GEMI5_HUMAN
ID GEMI5_HUMAN Reviewed; 1508 AA.
AC Q8TEQ6; Q14CV0; Q8WWV4; Q969W4; Q9H9K3; Q9UFI5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Gem-associated protein 5;
DE Short=Gemin5;
GN Name=GEMIN5;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION
RP WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION,
RP AND VARIANT GLN-682.
RC TISSUE=Cervix carcinoma;
RX PubMed=11714716; DOI=10.1074/jbc.m109448200;
RA Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.;
RT "Gemin5, a novel WD repeat protein component of the SMN complex that binds
RT Sm proteins.";
RL J. Biol. Chem. 277:5631-5636(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-682.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-682.
RC TISSUE=Cerebellum, and Lymph;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-737, AND VARIANT GLN-682.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1508, AND VARIANT GLN-682.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, AND IDENTIFICATION IN SMN-SM
RP COMPLEX.
RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005;
RA Golembe T.J., Yong J., Dreyfuss G.;
RT "Specific sequence features, recognized by the SMN complex, identify snRNAs
RT and determine their fate as snRNPs.";
RL Mol. Cell. Biol. 25:10989-11004(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, 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 FUNCTION.
RX PubMed=16857593; DOI=10.1016/j.molcel.2006.05.036;
RA Battle D.J., Lau C.-K., Wan L., Deng H., Lotti F., Dreyfuss G.;
RT "The Gemin5 protein of the SMN complex identifies snRNAs.";
RL Mol. Cell 23:273-279(2006).
RN [10]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN2.
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-751; SER-770; SER-778
RP AND SER-847, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
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 [14]
RP FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, AND MUTAGENESIS OF
RP 271-LYS--ARG-273; TRP-286 AND HIS-290.
RX PubMed=19377484; DOI=10.1038/nsmb.1584;
RA Lau C.K., Bachorik J.L., Dreyfuss G.;
RT "Gemin5-snRNA interaction reveals an RNA binding function for WD repeat
RT domains.";
RL Nat. Struct. Mol. Biol. 16:486-491(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH DDX20 AND GEMIN4, AND MUTAGENESIS OF TRP-286.
RX PubMed=19750007; DOI=10.1371/journal.pone.0007030;
RA Bradrick S.S., Gromeier M.;
RT "Identification of gemin5 as a novel 7-methylguanosine cap-binding
RT protein.";
RL PLoS ONE 4:E7030-E7030(2009).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20513430; DOI=10.1016/j.molcel.2010.03.014;
RA Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.;
RT "Gemin5 delivers snRNA precursors to the SMN complex for snRNP
RT biogenesis.";
RL Mol. Cell 38:551-562(2010).
RN [17]
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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND SER-778, AND
RP IDENTIFICATION BY 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-51; SER-624; SER-757
RP AND SER-778, 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 [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25911097; DOI=10.1074/jbc.m115.646257;
RA Workman E., Kalda C., Patel A., Battle D.J.;
RT "Gemin5 binds to the survival motor neuron mRNA to regulate SMN
RT expression.";
RL J. Biol. Chem. 290:15662-15669(2015).
RN [22]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS
RP RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN
RP COMPLEX, DOMAIN, AND MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381.
RX PubMed=27507887; DOI=10.1093/nar/gkw702;
RA Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.;
RT "The RNA-binding protein Gemin5 binds directly to the ribosome and
RT regulates global translation.";
RL Nucleic Acids Res. 44:8335-8351(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-754, AND IDENTIFICATION BY MASS
RP 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 [24]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-740 IN COMPLEXES WITH
RP 7-METHYLGUANOSINE CAP AND SNRNA ANALOGS, FUNCTION, DOMAIN, AND MUTAGENESIS
RP OF TRP-14; TYR-15; PHE-381; TYR-474; LYS-641; TYR-660 AND ARG-684.
RX PubMed=27834343; DOI=10.1038/cr.2016.133;
RA Tang X., Bharath S.R., Piao S., Tan V.Q., Bowler M.W., Song H.;
RT "Structural basis for specific recognition of pre-snRNA by Gemin5.";
RL Cell Res. 26:1353-1356(2016).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA
RP FRAGMENT AND 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, AND MUTAGENESIS OF
RP TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641.
RX PubMed=27881600; DOI=10.1101/gad.288340.116;
RA Xu C., Ishikawa H., Izumikawa K., Li L., He H., Nobe Y., Yamauchi Y.,
RA Shahjee H.M., Wu X.H., Yu Y.T., Isobe T., Takahashi N., Min J.;
RT "Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP
RT assembly.";
RL Genes Dev. 30:2376-2390(2016).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA
RP FRAGMENT AND 7-METHYLGUANOSINE CAP, DOMAIN, FUNCTION, AND MUTAGENESIS OF
RP TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422.
RX PubMed=27881601; DOI=10.1101/gad.291377.116;
RA Jin W., Wang Y., Liu C.P., Yang N., Jin M., Cong Y., Wang M., Xu R.M.;
RT "Structural basis for snRNA recognition by the double-WD40 repeat domain of
RT Gemin5.";
RL Genes Dev. 30:2391-2403(2016).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-739 IN COMPLEX WITH
RP 7-METHYLGUANOSINE CAP, FUNCTION, AND DOMAIN.
RA Chao X., Tempel W., Bian C., He H., Cerovina T., Bountra C.,
RA Arrowsmith C.H., Edwards A.M., Min J.;
RT "Crystal structure of Gemin5 WD40 repeats in complex with m7GpppG.";
RL Submitted (SEP-2016) to the PDB data bank.
RN [28]
RP VARIANTS NEDCAM PRO-73; 94-TRP--MET-1508 DEL; ARG-105; ARG-162; TYR-210;
RP 252-ARG--MET-1508 DEL; 534-TYR--MET-1508 DEL; MET-611; GLU-704; ARG-913;
RP PRO-923; PHE-925; HIS-958; PHE-988; PRO-1000; THR-1007; GLU-1019; PRO-1068;
RP SER-1119; HIS-1282; ASN-1286; CYS-1286; PRO-1364 AND PRO-1367, INVOLVEMENT
RP IN NEDCAM, CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068,
RP FUNCTION, AND INTERACTION WITH DDX20 AND GEMIN4.
RX PubMed=33963192; DOI=10.1038/s41467-021-22627-w;
RA Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S.,
RA Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J.,
RA Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K.,
RA Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P.,
RA Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C.,
RA Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N.,
RA Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S.,
RA Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A.,
RA Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M.,
RA Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J.,
RA Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y.,
RA Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S.,
RA Senderek J., Pandey U.B.;
RT "Loss of function mutations in GEMIN5 cause a neurodevelopmental
RT disorder.";
RL Nat. Commun. 12:2558-2558(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:16857593, PubMed:18984161, PubMed:20513430,
CC PubMed:33963192). Most spliceosomal snRNPs contain a common set of Sm
CC proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm
CC proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an
CC inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the
CC assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs,
CC the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an
CC intermediate (PubMed:18984161). Binding of snRNA inside 5Sm ultimately
CC triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN
CC complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs)
CC to the SMN complex (PubMed:11714716, PubMed:16857593, PubMed:19377484,
CC PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600,
CC PubMed:27881601, PubMed:16314521). Binds to the 7-methylguanosine cap
CC of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600,
CC PubMed:27881601, Ref.27). Binds to the 3'-UTR of SMN1 mRNA and
CC regulates its translation; does not affect mRNA stability
CC (PubMed:25911097). May play a role in the regulation of protein
CC synthesis via its interaction with ribosomes (PubMed:27507887).
CC {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:16314521,
CC ECO:0000269|PubMed:16857593, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007,
CC ECO:0000269|PubMed:20513430, ECO:0000269|PubMed:25911097,
CC ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343,
CC ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
CC ECO:0000269|PubMed:33963192, ECO:0000269|Ref.27}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (PubMed:20513430, PubMed:27507887, PubMed:16314521, PubMed:19377484,
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:11714716, PubMed:20513430, PubMed:16314521).
CC Interacts with GEMIN2; the interaction is direct (PubMed:17178713).
CC Interacts with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE; the
CC interaction is direct (PubMed:11714716). Interacts with cytosolic
CC DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887,
CC PubMed:33963192). Interacts with SNRNP70 and HNRNPU (PubMed:27507887).
CC Identified in a complex with 80S ribosomes; binds to the 60S large
CC ribosomal subunit (PubMed:27507887). Interacts with the ribosomal
CC subunits RPL3 and RPL4 (PubMed:27507887). {ECO:0000269|PubMed:11714716,
CC ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007,
CC ECO:0000269|PubMed:20513430, ECO:0000269|PubMed:27507887,
CC ECO:0000269|PubMed:33963192}.
CC -!- INTERACTION:
CC Q8TEQ6; P06730: EIF4E; NbExp=3; IntAct=EBI-443630, EBI-73440;
CC Q8TEQ6; Q16637: SMN2; NbExp=7; IntAct=EBI-443630, EBI-395421;
CC Q8TEQ6; P62304: SNRPE; NbExp=3; IntAct=EBI-443630, EBI-348082;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11714716}. Nucleus, gem
CC {ECO:0000269|PubMed:11714716}. Cytoplasm {ECO:0000269|PubMed:11714716,
CC ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:20513430,
CC ECO:0000269|PubMed:25911097, ECO:0000269|PubMed:27507887}. Note=Found
CC both in the nucleoplasm and in nuclear bodies called gems (Gemini of
CC Cajal bodies) that are often in proximity to Cajal (coiled) bodies.
CC Also found in the cytoplasm. {ECO:0000269|PubMed:11714716}.
CC -!- DOMAIN: The WD repeat domain mediates binding to U1 snRNA and to U4
CC snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343,
CC PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates
CC binding to the 7-methylguanosine cap that is found both on mRNA and
CC snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600,
CC PubMed:27881601, Ref.27). The regions that bind snRNA molecules and the
CC isolated 7-methylguanosine cap overlap at least partially
CC (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD
CC repeat domain mediates interaction with the 60S large ribosomal subunit
CC (PubMed:27507887). {ECO:0000269|PubMed:19377484,
CC ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:27507887,
CC ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600,
CC ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27}.
CC -!- DISEASE: Neurodevelopmental disorder with cerebellar atrophy and motor
CC dysfunction (NEDCAM) [MIM:619333]: An autosomal recessive disorder
CC characterized by global developmental delay with predominantly motor
CC abnormalities, axial hypotonia with decreased or absent reflexes, gait
CC ataxia and appendicular spasticity. Affected individuals have cognitive
CC impairment and speech delay. Brain imaging shows cerebellar atrophy.
CC {ECO:0000269|PubMed:33963192}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat gemin-5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84892.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY063750; AAL38980.1; -; mRNA.
DR EMBL; AK074066; BAB84892.2; ALT_INIT; mRNA.
DR EMBL; AC008421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008776; AAH08776.2; -; mRNA.
DR EMBL; BC014147; AAH14147.2; -; mRNA.
DR EMBL; BC113614; AAI13615.1; -; mRNA.
DR EMBL; AK022748; BAB14222.1; -; mRNA.
DR EMBL; AL117665; CAB56035.2; -; mRNA.
DR CCDS; CCDS4330.1; -.
DR PIR; T17345; T17345.
DR RefSeq; NP_001239085.1; NM_001252156.1.
DR RefSeq; NP_056280.2; NM_015465.4.
DR PDB; 5GXH; X-ray; 1.80 A; A=1-739.
DR PDB; 5GXI; X-ray; 1.85 A; A=1-739.
DR PDB; 5H1J; X-ray; 2.00 A; A=1-726.
DR PDB; 5H1K; X-ray; 1.90 A; A/B=1-726.
DR PDB; 5H1L; X-ray; 2.10 A; A=1-726.
DR PDB; 5H1M; X-ray; 2.49 A; A=1-726.
DR PDB; 5H3S; X-ray; 3.00 A; A/B=1-740.
DR PDB; 5H3T; X-ray; 2.57 A; A/B/C/D=1-740.
DR PDB; 5H3U; X-ray; 2.50 A; A/B=1-740.
DR PDB; 5TEE; X-ray; 1.65 A; A=1-739.
DR PDB; 5TEF; X-ray; 1.95 A; A=1-739.
DR PDB; 5THA; X-ray; 1.80 A; A=1-739.
DR PDB; 6RNQ; X-ray; 1.95 A; A/B=845-1096.
DR PDB; 6RNS; X-ray; 2.69 A; A/B=845-1096.
DR PDBsum; 5GXH; -.
DR PDBsum; 5GXI; -.
DR PDBsum; 5H1J; -.
DR PDBsum; 5H1K; -.
DR PDBsum; 5H1L; -.
DR PDBsum; 5H1M; -.
DR PDBsum; 5H3S; -.
DR PDBsum; 5H3T; -.
DR PDBsum; 5H3U; -.
DR PDBsum; 5TEE; -.
DR PDBsum; 5TEF; -.
DR PDBsum; 5THA; -.
DR PDBsum; 6RNQ; -.
DR PDBsum; 6RNS; -.
DR AlphaFoldDB; Q8TEQ6; -.
DR SMR; Q8TEQ6; -.
DR BioGRID; 117429; 173.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; Q8TEQ6; -.
DR ELM; Q8TEQ6; -.
DR IntAct; Q8TEQ6; 68.
DR MINT; Q8TEQ6; -.
DR STRING; 9606.ENSP00000285873; -.
DR GlyGen; Q8TEQ6; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8TEQ6; -.
DR PhosphoSitePlus; Q8TEQ6; -.
DR SwissPalm; Q8TEQ6; -.
DR BioMuta; GEMIN5; -.
DR DMDM; 296439335; -.
DR EPD; Q8TEQ6; -.
DR jPOST; Q8TEQ6; -.
DR MassIVE; Q8TEQ6; -.
DR MaxQB; Q8TEQ6; -.
DR PaxDb; Q8TEQ6; -.
DR PeptideAtlas; Q8TEQ6; -.
DR PRIDE; Q8TEQ6; -.
DR ProteomicsDB; 74478; -.
DR Antibodypedia; 28334; 76 antibodies from 17 providers.
DR DNASU; 25929; -.
DR Ensembl; ENST00000285873.8; ENSP00000285873.6; ENSG00000082516.9.
DR GeneID; 25929; -.
DR KEGG; hsa:25929; -.
DR MANE-Select; ENST00000285873.8; ENSP00000285873.6; NM_015465.5; NP_056280.2.
DR UCSC; uc003lvx.4; human.
DR CTD; 25929; -.
DR DisGeNET; 25929; -.
DR GeneCards; GEMIN5; -.
DR HGNC; HGNC:20043; GEMIN5.
DR HPA; ENSG00000082516; Low tissue specificity.
DR MIM; 607005; gene.
DR MIM; 619333; phenotype.
DR neXtProt; NX_Q8TEQ6; -.
DR OpenTargets; ENSG00000082516; -.
DR PharmGKB; PA134945791; -.
DR VEuPathDB; HostDB:ENSG00000082516; -.
DR eggNOG; ENOG502QPYZ; Eukaryota.
DR GeneTree; ENSGT00620000088064; -.
DR HOGENOM; CLU_004491_0_1_1; -.
DR InParanoid; Q8TEQ6; -.
DR OMA; YWFNRND; -.
DR OrthoDB; 283127at2759; -.
DR PhylomeDB; Q8TEQ6; -.
DR TreeFam; TF328886; -.
DR PathwayCommons; Q8TEQ6; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; Q8TEQ6; -.
DR SIGNOR; Q8TEQ6; -.
DR BioGRID-ORCS; 25929; 731 hits in 1049 CRISPR screens.
DR ChiTaRS; GEMIN5; human.
DR GeneWiki; GEMIN5; -.
DR GenomeRNAi; 25929; -.
DR Pharos; Q8TEQ6; Tbio.
DR PRO; PR:Q8TEQ6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TEQ6; protein.
DR Bgee; ENSG00000082516; Expressed in oocyte and 164 other tissues.
DR Genevisible; Q8TEQ6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034718; C:SMN-Gemin2 complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:UniProtKB.
DR GO; GO:0030622; F:U4atac snRNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR DisProt; DP03070; -.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 2.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Disease variant; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding; Translation regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..1508
FT /note="Gem-associated protein 5"
FT /id="PRO_0000051004"
FT REPEAT 62..104
FT /note="WD 1"
FT REPEAT 107..148
FT /note="WD 2"
FT REPEAT 150..189
FT /note="WD 3"
FT REPEAT 193..264
FT /note="WD 4"
FT REPEAT 280..321
FT /note="WD 5"
FT REPEAT 333..374
FT /note="WD 6"
FT REPEAT 377..417
FT /note="WD 7"
FT REPEAT 424..464
FT /note="WD 8"
FT REPEAT 468..509
FT /note="WD 9"
FT REPEAT 533..573
FT /note="WD 10"
FT REPEAT 576..622
FT /note="WD 11"
FT REPEAT 637..677
FT /note="WD 12"
FT REPEAT 680..720
FT /note="WD 13"
FT REGION 1..124
FT /note="Important for interaction with U1 snRNA"
FT /evidence="ECO:0000269|PubMed:19377484"
FT REGION 13..15
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
FT ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L"
FT REGION 715..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1362..1393
FT /evidence="ECO:0000255"
FT COMPBIAS 721..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 33
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
FT ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L"
FT SITE 284
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K"
FT SITE 335
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K"
FT SITE 359
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5GXI, ECO:0007744|PDB:5H1K,
FT ECO:0007744|PDB:5H1L"
FT SITE 381
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
FT ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L"
FT SITE 422
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K"
FT SITE 426
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5H1K"
FT SITE 470
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5H1K"
FT SITE 474
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
FT ECO:0007744|PDB:5H1M, ECO:0007744|PDB:5TEF"
FT SITE 556
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5H1K"
FT SITE 579
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5H1K"
FT SITE 641
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
FT ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5TEF"
FT SITE 660
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
FT ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1M,
FT ECO:0007744|PDB:5TEF"
FT SITE 684
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
FT ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5H1K"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 73
FT /note="S -> P (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085836"
FT VARIANT 94..1508
FT /note="Missing (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085837"
FT VARIANT 105
FT /note="H -> R (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085838"
FT VARIANT 162
FT /note="H -> R (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085839"
FT VARIANT 210
FT /note="D -> Y (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085840"
FT VARIANT 252..1508
FT /note="Missing (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085841"
FT VARIANT 534..1508
FT /note="Missing (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085842"
FT VARIANT 611
FT /note="V -> M (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085843"
FT VARIANT 682
FT /note="R -> Q (in dbSNP:rs1974777)"
FT /evidence="ECO:0000269|PubMed:11714716,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2"
FT /id="VAR_033807"
FT VARIANT 704
FT /note="D -> E (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085844"
FT VARIANT 913
FT /note="H -> R (in NEDCAM; impaired function in spliceosomal
FT snRNP assembly; decreased protein abundance; decreased
FT protein stability; decreased interaction with DDX20;
FT decreased interaction with GEMIN4)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085845"
FT VARIANT 923
FT /note="H -> P (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085846"
FT VARIANT 925
FT /note="L -> F (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085847"
FT VARIANT 958
FT /note="Y -> H (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085848"
FT VARIANT 988
FT /note="I -> F (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085849"
FT VARIANT 1000
FT /note="S -> P (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085850"
FT VARIANT 1007
FT /note="A -> T (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085851"
FT VARIANT 1019
FT /note="D -> E (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085852"
FT VARIANT 1068
FT /note="L -> P (in NEDCAM; impaired function in spliceosomal
FT snRNP assembly; decreased protein abundance; decreased
FT protein stability; decreased interaction with DDX20;
FT decreased interaction with GEMIN4)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085853"
FT VARIANT 1119
FT /note="L -> S (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085854"
FT VARIANT 1155
FT /note="P -> S (in dbSNP:rs6865950)"
FT /id="VAR_057604"
FT VARIANT 1282
FT /note="Y -> H (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085855"
FT VARIANT 1286
FT /note="Y -> C (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085856"
FT VARIANT 1286
FT /note="Y -> N (in NEDCAM)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085857"
FT VARIANT 1364
FT /note="H -> P (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085858"
FT VARIANT 1367
FT /note="L -> P (in NEDCAM; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33963192"
FT /id="VAR_085859"
FT MUTAGEN 14
FT /note="W->A: Abolishes interaction with U4 snRNA. No effect
FT on interaction with the isolated 7-methylguanosine cap that
FT is normally part of RNA molecules. No effect on interaction
FT with 80S ribosomes."
FT /evidence="ECO:0000269|PubMed:27507887,
FT ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600,
FT ECO:0000269|PubMed:27881601"
FT MUTAGEN 15
FT /note="Y->A: Abolishes interaction with U4 snRNA. No effect
FT on interaction with the isolated 7-methylguanosine cap that
FT is normally part of RNA molecules. No effect on interaction
FT with 80S ribosomes."
FT /evidence="ECO:0000269|PubMed:27507887,
FT ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600,
FT ECO:0000269|PubMed:27881601"
FT MUTAGEN 33
FT /note="R->A: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881601"
FT MUTAGEN 197
FT /note="E->A: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881600"
FT MUTAGEN 271..273
FT /note="KRR->AAA: No effect in interaction with U4 snRNA. No
FT effect on interaction with SMN complex."
FT /evidence="ECO:0000269|PubMed:19377484"
FT MUTAGEN 286
FT /note="W->A: Abolishes interaction with U4 snRNA. Abolishes
FT interaction with the 7-methylguanosine cap of RNA
FT molecules. No effect on interaction with SMN complex."
FT /evidence="ECO:0000269|PubMed:19377484,
FT ECO:0000269|PubMed:19750007"
FT MUTAGEN 290
FT /note="H->A: No effect in interaction with U4 snRNA. No
FT effect on interaction with SMN complex."
FT /evidence="ECO:0000269|PubMed:19377484"
FT MUTAGEN 335
FT /note="R->E: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881601"
FT MUTAGEN 359
FT /note="R->A: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881601"
FT MUTAGEN 381
FT /note="F->A: Strongly decreases interaction with U4 snRNA.
FT No effect on interaction with the isolated 7-
FT methylguanosine cap that is normally part of RNA molecules.
FT Abolishes interaction with 80S ribosomes."
FT /evidence="ECO:0000269|PubMed:27507887,
FT ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600"
FT MUTAGEN 381
FT /note="F->D: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881601"
FT MUTAGEN 422
FT /note="W->E: Abolishes interaction with U4 snRNA."
FT /evidence="ECO:0000269|PubMed:27881601"
FT MUTAGEN 474
FT /note="Y->A: Abolishes interaction with the isolated 7-
FT methylguanosine cap that is normally part of RNA
FT molecules."
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600"
FT MUTAGEN 641
FT /note="K->A: Abolishes interaction with the isolated 7-
FT methylguanosine cap that is normally part of RNA
FT molecules."
FT /evidence="ECO:0000269|PubMed:27834343,
FT ECO:0000269|PubMed:27881600"
FT MUTAGEN 660
FT /note="Y->A: Abolishes interaction with the isolated 7-
FT methylguanosine cap that is normally part of RNA
FT molecules."
FT /evidence="ECO:0000269|PubMed:27834343"
FT MUTAGEN 684
FT /note="R->A: Abolishes interaction with the isolated 7-
FT methylguanosine cap that is normally part of RNA
FT molecules."
FT /evidence="ECO:0000269|PubMed:27834343"
FT CONFLICT 299
FT /note="L -> P (in Ref. 5; BAB14222)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="T -> A (in Ref. 5; BAB14222)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5H3U"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5H1L"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5H3T"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5THA"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5H1K"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5H1J"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:5GXI"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:5H3T"
FT STRAND 473..479
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:5H1J"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:5H1M"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:5TEF"
FT HELIX 523..530
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:5TEE"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 594..598
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 599..607
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 615..620
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 651..659
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 707..711
FT /evidence="ECO:0007829|PDB:5TEE"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:5TEE"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:5GXH"
FT HELIX 850..856
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 860..874
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 885..889
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 891..895
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 899..916
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 919..929
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 932..942
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 947..952
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 953..956
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 958..974
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 978..987
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 991..1000
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1004..1014
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1020..1035
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1039..1048
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1052..1060
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1065..1078
FT /evidence="ECO:0007829|PDB:6RNQ"
FT HELIX 1081..1095
FT /evidence="ECO:0007829|PDB:6RNQ"
SQ SEQUENCE 1508 AA; 168589 MW; EA5293F395BBF14E CRC64;
MGQEPRTLPP SPNWYCARCS DAVPGGLFGF AARTSVFLVR VGPGAGESPG TPPFRVIGEL
VGHTERVSGF TFSHHPGQYN LCATSSDDGT VKIWDVETKT VVTEHALHQH TISTLHWSPR
VKDLIVSGDE KGVVFCYWFN RNDSQHLFIE PRTIFCLTCS PHHEDLVAIG YKDGIVVIID
ISKKGEVIHR LRGHDDEIHS IAWCPLPGED CLSINQEETS EEAEITNGNA VAQAPVTKGC
YLATGSKDQT IRIWSCSRGR GVMILKLPFL KRRGGGIDPT VKERLWLTLH WPSNQPTQLV
SSCFGGELLQ WDLTQSWRRK YTLFSASSEG QNHSRIVFNL CPLQTEDDKQ LLLSTSMDRD
VKCWDIATLE CSWTLPSLGG FAYSLAFSSV DIGSLAIGVG DGMIRVWNTL SIKNNYDVKN
FWQGVKSKVT ALCWHPTKEG CLAFGTDDGK VGLYDTYSNK PPQISSTYHK KTVYTLAWGP
PVPPMSLGGE GDRPSLALYS CGGEGIVLQH NPWKLSGEAF DINKLIRDTN SIKYKLPVHT
EISWKADGKI MALGNEDGSI EIFQIPNLKL ICTIQQHHKL VNTISWHHEH GSQPELSYLM
ASGSNNAVIY VHNLKTVIES SPESPVTITE PYRTLSGHTA KITSVAWSPH HDGRLVSASY
DGTAQVWDAL REEPLCNFRG HRGRLLCVAW SPLDPDCIYS GADDFCVHKW LTSMQDHSRP
PQGKKSIELE KKRLSQPKAK PKKKKKPTLR TPVKLESIDG NEEESMKENS GPVENGVSDQ
EGEEQAREPE LPCGLAPAVS REPVICTPVS SGFEKSKVTI NNKVILLKKE PPKEKPETLI
KKRKARSLLP LSTSLDHRSK EELHQDCLVL ATAKHSRELN EDVSADVEER FHLGLFTDRA
TLYRMIDIEG KGHLENGHPE LFHQLMLWKG DLKGVLQTAA ERGELTDNLV AMAPAAGYHV
WLWAVEAFAK QLCFQDQYVK AASHLLSIHK VYEAVELLKS NHFYREAIAI AKARLRPEDP
VLKDLYLSWG TVLERDGHYA VAAKCYLGAT CAYDAAKVLA KKGDAASLRT AAELAAIVGE
DELSASLALR CAQELLLANN WVGAQEALQL HESLQGQRLV FCLLELLSRH LEEKQLSEGK
SSSSYHTWNT GTEGPFVERV TAVWKSIFSL DTPEQYQEAF QKLQNIKYPS ATNNTPAKQL
LLHICHDLTL AVLSQQMASW DEAVQALLRA VVRSYDSGSF TIMQEVYSAF LPDGCDHLRD
KLGDHQSPAT PAFKSLEAFF LYGRLYEFWW SLSRPCPNSS VWVRAGHRTL SVEPSQQLDT
ASTEETDPET SQPEPNRPSE LDLRLTEEGE RMLSTFKELF SEKHASLQNS QRTVAEVQET
LAEMIRQHQK SQLCKSTANG PDKNEPEVEA EQPLCSSQSQ CKEEKNEPLS LPELTKRLTE
ANQRMAKFPE SIKAWPFPDV LECCLVLLLI RSHFPGCLAQ EMQQQAQELL QKYGNTKTYR
RHCQTFCM