RSMB_MOUSE
ID RSMB_MOUSE Reviewed; 231 AA.
AC P27048; Q3UJT1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Small nuclear ribonucleoprotein-associated protein B;
DE Short=snRNP-B;
DE Short=snRPB;
DE AltName: Full=Sm protein B;
DE Short=Sm-B;
DE Short=SmB;
GN Name=Snrpb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1376292; DOI=10.1016/0378-1119(92)90574-9;
RA Griffith A., deJonge E., Huang S., Ohosone Y., Craft J.E.;
RT "The murine gene encoding the highly conserved Sm B protein contains a
RT nonfunctional alternative 3' splice site.";
RL Gene 114:195-201(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A HISTONE PRE-MRNA
RP COMPLEX, RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [5]
RP FUNCTION, INTERACTION WITH TDRD6 AND PRMT5, AND METHYLATION.
RX PubMed=28263986; DOI=10.1371/journal.pgen.1006660;
RA Akpinar M., Lesche M., Fanourgakis G., Fu J., Anastassiadis K., Dahl A.,
RA Jessberger R.;
RT "TDRD6 mediates early steps of spliceosome maturation in primary
RT spermatocytes.";
RL PLoS Genet. 13:E1006660-E1006660(2017).
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:28263986).
CC Component of both the pre-catalytic spliceosome B complex and activated
CC spliceosome C complexes (By similarity). Is also a component of the
CC minor U12 spliceosome (By similarity). As part of the U7 snRNP it is
CC involved in histone pre-mRNA 3'-end processing (PubMed:19470752).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000269|PubMed:19470752,
CC ECO:0000269|PubMed:28263986}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome. 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. Component of the U1 snRNP. The U1
CC snRNP is composed of the U1 snRNA and the 7 core Sm proteins SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1
CC snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C.
CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3,
CC LSM4, LSM5, LSM6, LSM7 and LSM8 (By similarity). Component of the U7
CC snRNP complex, or U7 Sm protein core complex, that is composed of the
CC U7 snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and
CC SNRPG; the complex does not contain SNRPD1 and SNRPD2
CC (PubMed:19470752). Component of the U11/U12 snRNPs that are part of the
CC U12-type spliceosome. 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; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm
CC complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and
CC SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm
CC proteins and which is unable to assemble into the core snRNP (By
CC similarity). Identified in a histone pre-mRNA complex, at least
CC composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1
CC (PubMed:19470752). Interacts with TDRD3 and SNUPN (By similarity).
CC Interacts with PRMT5; interaction leads to its symmetric arginine
CC dimethylation (PubMed:28263986). Interacts with TDRD6; interaction
CC promotes association with PRMT5 (PubMed:28263986). Interacts with SMN1;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000269|PubMed:19470752,
CC ECO:0000269|PubMed:28263986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000269|PubMed:19470752}.
CC Note=SMN-mediated assembly into core snRNPs occurs in the cytosol
CC before SMN-mediated transport to the nucleus to be included in
CC spliceosomes. {ECO:0000250|UniProtKB:P14678}.
CC -!- PTM: Methylated by PRMT5 (PubMed:28263986). Arg-108 and Arg-112 are
CC dimethylated, probably to asymmetric dimethylarginine (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000305|PubMed:28263986}.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M58761; AAA40119.1; -; mRNA.
DR EMBL; AK146319; BAE27074.1; -; mRNA.
DR CCDS; CCDS16735.1; -.
DR PIR; I53659; I53659.
DR RefSeq; NP_033251.1; NM_009225.2.
DR AlphaFoldDB; P27048; -.
DR SMR; P27048; -.
DR BioGRID; 203377; 11.
DR IntAct; P27048; 4.
DR MINT; P27048; -.
DR STRING; 10090.ENSMUSP00000099488; -.
DR iPTMnet; P27048; -.
DR PhosphoSitePlus; P27048; -.
DR SwissPalm; P27048; -.
DR EPD; P27048; -.
DR MaxQB; P27048; -.
DR PaxDb; P27048; -.
DR PeptideAtlas; P27048; -.
DR PRIDE; P27048; -.
DR ProteomicsDB; 260858; -.
DR Antibodypedia; 4041; 158 antibodies from 27 providers.
DR DNASU; 20638; -.
DR Ensembl; ENSMUST00000103199; ENSMUSP00000099488; ENSMUSG00000027404.
DR GeneID; 20638; -.
DR KEGG; mmu:20638; -.
DR UCSC; uc008mij.1; mouse.
DR CTD; 6628; -.
DR MGI; MGI:98342; Snrpb.
DR VEuPathDB; HostDB:ENSMUSG00000027404; -.
DR eggNOG; KOG3168; Eukaryota.
DR GeneTree; ENSGT00940000155052; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR InParanoid; P27048; -.
DR OMA; KMINYRM; -.
DR OrthoDB; 1630470at2759; -.
DR PhylomeDB; P27048; -.
DR TreeFam; TF314232; -.
DR Reactome; R-MMU-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 20638; 28 hits in 111 CRISPR screens.
DR ChiTaRS; Snrpb; mouse.
DR PRO; PR:P27048; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P27048; protein.
DR Bgee; ENSMUSG00000027404; Expressed in choroid plexus of fourth ventricle and 264 other tissues.
DR ExpressionAtlas; P27048; baseline and differential.
DR Genevisible; P27048; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; ISO:MGI.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0005683; C:U7 snRNP; ISS:UniProtKB.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:1990447; F:U2 snRNP binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..231
FT /note="Small nuclear ribonucleoprotein-associated protein
FT B"
FT /id="PRO_0000125519"
FT REPEAT 175..181
FT REPEAT 191..196
FT REPEAT 216..221
FT REPEAT 222..228
FT REGION 163..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..228
FT /note="Repeat-rich region"
FT COMPBIAS 169..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 112
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P14678"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P63162"
SQ SEQUENCE 231 AA; 23656 MW; 5CB0BE7E20B93D4A CRC64;
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGIGRAA GRGIPAGVPM
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQYPP GRGGPPPPMG
RGAPPPGMMG PPPGMRPPMG PPMGLPPGRG TPMGMPPPGM RPPPPGMRGL L
