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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
 
 
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