SMG9_HUMAN
ID SMG9_HUMAN Reviewed; 520 AA.
AC Q9H0W8; O60429; Q9H9A9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG9 {ECO:0000312|HGNC:HGNC:25763};
GN Name=SMG9 {ECO:0000312|HGNC:HGNC:25763};
GN Synonyms=C19orf61 {ECO:0000312|HGNC:HGNC:25763};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-53 AND SER-451, AND
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [8]
RP FUNCTION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE SMG1C COMPLEX.
RX PubMed=19417104; DOI=10.1101/gad.1767209;
RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y.,
RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H.,
RA Anderson P., Ohno S.;
RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA
RT decay.";
RL Genes Dev. 23:1091-1105(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7 AND SER-32, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP INTERACTION WITH SMG1 AND SMG8, AND ELECTRON MICROSCOPY OF THE SMG1C
RP COMPLEX.
RX PubMed=21245168; DOI=10.1101/gad.606911;
RA Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y.,
RA Izumi N., Ohno S., Llorca O.;
RT "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale
RT conformational changes controlled by SMG-8.";
RL Genes Dev. 25:153-164(2011).
RN [13]
RP SUBUNIT.
RX PubMed=20817927; DOI=10.1093/nar/gkq749;
RA Fernandez I.S., Yamashita A., Arias-Palomo E., Bamba Y., Bartolome R.A.,
RA Canales M.A., Teixido J., Ohno S., Llorca O.;
RT "Characterization of SMG-9, an essential component of the nonsense-mediated
RT mRNA decay SMG1C complex.";
RL Nucleic Acids Res. 39:347-358(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7 AND SER-32, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-7; SER-32 AND
RP SER-53, AND 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INVOLVEMENT IN HBMS.
RX PubMed=27018474; DOI=10.1016/j.ajhg.2016.02.010;
RA Shaheen R., Anazi S., Ben-Omran T., Seidahmed M.Z., Caddle L.B., Palmer K.,
RA Ali R., Alshidi T., Hagos S., Goodwin L., Hashem M., Wakil S.M.,
RA Abouelhoda M., Colak D., Murray S.A., Alkuraya F.S.;
RT "Mutations in SMG9, Encoding an Essential Component of Nonsense-Mediated
RT Decay Machinery, Cause a multiple congenital anomaly syndrome in humans and
RT mice.";
RL Am. J. Hum. Genet. 98:643-652(2016).
RN [19]
RP INTERACTION WITH SMG1.
RX PubMed=33205750; DOI=10.7554/elife.63042;
RA Lopez-Perrote A., Hug N., Gonzalez-Corpas A., Rodriguez C.F., Serna M.,
RA Garcia-Martin C., Boskovic J., Fernandez-Leiro R., Caceres J.F., Llorca O.;
RT "Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA
RT decay factor DHX34, as evidenced by Cryo-EM.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing
CC premature stop codons (PubMed:19417104). Is recruited by release
CC factors to stalled ribosomes together with SMG1 and SMG8 (forming the
CC SMG1C protein kinase complex) and, in the SMG1C complex, is required
CC for the efficient association between SMG1 and SMG8 (PubMed:19417104).
CC Plays a role in brain, heart, and eye development (By similarity).
CC {ECO:0000250|UniProtKB:Q9DB90, ECO:0000269|PubMed:19417104}.
CC -!- SUBUNIT: Self-associates to form homodimers and forms heterodimers with
CC SMG8; these assembly forms may represent SMG1C intermediate forms
CC (PubMed:20817927). Component of the SMG1C complex composed of SMG1,
CC SMG8 and SMG9 (PubMed:33205750). Interacts with DHX34; the interaction
CC is RNA-independent (PubMed:25220460). {ECO:0000269|PubMed:19417104,
CC ECO:0000269|PubMed:20817927, ECO:0000269|PubMed:25220460,
CC ECO:0000269|PubMed:33205750}.
CC -!- INTERACTION:
CC Q9H0W8; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2872322, EBI-11522760;
CC Q9H0W8; Q96MA6: AK8; NbExp=3; IntAct=EBI-2872322, EBI-8466265;
CC Q9H0W8; P53365: ARFIP2; NbExp=3; IntAct=EBI-2872322, EBI-638194;
CC Q9H0W8; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2872322, EBI-10961624;
CC Q9H0W8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2872322, EBI-742887;
CC Q9H0W8; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-2872322, EBI-17278014;
CC Q9H0W8; P78358: CTAG1B; NbExp=5; IntAct=EBI-2872322, EBI-1188472;
CC Q9H0W8; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-2872322, EBI-12831978;
CC Q9H0W8; P49356: FNTB; NbExp=3; IntAct=EBI-2872322, EBI-602349;
CC Q9H0W8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2872322, EBI-618309;
CC Q9H0W8; Q2KHT4-3: GSG1; NbExp=3; IntAct=EBI-2872322, EBI-12951679;
CC Q9H0W8; O75031: HSF2BP; NbExp=3; IntAct=EBI-2872322, EBI-7116203;
CC Q9H0W8; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2872322, EBI-6509505;
CC Q9H0W8; Q15323: KRT31; NbExp=6; IntAct=EBI-2872322, EBI-948001;
CC Q9H0W8; O76011: KRT34; NbExp=5; IntAct=EBI-2872322, EBI-1047093;
CC Q9H0W8; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2872322, EBI-10171774;
CC Q9H0W8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2872322, EBI-11522433;
CC Q9H0W8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2872322, EBI-10271199;
CC Q9H0W8; Q99471: PFDN5; NbExp=3; IntAct=EBI-2872322, EBI-357275;
CC Q9H0W8; O43189: PHF1; NbExp=3; IntAct=EBI-2872322, EBI-530034;
CC Q9H0W8; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-2872322, EBI-949255;
CC Q9H0W8; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-2872322, EBI-11278955;
CC Q9H0W8; Q969Q6: PPP2R3C; NbExp=3; IntAct=EBI-2872322, EBI-2561661;
CC Q9H0W8; P31321: PRKAR1B; NbExp=3; IntAct=EBI-2872322, EBI-2805516;
CC Q9H0W8; A6NK89: RASSF10; NbExp=3; IntAct=EBI-2872322, EBI-6912267;
CC Q9H0W8; Q04864-2: REL; NbExp=3; IntAct=EBI-2872322, EBI-10829018;
CC Q9H0W8; Q9BYT1: SLC17A9; NbExp=3; IntAct=EBI-2872322, EBI-3940816;
CC Q9H0W8; Q9BRV3: SLC50A1; NbExp=3; IntAct=EBI-2872322, EBI-8634123;
CC Q9H0W8; Q8ND04: SMG8; NbExp=6; IntAct=EBI-2872322, EBI-3903643;
CC Q9H0W8; Q9H0W8: SMG9; NbExp=5; IntAct=EBI-2872322, EBI-2872322;
CC Q9H0W8; P08247: SYP; NbExp=3; IntAct=EBI-2872322, EBI-9071725;
CC Q9H0W8; P15884-3: TCF4; NbExp=3; IntAct=EBI-2872322, EBI-13636688;
CC Q9H0W8; Q12933: TRAF2; NbExp=6; IntAct=EBI-2872322, EBI-355744;
CC Q9H0W8; P36406: TRIM23; NbExp=6; IntAct=EBI-2872322, EBI-740098;
CC Q9H0W8; P14373: TRIM27; NbExp=3; IntAct=EBI-2872322, EBI-719493;
CC Q9H0W8; Q15654: TRIP6; NbExp=3; IntAct=EBI-2872322, EBI-742327;
CC Q9H0W8; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2872322, EBI-12806590;
CC Q9H0W8; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2872322, EBI-948354;
CC Q9H0W8; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2872322, EBI-12030590;
CC Q9H0W8; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2872322, EBI-625509;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0W8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0W8-2; Sequence=VSP_025946;
CC -!- PTM: Phosphorylated by SMG1. {ECO:0000269|PubMed:19417104}.
CC -!- DISEASE: Heart and brain malformation syndrome (HBMS) [MIM:616920]: An
CC autosomal recessive syndrome characterized by multiple congenital
CC anomalies such as cardiac defects, brain malformations, including
CC cerebellar vermis hypoplasia, hypoplastic corpus callosum and Dandy-
CC Walker malformation, profoundly delayed psychomotor development,
CC microphthalmia, and facial dysmorphism. {ECO:0000269|PubMed:27018474}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the SMG9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17932.1; Type=Erroneous gene model prediction; 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; AL136606; CAB66541.1; -; mRNA.
DR EMBL; AK022948; BAB14323.1; -; mRNA.
DR EMBL; AC004780; AAC17932.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC008869; AAH08869.1; -; mRNA.
DR CCDS; CCDS33043.2; -. [Q9H0W8-1]
DR RefSeq; NP_061981.2; NM_019108.3. [Q9H0W8-1]
DR PDB; 6L54; EM; 3.43 A; C=1-520.
DR PDB; 6SYT; EM; 3.45 A; C=1-520.
DR PDB; 6Z3R; EM; 2.97 A; C=1-520.
DR PDB; 7PW4; EM; 3.27 A; C=1-520.
DR PDB; 7PW5; EM; 3.40 A; C=1-520.
DR PDB; 7PW7; EM; 3.59 A; C=1-520.
DR PDB; 7PW8; EM; 2.82 A; C=1-520.
DR PDB; 7PW9; EM; 3.12 A; C=169-520.
DR PDBsum; 6L54; -.
DR PDBsum; 6SYT; -.
DR PDBsum; 6Z3R; -.
DR PDBsum; 7PW4; -.
DR PDBsum; 7PW5; -.
DR PDBsum; 7PW7; -.
DR PDBsum; 7PW8; -.
DR PDBsum; 7PW9; -.
DR AlphaFoldDB; Q9H0W8; -.
DR SMR; Q9H0W8; -.
DR BioGRID; 121029; 63.
DR IntAct; Q9H0W8; 49.
DR STRING; 9606.ENSP00000270066; -.
DR iPTMnet; Q9H0W8; -.
DR PhosphoSitePlus; Q9H0W8; -.
DR BioMuta; SMG9; -.
DR DMDM; 74733529; -.
DR EPD; Q9H0W8; -.
DR jPOST; Q9H0W8; -.
DR MassIVE; Q9H0W8; -.
DR MaxQB; Q9H0W8; -.
DR PaxDb; Q9H0W8; -.
DR PeptideAtlas; Q9H0W8; -.
DR PRIDE; Q9H0W8; -.
DR ProteomicsDB; 80333; -. [Q9H0W8-1]
DR ProteomicsDB; 80334; -. [Q9H0W8-2]
DR Antibodypedia; 31101; 65 antibodies from 20 providers.
DR DNASU; 56006; -.
DR Ensembl; ENST00000270066.11; ENSP00000270066.6; ENSG00000105771.14. [Q9H0W8-1]
DR Ensembl; ENST00000601170.5; ENSP00000471398.1; ENSG00000105771.14. [Q9H0W8-2]
DR GeneID; 56006; -.
DR KEGG; hsa:56006; -.
DR MANE-Select; ENST00000270066.11; ENSP00000270066.6; NM_019108.4; NP_061981.2.
DR UCSC; uc002oxj.3; human. [Q9H0W8-1]
DR CTD; 56006; -.
DR DisGeNET; 56006; -.
DR GeneCards; SMG9; -.
DR HGNC; HGNC:25763; SMG9.
DR HPA; ENSG00000105771; Low tissue specificity.
DR MalaCards; SMG9; -.
DR MIM; 613176; gene.
DR MIM; 616920; phenotype.
DR neXtProt; NX_Q9H0W8; -.
DR OpenTargets; ENSG00000105771; -.
DR PharmGKB; PA162378734; -.
DR VEuPathDB; HostDB:ENSG00000105771; -.
DR eggNOG; KOG4181; Eukaryota.
DR GeneTree; ENSGT00390000003568; -.
DR HOGENOM; CLU_037795_0_0_1; -.
DR InParanoid; Q9H0W8; -.
DR OMA; FRTQSQE; -.
DR OrthoDB; 1436399at2759; -.
DR PhylomeDB; Q9H0W8; -.
DR TreeFam; TF319763; -.
DR PathwayCommons; Q9H0W8; -.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q9H0W8; -.
DR BioGRID-ORCS; 56006; 35 hits in 1081 CRISPR screens.
DR ChiTaRS; SMG9; human.
DR GenomeRNAi; 56006; -.
DR Pharos; Q9H0W8; Tbio.
DR PRO; PR:Q9H0W8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H0W8; protein.
DR Bgee; ENSG00000105771; Expressed in left testis and 160 other tissues.
DR ExpressionAtlas; Q9H0W8; baseline and differential.
DR Genevisible; Q9H0W8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019354; SMG8/SMG9.
DR InterPro; IPR039177; SMG9.
DR PANTHER; PTHR14270; PTHR14270; 1.
DR Pfam; PF10220; Smg8_Smg9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Nonsense-mediated mRNA decay; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..520
FT /note="Nonsense-mediated mRNA decay factor SMG9"
FT /id="PRO_0000289163"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 496..520
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025946"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:7PW4"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6L54"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6L54"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:7PW8"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7PW8"
FT TURN 408..412
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:7PW9"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:7PW4"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 492..507
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 511..517
FT /evidence="ECO:0007829|PDB:7PW8"
SQ SEQUENCE 520 AA; 57651 MW; AA68A473F7F6BBCC CRC64;
MSESGHSQPG LYGIERRRRW KEPGSGGPQN LSGPGGRERD YIAPWERERR DASEETSTSV
MQKTPIILSK PPAERSKQPP PPTAPAAPPA PAPLEKPIVL MKPREEGKGP VAVTGASTPE
GTAPPPPAAP APPKGEKEGQ RPTQPVYQIQ NRGMGTAAPA AMDPVVGQAK LLPPERMKHS
IKLVDDQMNW CDSAIEYLLD QTDVLVVGVL GLQGTGKSMV MSLLSANTPE EDQRTYVFRA
QSAEMKERGG NQTSGIDFFI TQERIVFLDT QPILSPSILD HLINNDRKLP PEYNLPHTYV
EMQSLQIAAF LFTVCHVVIV VQDWFTDLSL YRFLQTAEMV KPSTPSPSHE SSSSSGSDEG
TEYYPHLVFL QNKARREDFC PRKLRQMHLM IDQLMAHSHL RYKGTLSMLQ CNVFPGLPPD
FLDSEVNLFL VPFMDSEAES ENPPRAGPGS SPLFSLLPGY RGHPSFQSLV SKLRSQVMSM
ARPQLSHTIL TEKNWFHYAA RIWDGVRKSS ALAEYSRLLA
