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Database: UniProt
Entry: P62308
LinkDB: P62308
Original site: P62308 
ID   RUXG_HUMAN              Reviewed;          76 AA.
AC   P62308; D6W5G6; Q15357; Q6IB86;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 170.
DE   RecName: Full=Small nuclear ribonucleoprotein G;
DE            Short=snRNP-G;
DE   AltName: Full=Sm protein G;
DE            Short=Sm-G;
DE            Short=SmG;
GN   Name=SNRPG; Synonyms=PBSCG;
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].
RX   PubMed=7744013; DOI=10.1002/j.1460-2075.1995.tb07199.x;
RA   Hermann H., Fabrizio P., Raker V.A., Foulaki K., Hornig H., Brahms H.,
RA   Luehrmann R.;
RT   "snRNP Sm proteins share two evolutionarily conserved sequence motifs which
RT   are involved in Sm protein-protein interactions.";
RL   EMBO J. 14:2076-2088(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone, Brain, Pancreas, and Placenta;
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   [6]
RP   IDENTIFICATION IN THE U7 SNRNP COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11574479; DOI=10.1093/emboj/20.19.5470;
RA   Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.;
RT   "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new
RT   14 kDa Sm D1-like protein.";
RL   EMBO J. 20:5470-5479(2001).
RN   [7]
RP   INTERACTION WITH TACC1.
RX   PubMed=12165861; DOI=10.1038/sj.onc.1205658;
RA   Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C.,
RA   Geneix J., Isnardon D., Jacquemier J., Birnbaum D.;
RT   "Carcinogenesis and translational controls: TACC1 is down-regulated in
RT   human cancers and associates with mRNA regulators.";
RL   Oncogene 21:5619-5630(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C
RP   COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
RN   [9]
RP   FUNCTION OF THE U7 SNRNP COMPLEX, AND SUBUNIT.
RX   PubMed=12975319; DOI=10.1101/gad.274403;
RA   Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U.,
RA   Schuemperli D.;
RT   "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT   complex and the role of a new component, Lsm11, in histone RNA
RT   processing.";
RL   Genes Dev. 17:2321-2333(2003).
RN   [10]
RP   IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15146077; DOI=10.1261/rna.7320604;
RA   Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA   Tuschl T., Luehrmann R.;
RT   "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT   the U2-dependent spliceosome.";
RL   RNA 10:929-941(2004).
RN   [11]
RP   IDENTIFICATION IN THE SMN-SM 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   [12]
RP   FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX,
RP   IDENTIFICATION IN SMN-SM COMPLEX, AND SUBCELLULAR LOCATION.
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   [13]
RP   X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 IN SPLICEOSOMAL U1 SNRNP,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19325628; DOI=10.1038/nature07851;
RA   Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.;
RT   "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.";
RL   Nature 458:475-480(2009).
RN   [14] {ECO:0007744|PDB:5XJL}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SNRPD1; SNRPD2;
RP   SNRPE; SNRPF; SMN1 AND GEMIN2, AND INTERACTION WITH GEMIN2 AND SNRPE.
RX   PubMed=21816274; DOI=10.1016/j.cell.2011.06.043;
RA   Zhang R., So B.R., Li P., Yong J., Glisovic T., Wan L., Dreyfuss G.;
RT   "Structure of a key intermediate of the SMN complex reveals Gemin2's
RT   crucial function in snRNP assembly.";
RL   Cell 146:384-395(2011).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP, AND
RP   SUBUNIT.
RX   PubMed=21516107; DOI=10.1038/nature09956;
RA   Leung A.K., Nagai K., Li J.;
RT   "Structure of the spliceosomal U4 snRNP core domain and its implication for
RT   snRNP biogenesis.";
RL   Nature 473:536-539(2011).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX,
RP   IDENTIFICATION IN 6S PICLN-SM COMPLEX, AND FUNCTION IN CORE U1 SNRNP
RP   BIOGENESIS.
RX   PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009;
RA   Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K.,
RA   Stark H., Schindelin H., Fischer U.;
RT   "Structural basis of assembly chaperone-mediated snRNP formation.";
RL   Mol. Cell 49:692-703(2013).
RN   [17] {ECO:0007744|PDB:4PJO}
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), AND SUBUNIT.
RX   PubMed=25555158; DOI=10.7554/elife.04986;
RA   Kondo Y., Oubridge C., van Roon A.M., Nagai K.;
RT   "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein
RT   particle, reveals the mechanism of 5' splice site recognition.";
RL   Elife 4:0-0(2015).
RN   [18] {ECO:0007744|PDB:3JCR}
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP   SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=26912367; DOI=10.1126/science.aad2085;
RA   Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA   Luhrmann R., Stark H.;
RT   "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL   Science 351:1416-1420(2016).
RN   [19] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [20] {ECO:0007744|PDB:5O9Z}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA   Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA   Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT   "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT   Activation.";
RL   Cell 170:701-713(2017).
RN   [21] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
RN   [22] {ECO:0007744|PDB:5XJQ, ECO:0007744|PDB:5XJR}
RP   X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) IN COMPLEX WITH GEMIN2; SNRPD1;
RP   SNRPD2; SNRPE; SNRPF AND SMN1, AND INTERACTION WITH SNRPE.
RX   PubMed=31799625; DOI=10.1093/nar/gkz1135;
RA   Yi H., Mu L., Shen C., Kong X., Wang Y., Hou Y., Zhang R.;
RT   "Negative cooperativity between Gemin2 and RNA provides insights into RNA
RT   selection and the SMN complex's release in snRNP assembly.";
RL   Nucleic Acids Res. 48:895-911(2020).
CC   -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC       spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC       (snRNPs), the building blocks of the spliceosome (PubMed:11991638,
CC       PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158,
CC       PubMed:26912367, PubMed:28502770, PubMed:28781166, PubMed:28076346).
CC       Component of both the pre-catalytic spliceosome B complex and activated
CC       spliceosome C complexes (PubMed:11991638, PubMed:28502770,
CC       PubMed:28781166, PubMed:28076346). Is also a component of the minor U12
CC       spliceosome (PubMed:15146077). As part of the U7 snRNP it is involved
CC       in histone 3'-end processing (PubMed:12975319).
CC       {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12975319,
CC       ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161,
CC       ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:23333303,
CC       ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:28781166}.
CC   -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC       nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC       spliceosome (PubMed:11991638, PubMed:19325628, PubMed:21516107,
CC       PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC       PubMed:28076346). 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 (PubMed:19325628, PubMed:21516107,
CC       PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC       PubMed:28076346). Component of the U1 snRNP (PubMed:19325628,
CC       PubMed:25555158). The U1 snRNP is composed of the U1 snRNA and the 7
CC       core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG,
CC       and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-
CC       A and SNRPC/U1-C (PubMed:19325628, PubMed:25555158). Component of the
CC       U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC       least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC       SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2,
CC       PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5,
CC       LSM6, LSM7 and LSM8 (PubMed:26912367). Component of the U7 snRNP
CC       complex, or U7 Sm protein core complex, that is composed of the U7
CC       snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG;
CC       the complex does not contain SNRPD1 and SNRPD2 (PubMed:11574479,
CC       PubMed:12975319). Component of the U11/U12 snRNPs that are part of the
CC       U12-type spliceosome (PubMed:15146077). Part of the SMN-Sm complex that
CC       contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC       GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC       SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly
CC       (PubMed:18984161, PubMed:16314521). Forms a 6S pICln-Sm complex
CC       composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-
CC       like structure where CLNS1A/pICln mimics additional Sm proteins and
CC       which is unable to assemble into the core snRNP (PubMed:18984161,
CC       PubMed:23333303). Interacts with GEMIN2 (via N-terminus); the
CC       interaction is direct (PubMed:21816274). Interacts with SNRPE; the
CC       interaction is direct (PubMed:21816274, PubMed:31799625).
CC       {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:12975319, ECO:0000269|PubMed:15146077,
CC       ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19325628,
CC       ECO:0000269|PubMed:21516107, ECO:0000269|PubMed:21816274,
CC       ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:25555158,
CC       ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC       ECO:0000269|PubMed:31799625}.
CC   -!- INTERACTION:
CC       P62308; P54105: CLNS1A; NbExp=9; IntAct=EBI-624585, EBI-724693;
CC       P62308; Q96D03: DDIT4L; NbExp=13; IntAct=EBI-624585, EBI-742054;
CC       P62308; Q13643: FHL3; NbExp=6; IntAct=EBI-624585, EBI-741101;
CC       P62308; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-624585, EBI-9088619;
CC       P62308; Q8NCF5-2: NFATC2IP; NbExp=3; IntAct=EBI-624585, EBI-12305293;
CC       P62308; P62304: SNRPE; NbExp=8; IntAct=EBI-624585, EBI-348082;
CC       P62308; O75410-1: TACC1; NbExp=5; IntAct=EBI-624585, EBI-624252;
CC       P62308; O95988: TCL1B; NbExp=3; IntAct=EBI-624585, EBI-727338;
CC       P62308; Q03403: TFF2; NbExp=3; IntAct=EBI-624585, EBI-4314702;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}.
CC       Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-
CC       mediated assembly into core snRNPs occurs in the cytosol before SMN-
CC       mediated transport to the nucleus to be included in spliceosomes.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; X85373; CAA59689.1; -; mRNA.
DR   EMBL; CR456918; CAG33199.1; -; mRNA.
DR   EMBL; AC079338; AAX81996.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99817.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99818.1; -; Genomic_DNA.
DR   EMBL; BC000070; AAH00070.1; -; mRNA.
DR   EMBL; BC022432; AAH22432.1; -; mRNA.
DR   EMBL; BC066302; AAH66302.1; -; mRNA.
DR   EMBL; BC070166; AAH70166.1; -; mRNA.
DR   EMBL; BC071880; AAH71880.1; -; mRNA.
DR   EMBL; BC106055; AAI06056.1; -; mRNA.
DR   CCDS; CCDS1903.1; -.
DR   PIR; S55054; S55054.
DR   RefSeq; NP_003087.1; NM_003096.3.
DR   PDB; 3CW1; X-ray; 5.49 A; 3/4/5/G=1-76.
DR   PDB; 3JCR; EM; 7.00 A; U/u=1-76.
DR   PDB; 3PGW; X-ray; 4.40 A; G/J=1-76.
DR   PDB; 4F7U; X-ray; 1.90 A; G/J=1-76.
DR   PDB; 4PJO; X-ray; 3.30 A; G/U/g/u=1-76.
DR   PDB; 4V98; X-ray; 3.10 A; A4/AH/AP/AX/Af/An/Av/B4/BH/BP/BX/Bf/Bn/Bv/CH/CP/CX/Cf/Cn/Cv=1-76.
DR   PDB; 4WZJ; X-ray; 3.60 A; AG/AN/AU/BG/BN/BU/CG/CN/CU/DG/DN/DU=1-76.
DR   PDB; 5MQF; EM; 5.90 A; d/k=1-76.
DR   PDB; 5O9Z; EM; 4.50 A; V/d/k=1-76.
DR   PDB; 5XJC; EM; 3.60 A; g/n=1-76.
DR   PDB; 5XJL; X-ray; 2.50 A; G=1-76.
DR   PDB; 5XJQ; X-ray; 3.28 A; G=1-76.
DR   PDB; 5XJR; X-ray; 3.12 A; G=1-76.
DR   PDB; 5XJT; X-ray; 2.92 A; G=1-76.
DR   PDB; 5XJU; X-ray; 2.58 A; G=1-76.
DR   PDB; 5YZG; EM; 4.10 A; g/n=1-76.
DR   PDB; 5Z56; EM; 5.10 A; g/n=1-76.
DR   PDB; 5Z57; EM; 6.50 A; g/n=1-76.
DR   PDB; 5Z58; EM; 4.90 A; g/n=1-76.
DR   PDB; 6AH0; EM; 5.70 A; S/d/n=1-76.
DR   PDB; 6AHD; EM; 3.80 A; S/f/n=1-76.
DR   PDB; 6FF7; EM; 4.50 A; d/k=1-76.
DR   PDB; 6ICZ; EM; 3.00 A; g/n=1-76.
DR   PDB; 6ID0; EM; 2.90 A; g/n=1-76.
DR   PDB; 6ID1; EM; 2.86 A; g/n=1-76.
DR   PDB; 6QDV; EM; 3.30 A; g/r=4-76.
DR   PDB; 6QW6; EM; 2.92 A; 4g/5g=1-76.
DR   PDB; 6QX9; EM; 3.28 A; 1g/2g/4g/5g=1-76.
DR   PDB; 6V4X; EM; 3.20 A; G=1-76.
DR   PDB; 6Y53; EM; 7.10 A; k=1-76.
DR   PDB; 6Y5Q; EM; 7.10 A; k=1-76.
DR   PDB; 7A5P; EM; 5.00 A; g/k=1-76.
DR   PDB; 7ABG; EM; 7.80 A; d/k=1-76.
DR   PDB; 7ABI; EM; 8.00 A; d/k=1-76.
DR   PDB; 7B0Y; EM; 3.60 A; h=1-76.
DR   PDB; 7DVQ; EM; 2.89 A; g/n=1-76.
DR   PDBsum; 3CW1; -.
DR   PDBsum; 3JCR; -.
DR   PDBsum; 3PGW; -.
DR   PDBsum; 4F7U; -.
DR   PDBsum; 4PJO; -.
DR   PDBsum; 4V98; -.
DR   PDBsum; 4WZJ; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5O9Z; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5XJL; -.
DR   PDBsum; 5XJQ; -.
DR   PDBsum; 5XJR; -.
DR   PDBsum; 5XJT; -.
DR   PDBsum; 5XJU; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 5Z58; -.
DR   PDBsum; 6AH0; -.
DR   PDBsum; 6AHD; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6QW6; -.
DR   PDBsum; 6QX9; -.
DR   PDBsum; 6V4X; -.
DR   PDBsum; 6Y53; -.
DR   PDBsum; 6Y5Q; -.
DR   PDBsum; 7A5P; -.
DR   PDBsum; 7ABG; -.
DR   PDBsum; 7ABI; -.
DR   PDBsum; 7B0Y; -.
DR   PDBsum; 7DVQ; -.
DR   SMR; P62308; -.
DR   BioGRID; 112521; 151.
DR   ComplexPortal; CPX-6033; Sm complex.
DR   CORUM; P62308; -.
DR   DIP; DIP-34627N; -.
DR   IntAct; P62308; 52.
DR   MINT; P62308; -.
DR   STRING; 9606.ENSP00000272348; -.
DR   iPTMnet; P62308; -.
DR   PhosphoSitePlus; P62308; -.
DR   SwissPalm; P62308; -.
DR   BioMuta; SNRPG; -.
DR   DMDM; 59800216; -.
DR   EPD; P62308; -.
DR   jPOST; P62308; -.
DR   MassIVE; P62308; -.
DR   MaxQB; P62308; -.
DR   PaxDb; P62308; -.
DR   PeptideAtlas; P62308; -.
DR   PRIDE; P62308; -.
DR   ProteomicsDB; 57388; -.
DR   TopDownProteomics; P62308; -.
DR   Antibodypedia; 31102; 143 antibodies.
DR   DNASU; 6637; -.
DR   Ensembl; ENST00000272348; ENSP00000272348; ENSG00000143977.
DR   GeneID; 6637; -.
DR   KEGG; hsa:6637; -.
DR   UCSC; uc002sgp.4; human.
DR   CTD; 6637; -.
DR   DisGeNET; 6637; -.
DR   GeneCards; SNRPG; -.
DR   HGNC; HGNC:11163; SNRPG.
DR   HPA; ENSG00000143977; Low tissue specificity.
DR   MIM; 603542; gene.
DR   neXtProt; NX_P62308; -.
DR   OpenTargets; ENSG00000143977; -.
DR   PharmGKB; PA36004; -.
DR   VEuPathDB; HostDB:ENSG00000143977; -.
DR   eggNOG; KOG1780; Eukaryota.
DR   GeneTree; ENSGT00510000046985; -.
DR   HOGENOM; CLU_076902_10_1_1; -.
DR   InParanoid; P62308; -.
DR   OMA; NANRMIV; -.
DR   TreeFam; TF315099; -.
DR   PathwayCommons; P62308; -.
DR   Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR   Reactome; R-HSA-191859; snRNP Assembly.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR   BioGRID-ORCS; 6637; 742 hits in 951 CRISPR screens.
DR   ChiTaRS; SNRPG; human.
DR   EvolutionaryTrace; P62308; -.
DR   GeneWiki; SNRPG; -.
DR   GenomeRNAi; 6637; -.
DR   Pharos; P62308; Tbio.
DR   PRO; PR:P62308; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P62308; protein.
DR   Bgee; ENSG00000143977; Expressed in subventricular zone (inner) (primate) and 115 other tissues.
DR   ExpressionAtlas; P62308; baseline and differential.
DR   Genevisible; P62308; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; NAS:UniProtKB.
DR   GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; TAS:UniProtKB.
DR   GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR   GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR   GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR   GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:1990446; F:U1 snRNP binding; IEA:Ensembl.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR   GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR   CDD; cd01719; Sm_G; 1.
DR   IDEAL; IID00158; -.
DR   InterPro; IPR044641; Lsm7/SmG-like.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR034098; Sm_G.
DR   PANTHER; PTHR10553; PTHR10553; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..76
FT                   /note="Small nuclear ribonucleoprotein G"
FT                   /id="PRO_0000125545"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          25..34
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          40..47
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:5XJT"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:5XJL"
SQ   SEQUENCE   76 AA;  8496 MW;  623302BF6BE758FE CRC64;
     MSKAHPPELK KFMDKKLSLK LNGGRHVQGI LRGFDPFMNL VIDECVEMAT SGQQNNIGMV
     VIRGNSIIML EALERV
//
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