ID PSPC1_HUMAN Reviewed; 523 AA. AC Q8WXF1; Q5JTQ3; Q8NCZ9; Q8WXE8; Q9NV36; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Paraspeckle component 1; DE AltName: Full=Paraspeckle protein 1; GN Name=PSPC1; Synonyms=PSP1; 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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 21-83; RP 105-124; 135-143; 185-194; 199-210; 252-259; 265-289; 327-345; 352-357; RP 366-374 AND 483-507, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11790299; DOI=10.1016/s0960-9822(01)00632-7; RA Fox A.H., Lam Y.W., Leung A.K.L., Lyon C.E., Andersen J., Mann M., RA Lamond A.I.; RT "Paraspeckles: a novel nuclear domain."; RL Curr. Biol. 12:13-25(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-523 (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-523 (ISOFORM 2). RC TISSUE=Kidney; 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 SUBUNIT, INTERACTION WITH NONO, MUTAGENESIS OF PHE-119; PHE-121; LYS-198 RP AND PHE-200, AND SUBCELLULAR LOCATION. RX PubMed=16148043; DOI=10.1091/mbc.e05-06-0587; RA Fox A.H., Bond C.S., Lamond A.I.; RT "P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RT RNA-dependent manner."; RL Mol. Biol. Cell 16:5304-5315(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-473 AND SER-477, AND RP 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 [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] 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 [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-507, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; XRCC6; RP SFPQ; NONO; HEXIM1; RBM14 AND MATR3. RX PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020; RA Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D., RA Dubois E., Schwartz O., Bennasser Y., Benkirane M.; RT "HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex that RT regulates DNA-mediated innate immune response."; RL Mol. Cell 67:387-399(2017). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 61-320 IN COMPLEX WITH NONO, RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-275 AND TRP-279. RX PubMed=22416126; DOI=10.1073/pnas.1120792109; RA Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A., Filipovska A., RA Fox A.H., Bond C.S.; RT "Structure of the heterodimer of human NONO and paraspeckle protein RT component 1 and analysis of its role in subnuclear body formation."; RL Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012). CC -!- FUNCTION: Regulates, cooperatively with NONO and SFPQ, androgen CC receptor-mediated gene transcription activity in Sertoli cell line (By CC similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. CC Regulates the circadian clock by repressing the transcriptional CC activator activity of the CLOCK-BMAL1 heterodimer (By similarity). CC Together with NONO, required for the formation of nuclear paraspeckles. CC Plays a role in the regulation of DNA virus-mediated innate immune CC response by assembling into the HDP-RNP complex, a complex that serves CC as a platform for IRF3 phosphorylation and subsequent innate immune CC response activation through the cGAS-STING pathway. CC {ECO:0000250|UniProtKB:Q8R326, ECO:0000269|PubMed:22416126, CC ECO:0000269|PubMed:28712728}. CC -!- SUBUNIT: Forms heterodimers with NONO; this involves formation of a CC coiled coil domain by helices from both proteins. Found in a RNP CC complex with CAT2 transcribed nuclear RNA (CTN-RNA). Interaction with CC NONO is required for its targeting to paraspeckles and perinucleolar CC caps. Interacts with SFPQ (By similarity). Part of the HDP-RNP complex CC composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins CC (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. CC {ECO:0000250|UniProtKB:Q8R326, ECO:0000269|PubMed:16148043, CC ECO:0000269|PubMed:28712728}. CC -!- INTERACTION: CC Q8WXF1; Q15323: KRT31; NbExp=3; IntAct=EBI-1392258, EBI-948001; CC Q8WXF1; Q15233: NONO; NbExp=11; IntAct=EBI-1392258, EBI-350527; CC Q8WXF1; Q15233-2: NONO; NbExp=3; IntAct=EBI-1392258, EBI-10203843; CC Q8WXF1-1; Q15233: NONO; NbExp=7; IntAct=EBI-15974663, EBI-350527; CC Q8WXF1-2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-12135327, EBI-11988027; CC Q8WXF1-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-12135327, EBI-1216080; CC Q8WXF1-2; Q15233: NONO; NbExp=4; IntAct=EBI-12135327, EBI-350527; CC Q8WXF1-2; O43809: NUDT21; NbExp=3; IntAct=EBI-12135327, EBI-355720; CC Q8WXF1-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-12135327, EBI-527853; CC Q8WXF1-2; A6NJL1: ZSCAN5B; NbExp=3; IntAct=EBI-12135327, EBI-17968892; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus matrix {ECO:0000250}. CC Cytoplasm {ECO:0000250}. Nucleus speckle. Note=In punctate subnuclear CC structures often located adjacent to splicing speckles, called CC paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and CC perinucleolar caps in an RNA-dependent manner. May cycle between CC paraspeckles and nucleolus. In telophase, when daughter nuclei form, CC localizes to perinucleolar caps. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=PSP1-alpha; CC IsoId=Q8WXF1-1; Sequence=Displayed; CC Name=2; Synonyms=PSP1-beta; CC IsoId=Q8WXF1-2; Sequence=VSP_027274, VSP_027275; CC -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, CC liver, lung, placenta, brain and heart. {ECO:0000269|PubMed:11790299}. CC -!- SIMILARITY: Belongs to the PSPC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91924.1; Type=Erroneous termination; Note=Truncated C-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; AF448795; AAL59601.1; -; mRNA. DR EMBL; AF449627; AAL59602.1; -; mRNA. DR EMBL; AK001817; BAA91924.1; ALT_SEQ; mRNA. DR EMBL; AL354808; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08232.1; -; Genomic_DNA. DR EMBL; BC014184; AAH14184.2; -; mRNA. DR EMBL; CR457272; CAG33553.1; -; mRNA. DR EMBL; AL834505; CAD39162.1; -; mRNA. DR CCDS; CCDS41870.1; -. [Q8WXF1-1] DR CCDS; CCDS86343.1; -. [Q8WXF1-2] DR RefSeq; NP_001035879.1; NM_001042414.2. [Q8WXF1-1] DR RefSeq; XP_006719907.1; XM_006719844.3. DR RefSeq; XP_016876139.1; XM_017020650.1. DR PDB; 3SDE; X-ray; 1.90 A; A=61-320. DR PDB; 5IFN; X-ray; 3.17 A; A/B=61-320. DR PDB; 5WPA; X-ray; 2.29 A; B=61-320. DR PDBsum; 3SDE; -. DR PDBsum; 5IFN; -. DR PDBsum; 5WPA; -. DR AlphaFoldDB; Q8WXF1; -. DR SMR; Q8WXF1; -. DR BioGRID; 120558; 489. DR ComplexPortal; CPX-7764; SFPQ-PSPC1 RNA-binding complex. DR ComplexPortal; CPX-7783; PSPC1 RNA-binding homodimer. DR ComplexPortal; CPX-889; NONO-PSPC1 RNA-binding complex. DR CORUM; Q8WXF1; -. DR DIP; DIP-39028N; -. DR IntAct; Q8WXF1; 49. DR MINT; Q8WXF1; -. DR STRING; 9606.ENSP00000343966; -. DR GlyGen; Q8WXF1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8WXF1; -. DR MetOSite; Q8WXF1; -. DR PhosphoSitePlus; Q8WXF1; -. DR SwissPalm; Q8WXF1; -. DR BioMuta; PSPC1; -. DR DMDM; 74762636; -. DR CPTAC; CPTAC-430; -. DR CPTAC; CPTAC-431; -. DR EPD; Q8WXF1; -. DR jPOST; Q8WXF1; -. DR MassIVE; Q8WXF1; -. DR MaxQB; Q8WXF1; -. DR PaxDb; 9606-ENSP00000343966; -. DR PeptideAtlas; Q8WXF1; -. DR ProteomicsDB; 75023; -. [Q8WXF1-1] DR ProteomicsDB; 75024; -. [Q8WXF1-2] DR Pumba; Q8WXF1; -. DR Antibodypedia; 22257; 96 antibodies from 20 providers. DR DNASU; 55269; -. DR Ensembl; ENST00000338910.9; ENSP00000343966.4; ENSG00000121390.19. [Q8WXF1-1] DR Ensembl; ENST00000471658.5; ENSP00000436038.1; ENSG00000121390.19. [Q8WXF1-2] DR Ensembl; ENST00000492741.5; ENSP00000435921.1; ENSG00000121390.19. [Q8WXF1-2] DR Ensembl; ENST00000619300.4; ENSP00000481916.1; ENSG00000121390.19. [Q8WXF1-1] DR GeneID; 55269; -. DR KEGG; hsa:55269; -. DR MANE-Select; ENST00000338910.9; ENSP00000343966.4; NM_001354909.2; NP_001341838.1. DR UCSC; uc021rgx.2; human. [Q8WXF1-1] DR AGR; HGNC:20320; -. DR CTD; 55269; -. DR DisGeNET; 55269; -. DR GeneCards; PSPC1; -. DR HGNC; HGNC:20320; PSPC1. DR HPA; ENSG00000121390; Low tissue specificity. DR MIM; 612408; gene. DR neXtProt; NX_Q8WXF1; -. DR OpenTargets; ENSG00000121390; -. DR PharmGKB; PA134968603; -. DR VEuPathDB; HostDB:ENSG00000121390; -. DR eggNOG; KOG0115; Eukaryota. DR GeneTree; ENSGT00940000157358; -. DR HOGENOM; CLU_027185_0_0_1; -. DR InParanoid; Q8WXF1; -. DR OMA; EQDMRMG; -. DR OrthoDB; 5403433at2759; -. DR PhylomeDB; Q8WXF1; -. DR TreeFam; TF315795; -. DR PathwayCommons; Q8WXF1; -. DR SignaLink; Q8WXF1; -. DR SIGNOR; Q8WXF1; -. DR BioGRID-ORCS; 55269; 80 hits in 1153 CRISPR screens. DR ChiTaRS; PSPC1; human. DR GenomeRNAi; 55269; -. DR Pharos; Q8WXF1; Tbio. DR PRO; PR:Q8WXF1; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q8WXF1; Protein. DR Bgee; ENSG00000121390; Expressed in ventricular zone and 191 other cell types or tissues. DR ExpressionAtlas; Q8WXF1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0042382; C:paraspeckles; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; IDA:UniProt. DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0140694; P:non-membrane-bounded organelle assembly; IDA:UniProt. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR CDD; cd12949; NOPS_PSPC1; 1. DR CDD; cd12586; RRM1_PSP1; 1. DR CDD; cd12589; RRM2_PSP1; 1. DR Gene3D; 3.30.70.330; -; 2. DR Gene3D; 6.10.250.1170; -; 1. DR InterPro; IPR012975; NOPS. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR034522; PSP1_RRM1. DR InterPro; IPR034523; PSP1_RRM2. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23189:SF14; PARASPECKLE COMPONENT 1; 1. DR PANTHER; PTHR23189; RNA RECOGNITION MOTIF-CONTAINING; 1. DR Pfam; PF08075; NOPS; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 2. DR Genevisible; Q8WXF1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Biological rhythms; Coiled coil; Cytoplasm; Direct protein sequencing; KW Immunity; Innate immunity; Methylation; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription; KW Transcription regulation. FT CHAIN 1..523 FT /note="Paraspeckle component 1" FT /id="PRO_0000297540" FT DOMAIN 82..154 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 156..237 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 125..358 FT /note="Sufficient for paraspeckles localization" FT REGION 231..358 FT /note="Sufficient for perinucleolar caps localization and FT interaction with NONO" FT /evidence="ECO:0000269|PubMed:16148043" FT REGION 460..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 283..377 FT /evidence="ECO:0000255" FT COMPBIAS 470..492 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 507 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT VAR_SEQ 387..393 FT /note="REQEMRM -> GDKRKCG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11790299, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6" FT /id="VSP_027274" FT VAR_SEQ 394..523 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11790299, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6" FT /id="VSP_027275" FT MUTAGEN 119 FT /note="F->A: Abolishes accumulation in paraspeckles, but FT not in perinucleolar caps; when associated with A-121; FT A-198 and A-200." FT /evidence="ECO:0000269|PubMed:16148043" FT MUTAGEN 121 FT /note="F->A: Abolishes accumulation in paraspeckles, but FT not in perinucleolar caps; when associated with A-119; FT A-198 and A-200." FT /evidence="ECO:0000269|PubMed:16148043" FT MUTAGEN 198 FT /note="K->A: Abolishes accumulation in paraspeckles, but FT not in perinucleolar caps; when associated with A-119; FT A-121 and A-200." FT /evidence="ECO:0000269|PubMed:16148043" FT MUTAGEN 200 FT /note="F->A: Abolishes accumulation in paraspeckles, but FT not in perinucleolar caps; when associated with A-119; FT A-121 and A-198." FT /evidence="ECO:0000269|PubMed:16148043" FT MUTAGEN 275 FT /note="Y->A: Abolishes interaction with NONO and FT localization in nuclear paraspeckles; when associated with FT A-279." FT /evidence="ECO:0000269|PubMed:22416126" FT MUTAGEN 279 FT /note="W->A: Abolishes interaction with NONO and FT localization in nuclear paraspeckles; when associated with FT A-275." FT /evidence="ECO:0000269|PubMed:22416126" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:5IFN" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 95..101 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:3SDE" FT TURN 115..118 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 127..137 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:5WPA" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 155..162 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 169..176 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 182..190 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 195..205 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 206..218 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 253..259 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 271..318 FT /evidence="ECO:0007829|PDB:3SDE" SQ SEQUENCE 523 AA; 58744 MW; 3A8C44079D64BBF0 CRC64; MMLRGNLKQV RIEKNPARLR ALESAVGESE PAAAAAMALA LAGEPAPPAP APPEDHPDEE MGFTIDIKSF LKPGEKTYTQ RCRLFVGNLP TDITEEDFKR LFERYGEPSE VFINRDRGFG FIRLESRTLA EIAKAELDGT ILKSRPLRIR FATHGAALTV KNLSPVVSNE LLEQAFSQFG PVEKAVVVVD DRGRATGKGF VEFAAKPPAR KALERCGDGA FLLTTTPRPV IVEPMEQFDD EDGLPEKLMQ KTQQYHKERE QPPRFAQPGT FEFEYASRWK ALDEMEKQQR EQVDRNIREA KEKLEAEMEA ARHEHQLMLM RQDLMRRQEE LRRLEELRNQ ELQKRKQIQL RHEEEHRRRE EEMIRHREQE ELRRQQEGFK PNYMENREQE MRMGDMGPRG AINMGDAFSP APAGNQGPPP MMGMNMNNRA TIPGPPMGPG PAMGPEGAAN MGTPMMPDNG AVHNDRFPQG PPSQMGSPMG SRTGSETPQA PMSGVGPVSG GPGGFGRGSQ GGNFEGPNKR RRY //