ID SMG7_HUMAN Reviewed; 1137 AA. AC Q92540; B4DRB2; E9PCI0; E9PEH2; Q5T1Q0; Q6PIE0; Q7Z7H9; Q8IXC1; Q8IXC2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Nonsense-mediated mRNA decay factor SMG7 {ECO:0000312|HGNC:HGNC:16792}; DE AltName: Full=SMG-7 homolog {ECO:0000312|HGNC:HGNC:16792}; DE Short=hSMG-7; GN Name=SMG7 {ECO:0000312|HGNC:HGNC:16792}; GN Synonyms=C1orf16 {ECO:0000312|HGNC:HGNC:16792}, EST1C GN {ECO:0000312|HGNC:HGNC:16792}, KIAA0250 {ECO:0000312|HGNC:HGNC:16792}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP IDENTIFICATION IN A COMPLEX CONTAINING SMG5; SMG7; UPF1; PPP2CA AND UPF3. RX PubMed=14636577; DOI=10.1016/s1097-2765(03)00443-x; RA Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., RA Hachiya T., Hentze M.W., Anderson P., Ohno S.; RT "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes RT containing hSMG-5 and hSMG-7."; RL Mol. Cell 12:1187-1200(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-900. RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT RP ILE-900. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH CYTOPLASMIC MRNA DECAY RP BODIES. RX PubMed=15546618; DOI=10.1016/j.molcel.2004.10.013; RA Unterholzner L., Izaurralde E.; RT "SMG7 acts as a molecular link between mRNA surveillance and mRNA decay."; RL Mol. Cell 16:587-596(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-781, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-624; SER-781 AND SER-897, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP INTERACTION WITH DHX34. RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020; RA Hug N., Caceres J.F.; RT "The RNA helicase DHX34 activates NMD by promoting a transition from the RT surveillance to the decay-inducing complex."; RL Cell Rep. 8:1845-1856(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-497, FUNCTION, INTERACTION WITH RP SMG5 AND PHOSPHORYLATED RENT1, SUBCELLULAR LOCATION, TPR REPEAT, AND RP MUTAGENESIS OF LYS-66 AND ARG-163. RX PubMed=15721257; DOI=10.1016/j.molcel.2005.01.010; RA Fukuhara N., Ebert J., Unterholzner L., Lindner D., Izaurralde E., RA Conti E.; RT "SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay RT pathway."; RL Mol. Cell 17:537-547(2005). CC -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 CC to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to CC provide a link to the mRNA degradation machinery involving CC exonucleolytic pathways, and to serve as an adapter for UPF1 to protein CC phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. CC {ECO:0000269|PubMed:15546618, ECO:0000269|PubMed:15721257}. CC -!- SUBUNIT: Part of a complex that contains SMG5, SMG7, PPP2CA, a short CC isoform of UPF3A (isoform UPF3AS, but not isoform UPF3AL) and CC phosphorylated UPF1 (PubMed:14636577). Interacts with DHX34; the CC interaction is RNA-independent (PubMed:25220460). CC {ECO:0000269|PubMed:14636577, ECO:0000269|PubMed:25220460}. CC -!- INTERACTION: CC Q92540; Q9UPR3: SMG5; NbExp=5; IntAct=EBI-719830, EBI-3400861; CC Q92540; Q92900: UPF1; NbExp=3; IntAct=EBI-719830, EBI-373471; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14636577}. Nucleus CC {ECO:0000269|PubMed:14636577}. Note=Predominantly cytoplasmic, and CC nuclear. Shuttles between nucleus and cytoplasm. CC {ECO:0000269|PubMed:14636577}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q92540-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92540-2; Sequence=VSP_016574; CC Name=4; CC IsoId=Q92540-4; Sequence=VSP_016574, VSP_016575, VSP_016576; CC Name=5; CC IsoId=Q92540-5; Sequence=VSP_047130, VSP_016575; CC -!- SEQUENCE CAUTION: CC Sequence=BAA13381.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB085674; BAC53621.1; -; mRNA. DR EMBL; D87437; BAA13381.2; ALT_INIT; mRNA. DR EMBL; AK299178; BAG61224.1; -; mRNA. DR EMBL; AL449223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137800; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC036381; AAH36381.1; -; mRNA. DR EMBL; BC052565; AAH52565.1; -; mRNA. DR CCDS; CCDS1355.1; -. [Q92540-1] DR CCDS; CCDS41445.2; -. [Q92540-4] DR CCDS; CCDS53444.1; -. [Q92540-2] DR CCDS; CCDS53445.1; -. [Q92540-5] DR RefSeq; NP_001167532.1; NM_001174061.1. [Q92540-5] DR RefSeq; NP_775179.1; NM_173156.2. [Q92540-1] DR RefSeq; NP_963862.1; NM_201568.2. [Q92540-2] DR RefSeq; NP_963863.2; NM_201569.2. [Q92540-4] DR PDB; 1YA0; X-ray; 2.55 A; A/B=1-497. DR PDBsum; 1YA0; -. DR AlphaFoldDB; Q92540; -. DR SMR; Q92540; -. DR BioGRID; 115218; 318. DR IntAct; Q92540; 39. DR MINT; Q92540; -. DR STRING; 9606.ENSP00000425133; -. DR GlyCosmos; Q92540; 3 sites, 2 glycans. DR GlyGen; Q92540; 4 sites, 2 O-linked glycans (4 sites). DR iPTMnet; Q92540; -. DR PhosphoSitePlus; Q92540; -. DR BioMuta; SMG7; -. DR DMDM; 84028262; -. DR EPD; Q92540; -. DR jPOST; Q92540; -. DR MassIVE; Q92540; -. DR MaxQB; Q92540; -. DR PaxDb; 9606-ENSP00000425133; -. DR PeptideAtlas; Q92540; -. DR ProteomicsDB; 19450; -. DR ProteomicsDB; 19888; -. DR ProteomicsDB; 75298; -. [Q92540-1] DR ProteomicsDB; 75299; -. [Q92540-2] DR ProteomicsDB; 75300; -. [Q92540-4] DR Pumba; Q92540; -. DR Antibodypedia; 34445; 124 antibodies from 23 providers. DR DNASU; 9887; -. DR Ensembl; ENST00000347615.6; ENSP00000340766.2; ENSG00000116698.22. [Q92540-1] DR Ensembl; ENST00000507469.5; ENSP00000425133.1; ENSG00000116698.22. [Q92540-4] DR Ensembl; ENST00000508461.5; ENSP00000426915.1; ENSG00000116698.22. [Q92540-5] DR Ensembl; ENST00000515829.6; ENSP00000421358.2; ENSG00000116698.22. [Q92540-2] DR GeneID; 9887; -. DR KEGG; hsa:9887; -. DR UCSC; uc001gqf.4; human. [Q92540-1] DR AGR; HGNC:16792; -. DR CTD; 9887; -. DR DisGeNET; 9887; -. DR GeneCards; SMG7; -. DR HGNC; HGNC:16792; SMG7. DR HPA; ENSG00000116698; Low tissue specificity. DR MIM; 610964; gene. DR neXtProt; NX_Q92540; -. DR OpenTargets; ENSG00000116698; -. DR PharmGKB; PA25605; -. DR VEuPathDB; HostDB:ENSG00000116698; -. DR eggNOG; KOG2162; Eukaryota. DR GeneTree; ENSGT00940000158333; -. DR HOGENOM; CLU_009299_0_0_1; -. DR InParanoid; Q92540; -. DR OMA; WHQAGSA; -. DR OrthoDB; 1356823at2759; -. DR PhylomeDB; Q92540; -. DR TreeFam; TF327119; -. DR PathwayCommons; Q92540; -. DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q92540; -. DR BioGRID-ORCS; 9887; 401 hits in 1181 CRISPR screens. DR ChiTaRS; SMG7; human. DR EvolutionaryTrace; Q92540; -. DR GeneWiki; SMG7; -. DR GenomeRNAi; 9887; -. DR Pharos; Q92540; Tbio. DR PRO; PR:Q92540; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q92540; Protein. DR Bgee; ENSG00000116698; Expressed in medial globus pallidus and 203 other cell types or tissues. DR ExpressionAtlas; Q92540; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL. DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central. DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:HGNC-UCL. DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central. DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL. 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; IBA:GO_Central. DR GO; GO:0035303; P:regulation of dephosphorylation; TAS:HGNC-UCL. DR DisProt; DP01844; -. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR IDEAL; IID00090; -. DR InterPro; IPR018834; DNA/RNA-bd_Est1-type. DR InterPro; IPR019458; Est1-like_N. DR InterPro; IPR045153; Est1/Ebs1-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR15696:SF5; NONSENSE-MEDIATED MRNA DECAY FACTOR SMG7; 1. DR PANTHER; PTHR15696; SMG-7 SUPPRESSOR WITH MORPHOLOGICAL EFFECT ON GENITALIA PROTEIN 7; 1. DR Pfam; PF10374; EST1; 1. DR Pfam; PF10373; EST1_DNA_bind; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR Genevisible; Q92540; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; TPR repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..1137 FT /note="Nonsense-mediated mRNA decay factor SMG7" FT /id="PRO_0000076324" FT REPEAT 152..185 FT /note="TPR 1" FT /evidence="ECO:0000269|PubMed:15721257" FT REPEAT 187..219 FT /note="TPR 2" FT /evidence="ECO:0000269|PubMed:15721257" FT REGION 620..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 696..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 890..911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 988..1055 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1069..1089 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1104..1137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 629..646 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 696..775 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 988..1030 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1069..1087 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 624 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 781 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 897 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..42 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047130" FT VAR_SEQ 569..614 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9039502" FT /id="VSP_016574" FT VAR_SEQ 914 FT /note="E -> EDPKSSPLLPPDLLKSLAALEEEEELIFSNPPDLYPALLGPLASLPG FT RSLF (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_016575" FT VAR_SEQ 1101..1137 FT /note="SIWSSSMMHPGPSALEQLLMQQKQKQQRGQGTMNPPH -> KQQHGVQQLGP FT KRQSEEEGSSSICVAHRGPRPLPSCSLPASTFRVKFKAARTCAHQAQKKTRRRPFWKRR FT KKGK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016576" FT VARIANT 627 FT /note="S -> F (in dbSNP:rs34221194)" FT /id="VAR_051363" FT VARIANT 900 FT /note="V -> I (in dbSNP:rs2298083)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9039502" FT /id="VAR_051364" FT MUTAGEN 66 FT /note="K->E: Abolishes interaction with UPF1; when FT associated with E-163." FT /evidence="ECO:0000269|PubMed:15721257" FT MUTAGEN 163 FT /note="R->E: Abolishes interaction with UPF1; when FT associated with E-66." FT /evidence="ECO:0000269|PubMed:15721257" FT CONFLICT 187 FT /note="Q -> R (in Ref. 4; BAG61224)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="R -> E (in Ref. 1; BAC53621)" FT /evidence="ECO:0000305" FT HELIX 2..16 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 30..46 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 48..54 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 56..64 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 66..76 FT /evidence="ECO:0007829|PDB:1YA0" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 86..109 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 145..164 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 168..181 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 187..198 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 202..213 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 220..233 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 246..262 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 269..285 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 291..308 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 311..314 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 322..347 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 361..371 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 375..379 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 381..384 FT /evidence="ECO:0007829|PDB:1YA0" FT TURN 385..388 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 390..397 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 416..420 FT /evidence="ECO:0007829|PDB:1YA0" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 425..427 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 428..431 FT /evidence="ECO:0007829|PDB:1YA0" FT HELIX 449..469 FT /evidence="ECO:0007829|PDB:1YA0" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 475..479 FT /evidence="ECO:0007829|PDB:1YA0" FT STRAND 482..486 FT /evidence="ECO:0007829|PDB:1YA0" FT CONFLICT Q92540-4:854 FT /note="V -> I (in Ref. 5; AAH36381)" FT /evidence="ECO:0000305" FT CONFLICT Q92540-4:898 FT /note="P -> T (in Ref. 5; AAH36381)" FT /evidence="ECO:0000305" SQ SEQUENCE 1137 AA; 127282 MW; E152AFAFEF8F3A42 CRC64; MSLQSAQYLR QAEVLKADMT DSKLGPAEVW TSRQALQDLY QKMLVTDLEY ALDKKVEQDL WNHAFKNQIT TLQGQAKNRA NPNRSEVQAN LSLFLEAASG FYTQLLQELC TVFNVDLPCR VKSSQLGIIS NKQTHTSAIV KPQSSSCSYI CQHCLVHLGD IARYRNQTSQ AESYYRHAAQ LVPSNGQPYN QLAILASSKG DHLTTIFYYC RSIAVKFPFP AASTNLQKAL SKALESRDEV KTKWGVSDFI KAFIKFHGHV YLSKSLEKLS PLREKLEEQF KRLLFQKAFN SQQLVHVTVI NLFQLHHLRD FSNETEQHTY SQDEQLCWTQ LLALFMSFLG ILCKCPLQNE SQEESYNAYP LPAVKVSMDW LRLRPRVFQE AVVDERQYIW PWLISLLNSF HPHEEDLSSI SATPLPEEFE LQGFLALRPS FRNLDFSKGH QGITGDKEGQ QRRIRQQRLI SIGKWIADNQ PRLIQCENEV GKLLFITEIP ELILEDPSEA KENLILQETS VIESLAADGS PGLKSVLSTS RNLSNNCDTG EKPVVTFKEN IKTREVNRDQ GRSFPPKEVR RDYSKGITVT KNDGKKDNNK RKTETKKCTL EKLQETGKQN VAVQVKSQTE LRKTPVSEAR KTPVTQTPTQ ASNSQFIPIH HPGAFPPLPS RPGFPPPTYV IPPPVAFSMG SGYTFPAGVS VPGTFLQPTA HSPAGNQVQA GKQSHIPYSQ QRPSGPGPMN QGPQQSQPPS QQPLTSLPAQ PTAQSTSQLQ VQALTQQQQS PTKAVPALGK SPPHHSGFQQ YQQADASKQL WNPPQVQGPL GKIMPVKQPY YLQTQDPIKL FEPSLQPPVM QQQPLEKKMK PFPMEPYNHN PSEVKVPEFY WDSSYSMADN RSVMAQQANI DRRGKRSPGV FRPEQDPVPR MPFEKSLLEK PSELMSHSSS FLSLTGFSLN QERYPNNSMF NEVYGKNLTS SSKAELSPSM APQETSLYSL FEGTPWSPSL PASSDHSTPA SQSPHSSNPS SLPSSPPTHN HNSVPFSNFG PIGTPDNRDR RTADRWKTDK PAMGGFGIDY LSATSSSESS WHQASTPSGT WTGHGPSMED SSAVLMESLK SIWSSSMMHP GPSALEQLLM QQKQKQQRGQ GTMNPPH //