RENT2_HUMAN
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 03-AUG-2022, entry version 184.
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};
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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 PDBsum; 1UW4; -.
DR PDBsum; 2WJV; -.
DR PDBsum; 4CEK; -.
DR PDBsum; 4CEM; -.
DR AlphaFoldDB; Q9HAU5; -.
DR SMR; Q9HAU5; -.
DR BioGRID; 117490; 143.
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 iPTMnet; Q9HAU5; -.
DR MetOSite; Q9HAU5; -.
DR PhosphoSitePlus; Q9HAU5; -.
DR BioMuta; UPF2; -.
DR DMDM; 60390647; -.
DR EPD; Q9HAU5; -.
DR jPOST; Q9HAU5; -.
DR MassIVE; Q9HAU5; -.
DR MaxQB; Q9HAU5; -.
DR PaxDb; Q9HAU5; -.
DR PeptideAtlas; Q9HAU5; -.
DR PRIDE; Q9HAU5; -.
DR Antibodypedia; 24600; 172 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 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; 653534at2759; -.
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; 748 hits in 1098 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 216 other tissues.
DR Genevisible; Q9HAU5; HS.
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 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; PTHR12839; 1.
DR Pfam; PF02854; MIF4G; 3.
DR Pfam; PF04050; Upf2; 1.
DR SMART; SM00543; MIF4G; 3.
DR SUPFAM; SSF48371; SSF48371; 3.
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 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
