ID RUXE_MOUSE Reviewed; 92 AA. AC P62305; P08578; Q15498; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Small nuclear ribonucleoprotein E; DE Short=snRNP-E; DE AltName: Full=Sm protein E; DE Short=Sm-E; DE Short=SmE; GN Name=Snrpe; 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]. RC TISSUE=Liver; RX PubMed=1478669; DOI=10.1016/s0888-7543(05)80109-0; RA Fautsch M., Thompson M.A., Holicky E.L., Schultz P.J., Hallett J.B., RA Wieben E.D.; RT "Conservation of coding and transcriptional control sequences within the RT snRNP E protein gene."; RL Genomics 14:883-890(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Placenta; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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. Component of both the CC pre-catalytic spliceosome B complex and activated spliceosome C CC complexes. As a component of the minor spliceosome, involved in the CC splicing of U12-type introns in pre-mRNAs. As part of the U7 snRNP it CC is involved in histone 3'-end processing. CC {ECO:0000250|UniProtKB:P62304}. 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. Component of the U7 snRNP complex, or CC U7 Sm protein core complex, that is composed of the U7 snRNA and at CC least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex CC does not contain SNRPD1 and SNRPD2. Component of the minor spliceosome, CC which splices U12-type introns. 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. Forms a CC 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, CC SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics CC additional Sm proteins and which is unable to assemble into the core CC snRNP. Interacts with SMN1; the interaction is direct. Interacts with CC GEMIN2 (via N-terminus); the interaction is direct. Interacts with CC SNRPF; the interaction is direct. Interacts with SNRPG; the interaction CC is direct. {ECO:0000250|UniProtKB:P62304}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P62304}. Nucleus {ECO:0000250|UniProtKB:P62304}. 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:P62304}. CC -!- SIMILARITY: Belongs to the snRNP Sm proteins 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; X65703; CAA46625.1; ALT_SEQ; Genomic_DNA. DR EMBL; X65704; CAA46626.1; -; mRNA. DR EMBL; AK019462; BAB31734.1; -; mRNA. DR EMBL; BC008262; AAH08262.1; -; mRNA. DR EMBL; BC051207; AAH51207.1; -; mRNA. DR EMBL; BC055765; AAH55765.1; -; mRNA. DR CCDS; CCDS48364.1; -. DR PIR; I48778; I48778. DR RefSeq; NP_033253.1; NM_009227.3. DR AlphaFoldDB; P62305; -. DR SMR; P62305; -. DR BioGRID; 203380; 32. DR IntAct; P62305; 4. DR MINT; P62305; -. DR STRING; 10090.ENSMUSP00000128400; -. DR iPTMnet; P62305; -. DR PhosphoSitePlus; P62305; -. DR SwissPalm; P62305; -. DR EPD; P62305; -. DR jPOST; P62305; -. DR MaxQB; P62305; -. DR PaxDb; 10090-ENSMUSP00000128400; -. DR PeptideAtlas; P62305; -. DR ProteomicsDB; 256664; -. DR Pumba; P62305; -. DR TopDownProteomics; P62305; -. DR Antibodypedia; 53843; 230 antibodies from 24 providers. DR DNASU; 20643; -. DR Ensembl; ENSMUST00000166915.8; ENSMUSP00000128400.2; ENSMUSG00000090553.9. DR GeneID; 20643; -. DR KEGG; mmu:20643; -. DR UCSC; uc007cql.2; mouse. DR AGR; MGI:98346; -. DR CTD; 6635; -. DR MGI; MGI:98346; Snrpe. DR VEuPathDB; HostDB:ENSMUSG00000090553; -. DR eggNOG; KOG1774; Eukaryota. DR GeneTree; ENSGT00390000012818; -. DR HOGENOM; CLU_125186_1_0_1; -. DR InParanoid; P62305; -. DR OMA; VPPINCI; -. DR OrthoDB; 5113494at2759; -. DR PhylomeDB; P62305; -. DR TreeFam; TF314419; -. 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; 20643; 38 hits in 116 CRISPR screens. DR ChiTaRS; Snrpe; mouse. DR PRO; PR:P62305; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P62305; Protein. DR Bgee; ENSMUSG00000090553; Expressed in medial ganglionic eminence and 255 other cell types or tissues. DR ExpressionAtlas; P62305; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0034709; C:methylosome; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0034715; C:pICln-Sm protein complex; ISS:UniProtKB. DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central. 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; IBA:GO_Central. 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:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB. 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:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB. DR CDD; cd01718; Sm_E; 1. DR Gene3D; 2.30.30.100; -; 1. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR047575; Sm. DR InterPro; IPR001163; Sm_dom_euk/arc. DR InterPro; IPR027078; snRNP-E. DR PANTHER; PTHR11193; SMALL NUCLEAR RIBONUCLEOPROTEIN E; 1. DR PANTHER; PTHR11193:SF9; SMALL NUCLEAR RIBONUCLEOPROTEIN E; 1. DR Pfam; PF01423; LSM; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1. DR PROSITE; PS52002; SM; 1. DR Genevisible; P62305; MM. PE 1: Evidence at protein level; KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome; KW Ribonucleoprotein; RNA-binding; Spliceosome. FT CHAIN 1..92 FT /note="Small nuclear ribonucleoprotein E" FT /id="PRO_0000125530" FT DOMAIN 18..92 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" SQ SEQUENCE 92 AA; 10804 MW; 7D8881CE1F4FA2FD CRC64; MAYRGQGQKV QKVMVQPINL IFRYLQNRSR IQVWLYEQVN MRIEGCIIGF DEYMNLVLDD AEEIHSKTKS RKQLGRIMLK GDNITLLQSV SN //