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U1 small nuclear ribonucleoprotein 70 kDa (U1 snRNP 70 kDa) (U1-70K) (snRNP70)

 RU17_MOUSE              Reviewed;         448 AA.
Q62376; Q3UIW4;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
20-JUN-2018, entry version 153.
RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
Short=U1 snRNP 70 kDa;
Short=U1-70K;
Short=snRNP70;
Name=Snrnp70; Synonyms=Snrp70;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-448 (ISOFORMS 1 AND 2).
STRAIN=BALB/cJ;
PubMed=2525092; DOI=10.1111/j.1432-1033.1989.tb14798.x;
Hornig H., Fischer U., Costas M., Rauh A., Luehrmann R.;
"Analysis of genomic clones of the murine U1RNA-associated 70-kDa
protein reveals a high evolutionary conservation of the protein
between human and mouse.";
Eur. J. Biochem. 182:45-50(1989).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[4]
INTERACTION WITH SCNM1, AND SUBCELLULAR LOCATION.
PubMed=17656373; DOI=10.1093/hmg/ddm206;
Howell V.M., Jones J.M., Bergren S.K., Li L., Billi A.C.,
Avenarius M.R., Meisler M.H.;
"Evidence for a direct role of the disease modifier SCNM1 in
splicing.";
Hum. Mol. Genet. 16:2506-2516(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-419, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-408, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of the spliceosomal U1 snRNP, which is
essential for recognition of the pre-mRNA 5' splice-site and the
subsequent assembly of the spliceosome. SNRNP70 binds to the loop
I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA
(By similarity). {ECO:0000250}.
-!- SUBUNIT: U1 snRNP is composed of the 7 core Sm proteins SNRPB,
SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a
heptameric protein ring on the Sm site of the small nuclear RNA to
form the core snRNP, and at least three U1 snRNP-specific proteins
SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C (By similarity).
Interacts with SCNM1 (PubMed:17656373). Found in a pre-mRNA
splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and
SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex
with SNRNP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Interacts with
dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5,
CPSF6, SCAF11, and ZRANB2. Interacts with GEMIN5 (By similarity).
{ECO:0000250|UniProtKB:P08621, ECO:0000269|PubMed:17656373}.
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:17656373}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:17656373}. Note=Colocalizes with SCNM1 and
LUC7L2 in nuclear speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q62376-1; Sequence=Displayed;
Name=2;
IsoId=Q62376-2; Sequence=VSP_005851, VSP_005852;
-!- PTM: Extensively phosphorylated on serine residues in the C-
terminal region. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AK133115; BAE21515.1; -; mRNA.
EMBL; AK146729; BAE27392.1; -; mRNA.
EMBL; X15769; CAA33777.1; -; Genomic_DNA.
EMBL; X15770; CAA33777.1; JOINED; Genomic_DNA.
EMBL; X15771; CAA33777.1; JOINED; Genomic_DNA.
EMBL; X15772; CAA33777.1; JOINED; Genomic_DNA.
EMBL; X15774; CAA33777.1; JOINED; Genomic_DNA.
EMBL; X15775; CAA33777.1; JOINED; Genomic_DNA.
EMBL; X15776; CAA33777.1; JOINED; Genomic_DNA.
CCDS; CCDS21240.1; -. [Q62376-1]
PIR; S04336; S04336.
PIR; S04824; S04824.
RefSeq; NP_033250.3; NM_009224.5. [Q62376-1]
RefSeq; XP_006540795.1; XM_006540732.3. [Q62376-1]
UniGene; Mm.216386; -.
ProteinModelPortal; Q62376; -.
SMR; Q62376; -.
BioGrid; 203376; 33.
IntAct; Q62376; 31.
MINT; Q62376; -.
STRING; 10090.ENSMUSP00000074160; -.
iPTMnet; Q62376; -.
PhosphoSitePlus; Q62376; -.
SwissPalm; Q62376; -.
EPD; Q62376; -.
PaxDb; Q62376; -.
PeptideAtlas; Q62376; -.
PRIDE; Q62376; -.
Ensembl; ENSMUST00000074575; ENSMUSP00000074160; ENSMUSG00000063511. [Q62376-1]
GeneID; 20637; -.
KEGG; mmu:20637; -.
UCSC; uc009guw.2; mouse. [Q62376-1]
CTD; 6625; -.
MGI; MGI:98341; Snrnp70.
eggNOG; KOG0113; Eukaryota.
eggNOG; COG0724; LUCA.
GeneTree; ENSGT00530000063750; -.
HOGENOM; HOG000236289; -.
HOVERGEN; HBG094947; -.
InParanoid; Q62376; -.
KO; K11093; -.
OMA; NDVNIKH; -.
OrthoDB; EOG091G0R0Z; -.
PhylomeDB; Q62376; -.
TreeFam; TF314215; -.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
ChiTaRS; Snrnp70; mouse.
PRO; PR:Q62376; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000063511; -.
ExpressionAtlas; Q62376; baseline and differential.
Genevisible; Q62376; MM.
GO; GO:0000243; C:commitment complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:MGI.
GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
GO; GO:1990446; F:U1 snRNP binding; ISO:MGI.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
CDD; cd12236; RRM_snRNP70; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034143; snRNP70_RRM.
InterPro; IPR022023; U1snRNP70_N.
Pfam; PF00076; RRM_1; 1.
Pfam; PF12220; U1snRNP70_N; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
RNA-binding; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08621}.
CHAIN 2 448 U1 small nuclear ribonucleoprotein 70
kDa.
/FTId=PRO_0000081881.
DOMAIN 103 181 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 231 310 Arg/Glu-rich (mixed charge).
COMPBIAS 311 326 Poly-Gly.
COMPBIAS 356 403 Arg/Asp/Glu-rich (mixed charge).
COMPBIAS 404 409 Poly-Gly.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P08621}.
MOD_RES 118 118 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08621}.
MOD_RES 126 126 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08621}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000250|UniProtKB:P08621}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:P08621}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
CROSSLNK 358 358 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08621}.
VAR_SEQ 160 166 AYKHADG -> TTQLACS (in isoform 2).
{ECO:0000305}.
/FTId=VSP_005851.
VAR_SEQ 167 448 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_005852.
CONFLICT 263 263 R -> Q (in Ref. 2; CAA33777).
{ECO:0000305}.
CONFLICT 281 281 S -> T (in Ref. 2; CAA33777).
{ECO:0000305}.
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


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