:0000269|PubMed:16452507" FT MUTAGEN 894 FT /note="Y->A: Does not impair RNA-binding; when associated FT with A-932." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 932 FT /note="Y->A: Does not impair RNA-binding; when associated FT with A-894." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 1113 FT /note="F->E: Abolishes interaction with UPF1." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1120 FT /note="M->E: Decreases interaction with UPF1; does not FT reduce NMD efficiency." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1121 FT /note="M->E: Decreases interaction with UPF1; does not FT reduce NMD efficiency." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1123 FT /note="E->R: Decreases interaction with UPF1." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1169 FT /note="M->E: Decreases interaction with UPF1." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1171 FT /note="F->E: Abolishes interaction with UPF1; reduces NMD FT efficiency." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1171 FT /note="F->E: Greatly reduces NMD efficiency; when FT associated with E-1173 and E-1174." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1173 FT /note="M->E: Abolishes interaction with UPF1." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1173 FT /note="M->E: Greatly reduces NMD efficiency; when FT associated with E-1171 and E-1174." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1174 FT /note="L->E: Abolishes interaction with UPF1; reduces NMD FT efficiency." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1174 FT /note="L->E: Greatly reduces NMD efficiency; when FT associated with E-1171 and E-1173." FT /evidence="ECO:0000269|PubMed:19556969" FT MUTAGEN 1176 FT /note="R->E: Decreases interaction with UPF1." FT /evidence="ECO:0000269|PubMed:19556969" FT CONFLICT 119 FT /note="A -> T (in Ref. 5; BAC04721)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="F -> L (in Ref. 5; BAC04721)" FT /evidence="ECO:0000305" FT CONFLICT 844 FT /note="H -> Q (in Ref. 2; AAG48509 and 4; BAA92646)" FT /evidence="ECO:0000305" FT CONFLICT 969 FT /note="P -> S (in Ref. 4; BAA92646)" FT /evidence="ECO:0000305" FT HELIX 122..149 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 158..162 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 168..177 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 186..195 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 202..211 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 219..232 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 236..253 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 259..274 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 280..297 FT /evidence="ECO:0007829|PDB:4CEM" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 305..320 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 325..334 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 346..375 FT /evidence="ECO:0007829|PDB:4CEM" FT TURN 376..382 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:4CEM" FT TURN 387..389 FT /evidence="ECO:0007829|PDB:4CEM" FT TURN 395..398 FT /evidence="ECO:0007829|PDB:4CEM" FT HELIX 399..419 FT /evidence="ECO:0007829|PDB:4CEM" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 463..469 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 474..476 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 539..549 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 560..574 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 581..594 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 598..609 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 613..618 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 619..629 FT /evidence="ECO:0007829|PDB:4CEK" FT TURN 630..632 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 635..653 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 660..675 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 681..693 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 697..716 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 718..737 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 742..755 FT /evidence="ECO:0007829|PDB:4CEK" FT HELIX 770..780 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 782..785 FT /evidence="ECO:0007829|PDB:7NWU" FT HELIX 788..796 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 803..814 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 816..818 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 824..834 FT /evidence="ECO:0007829|PDB:1UW4" FT TURN 835..837 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 839..859 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 862..864 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 865..880 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 886..898 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 909..911 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 917..929 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 930..932 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 936..957 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 970..983 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 993..1011 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 1108..1126 FT /evidence="ECO:0007829|PDB:2WJV" FT STRAND 1168..1174 FT /evidence="ECO:0007829|PDB:2WJV" FT STRAND 1183..1192 FT /evidence="ECO:0007829|PDB:2WJV" FT HELIX 1193..1197 FT /evidence="ECO:0007829|PDB:2WJV" SQ SEQUENCE 1272 AA; 147810 MW; 95F3C57D2854BB44 CRC64; MPAERKKPAS MEEKDSLPNN KEKDCSERRT VSSKERPKDD IKLTAKKEVS KAPEDKKKRL EDDKRKKEDK ERKKKDEEKV KAEEESKKKE EEEKKKHQEE ERKKQEEQAK RQQEEEAAAQ MKEKEESIQL HQEAWERHHL RKELRSKNQN APDSRPEENF FSRLDSSLKK NTAFVKKLKT ITEQQRDSLS HDFNGLNLSK YIAEAVASIV EAKLKISDVN CAVHLCSLFH QRYADFAPSL LQVWKKHFEA RKEEKTPNIT KLRTDLRFIA ELTIVGIFTD KEGLSLIYEQ LKNIINADRE SHTHVSVVIS FCRHCGDDIA GLVPRKVKSA AEKFNLSFPP SEIISPEKQQ PFQNLLKEYF TSLTKHLKRD HRELQNTERQ NRRILHSKGE LSEDRHKQYE EFAMSYQKLL ANSQSLADLL DENMPDLPQD KPTPEEHGPG IDIFTPGKPG EYDLEGGIWE DEDARNFYEN LIDLKAFVPA ILFKDNEKSC QNKESNKDDT KEAKESKENK EVSSPDDLEL ELENLEINDD TLELEGGDEA EDLTKKLLDE QEQEDEEAST GSHLKLIVDA FLQQLPNCVN RDLIDKAAMD FCMNMNTKAN RKKLVRALFI VPRQRLDLLP FYARLVATLH PCMSDVAEDL CSMLRGDFRF HVRKKDQINI ETKNKTVRFI GELTKFKMFT KNDTLHCLKM LLSDFSHHHI EMACTLLETC GRFLFRSPES HLRTSVLLEQ MMRKKQAMHL DARYVTMVEN AYYYCNPPPA EKTVKKKRPP LQEYVRKLLY KDLSKVTTEK VLRQMRKLPW QDQEVKDYVI CCMINIWNVK YNSIHCVANL LAGLVLYQED VGIHVVDGVL EDIRLGMEVN QPKFNQRRIS SAKFLGELYN YRMVESAVIF RTLYSFTSFG VNPDGSPSSL DPPEHLFRIR LVCTILDTCG QYFDRGSSKR KLDCFLVYFQ RYVWWKKSLE VWTKDHPFPI DIDYMISDTL ELLRPKIKLC NSLEESIRQV QDLEREFLIK LGLVNDKDSK DSMTEGENLE EDEEEEEGGA ETEEQSGNES EVNEPEEEEG SDNDDDEGEE EEEENTDYLT DSNKENETDE ENTEVMIKGG GLKHVPCVED EDFIQALDKM MLENLQQRSG ESVKVHQLDV AIPLHLKSQL RKGPPLGGGE GEAESADTMP FVMLTRKGNK QQFKILNVPM SSQLAANHWN QQQAEQEERM RMKKLTLDIN ERQEQEDYQE MLQSLAQRPA PANTNRERRP RYQHPKGAPN ADLIFKTGGR RR //