RU17_HUMAN
ID RU17_HUMAN Reviewed; 437 AA.
AC P08621; B3KUA3; P78493; P78494; Q15364; Q15686; Q15687; Q15689; Q99377;
AC Q9UE45; Q9UE46; Q9UE47; Q9UE48; Q9UFQ6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 2.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE Short=U1 snRNP 70 kDa {ECO:0000303|PubMed:3028775};
DE Short=U1-70K {ECO:0000303|PubMed:2447561, ECO:0000303|PubMed:25555158};
DE Short=snRNP70;
GN Name=SNRNP70; Synonyms=RNPU1Z, RPU1, SNRP70, U1AP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3028775; DOI=10.1002/j.1460-2075.1986.tb04631.x;
RA Theissen H., Etzerodt M., Reuter R., Schneider C., Lottspeich F., Argos P.,
RA Luehrmann R., Philipson L.;
RT "Cloning of the human cDNA for the U1 RNA-associated 70K protein.";
RL EMBO J. 5:3209-3217(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=2447561; DOI=10.1093/nar/15.24.10373;
RA Spritz R.A., Strunk K., Surowy C.S., Hoch S.O., Barton D.E., Francke U.;
RT "The human U1-70K snRNP protein: cDNA cloning, chromosomal localization,
RT expression, alternative splicing and RNA-binding.";
RL Nucleic Acids Res. 15:10373-10391(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING DOMAIN, AND FUNCTION.
RX PubMed=2467746; DOI=10.1016/0092-8674(89)90175-x;
RA Query C.C., Bentley R.C., Keene J.D.;
RT "A common RNA recognition motif identified within a defined U1 RNA binding
RT domain of the 70K U1 snRNP protein.";
RL Cell 57:89-101(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=2147422; DOI=10.1016/0888-7543(90)90295-6;
RA Spritz R.A., Strunk K., Surowy C.S., Mohrenweiser H.W.;
RT "Human U1-70K ribonucleoprotein antigen gene: organization, nucleotide
RT sequence, and mapping to locus 19q13.3.";
RL Genomics 8:371-379(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8746626; DOI=10.1006/prep.1995.0005;
RA Northemann W., Berg H., Stahnke G., Walter M., Hunt N., Fenning S.;
RT "Identification of an inhibitory element within the human 68-kDa (U1)
RT ribonucleoprotein antigen.";
RL Protein Expr. Purif. 6:748-756(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [10]
RP PROTEIN SEQUENCE OF 219-348, AND PHOSPHORYLATION.
RX PubMed=8332490; DOI=10.1093/nar/21.12.2815;
RA Woppmann A., Will C.L., Kornstaedt U., Zuo P., Manley J.L., Luehrmann R.;
RT "Identification of an snRNP-associated kinase activity that phosphorylates
RT arginine/serine rich domains typical of splicing factors.";
RL Nucleic Acids Res. 21:2815-2822(1993).
RN [11]
RP IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRPA1; SRRM1
RP AND SRRM2.
RX PubMed=9531537; DOI=10.1101/gad.12.7.996;
RA Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
RT "A coactivator of pre-mRNA splicing.";
RL Genes Dev. 12:996-1009(1998).
RN [12]
RP INTERACTION WITH SCAF11.
RX PubMed=9447963; DOI=10.1128/mcb.18.2.676;
RA Zhang W.-J., Wu J.Y.;
RT "Sip1, a novel RS domain-containing protein essential for pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 18:676-684(1998).
RN [13]
RP IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH
RP SNRPA1; SRRM1 AND TRA2B.
RX PubMed=10339552; DOI=10.1073/pnas.96.11.6125;
RA Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
RT "The SRm160/300 splicing coactivator is required for exon-enhancer
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
RN [14]
RP INTERACTION WITH ZRANB2.
RX PubMed=11448987; DOI=10.1083/jcb.200010059;
RA Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J.,
RA Rasko J.E.J.;
RT "ZNF265 -- a novel spliceosomal protein able to induce alternative
RT splicing.";
RL J. Cell Biol. 154:25-32(2001).
RN [15]
RP INTERACTION WITH SFPQ.
RX PubMed=11514619; DOI=10.1091/mbc.12.8.2328;
RA Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J.,
RA Zipori D.;
RT "Nuclear relocalization of the pre-mRNA splicing factor PSF during
RT apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and
RT changes in protein interactions.";
RL Mol. Biol. Cell 12:2328-2340(2001).
RN [16]
RP INTERACTION WITH NUDT21/CPSF5 AND CPSF6.
RX PubMed=14561889; DOI=10.1261/rna.5104603;
RA Awasthi S., Alwine J.C.;
RT "Association of polyadenylation cleavage factor I with U1 snRNP.";
RL RNA 9:1400-1409(2003).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [18]
RP INTERACTION WITH SFRS13A.
RX PubMed=14765198; DOI=10.1038/nature02288;
RA Shin C., Feng Y., Manley J.L.;
RT "Dephosphorylated SRp38 acts as a splicing repressor in response to heat
RT shock.";
RL Nature 427:553-558(2004).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-320 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [21]
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-268; SER-320 AND
RP SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-320 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-126; SER-226; SER-320 AND
RP SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-320, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP INTERACTION WITH GEMIN5.
RX PubMed=25911097; DOI=10.1074/jbc.m115.646257;
RA Workman E., Kalda C., Patel A., Battle D.J.;
RT "Gemin5 binds to the survival motor neuron mRNA to regulate SMN
RT expression.";
RL J. Biol. Chem. 290:15662-15669(2015).
RN [36]
RP INTERACTION WITH FUS.
RX PubMed=26124092; DOI=10.1073/pnas.1506282112;
RA Yu Y., Reed R.;
RT "FUS functions in coupling transcription to splicing by mediating an
RT interaction between RNAP II and U1 snRNP.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8608-8613(2015).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-346, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-216 IN SPLICEOSOMAL U1 SNRNP,
RP FUNCTION, AND SUBUNIT.
RX PubMed=19325628; DOI=10.1038/nature07851;
RA Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.;
RT "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution.";
RL Nature 458:475-480(2009).
RN [39] {ECO:0007744|PDB:3PGW}
RP X-RAY CRYSTALLOGRAPHY (4.40 ANGSTROMS), IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21113136; DOI=10.1038/emboj.2010.295;
RA Weber G., Trowitzsch S., Kastner B., Luhrmann R., Wahl M.C.;
RT "Functional organization of the Sm core in the crystal structure of human
RT U1 snRNP.";
RL EMBO J. 29:4172-4184(2010).
RN [40] {ECO:0007744|PDB:4PJO, ECO:0007744|PDB:4PKD}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 60-215 IN COMPLEX WITH U1 SNRNP,
RP SUBUNIT, RNA-BINDING, FUNCTION, AND DOMAIN.
RX PubMed=25555158; DOI=10.7554/elife.04986;
RA Kondo Y., Oubridge C., van Roon A.M., Nagai K.;
RT "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein
RT particle, reveals the mechanism of 5' splice site recognition.";
RL Elife 4:0-0(2015).
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 (PubMed:19325628, PubMed:25555158). SNRNP70
CC binds to the loop I region of U1-snRNA (PubMed:2467746,
CC PubMed:19325628, PubMed:25555158). {ECO:0000269|PubMed:19325628,
CC ECO:0000269|PubMed:2467746, ECO:0000269|PubMed:25555158}.
CC -!- FUNCTION: [Isoform 3]: Truncated isoforms that lack the RRM domain
CC cannot bind U1-snRNA. {ECO:0000269|PubMed:2467746}.
CC -!- FUNCTION: [Isoform 4]: Truncated isoforms that lack the RRM domain
CC cannot bind U1-snRNA. {ECO:0000269|PubMed:2467746}.
CC -!- SUBUNIT: Component of the U1 snRNP (PubMed:19325628, PubMed:21113136,
CC PubMed:25555158). The U1 snRNP is composed of the U1 snRNA and the 7
CC core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG
CC that assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP, and at least three U1 snRNP-
CC specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C
CC (PubMed:19325628, PubMed:21113136, PubMed:25555158). Interacts with
CC SCNM1 (By similarity). Found in a pre-mRNA splicing complex with SFRS4,
CC SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2 (PubMed:9531537). Found in a
CC pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1,
CC SRRM1 and TRA2B/SFRS10 (PubMed:10339552). Interacts with
CC dephosphorylated SFRS13A and SFPQ (PubMed:11514619, PubMed:14765198).
CC Interacts with NUDT21/CPSF5, CPSF6, SCAF11, and ZRANB2
CC (PubMed:14561889, PubMed:11448987, PubMed:9447963). Interacts with
CC GEMIN5 (PubMed:25911097). Interacts with FUS.
CC {ECO:0000250|UniProtKB:Q62376, ECO:0000269|PubMed:10339552,
CC ECO:0000269|PubMed:11448987, ECO:0000269|PubMed:11514619,
CC ECO:0000269|PubMed:14561889, ECO:0000269|PubMed:14765198,
CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:21113136,
CC ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:25911097,
CC ECO:0000269|PubMed:26124092, ECO:0000269|PubMed:9447963,
CC ECO:0000269|PubMed:9531537}.
CC -!- INTERACTION:
CC P08621; P49760: CLK2; NbExp=5; IntAct=EBI-1049228, EBI-750020;
CC P08621; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-1049228, EBI-6115579;
CC P08621; Q16637: SMN2; NbExp=5; IntAct=EBI-1049228, EBI-395421;
CC P08621; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-1049228, EBI-539478;
CC P08621; P78362: SRPK2; NbExp=4; IntAct=EBI-1049228, EBI-593303;
CC P08621; A7MD48: SRRM4; NbExp=3; IntAct=EBI-1049228, EBI-3867173;
CC P08621; Q07955: SRSF1; NbExp=3; IntAct=EBI-1049228, EBI-398920;
CC P08621; P31483: TIA1; NbExp=2; IntAct=EBI-1049228, EBI-1387216;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17656373}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373,
CC ECO:0000269|PubMed:21113136}. Note=Colocalizes with SCNM1 and LUC7L2 in
CC nuclear speckles. {ECO:0000250|UniProtKB:Q62376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P08621-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08621-2; Sequence=VSP_005850;
CC Name=3;
CC IsoId=P08621-3; Sequence=VSP_005848, VSP_005849;
CC Name=4;
CC IsoId=P08621-4; Sequence=VSP_005847;
CC -!- DOMAIN: The RRM domain mediates interaction with U1 RNA.
CC {ECO:0000269|PubMed:2467746, ECO:0000269|PubMed:25555158}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Extensively phosphorylated on serine residues in the C-terminal
CC region. {ECO:0000269|PubMed:8332490}.
CC -!- MISCELLANEOUS: Major ribonucleoprotein antigen recognized by the sera
CC from patients with autoimmune diseases, such as systemic lupus
CC erythematosus.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28352.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA29964.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA29966.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; X04654; CAA28352.1; ALT_INIT; mRNA.
DR EMBL; X06814; CAA29963.1; -; mRNA.
DR EMBL; X06815; CAA29964.1; ALT_INIT; mRNA.
DR EMBL; X06817; CAA29966.1; ALT_INIT; mRNA.
DR EMBL; X07402; CAA30304.1; -; mRNA.
DR EMBL; X06816; CAA29965.1; -; mRNA.
DR EMBL; X06812; CAA29961.1; -; mRNA.
DR EMBL; X06811; CAA29960.1; -; mRNA.
DR EMBL; X07401; CAA30303.1; -; mRNA.
DR EMBL; X07403; CAA30305.1; -; mRNA.
DR EMBL; M22636; AAA03001.1; -; mRNA.
DR EMBL; M57939; AAA36572.1; -; Genomic_DNA.
DR EMBL; M57929; AAA36572.1; JOINED; Genomic_DNA.
DR EMBL; M57930; AAA36572.1; JOINED; Genomic_DNA.
DR EMBL; M57932; AAA36572.1; JOINED; Genomic_DNA.
DR EMBL; M57934; AAA36572.1; JOINED; Genomic_DNA.
DR EMBL; M57937; AAA36572.1; JOINED; Genomic_DNA.
DR EMBL; M57939; AAA36573.1; -; Genomic_DNA.
DR EMBL; M57929; AAA36573.1; JOINED; Genomic_DNA.
DR EMBL; M57930; AAA36573.1; JOINED; Genomic_DNA.
DR EMBL; M57932; AAA36573.1; JOINED; Genomic_DNA.
DR EMBL; M57934; AAA36573.1; JOINED; Genomic_DNA.
DR EMBL; M57937; AAA36573.1; JOINED; Genomic_DNA.
DR EMBL; M57935; AAA36571.1; -; Genomic_DNA.
DR EMBL; M57929; AAA36571.1; JOINED; Genomic_DNA.
DR EMBL; M57930; AAA36571.1; JOINED; Genomic_DNA.
DR EMBL; M57932; AAA36571.1; JOINED; Genomic_DNA.
DR EMBL; M57934; AAA36571.1; JOINED; Genomic_DNA.
DR EMBL; AK096783; BAG53365.1; -; mRNA.
DR EMBL; X84841; CAA59278.1; -; mRNA.
DR EMBL; AL117507; CAB55969.1; -; mRNA.
DR EMBL; CH471177; EAW52449.1; -; Genomic_DNA.
DR EMBL; BC001315; AAH01315.1; -; mRNA.
DR CCDS; CCDS12756.1; -. [P08621-1]
DR CCDS; CCDS74417.1; -. [P08621-2]
DR PIR; A25707; A25707.
DR PIR; S00674; S00674.
DR RefSeq; NP_001287998.1; NM_001301069.1. [P08621-2]
DR RefSeq; NP_003080.2; NM_003089.5. [P08621-1]
DR PDB; 2L5I; NMR; -; A=131-151.
DR PDB; 2L5J; NMR; -; A=131-151.
DR PDB; 3CW1; X-ray; 5.49 A; 6/7/8/K=1-216.
DR PDB; 3PGW; X-ray; 4.40 A; L/S=1-437.
DR PDB; 4PJO; X-ray; 3.30 A; K/N/k/n=2-60.
DR PDB; 4PKD; X-ray; 2.50 A; B=60-215.
DR PDB; 6QX9; EM; 3.28 A; 1K=1-437.
DR PDB; 7B0Y; EM; 3.60 A; b=1-437.
DR PDBsum; 2L5I; -.
DR PDBsum; 2L5J; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 3PGW; -.
DR PDBsum; 4PJO; -.
DR PDBsum; 4PKD; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7B0Y; -.
DR AlphaFoldDB; P08621; -.
DR SMR; P08621; -.
DR BioGRID; 112509; 907.
DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex.
DR CORUM; P08621; -.
DR DIP; DIP-29406N; -.
DR ELM; P08621; -.
DR IntAct; P08621; 203.
DR MINT; P08621; -.
DR STRING; 9606.ENSP00000472998; -.
DR MoonDB; P08621; Predicted.
DR GlyGen; P08621; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08621; -.
DR PhosphoSitePlus; P08621; -.
DR SwissPalm; P08621; -.
DR BioMuta; SNRNP70; -.
DR DMDM; 13635663; -.
DR CPTAC; CPTAC-1007; -.
DR EPD; P08621; -.
DR jPOST; P08621; -.
DR MassIVE; P08621; -.
DR MaxQB; P08621; -.
DR PaxDb; P08621; -.
DR PeptideAtlas; P08621; -.
DR PRIDE; P08621; -.
DR ProteomicsDB; 52138; -. [P08621-1]
DR ProteomicsDB; 52139; -. [P08621-2]
DR ProteomicsDB; 52140; -. [P08621-3]
DR ProteomicsDB; 52141; -. [P08621-4]
DR Antibodypedia; 3444; 193 antibodies from 25 providers.
DR DNASU; 6625; -.
DR Ensembl; ENST00000221448.9; ENSP00000221448.5; ENSG00000104852.15. [P08621-2]
DR Ensembl; ENST00000401730.5; ENSP00000385077.1; ENSG00000104852.15. [P08621-3]
DR Ensembl; ENST00000595231.5; ENSP00000471006.1; ENSG00000104852.15. [P08621-3]
DR Ensembl; ENST00000598441.6; ENSP00000472998.1; ENSG00000104852.15. [P08621-1]
DR Ensembl; ENST00000601065.5; ENSP00000468952.1; ENSG00000104852.15. [P08621-3]
DR GeneID; 6625; -.
DR KEGG; hsa:6625; -.
DR MANE-Select; ENST00000598441.6; ENSP00000472998.1; NM_003089.6; NP_003080.2.
DR UCSC; uc002pmk.4; human. [P08621-1]
DR CTD; 6625; -.
DR DisGeNET; 6625; -.
DR GeneCards; SNRNP70; -.
DR HGNC; HGNC:11150; SNRNP70.
DR HPA; ENSG00000104852; Low tissue specificity.
DR MIM; 180740; gene.
DR neXtProt; NX_P08621; -.
DR OpenTargets; ENSG00000104852; -.
DR PharmGKB; PA35992; -.
DR VEuPathDB; HostDB:ENSG00000104852; -.
DR eggNOG; KOG0113; Eukaryota.
DR GeneTree; ENSGT00940000160292; -.
DR HOGENOM; CLU_045151_5_1_1; -.
DR InParanoid; P08621; -.
DR OMA; GVAKFMA; -.
DR PhylomeDB; P08621; -.
DR TreeFam; TF314215; -.
DR PathwayCommons; P08621; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P08621; -.
DR SIGNOR; P08621; -.
DR BioGRID-ORCS; 6625; 781 hits in 1099 CRISPR screens.
DR ChiTaRS; SNRNP70; human.
DR EvolutionaryTrace; P08621; -.
DR GeneWiki; SnRNP70; -.
DR GenomeRNAi; 6625; -.
DR Pharos; P08621; Tbio.
DR PRO; PR:P08621; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P08621; protein.
DR Bgee; ENSG00000104852; Expressed in right hemisphere of cerebellum and 203 other tissues.
DR ExpressionAtlas; P08621; baseline and differential.
DR Genevisible; P08621; HS.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; IDA: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; IMP:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0061084; P:negative regulation of protein refolding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR CDD; cd12236; RRM_snRNP70; 1.
DR DisProt; DP02171; -.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00138; -.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..437
FT /note="U1 small nuclear ribonucleoprotein 70 kDa"
FT /id="PRO_0000081880"
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:0000269|PubMed:2467746"
FT REGION 187..437
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..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..159
FT /note="MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPR
FT DAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVN
FT YDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHS -> MEQALHR
FT FGRGLVWLSVAWLSVGRVRVRDDGDTGRGFCRAGPVLTRGPSGDSSPLPLPTSVTA
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_005847"
FT VAR_SEQ 160..166
FT /note="AYKHADG -> TTQLACS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005848"
FT VAR_SEQ 167..437
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005849"
FT VAR_SEQ 223..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005850"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4PJO"
FT HELIX 63..86
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:4PKD"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4PKD"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4PKD"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4PKD"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4PKD"
SQ SEQUENCE 437 AA; 51557 MW; F1020BF5C40CF97D 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 KEERRRSRER SKDKDRDRKR RSSRSRERAR
RERERKEELR GGGGDMAEPS EAGDAPPDDG PPGELGPDGP DGPEEKGRDR DRERRRSHRS
ERERRRDRDR DRDRDREHKR GERGSERGRD EARGGGGGQD NGLEGLGNDS RDMYMESEGG
DGYLAPENGY LMEAAPE
