RSMB_RAT
ID RSMB_RAT Reviewed; 231 AA.
AC P17136; B0BN51;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Small nuclear ribonucleoprotein-associated protein B;
DE Short=snRNP-B;
DE Short=snRPB;
DE AltName: Full=SM11;
DE AltName: Full=Sm protein B;
DE Short=Sm-B;
DE Short=SmB;
GN Name=Snrpb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAI58687.1};
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-231.
RX PubMed=2532363; DOI=10.1073/pnas.86.24.9778;
RA Li S., Klein E.S., Russo A.F., Simmons D.M., Rosenfeld M.G.;
RT "Isolation of cDNA clones encoding small nuclear ribonucleoparticle-
RT associated proteins with different tissue specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9778-9782(1989).
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 (By similarity).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P14678}.
CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC spliceosome (By similarity). Most spliceosomal snRNPs contain a common
CC set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
CC SNRPG that assemble in a heptameric protein ring on the Sm site of the
CC small nuclear RNA to form the core snRNP (By similarity). Component of
CC the U1 snRNP (By similarity). The U1 snRNP is composed of the U1 snRNA
CC and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF
CC and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-
CC 70K, SNRPA/U1-A and SNRPC/U1-C (By similarity). Component of the U4/U6-
CC U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC and LSM8 (By similarity). Component of the U7 snRNP complex, or U7 Sm
CC protein core complex, that is composed of the U7 snRNA and at least
CC LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does
CC not contain SNRPD1 and SNRPD2 (By similarity). Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome (By similarity). Part
CC of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3,
CC GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core
CC snRNPs assembly (By similarity). Forms a 6S pICln-Sm complex composed
CC of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC unable to assemble into the core snRNP (By similarity). Identified in a
CC histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC SNRPB, SYNCRIP and YBX1 (By similarity). Interacts with TDRD3 and SNUPN
CC (By similarity). Interacts with PRMT5; interaction leads to its
CC symmetric arginine dimethylation (By similarity). Interacts with TDRD6;
CC interaction promotes association with PRMT5 (By similarity). Interacts
CC with SMN1; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000250|UniProtKB:P14678}.
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 -!- TISSUE SPECIFICITY: Heart, and less in brain, pituitary and liver.
CC -!- PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are
CC dimethylated, probably to asymmetric dimethylarginine (By similarity).
CC {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR07053729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473949; EDL80174.1; -; Genomic_DNA.
DR EMBL; BC158686; AAI58687.1; -; mRNA.
DR EMBL; M29295; AAA42159.1; ALT_INIT; mRNA.
DR PIR; B34503; B34503.
DR RefSeq; NP_599185.1; NM_134358.1.
DR AlphaFoldDB; P17136; -.
DR SMR; P17136; -.
DR STRING; 10116.ENSRNOP00000039298; -.
DR PhosphoSitePlus; P17136; -.
DR jPOST; P17136; -.
DR PaxDb; P17136; -.
DR PeptideAtlas; P17136; -.
DR PRIDE; P17136; -.
DR Ensembl; ENSRNOT00000049857; ENSRNOP00000039298; ENSRNOG00000006961.
DR GeneID; 171365; -.
DR KEGG; rno:171365; -.
DR UCSC; RGD:621301; rat.
DR CTD; 6628; -.
DR RGD; 621301; Snrpb.
DR eggNOG; KOG3168; Eukaryota.
DR GeneTree; ENSGT00940000155052; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR InParanoid; P17136; -.
DR OMA; KMINYRM; -.
DR OrthoDB; 1630470at2759; -.
DR PhylomeDB; P17136; -.
DR TreeFam; TF314232; -.
DR Reactome; R-RNO-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-RNO-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR PRO; PR:P17136; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000006961; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P17136; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISO:RGD.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:RGD.
DR GO; GO:0005685; C:U1 snRNP; IDA:RGD.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:RGD.
DR GO; GO:0005686; C:U2 snRNP; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:1990446; F:U1 snRNP binding; IDA:RGD.
DR GO; GO:1990447; F:U2 snRNP binding; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006479; P:protein methylation; ISO:RGD.
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 2: Evidence at transcript 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_0000125520"
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:0000250|UniProtKB:P14678"
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:0000250|UniProtKB:P14678"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14678"
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"
FT CONFLICT 20
FT /note="I -> S (in Ref. 4; AAA42159)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="D -> N (in Ref. 4; AAA42159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 23656 MW; 5CB0BB2E75B93D4A CRC64;
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGIGRAA GRGIPAGVPM
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQYPP GRGGPPPPMG
RGAPPPGMMG PPPGMRPPMG PPMGIPPGRG TPMGMPPPGM RPPPPGMRGL L
