RNPS1_HUMAN
ID RNPS1_HUMAN Reviewed; 305 AA.
AC Q15287; A8K1P0; B4DDU8; B4DZU7; B7ZA17; O75308; Q32P25; Q8WY42; Q9NYG3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=RNA-binding protein with serine-rich domain 1;
DE AltName: Full=SR-related protein LDC2;
GN Name=RNPS1; Synonyms=LDC2;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8543184; DOI=10.1016/0378-1119(95)00571-4;
RA Badolato J., Gardiner E., Morrison N., Eisman J.;
RT "Identification and characterisation of a novel human RNA-binding
RT protein.";
RL Gene 166:323-327(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC2L1, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=B-cell;
RX PubMed=9580558; DOI=10.1242/jcs.111.11.1495;
RA Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.;
RT "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-
RT related PITSLRE protein kinases in vivo.";
RL J. Cell Sci. 111:1495-1506(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RA Harada K., Yang D., Yamada A., Shichijo S., Itoh K.;
RT "Identification of an alternatively spliced form of RNPS1.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Hippocampus, and Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-305.
RC TISSUE=Kidney;
RA Lee D.-C., Ouyang P.;
RT "Direct interaction of LDC2, a SR-related protein with pinin.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE SPLICEOSOME, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10449421; DOI=10.1093/emboj/18.16.4560;
RA Mayeda A., Badolato J., Kobayashi R., Zhang M.Q., Gardiner E.M.,
RA Krainer A.R.;
RT "Purification and characterization of human RNPS1: a general activator of
RT pre-mRNA splicing.";
RL EMBO J. 18:4560-4570(1999).
RN [10]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH DEK; RBM8A; SRRM1 AND ALYREF/THOC4.
RX PubMed=11118221; DOI=10.1093/emboj/19.24.6860;
RA Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
RT "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of
RT mRNA exon-exon junctions.";
RL EMBO J. 19:6860-6869(2000).
RN [11]
RP INTERACTION WITH SART3, AND SUBCELLULAR LOCATION.
RX PubMed=11477570; DOI=10.1002/ijc.1391;
RA Harada K., Yamada A., Yang D., Itoh K., Shichijo S.;
RT "Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor
RT RNPS1: a possible regulation of splicing by a complex formation.";
RL Int. J. Cancer 93:623-628(2001).
RN [12]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A POST-SPLICING
RP COMPLEX WITH NXF1; RBM8A; UPF1; UPF2; UPF3A AND UPF3B, RNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11546874; DOI=10.1126/science.1062786;
RA Lykke-Andersen J., Shu M.-D., Steitz J.A.;
RT "Communication of the position of exon-exon junctions to the mRNA
RT surveillance machinery by the protein RNPS1.";
RL Science 293:1836-1839(2001).
RN [13]
RP FUNCTION IN MRNA 3'-END FORMATION, AND INTERACTION WITH SRRM1.
RX PubMed=12944400; DOI=10.1074/jbc.m306856200;
RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
RT "An evolutionarily conserved role for SRm160 in 3'-end processing that
RT functions independently of exon junction complex formation.";
RL J. Biol. Chem. 278:44153-44160(2003).
RN [14]
RP IDENTIFICATION IN A MRNP COMPLEX WITH PNN, INTERACTION WITH PNN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14517304; DOI=10.1128/mcb.23.20.7363-7376.2003;
RA Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.;
RT "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA
RT processing and export via interaction with RNPS1.";
RL Mol. Cell. Biol. 23:7363-7376(2003).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [16]
RP FUNCTION IN TRANSLATIONAL ACTIVITY AND NONSENSE-MEDIATED MRNA DECAY, AND
RP ASSOCIATION WITH POLYSOMES.
RX PubMed=14752011; DOI=10.1101/gad.1163204;
RA Nott A., Le Hir H., Moore M.J.;
RT "Splicing enhances translation in mammalian cells: an additional function
RT of the exon junction complex.";
RL Genes Dev. 18:210-222(2004).
RN [17]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH RBM8A AND SRRM1.
RX PubMed=14625303; DOI=10.1074/jbc.m307692200;
RA Kataoka N., Dreyfuss G.;
RT "A simple whole cell lysate system for in vitro splicing reveals a stepwise
RT assembly of the exon-exon junction complex.";
RL J. Biol. Chem. 279:7009-7013(2004).
RN [18]
RP FUNCTION IN ALTERNATIVE PRE-MRNA SPLICING, INTERACTION WITH PNN; SRP54 AND
RP TRA2B, MUTAGENESIS OF TYR-205 AND TYR-207, AND SUBCELLULAR LOCATION.
RX PubMed=14729963; DOI=10.1128/mcb.24.3.1174-1187.2004;
RA Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
RT "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA
RT splicing regulator in vivo.";
RL Mol. Cell. Biol. 24:1174-1187(2004).
RN [19]
RP FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE SPLICEOSOME,
RP PHOSPHORYLATION AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION
RP WITH CSNK2A1, MUTAGENESIS OF SER-53, AND SUBCELLULAR LOCATION.
RX PubMed=15684395; DOI=10.1128/mcb.25.4.1446-1457.2005;
RA Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
RA Suzuki H., Endo H., Kidd V.J., Mayeda A.;
RT "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
RT phosphorylation.";
RL Mol. Cell. Biol. 25:1446-1457(2005).
RN [20]
RP FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY, AND
RP IDENTIFICATION IN A COMPLEX WITH UPF2 AND UPF3B.
RX PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012;
RA Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W.,
RA Kulozik A.E.;
RT "Exon-junction complex components specify distinct routes of nonsense-
RT mediated mRNA decay with differential cofactor requirements.";
RL Mol. Cell 20:65-75(2005).
RN [21]
RP IDENTIFICATION IN THE ASAP COMPLEX, AND FUNCTION OF THE ASAP COMPLEX.
RX PubMed=12665594; DOI=10.1128/mcb.23.8.2981-2990.2003;
RA Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E.,
RA Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.;
RT "ASAP, a novel protein complex involved in RNA processing and apoptosis.";
RL Mol. Cell. Biol. 23:2981-2990(2003).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [23]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX,
RP IDENTIFICATION IN THE ASAP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314458; DOI=10.1261/rna.2155905;
RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT "Biochemical analysis of the EJC reveals two new factors and a stable
RT tetrameric protein core.";
RL RNA 11:1869-1883(2005).
RN [24]
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 [25]
RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD).
RX PubMed=17586820; DOI=10.1093/nar/gkm461;
RA Viegas M.H., Gehring N.H., Breit S., Hentze M.W., Kulozik A.E.;
RT "The abundance of RNPS1, a protein component of the exon junction complex,
RT can determine the variability in efficiency of the nonsense mediated decay
RT pathway.";
RL Nucleic Acids Res. 35:4542-4551(2007).
RN [26]
RP SUBCELLULAR LOCATION.
RX PubMed=19324961; DOI=10.1261/rna.1387009;
RA Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P.,
RA Wachsmuth M.;
RT "Assembly and mobility of exon-exon junction complexes in living cells.";
RL RNA 15:862-876(2009).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218, 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 [28]
RP INTERACTION WITH SAP18 AND ACIN1.
RX PubMed=20966198; DOI=10.1261/rna.2304410;
RA Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A.,
RA Schulze-Osthoff K., Schaal H., Schwerk C.;
RT "Human SAP18 mediates assembly of a splicing regulatory multiprotein
RT complex via its ubiquitin-like fold.";
RL RNA 16:2442-2454(2010).
RN [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-157 AND THR-161, 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 [31]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/mcb.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M.,
RA Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R.,
RA Elela S.A., Prinos P., Chabot B.;
RT "Proteins associated with the exon junction complex also control the
RT alternative splicing of apoptotic regulators.";
RL Mol. Cell. Biol. 32:954-967(2012).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-15, AND IDENTIFICATION
RP BY MASS 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 [33]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THE ASAP COMPLEX, IDENTIFICATION
RP IN THE PSAP COMPLEX, INTERACTION WITH SAP18, AND MUTAGENESIS OF ASN-171.
RX PubMed=22388736; DOI=10.1038/nsmb.2242;
RA Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.;
RT "The structure of the ASAP core complex reveals the existence of a Pinin-
RT containing PSAP complex.";
RL Nat. Struct. Mol. Biol. 19:378-386(2012).
CC -!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes.
CC Auxiliary component of the splicing-dependent multiprotein exon
CC junction complex (EJC) deposited at splice junction on mRNAs. The EJC
CC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. Component of the ASAP and PSAP complexes
CC which bind RNA in a sequence-independent manner and are proposed to be
CC recruited to the EJC prior to or during the splicing process and to
CC regulate specific excision of introns in specific transcription
CC subsets. The ASAP complex can inhibit RNA processing during in vitro
CC splicing reactions. The ASAP complex promotes apoptosis and is
CC disassembled after induction of apoptosis. Enhances the formation of
CC the ATP-dependent A complex of the spliceosome. Involved in both
CC constitutive splicing and, in association with SRP54 and TRA2B/SFRS10,
CC in distinctive modulation of alternative splicing in a substrate-
CC dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X
CC (and probably other apoptotic genes); specifically inhibits formation
CC of proapoptotic isoforms such as Bcl-X(S); the activity is different
CC from the established EJC assembly and function. Participates in mRNA
CC 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay
CC (NMD) of mRNAs containing premature stop codons. Also mediates increase
CC of mRNA abundance and translational efficiency. Binds spliced mRNA 20-
CC 25 nt upstream of exon-exon junctions. {ECO:0000269|PubMed:10449421,
CC ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12665594,
CC ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14729963,
CC ECO:0000269|PubMed:14752011, ECO:0000269|PubMed:15684395,
CC ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17586820,
CC ECO:0000269|PubMed:22203037}.
CC -!- SUBUNIT: Found in mRNA splicing-dependent exon junction complexes
CC (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2,
CC UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP
CC (apoptosis- and splicing-associated protein) and PSAP complexes
CC consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the
CC ASAP and PSAP complexes probably are formed mutually exclusive.
CC Component of the active spliceosome. Associates with polysomes.
CC Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3,
CC SRP54, SRRM1 and TRA2B/SFRS10. {ECO:0000269|PubMed:11118221,
CC ECO:0000269|PubMed:11477570, ECO:0000269|PubMed:11546874,
CC ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:12944400,
CC ECO:0000269|PubMed:14517304, ECO:0000269|PubMed:14625303,
CC ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:15684395,
CC ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22388736,
CC ECO:0000269|PubMed:9580558}.
CC -!- INTERACTION:
CC Q15287; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-395959, EBI-11096309;
CC Q15287; Q9UK58: CCNL1; NbExp=4; IntAct=EBI-395959, EBI-2836773;
CC Q15287; P49760: CLK2; NbExp=5; IntAct=EBI-395959, EBI-750020;
CC Q15287; P49761: CLK3; NbExp=4; IntAct=EBI-395959, EBI-745579;
CC Q15287; Q8IYF1: ELOA2; NbExp=3; IntAct=EBI-395959, EBI-741705;
CC Q15287; Q96LP2: FAM81B; NbExp=3; IntAct=EBI-395959, EBI-10290827;
CC Q15287; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-395959, EBI-5916454;
CC Q15287; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-395959, EBI-5460660;
CC Q15287; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-395959, EBI-3920396;
CC Q15287; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-395959, EBI-79165;
CC Q15287; O43586: PSTPIP1; NbExp=3; IntAct=EBI-395959, EBI-1050964;
CC Q15287; Q15415: RBMY1J; NbExp=3; IntAct=EBI-395959, EBI-8642021;
CC Q15287; Q15020: SART3; NbExp=5; IntAct=EBI-395959, EBI-308619;
CC Q15287; Q9H190: SDCBP2; NbExp=4; IntAct=EBI-395959, EBI-742426;
CC Q15287; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-395959, EBI-539478;
CC Q15287; P78362: SRPK2; NbExp=5; IntAct=EBI-395959, EBI-593303;
CC Q15287; A7MD48: SRRM4; NbExp=3; IntAct=EBI-395959, EBI-3867173;
CC Q15287; O75494: SRSF10; NbExp=3; IntAct=EBI-395959, EBI-353655;
CC Q15287; P84103: SRSF3; NbExp=3; IntAct=EBI-395959, EBI-372557;
CC Q15287; Q16629: SRSF7; NbExp=3; IntAct=EBI-395959, EBI-398885;
CC Q15287; Q13242: SRSF9; NbExp=3; IntAct=EBI-395959, EBI-2949710;
CC Q15287; O75558: STX11; NbExp=3; IntAct=EBI-395959, EBI-714135;
CC Q15287; Q13595: TRA2A; NbExp=3; IntAct=EBI-395959, EBI-2685506;
CC Q15287; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-395959, EBI-2849854;
CC Q15287; P49910: ZNF165; NbExp=3; IntAct=EBI-395959, EBI-741694;
CC Q15287; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-395959, EBI-10754950;
CC Q15287; Q14585: ZNF345; NbExp=3; IntAct=EBI-395959, EBI-2818408;
CC Q15287; Q53GI3: ZNF394; NbExp=3; IntAct=EBI-395959, EBI-10211248;
CC Q15287; P51814-6: ZNF41; NbExp=3; IntAct=EBI-395959, EBI-12700258;
CC Q15287; Q6AZW8: ZNF660; NbExp=3; IntAct=EBI-395959, EBI-12376497;
CC Q15287; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-395959, EBI-527853;
CC Q15287; Q86W11: ZSCAN30; NbExp=3; IntAct=EBI-395959, EBI-11793064;
CC Q15287-1; Q9UKV3-2: ACIN1; NbExp=4; IntAct=EBI-15972541, EBI-5279966;
CC Q15287-1; Q9H307: PNN; NbExp=3; IntAct=EBI-15972541, EBI-681904;
CC Q15287-1; Q9VJ12: Acn; Xeno; NbExp=4; IntAct=EBI-15972541, EBI-3418150;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC Note=Nucleocytoplasmic shuttling protein. Colocalizes with the core
CC EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15287-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15287-2; Sequence=VSP_016243;
CC Name=3;
CC IsoId=Q15287-3; Sequence=VSP_016243, VSP_037601;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8543184}.
CC -!- DOMAIN: The RRM domain is required for the formation of the ASAP
CC complex.
CC -!- PTM: Phosphorylated on one or more of the four Ser/Thr residues (Ser-
CC 43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important
CC for splicing and translation stimulation activity in vitro.
CC {ECO:0000269|PubMed:15684395}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; L37368; AAA92859.1; -; mRNA.
DR EMBL; AF015608; AAC39791.1; -; mRNA.
DR EMBL; AF274003; AAL56665.1; -; mRNA.
DR EMBL; AK289955; BAF82644.1; -; mRNA.
DR EMBL; AK293343; BAG56859.1; -; mRNA.
DR EMBL; AK303100; BAG64209.1; -; mRNA.
DR EMBL; AK316132; BAH14503.1; -; mRNA.
DR EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85516.1; -; Genomic_DNA.
DR EMBL; BC001659; AAH01659.1; -; mRNA.
DR EMBL; BC001838; AAH01838.1; -; mRNA.
DR EMBL; BC108316; AAI08317.1; -; mRNA.
DR EMBL; AF247662; AAF72519.1; -; mRNA.
DR CCDS; CCDS10465.1; -. [Q15287-1]
DR CCDS; CCDS66907.1; -. [Q15287-2]
DR PIR; JC4525; JC4525.
DR RefSeq; NP_001273554.1; NM_001286625.1. [Q15287-1]
DR RefSeq; NP_001273555.1; NM_001286626.1. [Q15287-2]
DR RefSeq; NP_001273556.1; NM_001286627.1.
DR RefSeq; NP_006702.1; NM_006711.4. [Q15287-1]
DR RefSeq; NP_542161.1; NM_080594.3. [Q15287-1]
DR RefSeq; XP_005255105.1; XM_005255048.1. [Q15287-1]
DR RefSeq; XP_005255106.1; XM_005255049.3. [Q15287-1]
DR RefSeq; XP_016878363.1; XM_017022874.1.
DR PDB; 4A8X; X-ray; 1.90 A; A=159-244.
DR PDBsum; 4A8X; -.
DR AlphaFoldDB; Q15287; -.
DR SMR; Q15287; -.
DR BioGRID; 116125; 392.
DR CORUM; Q15287; -.
DR DIP; DIP-32943N; -.
DR IntAct; Q15287; 140.
DR MINT; Q15287; -.
DR STRING; 9606.ENSP00000457723; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q15287; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15287; -.
DR PhosphoSitePlus; Q15287; -.
DR SwissPalm; Q15287; -.
DR BioMuta; RNPS1; -.
DR DMDM; 74754492; -.
DR EPD; Q15287; -.
DR jPOST; Q15287; -.
DR MassIVE; Q15287; -.
DR MaxQB; Q15287; -.
DR PaxDb; Q15287; -.
DR PeptideAtlas; Q15287; -.
DR PRIDE; Q15287; -.
DR ProteomicsDB; 60514; -. [Q15287-1]
DR ProteomicsDB; 60515; -. [Q15287-2]
DR ProteomicsDB; 60516; -. [Q15287-3]
DR Antibodypedia; 23681; 75 antibodies from 21 providers.
DR DNASU; 10921; -.
DR Ensembl; ENST00000301730.12; ENSP00000301730.8; ENSG00000205937.12. [Q15287-1]
DR Ensembl; ENST00000320225.10; ENSP00000315859.5; ENSG00000205937.12. [Q15287-1]
DR Ensembl; ENST00000397086.6; ENSP00000380275.2; ENSG00000205937.12. [Q15287-1]
DR Ensembl; ENST00000565678.5; ENSP00000457723.1; ENSG00000205937.12. [Q15287-1]
DR Ensembl; ENST00000566458.5; ENSP00000456352.1; ENSG00000205937.12. [Q15287-2]
DR Ensembl; ENST00000568631.5; ENSP00000457820.1; ENSG00000205937.12. [Q15287-1]
DR GeneID; 10921; -.
DR KEGG; hsa:10921; -.
DR MANE-Select; ENST00000320225.10; ENSP00000315859.5; NM_080594.4; NP_542161.1.
DR UCSC; uc002cpt.5; human. [Q15287-1]
DR CTD; 10921; -.
DR DisGeNET; 10921; -.
DR GeneCards; RNPS1; -.
DR HGNC; HGNC:10080; RNPS1.
DR HPA; ENSG00000205937; Low tissue specificity.
DR MIM; 606447; gene.
DR neXtProt; NX_Q15287; -.
DR OpenTargets; ENSG00000205937; -.
DR PharmGKB; PA34453; -.
DR VEuPathDB; HostDB:ENSG00000205937; -.
DR eggNOG; KOG4209; Eukaryota.
DR GeneTree; ENSGT00730000111029; -.
DR InParanoid; Q15287; -.
DR OMA; MRRPQGG; -.
DR PhylomeDB; Q15287; -.
DR TreeFam; TF314165; -.
DR PathwayCommons; Q15287; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q15287; -.
DR BioGRID-ORCS; 10921; 712 hits in 1074 CRISPR screens.
DR ChiTaRS; RNPS1; human.
DR GeneWiki; RNPS1; -.
DR GenomeRNAi; 10921; -.
DR Pharos; Q15287; Tbio.
DR PRO; PR:Q15287; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15287; protein.
DR Bgee; ENSG00000205937; Expressed in cerebellar hemisphere and 171 other tissues.
DR ExpressionAtlas; Q15287; baseline and differential.
DR Genevisible; Q15287; HS.
DR GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
DR CDD; cd12365; RRM_RNPS1; 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; IPR034201; RNPS1_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 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; Cytoplasm;
KW Isopeptide bond; mRNA processing; mRNA splicing;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..305
FT /note="RNA-binding protein with serine-rich domain 1"
FT /id="PRO_0000081816"
FT DOMAIN 161..240
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..220
FT /note="Necessary for interaction with the cleaved p110
FT isoform of CDC2L1"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..161
FT /note="Necessary for interaction with SRP54, nuclear
FT localization and exon-skipping"
FT /evidence="ECO:0000269|PubMed:14729963"
FT REGION 69..121
FT /note="Necessary for interactions with UPF2 and UPF3B and
FT UPF2-dependent NMD"
FT REGION 156..242
FT /note="Necessary for interaction with PNN and exon-
FT skipping"
FT REGION 159..244
FT /note="Interaction with SAP18 and ACIN1"
FT /evidence="ECO:0000269|PubMed:20966198"
FT REGION 238..305
FT /note="Necessary for interaction with TRA2B, nuclear
FT localization and exon-skipping"
FT /evidence="ECO:0000269|PubMed:14729963"
FT REGION 240..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..305
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15684395"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 2..24
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_016243"
FT VAR_SEQ 69..82
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037601"
FT MUTAGEN 53
FT /note="S->A: Abolishes phosphorylation by CSNK2A1 and
FT partially reduces splicing stimulation. Does not abolish
FT interaction with CSNK2A1 and subcellular localization."
FT /evidence="ECO:0000269|PubMed:15684395"
FT MUTAGEN 53
FT /note="S->E: Partially reduces splicing stimulation. Does
FT not abolish interaction with CSNK2A1 and subcellular
FT localization."
FT /evidence="ECO:0000269|PubMed:15684395"
FT MUTAGEN 171
FT /note="N->R: Impairs interaction with SAP18."
FT /evidence="ECO:0000269|PubMed:22388736"
FT MUTAGEN 205
FT /note="Y->A: Abolishes exon-skipping."
FT /evidence="ECO:0000269|PubMed:14729963"
FT MUTAGEN 207
FT /note="Y->A: Abolishes exon-skipping."
FT /evidence="ECO:0000269|PubMed:14729963"
FT CONFLICT 32
FT /note="K -> E (in Ref. 4; BAG56859)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="R -> G (in Ref. 2; AAC39791)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="R -> G (in Ref. 4; BAG56859)"
FT /evidence="ECO:0000305"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4A8X"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:4A8X"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4A8X"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4A8X"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:4A8X"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:4A8X"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4A8X"
SQ SEQUENCE 305 AA; 34208 MW; 930C9D36C2486144 CRC64;
MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD
KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS
SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI
FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA
PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS
SNSSR
