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 27-MAR-2024, entry version 246. 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; Q96MT8: CEP63; NbExp=3; IntAct=EBI-1049228, EBI-741977; 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 PDB; 7VPX; EM; 3.00 A; O=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 PDBsum; 7VPX; -. DR AlphaFoldDB; P08621; -. DR EMDB; EMD-11972; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-4665; -. DR SMR; P08621; -. DR BioGRID; 112509; 962. DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex. DR CORUM; P08621; -. DR DIP; DIP-29406N; -. DR ELM; P08621; -. DR IntAct; P08621; 225. 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; 9606-ENSP00000472998; -. DR PeptideAtlas; P08621; -. DR ProteomicsDB; 52138; -. [P08621-1] DR ProteomicsDB; 52139; -. [P08621-2] DR ProteomicsDB; 52140; -. [P08621-3] DR ProteomicsDB; 52141; -. [P08621-4] DR Pumba; P08621; -. DR Antibodypedia; 3444; 217 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 AGR; HGNC:11150; -. 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; GRTTKGW; -. DR OrthoDB; 180547at2759; -. 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; 812 hits in 1179 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 205 other cell types or tissues. DR ExpressionAtlas; P08621; baseline and differential. 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: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 PANTHER; PTHR13952; U1 SMALL NUCLEAR RIBONUCLEOPROTEIN 70 KD; 1. DR PANTHER; PTHR13952:SF5; U1 SMALL NUCLEAR RIBONUCLEOPROTEIN 70 KDA; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF12220; U1snRNP70_N; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR Genevisible; P08621; HS. 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 //