PSPC1_HUMAN
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 03-AUG-2022, entry version 182.
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-ARNTL/BMAL1 heterodimer (By
CC similarity). Together with NONO, required for the formation of nuclear
CC paraspeckles. Plays a role in the regulation of DNA virus-mediated
CC innate immune response by assembling into the HDP-RNP complex, a
CC complex that serves as a platform for IRF3 phosphorylation and
CC subsequent innate immune response activation through the cGAS-STING
CC pathway. {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};
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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; 166.
DR CORUM; Q8WXF1; -.
DR DIP; DIP-39028N; -.
DR IntAct; Q8WXF1; 45.
DR MINT; Q8WXF1; -.
DR STRING; 9606.ENSP00000343966; -.
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; Q8WXF1; -.
DR PeptideAtlas; Q8WXF1; -.
DR PRIDE; Q8WXF1; -.
DR ProteomicsDB; 75023; -. [Q8WXF1-1]
DR ProteomicsDB; 75024; -. [Q8WXF1-2]
DR Antibodypedia; 22257; 71 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 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; GDGYNQA; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; Q8WXF1; -.
DR TreeFam; TF315795; -.
DR PathwayCommons; Q8WXF1; -.
DR SignaLink; Q8WXF1; -.
DR SIGNOR; Q8WXF1; -.
DR BioGRID-ORCS; 55269; 76 hits in 1077 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 189 other tissues.
DR ExpressionAtlas; Q8WXF1; baseline and differential.
DR Genevisible; Q8WXF1; HS.
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; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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 transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd12586; RRM1_PSP1; 1.
DR CDD; cd12589; RRM2_PSP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
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 Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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
