SMN_HUMAN
ID SMN_HUMAN Reviewed; 294 AA.
AC Q16637; A8K0V4; Q13119; Q549U5; Q96J51;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Survival motor neuron protein;
DE AltName: Full=Component of gems 1;
DE AltName: Full=Gemin-1;
GN Name=SMN1; Synonyms=SMN, SMNT;
GN and
GN Name=SMN2; Synonyms=SMNC;
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 [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND VARIANT
RP SMA1 CYS-272.
RC TISSUE=Fetal brain;
RX PubMed=7813012; DOI=10.1016/0092-8674(95)90460-3;
RA Lefebvre S., Buerglen L., Reboullet S., Clermont O., Burlet P., Viollet L.,
RA Benichou B., Cruaud C., Millasseau P., Zeviani M., le Paslier D.,
RA Frezal J., Cohen D., Weissenbach J., Munnich A., Melki J.;
RT "Identification and characterization of a spinal muscular atrophy-
RT determining gene.";
RL Cell 80:155-165(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8838816; DOI=10.1006/geno.1996.0147;
RA Buerglen L., Lefebvre S., Clermont O., Burlet P., Viollet L., Cruaud C.,
RA Munnich A., Melki J.;
RT "Structure and organization of the human survival motor neurone (SMN)
RT gene.";
RL Genomics 32:479-482(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9503025; DOI=10.1006/geno.1997.5141;
RA Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R.,
RA Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G.,
RA MacKenzie A.E.;
RT "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular
RT atrophy candidate genes SMN and NAIP.";
RL Genomics 48:121-127(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Skeletal muscle;
RX PubMed=7639755; DOI=10.1006/bbrc.1995.2135;
RA Gennarelli M., Lucarelli M., Capon F., Pizzuti A., Merlini L., Angelini C.,
RA Novelli G., Dallapiccola B.;
RT "Survival motor neuron gene transcript analysis in muscles from spinal
RT muscular atrophy patients.";
RL Biochem. Biophys. Res. Commun. 213:342-348(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SMN-DELTA7).
RC TISSUE=Amygdala;
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SMN AND SMN-DELTA7).
RC TISSUE=Kidney, Lung, Placenta, and Prostate;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-294.
RX PubMed=7552146; DOI=10.1159/000472281;
RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
RA van Ommen G.J.B., Buys C.H.C.M.;
RT "A provisional transcript map of the spinal muscular atrophy (SMA) critical
RT region.";
RL Eur. J. Hum. Genet. 3:87-95(1995).
RN [9]
RP INVOLVEMENT IN SMA4.
RX PubMed=7658877; DOI=10.1016/s0140-6736(95)91507-9;
RA Brahe C., Servidei S., Zappata S., Ricci E., Tonali P., Neri G.;
RT "Genetic homogeneity between childhood-onset and adult-onset autosomal
RT recessive spinal muscular atrophy.";
RL Lancet 346:741-742(1995).
RN [10]
RP INVOLVEMENT IN SMA4.
RX PubMed=8551862; DOI=10.1016/s0140-6736(95)92881-2;
RA Clermont O., Burlet P., Lefebvre S., Buerglen L., Munnich A., Melki J.;
RT "SMN gene deletions in adult-onset spinal muscular atrophy.";
RL Lancet 346:1712-1713(1995).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=8670859; DOI=10.1002/j.1460-2075.1996.tb00725.x;
RA Liu Q., Dreyfuss G.;
RT "A novel nuclear structure containing the survival of motor neurons
RT protein.";
RL EMBO J. 15:3555-3565(1996).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=9259265; DOI=10.1093/hmg/6.8.1205;
RA Coovert D.D., Le T.T., McAndrew P.E., Strasswimmer J., Crawford T.O.,
RA Mendell J.R., Coulson S.E., Androphy E.J., Prior T.W., Burghes A.H.M.;
RT "The survival motor neuron protein in spinal muscular atrophy.";
RL Hum. Mol. Genet. 6:1205-1214(1997).
RN [13]
RP INTERACTION WITH GEMIN2.
RX PubMed=9323129; DOI=10.1016/s0092-8674(00)80367-0;
RA Liu Q., Fischer U., Wang F., Dreyfuss G.;
RT "The spinal muscular atrophy disease gene product, SMN, and its associated
RT protein SIP1 are in a complex with spliceosomal snRNP proteins.";
RL Cell 90:1013-1021(1997).
RN [14]
RP FUNCTION IN U12 INTRONS SPLICING.
RX PubMed=9845364; DOI=10.1016/s0092-8674(00)81632-3;
RA Pellizzoni L., Kataoka N., Charroux B., Dreyfuss G.;
RT "A novel function for SMN, the spinal muscular atrophy disease gene
RT product, in pre-mRNA splicing.";
RL Cell 95:615-624(1998).
RN [15]
RP INTERACTION WITH SYNCRIP.
RX PubMed=11574476; DOI=10.1093/emboj/20.19.5443;
RA Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G.;
RT "SMN interacts with a novel family of hnRNP and spliceosomal proteins.";
RL EMBO J. 20:5443-5452(2001).
RN [16]
RP INTERACTION WITH COIL.
RX PubMed=11641277; DOI=10.1101/gad.908401;
RA Hebert M.D., Szymczyk P.W., Shpargel K.B., Matera A.G.;
RT "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular
RT atrophy protein.";
RL Genes Dev. 15:2720-2729(2001).
RN [17]
RP INTERACTION WITH OSTF1, AND TISSUE SPECIFICITY.
RX PubMed=11551898; DOI=10.1074/jbc.m100233200;
RA Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V.;
RT "Osteoclast-stimulating factor interacts with the spinal muscular atrophy
RT gene product to stimulate osteoclast formation.";
RL J. Biol. Chem. 276:41035-41039(2001).
RN [18]
RP INTERACTION WITH ZPR1, AND SUBCELLULAR LOCATION.
RX PubMed=11283611; DOI=10.1038/35070059;
RA Gangwani L., Mikrut M., Theroux S., Sharma M., Davis R.J.;
RT "Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN
RT protein.";
RL Nat. Cell Biol. 3:376-383(2001).
RN [19]
RP REVIEW, AND SUBCELLULAR LOCATION.
RX PubMed=12067652; DOI=10.1016/s0955-0674(02)00332-0;
RA Paushkin S., Gubitz A.K., Massenet S., Dreyfuss G.;
RT "The SMN complex, an assemblyosome of ribonucleoproteins.";
RL Curr. Opin. Cell Biol. 14:305-312(2002).
RN [20]
RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX, AND INTERACTION WITH DDX20;
RP RNUT1 AND SNRPB.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex
RT with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [21]
RP INTERACTION WITH GEMIN FAMILY MEMBERS.
RX PubMed=12065586; DOI=10.1074/jbc.m203478200;
RA Baccon J., Pellizzoni L., Rappsilber J., Mann M., Dreyfuss G.;
RT "Identification and characterization of Gemin7, a novel component of the
RT survival of motor neuron complex.";
RL J. Biol. Chem. 277:31957-31962(2002).
RN [22]
RP INTERACTION WITH LSM11.
RC TISSUE=Cervix carcinoma;
RX PubMed=12975319; DOI=10.1101/gad.274403;
RA Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U.,
RA Schuemperli D.;
RT "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT complex and the role of a new component, Lsm11, in histone RNA
RT processing.";
RL Genes Dev. 17:2321-2333(2003).
RN [23]
RP SUBUNIT, INTERACTION WITH RPP20/POP7, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP GLU-134, CHARACTERIZATION OF VARIANTS SMA1 CYS-272 AND VAL-279,
RP CHARACTERIZATION OF VARIANT SMA2 AND SMA3 ILE-274, AND CHARACTERIZATION OF
RP VARIANT SMA3 ILE-262.
RX PubMed=14715275; DOI=10.1016/j.bbrc.2003.12.084;
RA Hua Y., Zhou J.;
RT "Rpp20 interacts with SMN and is re-distributed into SMN granules in
RT response to stress.";
RL Biochem. Biophys. Res. Commun. 314:268-276(2004).
RN [24]
RP INTERACTION WITH LSM10; LSM11 AND SNRPB.
RX PubMed=16087681; DOI=10.1074/jbc.m505077200;
RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA Fischer U., Schuemperli D.;
RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm
RT proteins with PRMT5 and SMN complexes.";
RL J. Biol. Chem. 280:34435-34440(2005).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31, AND
RP IDENTIFICATION BY 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 [26]
RP INTERACTION WITH FRG1.
RX PubMed=17103222; DOI=10.1007/s00412-006-0083-3;
RA van Koningsbruggen S., Straasheijm K.R., Sterrenburg E., de Graaf N.,
RA Dauwerse H.G., Frants R.R., van der Maarel S.M.;
RT "FRG1P-mediated aggregation of proteins involved in pre-mRNA processing.";
RL Chromosoma 116:53-64(2007).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [28]
RP SUBUNIT, IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN3;
RP GEMIN2 AND GEMIN8.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [29]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [30]
RP INTERACTION WITH FMR1, AND SUBCELLULAR LOCATION.
RX PubMed=18093976; DOI=10.1074/jbc.m707304200;
RA Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.;
RT "In vitro and in cellulo evidences for association of the survival of motor
RT neuron complex with the fragile X mental retardation protein.";
RL J. Biol. Chem. 283:5598-5610(2008).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-25; SER-28 AND SER-31,
RP AND 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, 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 [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND
RP IDENTIFICATION BY 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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [37]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH WRAP53.
RX PubMed=21072240; DOI=10.1371/journal.pbio.1000521;
RA Mahmoudi S., Henriksson S., Weibrecht I., Smith S., Soederberg O.,
RA Stroemblad S., Wiman K.G., Farnebo M.;
RT "WRAP53 is essential for Cajal body formation and for targeting the
RT survival of motor neuron complex to Cajal bodies.";
RL PLoS Biol. 8:E1000521-E1000521(2010).
RN [38]
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 [39]
RP PHOSPHORYLATION AT SER-4; SER-5; SER-8; THR-85 AND SER-187 BY PKA.
RX PubMed=21609790; DOI=10.1016/j.bbapap.2011.04.015;
RA Wu C.Y., Curtis A., Choi Y.S., Maeda M., Xu M.J., Berg A., Joneja U.,
RA Mason R.W., Lee K.H., Wang W.;
RT "Identification of the phosphorylation sites in the survival motor neuron
RT protein by protein kinase A.";
RL Biochim. Biophys. Acta 1814:1134-1139(2011).
RN [40]
RP INTERACTION WITH SETX.
RX PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
RA Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
RT "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause
RT sites to promote Xrn2-dependent termination.";
RL Mol. Cell 42:794-805(2011).
RN [41]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-5; SER-8 AND SER-28, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [42]
RP FUNCTION.
RX PubMed=23063131; DOI=10.1016/j.cell.2012.09.012;
RA Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W.,
RA Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.;
RT "An SMN-dependent U12 splicing event essential for motor circuit
RT function.";
RL Cell 151:440-454(2012).
RN [43]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [44]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-8; THR-25; SER-28;
RP SER-31 AND THR-69, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND
RP IDENTIFICATION BY 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 [47]
RP SUBUNIT, AND INTERACTION WITH GEMIN2.
RX PubMed=26092730; DOI=10.1074/jbc.m115.667279;
RA Gupta K., Martin R., Sharp R., Sarachan K.L., Ninan N.S., Van Duyne G.D.;
RT "Oligomeric Properties of Survival Motor Neuron.Gemin2 Complexes.";
RL J. Biol. Chem. 290:20185-20199(2015).
RN [48]
RP INTERACTION WITH SF3B2.
RX PubMed=25737013; DOI=10.1038/ncomms7428;
RA Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C.,
RA Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.;
RT "PRMT9 is a type II methyltransferase that methylates the splicing factor
RT SAP145.";
RL Nat. Commun. 6:6428-6428(2015).
RN [49]
RP FUNCTION, INTERACTION WITH POLR2A; PRMT5; SETX AND XRN2, AND DOMAIN TUDOR.
RX PubMed=26700805; DOI=10.1038/nature16469;
RA Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z., Schmitges F.W.,
RA Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J., Pawson T.J.,
RA Blencowe B.J., Greenblatt J.F.;
RT "SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal
RT domain control termination.";
RL Nature 529:48-53(2016).
RN [50]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [51] {ECO:0007744|PDB:1G5V}
RP STRUCTURE BY NMR OF 90-145, INTERACTION WITH SNRPD1 AND SNRPD3, AND
RP MUTAGENESIS OF GLU-134.
RX PubMed=11135666; DOI=10.1038/83014;
RA Selenko P., Sprangers R., Stier G., Buhler D., Fischer U., Sattler M.;
RT "SMN tudor domain structure and its interaction with the Sm proteins.";
RL Nat. Struct. Biol. 8:27-31(2001).
RN [52] {ECO:0007744|PDB:1MHN}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 89-147, INTERACTION WITH SNRPD3,
RP AND DOMAIN TUDOR.
RX PubMed=12628254; DOI=10.1016/s0022-2836(03)00148-7;
RA Sprangers R., Groves M.R., Sinning I., Sattler M.;
RT "High-resolution X-ray and NMR structures of the SMN Tudor domain:
RT conformational variation in the binding site for symmetrically dimethylated
RT arginine residues.";
RL J. Mol. Biol. 327:507-520(2003).
RN [53] {ECO:0007744|PDB:5XJL}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 26-62 IN COMPLEX WITH SNRPD1;
RP SNRPD2; SNRPE; SNRPF; SNRPG AND GEMIN2, FUNCTION, SUBUNIT, INTERACTION WITH
RP GEMIN2, VARIANT SMA3 VAL-44, AND MUTAGENESIS OF ASP-44.
RX PubMed=21816274; DOI=10.1016/j.cell.2011.06.043;
RA Zhang R., So B.R., Li P., Yong J., Glisovic T., Wan L., Dreyfuss G.;
RT "Structure of a key intermediate of the SMN complex reveals Gemin2's
RT crucial function in snRNP assembly.";
RL Cell 146:384-395(2011).
RN [54] {ECO:0007744|PDB:4A4E, ECO:0007744|PDB:4A4G}
RP STRUCTURE BY NMR OF 84-147 IN COMPLEX WITH DIMETHYLATED ARGININE, FUNCTION,
RP DOMAIN TUDOR, INTERACTION WITH SNRPD3, AND MUTAGENESIS OF TRP-92; TRP-102;
RP TYR-109; TYR-127; TYR-130; ASN-132; 134-GLU--GLN-136; GLU-134 AND GLN-136.
RX PubMed=22101937; DOI=10.1038/nsmb.2185;
RA Tripsianes K., Madl T., Machyna M., Fessas D., Englbrecht C., Fischer U.,
RA Neugebauer K.M., Sattler M.;
RT "Structural basis for dimethylarginine recognition by the Tudor domains of
RT human SMN and SPF30 proteins.";
RL Nat. Struct. Mol. Biol. 18:1414-1420(2011).
RN [55] {ECO:0007744|PDB:4GLI}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 263-294, SUBUNIT, INTERACTION
RP WITH GEMIN2, CHARACTERIZATION OF VARIANTS SMA1 CYS-272; SMA2/SMA3 ILE-274;
RP SMA3 SER-275 AND SMA1 VAL-279, AND MUTAGENESIS OF LEU-260; MET-263;
RP LEU-264; SER-266; TRP-267; TYR-268; GLY-271; TYR-272; THR-274; GLY-275 AND
RP GLY-279.
RX PubMed=23022347; DOI=10.1016/j.str.2012.08.024;
RA Martin R., Gupta K., Ninan N.S., Perry K., Van Duyne G.D.;
RT "The survival motor neuron protein forms soluble glycine zipper
RT oligomers.";
RL Structure 20:1929-1939(2012).
RN [56] {ECO:0007744|PDB:2LEH}
RP STRUCTURE BY NMR OF 26-51, INTERACTION WITH GEMIN2, AND MUTAGENESIS OF
RP TRP-34; LEU-39; TYR-43 AND ALA-46.
RX PubMed=22607171; DOI=10.1042/bj20120241;
RA Sarachan K.L., Valentine K.G., Gupta K., Moorman V.R., Gledhill J.M.,
RA Bernens M., Tommos C., Wand A.J., Van Duyne G.D.;
RT "Solution structure of the core SMN-Gemin2 complex.";
RL Biochem. J. 445:361-370(2012).
RN [57] {ECO:0007744|PDB:5XJQ, ECO:0007744|PDB:5XJR, ECO:0007744|PDB:5XJS}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 26-62 IN COMPLEX WITH GEMIN2;
RP SNRPD1; SNRPD2; SNRPE; SNRPF AND SNRPG, FUNCTION, AND INTERACTION WITH
RP GEMIN2.
RX PubMed=31799625; DOI=10.1093/nar/gkz1135;
RA Yi H., Mu L., Shen C., Kong X., Wang Y., Hou Y., Zhang R.;
RT "Negative cooperativity between Gemin2 and RNA provides insights into RNA
RT selection and the SMN complex's release in snRNP assembly.";
RL Nucleic Acids Res. 48:895-911(2020).
RN [58]
RP VARIANT SMA1 VAL-279.
RX PubMed=9147655; DOI=10.1093/hmg/6.3.497;
RA Talbot K., Ponting C.P., Theodosiou A.M., Rodriques N.R., Surtees R.,
RA Mountford R., Davies K.E.;
RT "Missense mutation clustering in the survival motor neuron gene: a role for
RT a conserved tyrosine and glycine rich region of the protein in RNA
RT metabolism?";
RL Hum. Mol. Genet. 6:497-500(1997).
RN [59]
RP VARIANT SMA3 ILE-262, AND VARIANT SMA2/SMA3 ILE-274.
RX PubMed=9158159; DOI=10.1093/hmg/6.5.821;
RA Hahnen E., Schoenling J., Rudnik-Schoeneborn S., Raschke H., Zerres K.,
RA Wirth B.;
RT "Missense mutations in exon 6 of the survival motor neuron gene in patients
RT with spinal muscular atrophy (SMA).";
RL Hum. Mol. Genet. 6:821-825(1997).
RN [60]
RP VARIANT SMA3 LEU-245, AND VARIANT SMA1 CYS-272.
RX PubMed=10732817; DOI=10.1007/s100480050021;
RA Rochette C.F., Surh L.C., Ray P.N., McAndrew P.E., Prior T.W.,
RA Burghes A.H.M., Vanasse M., Simard L.R.;
RT "Molecular diagnosis of non-deletion SMA patients using quantitative PCR of
RT SMN exon 7.";
RL Neurogenetics 1:141-147(1997).
RN [61]
RP VARIANT SMA2/SMA3 GLY-2, AND VARIANT SMA3 SER-275.
RX PubMed=9837824; DOI=10.1086/302160;
RA Parsons D.W., McAndrew P.E., Iannaccone S.T., Mendell J.R., Burghes A.H.,
RA Prior T.W.;
RT "Intragenic telSMN mutations: frequency, distribution, evidence of a
RT founder effect, and modification of the spinal muscular atrophy phenotype
RT by cenSMN copy number.";
RL Am. J. Hum. Genet. 63:1712-1723(1998).
RN [62]
RP VARIANT SMA2/SMA3 CYS-279.
RX PubMed=10732802; DOI=10.1007/s100480050040;
RA Wang C.H., Papendick B.D., Bruinsma P., Day J.K.;
RT "Identification of a novel missense mutation of the smnt gene in two
RT siblings with spinal muscular atrophy.";
RL Neurogenetics 1:273-276(1998).
RN [63]
RP SUBUNIT, INTERACTION WITH SNRPB; GEMIN2; SNRPD1; SNRPD2; SNRPD3 AND SNRPE,
RP AND CHARACTERIZATION OF VARIANT SMA1 CYS-272.
RX PubMed=10500148; DOI=10.1073/pnas.96.20.11167;
RA Pellizzoni L., Charroux B., Dreyfuss G.;
RT "SMN mutants of spinal muscular atrophy patients are defective in binding
RT to snRNP proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999).
RN [64]
RP VARIANTS SMA1 PHE-116 AND GLU-136.
RX PubMed=15249625; DOI=10.1212/01.wnl.0000132634.48815.13;
RA Cusco I., Barcelo M.J., del Rio E., Baiget M., Tizzano E.F.;
RT "Detection of novel mutations in the SMN Tudor domain in type I SMA
RT patients.";
RL Neurology 63:146-149(2004).
RN [65]
RP VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95; GLY-111; GLY-262; CYS-272
RP AND ILE-274, AND CHARACTERIZATION OF VARIANTS SMA1/SMA2/SMA3 ASN-30;
RP VAL-44; ARG-95 AND GLY-111.
RX PubMed=15580564; DOI=10.1002/humu.20111;
RA Sun Y., Grimmler M., Schwarzer V., Schoenen F., Fischer U., Wirth B.;
RT "Molecular and functional analysis of intragenic SMN1 mutations in patients
RT with spinal muscular atrophy.";
RL Hum. Mutat. 25:64-71(2005).
RN [66]
RP INTERACTION WITH ELAVL4, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS
RP SMA2 GLU-111; SMA1 PHE-116 AND SMA1 GLU-136, AND MUTAGENESIS OF GLU-134.
RX PubMed=21088113; DOI=10.1093/hmg/ddq500;
RA Hubers L., Valderrama-Carvajal H., Laframboise J., Timbers J., Sanchez G.,
RA Cote J.;
RT "HuD interacts with survival motor neuron protein and can rescue spinal
RT muscular atrophy-like neuronal defects.";
RL Hum. Mol. Genet. 20:553-579(2011).
RN [67]
RP INTERACTION WITH ELAVL4, VARIANT SMA1 VAL-279, AND MUTAGENESIS OF GLU-134.
RX PubMed=21389246; DOI=10.1523/jneurosci.3631-10.2011;
RA Fallini C., Zhang H., Su Y., Silani V., Singer R.H., Rossoll W.,
RA Bassell G.J.;
RT "The survival of motor neuron (SMN) protein interacts with the mRNA-binding
RT protein HuD and regulates localization of poly(A) mRNA in primary motor
RT neuron axons.";
RL J. Neurosci. 31:3914-3925(2011).
RN [68]
RP INTERACTION WITH ELAVL4, AND MUTAGENESIS OF GLU-134.
RX PubMed=29061699; DOI=10.1523/jneurosci.1528-17.2017;
RA Hao le T., Duy P.Q., An M., Talbot J., Iyer C.C., Wolman M., Beattie C.E.;
RT "HuD and the Survival Motor Neuron Protein Interact in Motoneurons and Are
RT Essential for Motoneuron Development, Function, and mRNA Regulation.";
RL J. Neurosci. 37:11559-11571(2017).
RN [69]
RP INTERACTION WITH GEMIN8, CHARACTERIZATION OF VARIANTS SMA1 CYS-272 AND SMA3
RP ILE-274, AND MUTAGENESIS OF MET-263; SER-266 AND HIS-273.
RX PubMed=33754639; DOI=10.1093/nar/gkab158;
RA Veepaschit J., Viswanathan A., Bordonne R., Grimm C., Fischer U.;
RT "Identification and structural analysis of the Schizosaccharomyces pombe
RT SMN complex.";
RL Nucleic Acids Res. 49:gkab158-gkab158(2021).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (PubMed:9845364, PubMed:18984161). Most spliceosomal snRNPs
CC contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on
CC the Sm site of the small nuclear RNA to form the core snRNP (Sm core)
CC (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2,
CC SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex
CC by the chaperone CLNS1A that controls the assembly of the core snRNP
CC (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the
CC trapped 5Sm proteins from CLNS1A forming an intermediate
CC (PubMed:18984161). Within the SMN complex, SMN1 acts as a structural
CC backbone and together with GEMIN2 it gathers the Sm complex subunits
CC (PubMed:21816274, PubMed:22101937, PubMed:17178713). Binding of snRNA
CC inside 5Sm ultimately triggers eviction of the SMN complex, thereby
CC allowing binding of SNRPD3 and SNRPB to complete assembly of the core
CC snRNP (PubMed:31799625). Ensures the correct splicing of U12 intron-
CC containing genes that may be important for normal motor and
CC proprioceptive neurons development (PubMed:23063131). Also required for
CC resolving RNA-DNA hybrids created by RNA polymerase II, that form R-
CC loop in transcription terminal regions, an important step in proper
CC transcription termination (PubMed:26700805). May also play a role in
CC the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
CC {ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:22101937,
CC ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:26700805,
CC ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9845364}.
CC -!- SUBUNIT: Homooligomer; may form higher order homooligomers in the dimer
CC to octamer range (PubMed:26092730, PubMed:10500148, PubMed:14715275,
CC PubMed:21816274, PubMed:17178713, PubMed:23022347). Part of the core
CC SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4,
CC GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:9323129,
CC PubMed:17178713). Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG (PubMed:12065586, PubMed:18984161). Component of an
CC import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259
CC (PubMed:12095920). Interacts with DDX20, FBL, NOLA1, RNUT1, SYNCRIP and
CC with several spliceosomal snRNP core Sm proteins, including SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3 (PubMed:11574476,
CC PubMed:12095920, PubMed:10500148). Interacts with GEMIN2; the
CC interaction is direct (PubMed:26092730, PubMed:10500148,
CC PubMed:21816274, PubMed:31799625, PubMed:17178713, PubMed:22607171,
CC PubMed:23022347). Interacts with GEMIN3; the interaction is direct
CC (PubMed:17178713). Interacts with GEMIN8; the interaction is direct
CC (PubMed:33754639, PubMed:17178713). Interacts with SNRPB; the
CC interaction is direct (PubMed:10500148). Interacts (via Tudor domain)
CC with SNRPD1 (via C-terminus); the interaction is direct
CC (PubMed:10500148, PubMed:11135666). Interacts with SNRPD2; the
CC interaction is direct (PubMed:10500148). Interacts (via Tudor domain)
CC with SNRPD3 (via C-terminus); the interaction is direct
CC (PubMed:10500148, PubMed:11135666, PubMed:22101937, PubMed:12628254).
CC Interacts with SNRPE; the interaction is direct (PubMed:10500148).
CC Interacts with OSTF1, LSM10, LSM11 and RPP20/POP7 (PubMed:11551898,
CC PubMed:12975319, PubMed:16087681, PubMed:14715275). Interacts (via C-
CC terminal region) with ZPR1 (via C-terminal region) (PubMed:11283611).
CC Interacts (via Tudor domain) with COIL (PubMed:11641277). Interacts
CC with SETX; recruits SETX to POLR2A (PubMed:21700224, PubMed:26700805).
CC Interacts with POLR2A (via the C-terminal domain (CTD))
CC (PubMed:26700805). Interacts with PRMT5 (PubMed:26700805). Interacts
CC with XRN2 (PubMed:26700805). Interacts (via C-terminus) with FMR1 (via
CC C-terminus); the interaction is direct and occurs in a RNA-independent
CC manner (PubMed:18093976). Interacts (via Tudor domain) with SF3B2
CC ('Arg-508'-methylated form) (PubMed:25737013). Interacts with
CC WRAP53/TCAB1 (PubMed:21072240). Interacts (via Tudor domain) with
CC ELAVL4 in an RNA-independent manner; the interaction is required for
CC localization of ELAVL4 to RNA granules (PubMed:21088113,
CC PubMed:21389246, PubMed:29061699). Interacts with FRG1
CC (PubMed:17103222). {ECO:0000269|PubMed:10500148,
CC ECO:0000269|PubMed:11135666, ECO:0000269|PubMed:11283611,
CC ECO:0000269|PubMed:11551898, ECO:0000269|PubMed:11574476,
CC ECO:0000269|PubMed:11641277, ECO:0000269|PubMed:12065586,
CC ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:12975319,
CC ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:16087681,
CC ECO:0000269|PubMed:17103222, ECO:0000269|PubMed:17178713,
CC ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:21072240, ECO:0000269|PubMed:21088113,
CC ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:21700224,
CC ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:22101937,
CC ECO:0000269|PubMed:22607171, ECO:0000269|PubMed:23022347,
CC ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:26092730,
CC ECO:0000269|PubMed:26700805, ECO:0000269|PubMed:29061699,
CC ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9323129}.
CC -!- SUBUNIT: [Isoform SMN-delta7]: Does not homooligomerize
CC (PubMed:10500148). Does not interact with SNRPB (PubMed:10500148).
CC {ECO:0000269|PubMed:10500148}.
CC -!- INTERACTION:
CC Q16637; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-395421, EBI-22011868;
CC Q16637; Q96GX9: APIP; NbExp=3; IntAct=EBI-395421, EBI-359248;
CC Q16637; Q96DX5: ASB9; NbExp=3; IntAct=EBI-395421, EBI-745641;
CC Q16637; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-395421, EBI-2410266;
CC Q16637; Q9UL45: BLOC1S6; NbExp=6; IntAct=EBI-395421, EBI-465781;
CC Q16637; Q13895: BYSL; NbExp=8; IntAct=EBI-395421, EBI-358049;
CC Q16637; Q96FZ7: CHMP6; NbExp=3; IntAct=EBI-395421, EBI-1049648;
CC Q16637; Q9Y3Y2: CHTOP; NbExp=3; IntAct=EBI-395421, EBI-347794;
CC Q16637; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-395421, EBI-11984237;
CC Q16637; P38432: COIL; NbExp=4; IntAct=EBI-395421, EBI-945751;
CC Q16637; Q9NR90-2: DAZ3; NbExp=3; IntAct=EBI-395421, EBI-25830216;
CC Q16637; Q9UHI6: DDX20; NbExp=10; IntAct=EBI-395421, EBI-347658;
CC Q16637; Q08426: EHHADH; NbExp=3; IntAct=EBI-395421, EBI-2339219;
CC Q16637; O75616: ERAL1; NbExp=3; IntAct=EBI-395421, EBI-6393536;
CC Q16637; Q8IZU0: FAM9B; NbExp=8; IntAct=EBI-395421, EBI-10175124;
CC Q16637; Q9UHY8: FEZ2; NbExp=3; IntAct=EBI-395421, EBI-396453;
CC Q16637; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-395421, EBI-744935;
CC Q16637; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-395421, EBI-10253815;
CC Q16637; P06241-3: FYN; NbExp=3; IntAct=EBI-395421, EBI-10691738;
CC Q16637; O14893: GEMIN2; NbExp=20; IntAct=EBI-395421, EBI-443648;
CC Q16637; Q8TEQ6: GEMIN5; NbExp=7; IntAct=EBI-395421, EBI-443630;
CC Q16637; Q8WVV9-3: HNRNPLL; NbExp=3; IntAct=EBI-395421, EBI-25845242;
CC Q16637; Q9BUJ2: HNRNPUL1; NbExp=4; IntAct=EBI-395421, EBI-1018153;
CC Q16637; P09017: HOXC4; NbExp=3; IntAct=EBI-395421, EBI-3923226;
CC Q16637; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-395421, EBI-21911304;
CC Q16637; Q8NA54: IQUB; NbExp=6; IntAct=EBI-395421, EBI-10220600;
CC Q16637; Q14974-1: KPNB1; NbExp=2; IntAct=EBI-395421, EBI-15488647;
CC Q16637; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-395421, EBI-10241252;
CC Q16637; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-395421, EBI-12811111;
CC Q16637; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-395421, EBI-1048945;
CC Q16637; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-395421, EBI-12805508;
CC Q16637; Q3SYF9: KRTAP19-7; NbExp=6; IntAct=EBI-395421, EBI-10241353;
CC Q16637; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-395421, EBI-18395721;
CC Q16637; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-395421, EBI-12111050;
CC Q16637; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-395421, EBI-11962084;
CC Q16637; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-395421, EBI-10261141;
CC Q16637; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-395421, EBI-716006;
CC Q16637; Q99683: MAP3K5; NbExp=3; IntAct=EBI-395421, EBI-476263;
CC Q16637; Q15759: MAPK11; NbExp=3; IntAct=EBI-395421, EBI-298304;
CC Q16637; Q9UBB5: MBD2; NbExp=2; IntAct=EBI-395421, EBI-923391;
CC Q16637; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-395421, EBI-4397720;
CC Q16637; O43196-2: MSH5; NbExp=3; IntAct=EBI-395421, EBI-25844576;
CC Q16637; Q9NV92: NDFIP2; NbExp=3; IntAct=EBI-395421, EBI-2933200;
CC Q16637; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-395421, EBI-10698339;
CC Q16637; O75925: PIAS1; NbExp=3; IntAct=EBI-395421, EBI-629434;
CC Q16637; O15160: POLR1C; NbExp=6; IntAct=EBI-395421, EBI-1055079;
CC Q16637; P24928: POLR2A; NbExp=12; IntAct=EBI-395421, EBI-295301;
CC Q16637; O75817: POP7; NbExp=5; IntAct=EBI-395421, EBI-366574;
CC Q16637; Q13427: PPIG; NbExp=4; IntAct=EBI-395421, EBI-396072;
CC Q16637; Q86UA1: PRPF39; NbExp=3; IntAct=EBI-395421, EBI-2803203;
CC Q16637; P57729: RAB38; NbExp=3; IntAct=EBI-395421, EBI-6552718;
CC Q16637; Q7Z333: SETX; NbExp=3; IntAct=EBI-395421, EBI-1220123;
CC Q16637; Q13435: SF3B2; NbExp=4; IntAct=EBI-395421, EBI-749111;
CC Q16637; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-395421, EBI-10182463;
CC Q16637; Q12824: SMARCB1; NbExp=3; IntAct=EBI-395421, EBI-358419;
CC Q16637; Q16637: SMN2; NbExp=21; IntAct=EBI-395421, EBI-395421;
CC Q16637; Q16637-3: SMN2; NbExp=3; IntAct=EBI-395421, EBI-395447;
CC Q16637; P08621: SNRNP70; NbExp=5; IntAct=EBI-395421, EBI-1049228;
CC Q16637; P62314: SNRPD1; NbExp=6; IntAct=EBI-395421, EBI-372177;
CC Q16637; P55769: SNU13; NbExp=3; IntAct=EBI-395421, EBI-712228;
CC Q16637; O60749: SNX2; NbExp=3; IntAct=EBI-395421, EBI-1046690;
CC Q16637; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-395421, EBI-12023934;
CC Q16637; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-395421, EBI-10696971;
CC Q16637; P37802: TAGLN2; NbExp=3; IntAct=EBI-395421, EBI-1056740;
CC Q16637; Q9NX07-2: TRNAU1AP; NbExp=3; IntAct=EBI-395421, EBI-21894090;
CC Q16637; Q99598: TSNAX; NbExp=3; IntAct=EBI-395421, EBI-742638;
CC Q16637; Q548N1: VPS28; NbExp=3; IntAct=EBI-395421, EBI-10243107;
CC Q16637; Q9UK41: VPS28; NbExp=5; IntAct=EBI-395421, EBI-727424;
CC Q16637; Q9BUR4: WRAP53; NbExp=5; IntAct=EBI-395421, EBI-2563542;
CC Q16637; Q9VV74: Smn; Xeno; NbExp=2; IntAct=EBI-395421, EBI-185315;
CC Q16637; A0A142I5B9; Xeno; NbExp=2; IntAct=EBI-395421, EBI-20625235;
CC Q16637-2; O14893: GEMIN2; NbExp=4; IntAct=EBI-16014970, EBI-443648;
CC Q16637-3; P01023: A2M; NbExp=3; IntAct=EBI-395447, EBI-640741;
CC Q16637-3; P50570-2: DNM2; NbExp=3; IntAct=EBI-395447, EBI-10968534;
CC Q16637-3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-395447, EBI-11110431;
CC Q16637-3; O43464: HTRA2; NbExp=3; IntAct=EBI-395447, EBI-517086;
CC Q16637-3; P42858: HTT; NbExp=9; IntAct=EBI-395447, EBI-466029;
CC Q16637-3; Q14974: KPNB1; NbExp=5; IntAct=EBI-395447, EBI-286758;
CC Q16637-3; P51608: MECP2; NbExp=3; IntAct=EBI-395447, EBI-1189067;
CC Q16637-3; P14678-1: SNRPB; NbExp=3; IntAct=EBI-395447, EBI-372471;
CC Q16637-3; Q9UK41: VPS28; NbExp=3; IntAct=EBI-395447, EBI-727424;
CC -!- SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000269|PubMed:11283611,
CC ECO:0000269|PubMed:8670859, ECO:0000305|PubMed:12067652}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:21072240,
CC ECO:0000305|PubMed:12067652}. Cytoplasm {ECO:0000269|PubMed:11283611,
CC ECO:0000269|PubMed:8670859, ECO:0000305|PubMed:12067652}. Cytoplasmic
CC granule {ECO:0000269|PubMed:14715275}. Perikaryon
CC {ECO:0000269|PubMed:18093976}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:18093976}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P97801}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P97801}. Note=Colocalizes with actin and at the
CC Z-line of skeletal muscle (By similarity). Under stress conditions
CC colocalizes with RPP20/POP7 in punctuated cytoplasmic granules
CC (PubMed:14715275). Colocalized and redistributed with ZPR1 from the
CC cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies
CC (PubMed:11283611). Colocalizes with FMR1 in cytoplasmic granules in the
CC soma and neurite cell processes (PubMed:18093976).
CC {ECO:0000250|UniProtKB:P97801, ECO:0000269|PubMed:11283611,
CC ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:18093976}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=SMN; Synonyms=Full-SMN;
CC IsoId=Q16637-1; Sequence=Displayed;
CC Name=SMN-delta5; Synonyms=Iso5-SMN;
CC IsoId=Q16637-2; Sequence=VSP_006183;
CC Name=SMN-delta7; Synonyms=Iso7-SMN;
CC IsoId=Q16637-3; Sequence=VSP_006184, VSP_006185;
CC Name=SMN-delta57; Synonyms=Iso57-SMN;
CC IsoId=Q16637-4; Sequence=VSP_006183, VSP_006184, VSP_006185;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues. Expressed
CC at high levels in brain, kidney and liver, moderate levels in skeletal
CC and cardiac muscle, and low levels in fibroblasts and lymphocytes. Also
CC seen at high levels in spinal cord. Present in osteoclasts and
CC mononuclear cells (at protein level). {ECO:0000269|PubMed:11551898,
CC ECO:0000269|PubMed:9259265}.
CC -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC which are common in snRNP proteins. {ECO:0000269|PubMed:12628254,
CC ECO:0000269|PubMed:22101937, ECO:0000269|PubMed:26700805}.
CC -!- DISEASE: Spinal muscular atrophy 1 (SMA1) [MIM:253300]: A form of
CC spinal muscular atrophy, a group of neuromuscular disorder
CC characterized by degeneration of the anterior horn cells of the spinal
CC cord, leading to symmetrical muscle weakness and atrophy. Autosomal
CC recessive forms are classified according to the age of onset, the
CC maximum muscular activity achieved, and survivorship. The severity of
CC the disease is mainly determined by the copy number of SMN2, a copy
CC gene which predominantly produces exon 7-skipped transcripts and only
CC low amount of full-length transcripts that encode for a protein
CC identical to SMN1. Only about 4% of SMA patients bear one SMN1 copy
CC with an intragenic mutation. SMA1 is a severe form, with onset before 6
CC months of age. SMA1 patients never achieve the ability to sit.
CC {ECO:0000269|PubMed:10500148, ECO:0000269|PubMed:10732817,
CC ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:15249625,
CC ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:21088113,
CC ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:23022347,
CC ECO:0000269|PubMed:33754639, ECO:0000269|PubMed:7813012,
CC ECO:0000269|PubMed:9147655}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinal muscular atrophy 2 (SMA2) [MIM:253550]: An autosomal
CC recessive form of spinal muscular atrophy, a neuromuscular disorder
CC characterized by degeneration of the anterior horn cells of the spinal
CC cord, leading to symmetrical muscle weakness and atrophy. It has
CC intermediate severity, with onset between 6 and 18 months. Patients do
CC not reach the motor milestone of standing, and survive into adulthood.
CC {ECO:0000269|PubMed:10732802, ECO:0000269|PubMed:14715275,
CC ECO:0000269|PubMed:21088113, ECO:0000269|PubMed:9158159,
CC ECO:0000269|PubMed:9837824}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinal muscular atrophy 3 (SMA3) [MIM:253400]: An autosomal
CC recessive form of spinal muscular atrophy, a neuromuscular disorder
CC characterized by degeneration of the anterior horn cells of the spinal
CC cord, leading to symmetrical muscle weakness and atrophy. Onset is
CC after 18 months. Patients develop ability to stand and walk and survive
CC into adulthood. {ECO:0000269|PubMed:10732817,
CC ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:21816274,
CC ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spinal muscular atrophy 4 (SMA4) [MIM:271150]: An autosomal
CC recessive form of spinal muscular atrophy, a neuromuscular disorder
CC characterized by degeneration of the anterior horn cells of the spinal
CC cord, leading to symmetrical muscle weakness and atrophy. Onset is in
CC adulthood, disease progression is slow, and patients can stand and
CC walk. {ECO:0000269|PubMed:7658877, ECO:0000269|PubMed:8551862}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: The SMN gene is present in two highly homologous and
CC functional copies (TelSMN/SMN1 and CenSMN/SMN2). The telomeric copy of
CC SMN gene (TelSMN/SMN1) seems to be the SMA-determining gene while the
CC centromeric copy seems unaffected.
CC -!- MISCELLANEOUS: [Isoform SMN]: Primarily derived from SMN1 gene.
CC -!- MISCELLANEOUS: [Isoform SMN-delta7]: Thought to be a non-functional
CC protein that lacks the capacity to oligomerize and thus cannot interact
CC with Sm proteins. Primarily derived from SMN2 gene.
CC {ECO:0000305|PubMed:10500148}.
CC -!- SIMILARITY: Belongs to the SMN family. {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; U43883; AAC50473.1; -; Genomic_DNA.
DR EMBL; U43876; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U43877; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U43878; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U43880; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U43881; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U43882; AAC50473.1; JOINED; Genomic_DNA.
DR EMBL; U18423; AAA66242.1; -; mRNA.
DR EMBL; U80017; AAC52048.1; -; Genomic_DNA.
DR EMBL; AK289669; BAF82358.1; -; mRNA.
DR EMBL; AC004999; AAC83178.1; -; Genomic_DNA.
DR EMBL; AC005031; AAC62262.1; -; Genomic_DNA.
DR EMBL; U21914; AAA64505.1; -; mRNA.
DR EMBL; BC000908; AAH00908.1; -; mRNA.
DR EMBL; BC015308; AAH15308.1; -; mRNA.
DR EMBL; BC062723; AAH62723.1; -; mRNA.
DR EMBL; BC070242; AAH70242.1; -; mRNA.
DR CCDS; CCDS34181.1; -. [Q16637-1]
DR CCDS; CCDS34182.1; -. [Q16637-2]
DR CCDS; CCDS4007.1; -. [Q16637-1]
DR CCDS; CCDS4008.1; -. [Q16637-2]
DR CCDS; CCDS54867.1; -. [Q16637-3]
DR CCDS; CCDS75256.1; -. [Q16637-3]
DR PIR; A55477; A55477.
DR RefSeq; NP_000335.1; NM_000344.3. [Q16637-1]
DR RefSeq; NP_001284644.1; NM_001297715.1. [Q16637-3]
DR RefSeq; NP_059107.1; NM_017411.3. [Q16637-1]
DR RefSeq; NP_075012.1; NM_022874.2. [Q16637-2]
DR RefSeq; NP_075013.1; NM_022875.2. [Q16637-3]
DR RefSeq; NP_075014.1; NM_022876.2. [Q16637-2]
DR RefSeq; NP_075015.1; NM_022877.2. [Q16637-4]
DR RefSeq; XP_016865275.1; XM_017009786.1. [Q16637-4]
DR PDB; 1G5V; NMR; -; A=90-145.
DR PDB; 1MHN; X-ray; 1.80 A; A=89-147.
DR PDB; 2LEH; NMR; -; B=26-51.
DR PDB; 4A4E; NMR; -; A=84-147.
DR PDB; 4A4G; NMR; -; A=84-147.
DR PDB; 4GLI; X-ray; 1.90 A; A=263-294.
DR PDB; 4QQ6; X-ray; 1.75 A; A=82-147.
DR PDB; 5XJL; X-ray; 2.50 A; M=26-62.
DR PDB; 5XJQ; X-ray; 3.28 A; M=26-62.
DR PDB; 5XJR; X-ray; 3.12 A; M=26-62.
DR PDB; 5XJS; X-ray; 3.38 A; M=26-62.
DR PDB; 5XJT; X-ray; 2.92 A; M=26-62.
DR PDB; 5XJU; X-ray; 2.58 A; M=26-62.
DR PDBsum; 1G5V; -.
DR PDBsum; 1MHN; -.
DR PDBsum; 2LEH; -.
DR PDBsum; 4A4E; -.
DR PDBsum; 4A4G; -.
DR PDBsum; 4GLI; -.
DR PDBsum; 4QQ6; -.
DR PDBsum; 5XJL; -.
DR PDBsum; 5XJQ; -.
DR PDBsum; 5XJR; -.
DR PDBsum; 5XJS; -.
DR PDBsum; 5XJT; -.
DR PDBsum; 5XJU; -.
DR AlphaFoldDB; Q16637; -.
DR BMRB; Q16637; -.
DR SMR; Q16637; -.
DR BioGRID; 112490; 276.
DR BioGRID; 112491; 84.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; Q16637; -.
DR DIP; DIP-31309N; -.
DR IntAct; Q16637; 245.
DR MINT; Q16637; -.
DR STRING; 9606.ENSP00000370083; -.
DR BindingDB; Q16637; -.
DR ChEMBL; CHEMBL1293232; -.
DR GlyGen; Q16637; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16637; -.
DR PhosphoSitePlus; Q16637; -.
DR BioMuta; SMN1; -.
DR DMDM; 2498924; -.
DR EPD; Q16637; -.
DR jPOST; Q16637; -.
DR MassIVE; Q16637; -.
DR MaxQB; Q16637; -.
DR PaxDb; Q16637; -.
DR PeptideAtlas; Q16637; -.
DR PRIDE; Q16637; -.
DR ProteomicsDB; 60992; -. [Q16637-1]
DR ProteomicsDB; 60993; -. [Q16637-2]
DR ProteomicsDB; 60994; -. [Q16637-3]
DR ProteomicsDB; 60995; -. [Q16637-4]
DR Antibodypedia; 12087; 397 antibodies from 24 providers.
DR Antibodypedia; 3991; 307 antibodies from 36 providers.
DR DNASU; 6606; -.
DR Ensembl; ENST00000351205.8; ENSP00000305857.5; ENSG00000172062.17. [Q16637-1]
DR Ensembl; ENST00000380707.9; ENSP00000370083.4; ENSG00000172062.17. [Q16637-1]
DR Ensembl; ENST00000380741.8; ENSP00000370117.5; ENSG00000205571.14. [Q16637-1]
DR Ensembl; ENST00000380742.8; ENSP00000370118.4; ENSG00000205571.14. [Q16637-2]
DR Ensembl; ENST00000380743.9; ENSP00000370119.4; ENSG00000205571.14. [Q16637-1]
DR Ensembl; ENST00000503079.6; ENSP00000428128.1; ENSG00000172062.17. [Q16637-2]
DR Ensembl; ENST00000506163.5; ENSP00000424926.1; ENSG00000172062.17. [Q16637-3]
DR Ensembl; ENST00000611442.4; ENSP00000483768.1; ENSG00000277773.4. [Q16637-2]
DR Ensembl; ENST00000614240.4; ENSP00000479279.1; ENSG00000205571.14. [Q16637-2]
DR Ensembl; ENST00000614610.2; ENSP00000479920.1; ENSG00000273772.4. [Q16637-1]
DR Ensembl; ENST00000614773.4; ENSP00000481427.1; ENSG00000273772.4. [Q16637-2]
DR Ensembl; ENST00000618251.4; ENSP00000483515.1; ENSG00000277773.4. [Q16637-1]
DR Ensembl; ENST00000618661.2; ENSP00000483819.1; ENSG00000277773.4. [Q16637-1]
DR Ensembl; ENST00000622158.4; ENSP00000480906.1; ENSG00000275349.4. [Q16637-2]
DR Ensembl; ENST00000622739.2; ENSP00000482966.1; ENSG00000275349.4. [Q16637-1]
DR Ensembl; ENST00000624634.3; ENSP00000485595.1; ENSG00000277773.4. [Q16637-2]
DR Ensembl; ENST00000626847.2; ENSP00000486152.1; ENSG00000205571.14. [Q16637-3]
DR Ensembl; ENST00000627341.2; ENSP00000487421.1; ENSG00000273772.4. [Q16637-1]
DR Ensembl; ENST00000628353.2; ENSP00000487029.1; ENSG00000275349.4. [Q16637-3]
DR Ensembl; ENST00000628642.2; ENSP00000487015.1; ENSG00000273772.4. [Q16637-3]
DR Ensembl; ENST00000629122.2; ENSP00000487206.1; ENSG00000275349.4. [Q16637-1]
DR GeneID; 6606; -.
DR GeneID; 6607; -.
DR KEGG; hsa:6606; -.
DR KEGG; hsa:6607; -.
DR MANE-Select; ENST00000380707.9; ENSP00000370083.4; NM_000344.4; NP_000335.1.
DR MANE-Select; ENST00000380743.9; ENSP00000370119.4; NM_017411.4; NP_059107.1.
DR UCSC; uc003jyd.4; human. [Q16637-1]
DR CTD; 6606; -.
DR CTD; 6607; -.
DR DisGeNET; 6606; -.
DR DisGeNET; 6607; -.
DR GeneCards; SMN1; -.
DR GeneCards; SMN2; -.
DR GeneReviews; SMN1; -.
DR GeneReviews; SMN2; -.
DR HGNC; HGNC:11117; SMN1.
DR HGNC; HGNC:11118; SMN2.
DR HPA; ENSG00000172062; Low tissue specificity.
DR HPA; ENSG00000205571; Low tissue specificity.
DR MalaCards; SMN1; -.
DR MalaCards; SMN2; -.
DR MIM; 253300; phenotype.
DR MIM; 253400; phenotype.
DR MIM; 253550; phenotype.
DR MIM; 271150; phenotype.
DR MIM; 600354; gene.
DR MIM; 601627; gene.
DR neXtProt; NX_Q16637; -.
DR OpenTargets; ENSG00000172062; -.
DR OpenTargets; ENSG00000205571; -.
DR Orphanet; 83330; Proximal spinal muscular atrophy type 1.
DR Orphanet; 83418; Proximal spinal muscular atrophy type 2.
DR Orphanet; 83419; Proximal spinal muscular atrophy type 3.
DR Orphanet; 83420; Proximal spinal muscular atrophy type 4.
DR PharmGKB; PA35967; -.
DR VEuPathDB; HostDB:ENSG00000172062; -.
DR VEuPathDB; HostDB:ENSG00000205571; -.
DR eggNOG; KOG4327; Eukaryota.
DR GeneTree; ENSGT00940000153352; -.
DR HOGENOM; CLU_077852_0_0_1; -.
DR InParanoid; Q16637; -.
DR OMA; LMAWYMS; -.
DR OrthoDB; 1316275at2759; -.
DR PhylomeDB; Q16637; -.
DR TreeFam; TF318390; -.
DR PathwayCommons; Q16637; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; Q16637; -.
DR SIGNOR; Q16637; -.
DR BioGRID-ORCS; 6606; 35 hits in 247 CRISPR screens.
DR BioGRID-ORCS; 6607; 402 hits in 609 CRISPR screens.
DR ChiTaRS; SMN1; human.
DR ChiTaRS; SMN2; human.
DR EvolutionaryTrace; Q16637; -.
DR GeneWiki; SMN1; -.
DR GeneWiki; SMN2; -.
DR Pharos; Q16637; Tchem.
DR PRO; PR:Q16637; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q16637; protein.
DR Bgee; ENSG00000172062; Expressed in ventricular zone and 96 other tissues.
DR ExpressionAtlas; Q16637; baseline and differential.
DR Genevisible; Q16637; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR IDEAL; IID00569; -.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF06003; SMN; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Disease variant; Isopeptide bond; mRNA processing;
KW mRNA splicing; Neurodegeneration; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..294
FT /note="Survival motor neuron protein"
FT /id="PRO_0000218903"
FT DOMAIN 91..151
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..51
FT /note="Interacts with GEMIN2"
FT /evidence="ECO:0000269|PubMed:21816274,
FT ECO:0000269|PubMed:22607171, ECO:0000269|PubMed:26092730"
FT REGION 59..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..209
FT /note="Required for interaction with RPP20/POP7"
FT REGION 156..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..267
FT /note="P2 (binding site for SNRPB)"
FT REGION 252..280
FT /note="Involved in homooligomerization"
FT /evidence="ECO:0000269|PubMed:10500148,
FT ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:17178713,
FT ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:26092730"
FT REGION 279..294
FT /note="Required for interaction with SYNCRIP"
FT /evidence="ECO:0000269|PubMed:11574476"
FT COMPBIAS 156..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21609790,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 5
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21609790,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 8
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21609790,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:21609790"
FT MOD_RES 187
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21609790"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 210..241
FT /note="Missing (in isoform SMN-delta5 and isoform SMN-
FT delta57)"
FT /evidence="ECO:0000305"
FT /id="VSP_006183"
FT VAR_SEQ 279..282
FT /note="GFRQ -> EMLA (in isoform SMN-delta7 and isoform SMN-
FT delta57)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006184"
FT VAR_SEQ 283..294
FT /note="Missing (in isoform SMN-delta7 and isoform SMN-
FT delta57)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006185"
FT VARIANT 2
FT /note="A -> G (in SMA2 and SMA3; dbSNP:rs75030631)"
FT /evidence="ECO:0000269|PubMed:9837824"
FT /id="VAR_005615"
FT VARIANT 30
FT /note="D -> N (in SMA2; dbSNP:rs104893930)"
FT /evidence="ECO:0000269|PubMed:15580564"
FT /id="VAR_034803"
FT VARIANT 44
FT /note="D -> V (in SMA3; impairs GEMIN2 binding;
FT dbSNP:rs104893931)"
FT /evidence="ECO:0000269|PubMed:15580564,
FT ECO:0000269|PubMed:21816274"
FT /id="VAR_034804"
FT VARIANT 95
FT /note="G -> R (in SMA3; reduces SMN binding to Sm proteins;
FT dbSNP:rs104893927)"
FT /evidence="ECO:0000269|PubMed:15580564"
FT /id="VAR_034805"
FT VARIANT 111
FT /note="A -> G (in SMA2; reduces SMN binding to Sm proteins;
FT abolishes the interaction with ELAVL4; dbSNP:rs104893935)"
FT /evidence="ECO:0000269|PubMed:15580564,
FT ECO:0000269|PubMed:21088113"
FT /id="VAR_034806"
FT VARIANT 116
FT /note="I -> F (in SMA1; abolishes the interaction with
FT ELAVL4; dbSNP:rs104893933)"
FT /evidence="ECO:0000269|PubMed:15249625,
FT ECO:0000269|PubMed:21088113"
FT /id="VAR_034807"
FT VARIANT 136
FT /note="Q -> E (in SMA1; abolishes the interaction with
FT ELAVL4; dbSNP:rs104893934)"
FT /evidence="ECO:0000269|PubMed:15249625,
FT ECO:0000269|PubMed:21088113"
FT /id="VAR_034808"
FT VARIANT 245
FT /note="P -> L (in SMA3; dbSNP:rs75586164)"
FT /evidence="ECO:0000269|PubMed:10732817"
FT /id="VAR_010051"
FT VARIANT 262
FT /note="S -> G (in SMA3; dbSNP:rs104893932)"
FT /evidence="ECO:0000269|PubMed:15580564"
FT /id="VAR_034809"
FT VARIANT 262
FT /note="S -> I (in SMA3; slightly reduces SMN binding to
FT RPP20/POP7; dbSNP:rs75660264)"
FT /evidence="ECO:0000269|PubMed:14715275,
FT ECO:0000269|PubMed:9158159"
FT /id="VAR_005616"
FT VARIANT 272
FT /note="Y -> C (in SMA1; abolishes SMN1 binding to RPP20/
FT POP7 and severely impairs binding to SNRPB, GEMIN8 and
FT homooligomerization; dbSNP:rs104893922)"
FT /evidence="ECO:0000269|PubMed:10500148,
FT ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:14715275,
FT ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:33754639, ECO:0000269|PubMed:7813012"
FT /id="VAR_005617"
FT VARIANT 274
FT /note="T -> I (in SMA2 and SMA3; Impairs SMN1 binding to
FT RPP20/POP7, GEMIN8 and homooligomerization;
FT dbSNP:rs76871093)"
FT /evidence="ECO:0000269|PubMed:14715275,
FT ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:33754639, ECO:0000269|PubMed:9158159"
FT /id="VAR_005618"
FT VARIANT 275
FT /note="G -> S (in SMA3; impairs homooligomerization.;
FT dbSNP:rs77301881)"
FT /evidence="ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:9837824"
FT /id="VAR_005619"
FT VARIANT 279
FT /note="G -> C (in SMA2 and SMA3; dbSNP:rs77969175)"
FT /evidence="ECO:0000269|PubMed:10732802"
FT /id="VAR_007990"
FT VARIANT 279
FT /note="G -> V (in SMA1; slightly reduces SMN binding to
FT RPP20/POP7. Impairs homooligomerization and axon
FT localization; dbSNP:rs76163360)"
FT /evidence="ECO:0000269|PubMed:14715275,
FT ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:9147655"
FT /id="VAR_005620"
FT MUTAGEN 34
FT /note="W->A: Impairs GEMIN2 binding."
FT /evidence="ECO:0000269|PubMed:22607171"
FT MUTAGEN 39
FT /note="L->A: Impairs GEMIN2 binding."
FT /evidence="ECO:0000269|PubMed:22607171"
FT MUTAGEN 43
FT /note="Y->A: Impairs GEMIN2 binding."
FT /evidence="ECO:0000269|PubMed:22607171"
FT MUTAGEN 44
FT /note="D->A: Impairs GEMIN2 binding."
FT /evidence="ECO:0000269|PubMed:21816274"
FT MUTAGEN 46
FT /note="A->N: Impairs GEMIN2 binding."
FT /evidence="ECO:0000269|PubMed:22607171"
FT MUTAGEN 92
FT /note="W->S: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 102
FT /note="W->L,V: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 109
FT /note="Y->H: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 127
FT /note="Y->L,F: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 130
FT /note="Y->D: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 132
FT /note="N->D,S: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 134..136
FT /note="EEQ->SEV: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 134
FT /note="E->K: Impairs SMN binding to RPP20/POP7. Abolishes
FT the interaction with ELAVL4. Abolishes interaction with
FT SNRPD1 and SNRPD3. Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:11135666,
FT ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:21088113,
FT ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:22101937,
FT ECO:0000269|PubMed:29061699"
FT MUTAGEN 136
FT /note="Q->E: Impairs binding to substrate containing
FT dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT MUTAGEN 260
FT /note="L->S: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 263
FT /note="M->R,T,A: Impairs homooligomerization and GEMIN8
FT binding."
FT /evidence="ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:33754639"
FT MUTAGEN 264
FT /note="L->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 266
FT /note="S->P: Impairs homooligomerization and GEMIN8
FT binding."
FT /evidence="ECO:0000269|PubMed:23022347,
FT ECO:0000269|PubMed:33754639"
FT MUTAGEN 267
FT /note="W->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 268
FT /note="Y->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 271
FT /note="G->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 272
FT /note="Y->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 273
FT /note="H->R: Impairs GEMIN8 binding."
FT /evidence="ECO:0000269|PubMed:33754639"
FT MUTAGEN 274
FT /note="T->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 275
FT /note="G->A: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT MUTAGEN 279
FT /note="G->E: Impairs homooligomerization."
FT /evidence="ECO:0000269|PubMed:23022347"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:5XJL"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:4A4E"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4QQ6"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4QQ6"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:4QQ6"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:4QQ6"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4QQ6"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4QQ6"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4QQ6"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4QQ6"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:4GLI"
SQ SEQUENCE 294 AA; 31849 MW; 8A9A2A94192DCB9B CRC64;
MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF KHALKNGDIC
ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA IWSEDGCIYP ATIASIDFKR
ETCVVVYTGY GNREEQNLSD LLSPICEVAN NIEQNAQENE NESQVSTDES ENSRSPGNKS
DNIKPKSAPW NSFLPPPPPM PGPRLGPGKP GLKFNGPPPP PPPPPPHLLS CWLPPFPSGP
PIIPPPPPIC PDSLDDADAL GSMLISWYMS GYHTGYYMGF RQNQKEGRCS HSLN
