RU17_MOUSE
ID RU17_MOUSE Reviewed; 448 AA.
AC Q62376; Q3UIW4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE Short=U1 snRNP 70 kDa;
DE Short=U1-70K;
DE Short=snRNP70;
GN Name=Snrnp70; Synonyms=Snrp70;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-448 (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RX PubMed=2525092; DOI=10.1111/j.1432-1033.1989.tb14798.x;
RA Hornig H., Fischer U., Costas M., Rauh A., Luehrmann R.;
RT "Analysis of genomic clones of the murine U1RNA-associated 70-kDa protein
RT reveals a high evolutionary conservation of the protein between human and
RT mouse.";
RL Eur. J. Biochem. 182:45-50(1989).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP INTERACTION WITH SCNM1, AND SUBCELLULAR LOCATION.
RX PubMed=17656373; DOI=10.1093/hmg/ddm206;
RA Howell V.M., Jones J.M., Bergren S.K., Li L., Billi A.C., Avenarius M.R.,
RA Meisler M.H.;
RT "Evidence for a direct role of the disease modifier SCNM1 in splicing.";
RL Hum. Mol. Genet. 16:2506-2516(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-419, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-408, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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: Component of the spliceosomal U1 snRNP, which is essential
CC for recognition of the pre-mRNA 5' splice-site and the subsequent
CC assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-
CC snRNA. {ECO:0000250|UniProtKB:P08621}.
CC -!- FUNCTION: [Isoform 2]: Truncated isoforms that lack the RRM domain
CC cannot bind U1-snRNA. {ECO:0000250|UniProtKB:P08621}.
CC -!- SUBUNIT: Component of the U1 snRNP. The U1 snRNP is composed of the U1
CC snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm
CC site of the small nuclear RNA to form the core snRNP, and at least
CC three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and
CC SNRPC/U1-C (By similarity). Interacts with SCNM1 (PubMed:17656373).
CC Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70,
CC SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer
CC (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Interacts
CC with dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5,
CC CPSF6, SCAF11, and ZRANB2. Interacts with GEMIN5 (By similarity).
CC Interacts with FUS (By similarity). {ECO:0000250|UniProtKB:P08621,
CC ECO:0000269|PubMed:17656373}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17656373}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373}. Note=Colocalizes
CC with SCNM1 and LUC7L2 in nuclear speckles.
CC {ECO:0000269|PubMed:17656373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62376-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62376-2; Sequence=VSP_005851, VSP_005852;
CC -!- DOMAIN: The RRM domain mediates interaction with U1 RNA.
CC {ECO:0000250|UniProtKB:P08621}.
CC -!- PTM: Extensively phosphorylated on serine residues in the C-terminal
CC region. {ECO:0000250|UniProtKB:P08621}.
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; AK133115; BAE21515.1; -; mRNA.
DR EMBL; AK146729; BAE27392.1; -; mRNA.
DR EMBL; X15769; CAA33777.1; -; Genomic_DNA.
DR EMBL; X15770; CAA33777.1; JOINED; Genomic_DNA.
DR EMBL; X15771; CAA33777.1; JOINED; Genomic_DNA.
DR EMBL; X15772; CAA33777.1; JOINED; Genomic_DNA.
DR EMBL; X15774; CAA33777.1; JOINED; Genomic_DNA.
DR EMBL; X15775; CAA33777.1; JOINED; Genomic_DNA.
DR EMBL; X15776; CAA33777.1; JOINED; Genomic_DNA.
DR CCDS; CCDS21240.1; -. [Q62376-1]
DR PIR; S04336; S04336.
DR PIR; S04824; S04824.
DR RefSeq; NP_033250.3; NM_009224.5. [Q62376-1]
DR RefSeq; XP_006540795.1; XM_006540732.3. [Q62376-1]
DR AlphaFoldDB; Q62376; -.
DR SMR; Q62376; -.
DR BioGRID; 203376; 53.
DR IntAct; Q62376; 31.
DR MINT; Q62376; -.
DR STRING; 10090.ENSMUSP00000074160; -.
DR iPTMnet; Q62376; -.
DR PhosphoSitePlus; Q62376; -.
DR SwissPalm; Q62376; -.
DR EPD; Q62376; -.
DR jPOST; Q62376; -.
DR MaxQB; Q62376; -.
DR PaxDb; Q62376; -.
DR PeptideAtlas; Q62376; -.
DR PRIDE; Q62376; -.
DR ProteomicsDB; 260745; -. [Q62376-1]
DR ProteomicsDB; 260746; -. [Q62376-2]
DR Antibodypedia; 3444; 193 antibodies from 25 providers.
DR DNASU; 20637; -.
DR Ensembl; ENSMUST00000074575; ENSMUSP00000074160; ENSMUSG00000063511. [Q62376-1]
DR GeneID; 20637; -.
DR KEGG; mmu:20637; -.
DR UCSC; uc009guw.2; mouse. [Q62376-1]
DR CTD; 6625; -.
DR MGI; MGI:98341; Snrnp70.
DR VEuPathDB; HostDB:ENSMUSG00000063511; -.
DR eggNOG; KOG0113; Eukaryota.
DR GeneTree; ENSGT00940000160292; -.
DR HOGENOM; CLU_045151_1_0_1; -.
DR InParanoid; Q62376; -.
DR OMA; GVAKFMA; -.
DR PhylomeDB; Q62376; -.
DR TreeFam; TF314215; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 20637; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Snrnp70; mouse.
DR PRO; PR:Q62376; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62376; protein.
DR Bgee; ENSMUSG00000063511; Expressed in retinal neural layer and 259 other tissues.
DR ExpressionAtlas; Q62376; baseline and differential.
DR Genevisible; Q62376; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR CDD; cd12236; RRM_snRNP70; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034143; snRNP70_RRM.
DR InterPro; IPR022023; U1snRNP70_N.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF12220; U1snRNP70_N; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT CHAIN 2..448
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000081881"
FT DOMAIN 103..181
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 48..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..202
FT /note="Required for interaction with U1 RNA"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT REGION 187..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08621"
FT VAR_SEQ 160..166
FT /note="AYKHADG -> TTQLACS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005851"
FT VAR_SEQ 167..448
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005852"
FT CONFLICT 263
FT /note="R -> Q (in Ref. 2; CAA33777)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> T (in Ref. 2; CAA33777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 51992 MW; 5B025A3B6992D0BD CRC64;
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA
ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR
REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER
GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE
RRERSRERDK ERERRRSRSR DRRRRSRSRD KDERRRSRER SKDKDRDRKR RSSRSRERAR
RERERKEELR GGGGGGGGGS GGGGGGDMAE PSEAGDGAPD DGPPGELGPE GPDGPEEKGR
DRDRERRRSH RSERERRRDR DRDRDREHKR GERGSERGRD EARGGGGSGQ DNGLEGLGSD
GRDMYMEAEG GDGYMAPENG YLMEAAPE
