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RNA-binding protein with serine-rich domain 1 (SR-related protein LDC2)

 RNPS1_HUMAN             Reviewed;         305 AA.
Q15287; A8K1P0; B4DDU8; B4DZU7; B7ZA17; O75308; Q32P25; Q8WY42;
Q9NYG3;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 175.
RecName: Full=RNA-binding protein with serine-rich domain 1;
AltName: Full=SR-related protein LDC2;
Name=RNPS1; Synonyms=LDC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8543184; DOI=10.1016/0378-1119(95)00571-4;
Badolato J., Gardiner E., Morrison N., Eisman J.;
"Identification and characterisation of a novel human RNA-binding
protein.";
Gene 166:323-327(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC2L1, AND
SUBCELLULAR LOCATION.
TISSUE=B-cell;
PubMed=9580558;
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.;
"The RNP protein, RNPS1, associates with specific isoforms of the
p34cdc2-related PITSLRE protein kinases in vivo.";
J. Cell Sci. 111:1495-1506(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Thymus;
Harada K., Yang D., Yamada A., Shichijo S., Itoh K.;
"Identification of an alternatively spliced form of RNPS1.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Hippocampus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 78-305.
TISSUE=Kidney;
Lee D.-C., Ouyang P.;
"Direct interaction of LDC2, a SR-related protein with pinin.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE SPLICEOSOME, AND
SUBCELLULAR LOCATION.
PubMed=10449421; DOI=10.1093/emboj/18.16.4560;
Mayeda A., Badolato J., Kobayashi R., Zhang M.Q., Gardiner E.M.,
Krainer A.R.;
"Purification and characterization of human RNPS1: a general activator
of pre-mRNA splicing.";
EMBO J. 18:4560-4570(1999).
[10]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX
(EJC) WITH DEK; RBM8A; SRRM1 AND ALYREF/THOC4.
PubMed=11118221; DOI=10.1093/emboj/19.24.6860;
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
"The spliceosome deposits multiple proteins 20-24 nucleotides upstream
of mRNA exon-exon junctions.";
EMBO J. 19:6860-6869(2000).
[11]
INTERACTION WITH SART3, AND SUBCELLULAR LOCATION.
PubMed=11477570; DOI=10.1002/ijc.1391;
Harada K., Yamada A., Yang D., Itoh K., Shichijo S.;
"Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing
factor RNPS1: a possible regulation of splicing by a complex
formation.";
Int. J. Cancer 93:623-628(2001).
[12]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A
POST-SPLICING COMPLEX WITH NXF1; RBM8A; UPF1; UPF2; UPF3A AND UPF3B,
RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=11546874; DOI=10.1126/science.1062786;
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Communication of the position of exon-exon junctions to the mRNA
surveillance machinery by the protein RNPS1.";
Science 293:1836-1839(2001).
[13]
FUNCTION IN MRNA 3'-END FORMATION, AND INTERACTION WITH SRRM1.
PubMed=12944400; DOI=10.1074/jbc.M306856200;
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
"An evolutionarily conserved role for SRm160 in 3'-end processing that
functions independently of exon junction complex formation.";
J. Biol. Chem. 278:44153-44160(2003).
[14]
IDENTIFICATION IN A MRNP COMPLEX WITH PNN, INTERACTION WITH PNN, AND
SUBCELLULAR LOCATION.
PubMed=14517304; DOI=10.1128/MCB.23.20.7363-7376.2003;
Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.;
"Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in
mRNA processing and export via interaction with RNPS1.";
Mol. Cell. Biol. 23:7363-7376(2003).
[15]
FUNCTION IN TRANSLATIONAL ACTIVITY AND NONSENSE-MEDIATED MRNA DECAY,
AND ASSOCIATION WITH POLYSOMES.
PubMed=14752011; DOI=10.1101/gad.1163204;
Nott A., Le Hir H., Moore M.J.;
"Splicing enhances translation in mammalian cells: an additional
function of the exon junction complex.";
Genes Dev. 18:210-222(2004).
[16]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX
(EJC) WITH RBM8A AND SRRM1.
PubMed=14625303; DOI=10.1074/jbc.M307692200;
Kataoka N., Dreyfuss G.;
"A simple whole cell lysate system for in vitro splicing reveals a
stepwise assembly of the exon-exon junction complex.";
J. Biol. Chem. 279:7009-7013(2004).
[17]
FUNCTION IN ALTERNATIVE PRE-MRNA SPLICING, INTERACTION WITH PNN; SRP54
AND TRA2B, MUTAGENESIS OF TYR-205 AND TYR-207, AND SUBCELLULAR
LOCATION.
PubMed=14729963; DOI=10.1128/MCB.24.3.1174-1187.2004;
Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
"Human RNPS1 and its associated factors: a versatile alternative pre-
mRNA splicing regulator in vivo.";
Mol. Cell. Biol. 24:1174-1187(2004).
[18]
FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE
SPLICEOSOME, PHOSPHORYLATION AT SER-53, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, AND
SUBCELLULAR LOCATION.
PubMed=15684395; DOI=10.1128/MCB.25.4.1446-1457.2005;
Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
Suzuki H., Endo H., Kidd V.J., Mayeda A.;
"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
phosphorylation.";
Mol. Cell. Biol. 25:1446-1457(2005).
[19]
FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY, AND
IDENTIFICATION IN A COMPLEX WITH UPF2 AND UPF3B.
PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012;
Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H.,
Hentze M.W., Kulozik A.E.;
"Exon-junction complex components specify distinct routes of nonsense-
mediated mRNA decay with differential cofactor requirements.";
Mol. Cell 20:65-75(2005).
[20]
IDENTIFICATION IN THE ASAP COMPLEX, AND FUNCTION OF THE ASAP COMPLEX.
PubMed=12665594; DOI=10.1128/MCB.23.8.2981-2990.2003;
Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E.,
Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.;
"ASAP, a novel protein complex involved in RNA processing and
apoptosis.";
Mol. Cell. Biol. 23:2981-2990(2003).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[22]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX,
IDENTIFICATION IN THE ASAP COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16314458; DOI=10.1261/rna.2155905;
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
"Biochemical analysis of the EJC reveals two new factors and a stable
tetrameric protein core.";
RNA 11:1869-1883(2005).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD).
PubMed=17586820; DOI=10.1093/nar/gkm461;
Viegas M.H., Gehring N.H., Breit S., Hentze M.W., Kulozik A.E.;
"The abundance of RNPS1, a protein component of the exon junction
complex, can determine the variability in efficiency of the nonsense
mediated decay pathway.";
Nucleic Acids Res. 35:4542-4551(2007).
[25]
SUBCELLULAR LOCATION.
PubMed=19324961; DOI=10.1261/rna.1387009;
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P.,
Wachsmuth M.;
"Assembly and mobility of exon-exon junction complexes in living
cells.";
RNA 15:862-876(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
INTERACTION WITH SAP18 AND ACIN1.
PubMed=20966198; DOI=10.1261/rna.2304410;
Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A.,
Schulze-Osthoff K., Schaal H., Schwerk C.;
"Human SAP18 mediates assembly of a splicing regulatory multiprotein
complex via its ubiquitin-like fold.";
RNA 16:2442-2454(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-157 AND
THR-161, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
FUNCTION.
PubMed=22203037; DOI=10.1128/MCB.06130-11;
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P.,
Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H.,
Klinck R., Elela S.A., Prinos P., Chabot B.;
"Proteins associated with the exon junction complex also control the
alternative splicing of apoptotic regulators.";
Mol. Cell. Biol. 32:954-967(2012).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[32]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THE ASAP COMPLEX,
IDENTIFICATION IN THE PSAP COMPLEX, INTERACTION WITH SAP18, AND
MUTAGENESIS OF ASN-171.
PubMed=22388736; DOI=10.1038/nsmb.2242;
Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.;
"The structure of the ASAP core complex reveals the existence of a
Pinin-containing PSAP complex.";
Nat. Struct. Mol. Biol. 19:378-386(2012).
-!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP
complexes. Auxiliary component of the splicing-dependent
multiprotein exon junction complex (EJC) deposited at splice
junction on mRNAs. The EJC is a dynamic structure consisting of
core proteins and several peripheral nuclear and cytoplasmic
associated factors that join the complex only transiently either
during EJC assembly or during subsequent mRNA metabolism.
Component of the ASAP and PSAP complexes which bind RNA in a
sequence-independent manner and are proposed to be recruited to
the EJC prior to or during the splicing process and to regulate
specific excision of introns in specific transcription subsets.
The ASAP complex can inhibit RNA processing during in vitro
splicing reactions. The ASAP complex promotes apoptosis and is
disassembled after induction of apoptosis. Enhances the formation
of the ATP-dependent A complex of the spliceosome. Involved in
both constitutive splicing and, in association with SRP54 and
TRA2B/SFRS10, in distinctive modulation of alternative splicing in
a substrate-dependent manner. Involved in the splicing modulation
of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically
inhibits formation of proapoptotic isoforms such as Bcl-X(S); the
activity is different from the established EJC assembly and
function. Participates in mRNA 3'-end cleavage. Involved in UPF2-
dependent nonsense-mediated decay (NMD) of mRNAs containing
premature stop codons. Also mediates increase of mRNA abundance
and translational efficiency. Binds spliced mRNA 20-25 nt upstream
of exon-exon junctions. {ECO:0000269|PubMed:10449421,
ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12665594,
ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14729963,
ECO:0000269|PubMed:14752011, ECO:0000269|PubMed:15684395,
ECO:0000269|PubMed:16209946, ECO:0000269|PubMed:17586820,
ECO:0000269|PubMed:22203037}.
-!- SUBUNIT: Found in mRNA splicing-dependent exon junction complexes
(EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1,
UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP
(apoptosis- and splicing-associated protein) and PSAP complexes
consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively;
the ASAP and PSAP complexes probably are formed mutually
exclusive. Component of the active spliceosome. Associates with
polysomes. Interacts with the cleaved p110 isoform of CDC2L1,
CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10.
{ECO:0000269|PubMed:11118221, ECO:0000269|PubMed:11477570,
ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:12665594,
ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14517304,
ECO:0000269|PubMed:14625303, ECO:0000269|PubMed:14729963,
ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:16209946,
ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:20966198,
ECO:0000269|PubMed:22388736, ECO:0000269|PubMed:9580558}.
-!- INTERACTION:
Q9UKV3-2:ACIN1; NbExp=4; IntAct=EBI-15972541, EBI-5279966;
Q9VJ12:Acn (xeno); NbExp=4; IntAct=EBI-15972541, EBI-3418150;
Q9UK58:CCNL1; NbExp=3; IntAct=EBI-395959, EBI-2836773;
P49760:CLK2; NbExp=4; IntAct=EBI-395959, EBI-750020;
Q9H307:PNN; NbExp=3; IntAct=EBI-15972541, EBI-681904;
Q15020:SART3; NbExp=5; IntAct=EBI-395959, EBI-308619;
Q96SB4:SRPK1; NbExp=2; IntAct=EBI-395959, EBI-539478;
P78362:SRPK2; NbExp=3; IntAct=EBI-395959, EBI-593303;
P84103:SRSF3; NbExp=4; IntAct=EBI-395959, EBI-372557;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
Note=Nucleocytoplasmic shuttling protein. Colocalizes with the
core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear
speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q15287-1; Sequence=Displayed;
Name=2;
IsoId=Q15287-2; Sequence=VSP_016243;
Name=3;
IsoId=Q15287-3; Sequence=VSP_016243, VSP_037601;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8543184}.
-!- DOMAIN: The RRM domain is required for the formation of the ASAP
complex.
-!- PTM: Phosphorylated on one or more of the four Ser/Thr residues
(Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is
important for splicing and translation stimulation activity in
vitro. {ECO:0000269|PubMed:15684395}.
-!- SIMILARITY: Belongs to the splicing factor SR family.
{ECO:0000305}.
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EMBL; L37368; AAA92859.1; -; mRNA.
EMBL; AF015608; AAC39791.1; -; mRNA.
EMBL; AF274003; AAL56665.1; -; mRNA.
EMBL; AK289955; BAF82644.1; -; mRNA.
EMBL; AK293343; BAG56859.1; -; mRNA.
EMBL; AK303100; BAG64209.1; -; mRNA.
EMBL; AK316132; BAH14503.1; -; mRNA.
EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85516.1; -; Genomic_DNA.
EMBL; BC001659; AAH01659.1; -; mRNA.
EMBL; BC001838; AAH01838.1; -; mRNA.
EMBL; BC108316; AAI08317.1; -; mRNA.
EMBL; AF247662; AAF72519.1; -; mRNA.
CCDS; CCDS10465.1; -. [Q15287-1]
CCDS; CCDS66907.1; -. [Q15287-2]
PIR; JC4525; JC4525.
RefSeq; NP_001273554.1; NM_001286625.1. [Q15287-1]
RefSeq; NP_001273555.1; NM_001286626.1. [Q15287-2]
RefSeq; NP_001273556.1; NM_001286627.1.
RefSeq; NP_006702.1; NM_006711.4. [Q15287-1]
RefSeq; NP_542161.1; NM_080594.3. [Q15287-1]
RefSeq; XP_005255105.1; XM_005255048.1. [Q15287-1]
RefSeq; XP_005255106.1; XM_005255049.3. [Q15287-1]
RefSeq; XP_016878363.1; XM_017022874.1. [Q15287-1]
UniGene; Hs.355643; -.
UniGene; Hs.507343; -.
UniGene; Hs.733012; -.
PDB; 4A8X; X-ray; 1.90 A; A=159-244.
PDBsum; 4A8X; -.
ProteinModelPortal; Q15287; -.
SMR; Q15287; -.
BioGrid; 116125; 189.
CORUM; Q15287; -.
DIP; DIP-32943N; -.
IntAct; Q15287; 87.
MINT; MINT-1474621; -.
STRING; 9606.ENSP00000301730; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
iPTMnet; Q15287; -.
PhosphoSitePlus; Q15287; -.
SwissPalm; Q15287; -.
DMDM; 74754492; -.
EPD; Q15287; -.
MaxQB; Q15287; -.
PaxDb; Q15287; -.
PeptideAtlas; Q15287; -.
PRIDE; Q15287; -.
DNASU; 10921; -.
Ensembl; ENST00000301730; ENSP00000301730; ENSG00000205937. [Q15287-1]
Ensembl; ENST00000320225; ENSP00000315859; ENSG00000205937. [Q15287-1]
Ensembl; ENST00000397086; ENSP00000380275; ENSG00000205937. [Q15287-1]
Ensembl; ENST00000565678; ENSP00000457723; ENSG00000205937. [Q15287-1]
Ensembl; ENST00000566458; ENSP00000456352; ENSG00000205937. [Q15287-2]
Ensembl; ENST00000568631; ENSP00000457820; ENSG00000205937. [Q15287-1]
GeneID; 10921; -.
KEGG; hsa:10921; -.
UCSC; uc002cpt.5; human. [Q15287-1]
CTD; 10921; -.
DisGeNET; 10921; -.
EuPathDB; HostDB:ENSG00000205937.11; -.
GeneCards; RNPS1; -.
H-InvDB; HIX0031789; -.
HGNC; HGNC:10080; RNPS1.
HPA; HPA044014; -.
MIM; 606447; gene.
neXtProt; NX_Q15287; -.
OpenTargets; ENSG00000205937; -.
PharmGKB; PA34453; -.
eggNOG; KOG4209; Eukaryota.
eggNOG; ENOG4111PFV; LUCA.
GeneTree; ENSGT00730000111029; -.
HOVERGEN; HBG053138; -.
InParanoid; Q15287; -.
KO; K14325; -.
OMA; PNFGRGV; -.
OrthoDB; EOG091G14LV; -.
PhylomeDB; Q15287; -.
TreeFam; TF314165; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RNPS1; human.
GeneWiki; RNPS1; -.
GenomeRNAi; 10921; -.
PRO; PR:Q15287; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205937; -.
CleanEx; HS_RNPS1; -.
ExpressionAtlas; Q15287; baseline and differential.
Genevisible; Q15287; HS.
GO; GO:0061574; C:ASAP complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
CDD; cd12365; RRM_RNPS1; 1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR034201; RNPS1_RRM.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Ubl conjugation.
CHAIN 1 305 RNA-binding protein with serine-rich
domain 1.
/FTId=PRO_0000081816.
DOMAIN 161 240 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 1 220 Necessary for interaction with the
cleaved p110 isoform of CDC2L1.
REGION 1 161 Necessary for interaction with SRP54,
nuclear localization and exon-skipping.
{ECO:0000269|PubMed:14729963}.
REGION 69 121 Necessary for interactions with UPF2 and
UPF3B and UPF2-dependent NMD.
REGION 156 242 Necessary for interaction with PNN and
exon-skipping.
REGION 159 244 Interaction with SAP18 and ACIN1.
{ECO:0000269|PubMed:20966198}.
REGION 238 305 Necessary for interaction with TRA2B,
nuclear localization and exon-skipping.
{ECO:0000269|PubMed:14729963}.
COMPBIAS 7 64 Lys-rich.
COMPBIAS 67 141 Ser-rich.
COMPBIAS 128 154 Arg-rich.
COMPBIAS 241 298 Arg/Pro-rich.
MOD_RES 53 53 Phosphoserine; by CK2.
{ECO:0000269|PubMed:15684395}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 161 161 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 218 218 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 2 24 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_016243.
VAR_SEQ 69 82 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037601.
MUTAGEN 53 53 S->A: Abolishes phosphorylation by
CSNK2A1 and partially reduces splicing
stimulation. Does not abolish interaction
with CSNK2A1 and subcellular
localization.
{ECO:0000269|PubMed:15684395}.
MUTAGEN 53 53 S->E: Partially reduces splicing
stimulation. Does not abolish interaction
with CSNK2A1 and subcellular
localization.
{ECO:0000269|PubMed:15684395}.
MUTAGEN 171 171 N->R: Impairs interaction with SAP18.
{ECO:0000269|PubMed:22388736}.
MUTAGEN 205 205 Y->A: Abolishes exon-skipping.
{ECO:0000269|PubMed:14729963}.
MUTAGEN 207 207 Y->A: Abolishes exon-skipping.
{ECO:0000269|PubMed:14729963}.
CONFLICT 32 32 K -> E (in Ref. 4; BAG56859).
{ECO:0000305}.
CONFLICT 66 66 R -> G (in Ref. 2; AAC39791).
{ECO:0000305}.
CONFLICT 249 249 R -> G (in Ref. 4; BAG56859).
{ECO:0000305}.
STRAND 162 166 {ECO:0000244|PDB:4A8X}.
HELIX 174 182 {ECO:0000244|PDB:4A8X}.
STRAND 187 191 {ECO:0000244|PDB:4A8X}.
STRAND 198 202 {ECO:0000244|PDB:4A8X}.
STRAND 204 212 {ECO:0000244|PDB:4A8X}.
HELIX 213 223 {ECO:0000244|PDB:4A8X}.
STRAND 234 238 {ECO:0000244|PDB:4A8X}.
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


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