RBM14_HUMAN
ID RBM14_HUMAN Reviewed; 669 AA.
AC Q96PK6; B0LM41; B3KMN4; D6RGD8; O75932; Q2PYN1; Q53GV1; Q68DQ9; Q96PK5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=RNA-binding protein 14;
DE AltName: Full=Paraspeckle protein 2;
DE Short=PSP2;
DE AltName: Full=RNA-binding motif protein 14;
DE AltName: Full=RRM-containing coactivator activator/modulator;
DE AltName: Full=Synaptotagmin-interacting protein;
DE Short=SYT-interacting protein;
GN Name=RBM14; Synonyms=SIP;
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), ALTERNATIVE SPLICING, AND
RP INTERACTION WITH CITED1; NCOA6 AND XRCC5.
RX PubMed=11443112; DOI=10.1074/jbc.m101517200;
RA Iwasaki T., Chin W.W., Ko L.;
RT "Identification and characterization of RRM-containing coactivator
RT activator (CoAA) as TRBP-interacting protein, and its splice variant as a
RT coactivator modulator (CoAM).";
RL J. Biol. Chem. 276:33375-33383(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=17337438; DOI=10.1093/nar/gkl1092;
RA Yang Z., Sui Y., Xiong S., Liour S.S., Phillips A.C., Ko L.;
RT "Switched alternative splicing of oncogene CoAA during embryonal carcinoma
RT stem cell differentiation.";
RL Nucleic Acids Res. 35:1919-1932(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=19416963; DOI=10.1074/jbc.m109.006999;
RA Brooks Y.S., Wang G., Yang Z., Smith K.K., Bieberich E., Ko L.;
RT "Functional pre- mRNA trans-splicing of coactivator CoAA and corepressor
RT RBM4 during stem/progenitor cell differentiation.";
RL J. Biol. Chem. 284:18033-18046(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Synovial sarcoma;
RA Antonson P., Goodwin G.;
RT "SIP, a novel protein interacting with SYT.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Leiomyosarcoma, and Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-669.
RC TISSUE=Liver;
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 [11]
RP SUBCELLULAR LOCATION.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP INTERACTION WITH SS18.
RX PubMed=15919756; DOI=10.1210/en.2004-1513;
RA Iwasaki T., Koibuchi N., Chin W.W.;
RT "Synovial sarcoma translocation (SYT) encodes a nuclear receptor
RT coactivator.";
RL Endocrinology 146:3892-3899(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-618, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP IDENTIFICATION BY MASS 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-572, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-206 AND SER-618, 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP 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 [25]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-206; SER-220;
RP SER-242; SER-244; SER-256; SER-272; SER-280; SER-520; SER-523; SER-527;
RP SER-582; SER-618; SER-620; SER-623; SER-627; SER-643 AND SER-649, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP 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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STIL AND
RP GAMMA-TUBULIN.
RX PubMed=25385835; DOI=10.15252/embj.201488979;
RA Shiratsuchi G., Takaoka K., Ashikawa T., Hamada H., Kitagawa D.;
RT "RBM14 prevents assembly of centriolar protein complexes and maintains
RT mitotic spindle integrity.";
RL EMBO J. 34:97-114(2015).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; XRCC6;
RP SFPQ; NONO; PSPC1; HEXIM1 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 [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-135; LYS-138; LYS-149;
RP LYS-153; LYS-164 AND LYS-600, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [32]
RP STRUCTURE BY NMR OF 77-153.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain 2 in RNA-binding protein 14.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Isoform 1 may function as a nuclear receptor coactivator,
CC enhancing transcription through other coactivators such as NCOA6 and
CC CITED1. Isoform 2, functions as a transcriptional repressor, modulating
CC transcriptional activities of coactivators including isoform 1, NCOA6
CC and CITED1 (PubMed:11443112). Regulates centriole biogenesis by
CC suppressing the formation of aberrant centriolar protein complexes in
CC the cytoplasm and thus preserving mitotic spindle integrity. Prevents
CC the formation of the STIL-CENPJ complex (which can induce the formation
CC of aberrant centriolar protein complexes) by interfering with the
CC interaction of STIL with CENPJ (PubMed:25385835). Plays a role in the
CC regulation of DNA virus-mediated innate immune response by assembling
CC into the HDP-RNP complex, a complex that serves as a platform for IRF3
CC phosphorylation and subsequent innate immune response activation
CC through the cGAS-STING pathway (PubMed:28712728).
CC {ECO:0000269|PubMed:11443112, ECO:0000269|PubMed:25385835,
CC ECO:0000269|PubMed:28712728}.
CC -!- SUBUNIT: Isoform 1: Interacts with NCOA6, CITED1 and XRCC5/KU86
CC (PubMed:11443112). Isoform 1: Interacts with SS18 isoform 1
CC (PubMed:15919756). Isoform 1: Interacts with SS18 isoform 2
CC (PubMed:15919756). Interacts with STIL and interferes with its
CC interaction with CENPJ. Interacts with gamma-tubulin
CC (PubMed:25385835).Part of the HDP-RNP complex composed of at least
CC HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1,
CC RBM14, and MATR3) and NEAT1 RNA. {ECO:0000269|PubMed:11443112,
CC ECO:0000269|PubMed:15919756, ECO:0000269|PubMed:25385835,
CC ECO:0000269|PubMed:28712728}.
CC -!- INTERACTION:
CC Q96PK6; Q86V38: ATN1; NbExp=3; IntAct=EBI-954272, EBI-11954292;
CC Q96PK6; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-954272, EBI-2872414;
CC Q96PK6; P28799: GRN; NbExp=3; IntAct=EBI-954272, EBI-747754;
CC Q96PK6; P61978: HNRNPK; NbExp=3; IntAct=EBI-954272, EBI-304185;
CC Q96PK6; P61978-2: HNRNPK; NbExp=4; IntAct=EBI-954272, EBI-7060731;
CC Q96PK6; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-954272, EBI-748420;
CC Q96PK6; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-954272, EBI-742808;
CC Q96PK6; O60333-2: KIF1B; NbExp=3; IntAct=EBI-954272, EBI-10975473;
CC Q96PK6; P07196: NEFL; NbExp=3; IntAct=EBI-954272, EBI-475646;
CC Q96PK6; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-954272, EBI-10271199;
CC Q96PK6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-954272, EBI-396669;
CC Q96PK6; O76024: WFS1; NbExp=3; IntAct=EBI-954272, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25385835}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11790299}. Cytoplasm
CC {ECO:0000269|PubMed:25385835}. Note=In punctate subnuclear structures
CC often located adjacent to splicing speckles, called paraspeckles
CC (PubMed:11790299). Cytoplasmic localization is crucial for its function
CC in suppressing the formation of aberrant centriolar protein complexes
CC (PubMed:25385835). {ECO:0000269|PubMed:11790299,
CC ECO:0000269|PubMed:25385835}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CoAA;
CC IsoId=Q96PK6-1; Sequence=Displayed;
CC Name=2; Synonyms=CoAM;
CC IsoId=Q96PK6-2; Sequence=VSP_015078, VSP_015079;
CC Name=3;
CC IsoId=Q96PK6-3; Sequence=VSP_044641, VSP_044642;
CC Name=4;
CC IsoId=Q96PK6-4; Sequence=VSP_047109, VSP_047110;
CC Name=5;
CC IsoId=Q96PK6-5; Sequence=VSP_047494, VSP_047495;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including brain,
CC heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small
CC intestine, placenta, lung and peripheral blood lymphocytes.
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DR EMBL; AF315632; AAK77961.1; -; mRNA.
DR EMBL; AF315633; AAK77962.1; -; mRNA.
DR EMBL; DQ294957; ABB99396.1; -; mRNA.
DR EMBL; EU287938; ABY74511.1; -; mRNA.
DR EMBL; AF080561; AAC64058.1; -; mRNA.
DR EMBL; AK021768; BAG51046.1; -; mRNA.
DR EMBL; AK222830; BAD96550.1; -; mRNA.
DR EMBL; AP001157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74552.1; -; Genomic_DNA.
DR EMBL; BC000488; AAH00488.1; -; mRNA.
DR EMBL; BE885635; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR749306; CAH18161.1; -; mRNA.
DR CCDS; CCDS55772.1; -. [Q96PK6-2]
DR CCDS; CCDS55773.1; -. [Q96PK6-4]
DR CCDS; CCDS8147.1; -. [Q96PK6-1]
DR RefSeq; NP_001185765.1; NM_001198836.1. [Q96PK6-2]
DR RefSeq; NP_001185766.1; NM_001198837.1. [Q96PK6-4]
DR RefSeq; NP_001185774.1; NM_001198845.1. [Q96PK6-5]
DR RefSeq; NP_006319.1; NM_006328.3. [Q96PK6-1]
DR PDB; 2DNP; NMR; -; A=77-153.
DR PDBsum; 2DNP; -.
DR AlphaFoldDB; Q96PK6; -.
DR SMR; Q96PK6; -.
DR BioGRID; 115700; 339.
DR BioGRID; 1529298; 107.
DR CORUM; Q96PK6; -.
DR DIP; DIP-50126N; -.
DR IntAct; Q96PK6; 119.
DR MINT; Q96PK6; -.
DR STRING; 9606.ENSP00000311747; -.
DR GlyConnect; 2869; 1 O-Linked glycan (4 sites).
DR GlyGen; Q96PK6; 20 sites, 2 O-linked glycans (20 sites).
DR iPTMnet; Q96PK6; -.
DR MetOSite; Q96PK6; -.
DR PhosphoSitePlus; Q96PK6; -.
DR SwissPalm; Q96PK6; -.
DR BioMuta; RBM14; -.
DR DMDM; 73913750; -.
DR EPD; Q96PK6; -.
DR jPOST; Q96PK6; -.
DR MassIVE; Q96PK6; -.
DR MaxQB; Q96PK6; -.
DR PaxDb; Q96PK6; -.
DR PeptideAtlas; Q96PK6; -.
DR PRIDE; Q96PK6; -.
DR ProteomicsDB; 14669; -.
DR ProteomicsDB; 2553; -.
DR ProteomicsDB; 61433; -.
DR ProteomicsDB; 77704; -. [Q96PK6-1]
DR ProteomicsDB; 77705; -. [Q96PK6-2]
DR Antibodypedia; 34813; 230 antibodies from 27 providers.
DR DNASU; 10432; -.
DR Ensembl; ENST00000310137.5; ENSP00000311747.5; ENSG00000239306.5. [Q96PK6-1]
DR Ensembl; ENST00000393979.3; ENSP00000377548.3; ENSG00000239306.5. [Q96PK6-2]
DR Ensembl; ENST00000409738.4; ENSP00000386995.4; ENSG00000239306.5. [Q96PK6-4]
DR GeneID; 100526737; -.
DR GeneID; 10432; -.
DR KEGG; hsa:100526737; -.
DR KEGG; hsa:10432; -.
DR MANE-Select; ENST00000310137.5; ENSP00000311747.5; NM_006328.4; NP_006319.1.
DR UCSC; uc001oit.4; human. [Q96PK6-1]
DR CTD; 100526737; -.
DR CTD; 10432; -.
DR DisGeNET; 100526737; -.
DR DisGeNET; 10432; -.
DR GeneCards; RBM14; -.
DR HGNC; HGNC:14219; RBM14.
DR HPA; ENSG00000239306; Low tissue specificity.
DR MIM; 612409; gene.
DR neXtProt; NX_Q96PK6; -.
DR OpenTargets; ENSG00000239306; -.
DR OpenTargets; ENSG00000248643; -.
DR PharmGKB; PA34263; -.
DR VEuPathDB; HostDB:ENSG00000239306; -.
DR eggNOG; ENOG502R6FF; Eukaryota.
DR GeneTree; ENSGT00940000154421; -.
DR GeneTree; ENSGT00940000157436; -.
DR HOGENOM; CLU_473775_0_0_1; -.
DR InParanoid; Q96PK6; -.
DR OMA; NPAMASH; -.
DR PhylomeDB; Q96PK6; -.
DR TreeFam; TF320661; -.
DR PathwayCommons; Q96PK6; -.
DR Reactome; R-HSA-8941326; RUNX2 regulates bone development.
DR SignaLink; Q96PK6; -.
DR BioGRID-ORCS; 100526737; 80 hits in 282 CRISPR screens.
DR BioGRID-ORCS; 10432; 769 hits in 1049 CRISPR screens.
DR ChiTaRS; RBM14; human.
DR EvolutionaryTrace; Q96PK6; -.
DR GeneWiki; RBM14; -.
DR Pharos; Q96PK6; Tbio.
DR PRO; PR:Q96PK6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96PK6; protein.
DR Bgee; ENSG00000239306; Expressed in right uterine tube and 156 other tissues.
DR ExpressionAtlas; Q96PK6; baseline and differential.
DR Genevisible; Q96PK6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; TAS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IPI:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0046600; P:negative regulation of centriole replication; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0009725; P:response to hormone; TAS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR CDD; cd12608; RRM1_CoAA; 1.
DR CDD; cd12609; RRM2_CoAA; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034506; RBM14_RRM1.
DR InterPro; IPR034507; RBM14_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Immunity;
KW Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..669
FT /note="RNA-binding protein 14"
FT /id="PRO_0000081774"
FT DOMAIN 1..73
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 79..149
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 147..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..354
FT /note="TRBP-interacting domain; interaction with STIL"
FT /evidence="ECO:0000269|PubMed:25385835"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 164
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C2Q3"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 112..339
FT /note="KDYAFVHMEKEADAKAAIAQLNGKEVKGKRINVELSTKGQKKGPGLAVQSGD
FT KTKKPGAGDTAFPGTGGFSATFDYQQAFGNSTGGFDGQARQPTPPFFGRDRSPLRRSPP
FT RASYVAPLTAQPATYRAQPSVSLGAAYRAQPSASLGVGYRTQPMTAQAASYRAQPSVSL
FT GAPYRGQLASPSSQSAAASSLGPYGGAQPSASALSSYGGQAAAASSLNSYGAQGSSLA
FT -> KGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPIDRSGRVADLTEQYNE
FT QYGAVRTPYTMSYGDSLYYNNAYGALDAYYKRCRAARSYEAVAAAAASVYNYAEQTLSQ
FT LPQVQNTAMASHLTSTSLDPYDRHLLPTSGAAATAAAAAAAAAAVTAASTSYYGRDRSP
FT LRRATAPVPTVGEGYGYGHESELSQASAAARNSLYDMARYEREQYADRARYSAF (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:19416963"
FT /id="VSP_047494"
FT VAR_SEQ 113..119
FT /note="DYAFVHM -> GMVPTGV (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047109"
FT VAR_SEQ 113..118
FT /note="DYAFVH -> GGMCVG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17337438"
FT /id="VSP_044641"
FT VAR_SEQ 119..669
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17337438"
FT /id="VSP_044642"
FT VAR_SEQ 120..669
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047110"
FT VAR_SEQ 151..156
FT /note="QKKGPG -> MVPTGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11443112"
FT /id="VSP_015078"
FT VAR_SEQ 157..669
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11443112"
FT /id="VSP_015079"
FT VAR_SEQ 340..669
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:19416963"
FT /id="VSP_047495"
FT CONFLICT 560
FT /note="S -> T (in Ref. 1; AAK77961)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="A -> V (in Ref. 6; BAD96550)"
FT /evidence="ECO:0000305"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2DNP"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:2DNP"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2DNP"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2DNP"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:2DNP"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2DNP"
SQ SEQUENCE 669 AA; 69492 MW; 565C5EF51B6881FD CRC64;
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGALR AIEALHGHEL
RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME
KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPGLAVQ SGDKTKKPGA GDTAFPGTGG
FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ
PSVSLGAAYR AQPSASLGVG YRTQPMTAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS
SLGPYGGAQP SASALSSYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA
AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYNAQPSASY NAQSAPYAAQ
QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASM
GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY
RGQPGNAYDG AGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ
MHSGYQRRM
