RNPS1_MOUSE
ID RNPS1_MOUSE Reviewed; 305 AA.
AC Q99M28; Q3TMJ1; Q922H8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein with serine-rich domain 1;
GN Name=Rnps1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic
CC shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1
CC and UAP56 in the nucleus and nuclear speckles (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99M28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99M28-2; Sequence=VSP_016244;
CC -!- DOMAIN: The RRM domain is required for the formation of the ASAP
CC complex. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AK146443; BAE27176.1; -; mRNA.
DR EMBL; AK151150; BAE30156.1; -; mRNA.
DR EMBL; AK165905; BAE38451.1; -; mRNA.
DR EMBL; BC002061; AAH02061.1; -; mRNA.
DR EMBL; BC008089; AAH08089.1; -; mRNA.
DR CCDS; CCDS37487.1; -. [Q99M28-2]
DR CCDS; CCDS37488.1; -. [Q99M28-1]
DR RefSeq; NP_001073596.1; NM_001080127.1. [Q99M28-1]
DR RefSeq; NP_001073597.1; NM_001080128.1. [Q99M28-2]
DR RefSeq; NP_033096.2; NM_009070.2. [Q99M28-1]
DR RefSeq; XP_017172851.1; XM_017317362.1.
DR AlphaFoldDB; Q99M28; -.
DR SMR; Q99M28; -.
DR BioGRID; 202923; 15.
DR IntAct; Q99M28; 9.
DR MINT; Q99M28; -.
DR STRING; 10090.ENSMUSP00000126345; -.
DR iPTMnet; Q99M28; -.
DR PhosphoSitePlus; Q99M28; -.
DR EPD; Q99M28; -.
DR jPOST; Q99M28; -.
DR MaxQB; Q99M28; -.
DR PaxDb; Q99M28; -.
DR PRIDE; Q99M28; -.
DR ProteomicsDB; 260992; -. [Q99M28-1]
DR ProteomicsDB; 260993; -. [Q99M28-2]
DR Antibodypedia; 23681; 75 antibodies from 21 providers.
DR DNASU; 19826; -.
DR Ensembl; ENSMUST00000088512; ENSMUSP00000085867; ENSMUSG00000034681. [Q99M28-1]
DR Ensembl; ENSMUST00000115371; ENSMUSP00000111028; ENSMUSG00000034681. [Q99M28-2]
DR Ensembl; ENSMUST00000163717; ENSMUSP00000126345; ENSMUSG00000034681. [Q99M28-1]
DR GeneID; 19826; -.
DR KEGG; mmu:19826; -.
DR UCSC; uc008avs.1; mouse. [Q99M28-1]
DR UCSC; uc008avu.1; mouse. [Q99M28-2]
DR CTD; 10921; -.
DR MGI; MGI:97960; Rnps1.
DR VEuPathDB; HostDB:ENSMUSG00000034681; -.
DR eggNOG; KOG4209; Eukaryota.
DR GeneTree; ENSGT00730000111029; -.
DR HOGENOM; CLU_076438_0_0_1; -.
DR InParanoid; Q99M28; -.
DR OMA; MRRPQGG; -.
DR OrthoDB; 1524222at2759; -.
DR PhylomeDB; Q99M28; -.
DR TreeFam; TF314165; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 19826; 17 hits in 76 CRISPR screens.
DR ChiTaRS; Rnps1; mouse.
DR PRO; PR:Q99M28; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99M28; protein.
DR Bgee; ENSMUSG00000034681; Expressed in embryonic post-anal tail and 231 other tissues.
DR Genevisible; Q99M28; MM.
DR GO; GO:0061574; C:ASAP complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
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 Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..305
FT /note="RNA-binding protein with serine-rich domain 1"
FT /id="PRO_0000081817"
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 /evidence="ECO:0000250"
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:0000250"
FT REGION 69..121
FT /note="Necessary for interactions with UPF2 and UPF3B and
FT UPF2-dependent NMD"
FT /evidence="ECO:0000250"
FT REGION 156..242
FT /note="Necessary for interaction with PNN and exon-
FT skipping"
FT /evidence="ECO:0000250"
FT REGION 159..244
FT /note="Interaction with SAP18 and ACIN1"
FT /evidence="ECO:0000250"
FT REGION 238..305
FT /note="Necessary for interaction with TRA2B, nuclear
FT localization and exon-skipping"
FT /evidence="ECO:0000250"
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"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15287"
FT VAR_SEQ 2..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016244"
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
