SMG7_HUMAN
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 03-AUG-2022, entry version 191.
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},
GN EST1C {ECO:0000312|HGNC:HGNC:16792},
GN 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};
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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; 303.
DR IntAct; Q92540; 37.
DR MINT; Q92540; -.
DR STRING; 9606.ENSP00000425133; -.
DR GlyGen; Q92540; 3 sites, 2 O-linked glycans (3 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 PeptideAtlas; Q92540; -.
DR PRIDE; Q92540; -.
DR ProteomicsDB; 19450; -.
DR ProteomicsDB; 19888; -.
DR ProteomicsDB; 75298; -. [Q92540-1]
DR ProteomicsDB; 75299; -. [Q92540-2]
DR ProteomicsDB; 75300; -. [Q92540-4]
DR Antibodypedia; 34445; 110 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 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; TWAGHGP; -.
DR OrthoDB; 556396at2759; -.
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; 374 hits in 1100 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 201 other tissues.
DR ExpressionAtlas; Q92540; baseline and differential.
DR Genevisible; Q92540; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; 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; -; 1.
DR IDEAL; IID00090; -.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR019458; Est1_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
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
