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   27-MAR-2024, entry version 203.
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   FUNCTION, AND INTERACTION WITH RBPMS.
RX   PubMed=37548402; DOI=10.1093/nar/gkad652;
RA   Yang Y., Lee G.C., Nakagaki-Silva E., Huang Y., Peacey M., Partridge R.,
RA   Gooding C., Smith C.W.J.;
RT   "Cell-type specific regulator RBPMS switches alternative splicing via
RT   higher-order oligomerization and heterotypic interactions with other
RT   splicing regulators.";
RL   Nucleic Acids Res. 0:0-0(2023).
RN   [33]
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). Also involved in the
CC       regulation of pre-mRNA alternative splicing (PubMed:37548402).
CC       {ECO:0000269|PubMed:11443112, ECO:0000269|PubMed:25385835,
CC       ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:37548402}.
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 (PubMed:25385835).
CC       Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5,
CC       XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and
CC       NEAT1 RNA. Interacts with RBPMS; the interaction allows cooperative
CC       assembly of RNA-bound stable cell-specific alternative splicing
CC       regulatory complexes (PubMed:37548402). {ECO:0000269|PubMed:11443112,
CC       ECO:0000269|PubMed:15919756, ECO:0000269|PubMed:25385835,
CC       ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:37548402}.
CC   -!- INTERACTION:
CC       Q96PK6; Q86V38: ATN1; NbExp=3; IntAct=EBI-954272, EBI-11954292;
CC       Q96PK6; P13569: CFTR; NbExp=13; IntAct=EBI-954272, EBI-349854;
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; Q8IUH3: RBM45; NbExp=4; IntAct=EBI-954272, EBI-2512147;
CC       Q96PK6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-954272, EBI-396669;
CC       Q96PK6; O76024: WFS1; NbExp=3; IntAct=EBI-954272, EBI-720609;
CC       Q96PK6; PRO_0000449619 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-954272, EBI-25475847;
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; 525.
DR   BioGRID; 1529298; 108.
DR   CORUM; Q96PK6; -.
DR   DIP; DIP-50126N; -.
DR   IntAct; Q96PK6; 148.
DR   MINT; Q96PK6; -.
DR   STRING; 9606.ENSP00000311747; -.
DR   GlyConnect; 2869; 1 O-GlcNAc glycan (4 sites).
DR   GlyCosmos; Q96PK6; 20 sites, 2 glycans.
DR   GlyGen; Q96PK6; 24 sites, 2 O-linked glycans (24 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; 9606-ENSP00000311747; -.
DR   PeptideAtlas; Q96PK6; -.
DR   ProteomicsDB; 14669; -.
DR   ProteomicsDB; 2553; -.
DR   ProteomicsDB; 61433; -.
DR   ProteomicsDB; 77704; -. [Q96PK6-1]
DR   ProteomicsDB; 77705; -. [Q96PK6-2]
DR   Pumba; Q96PK6; -.
DR   Antibodypedia; 34813; 253 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   AGR; HGNC:14219; -.
DR   AGR; HGNC:38840; -.
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; ENSGT00940000157436; -.
DR   HOGENOM; CLU_473775_0_0_1; -.
DR   InParanoid; Q96PK6; -.
DR   OrthoDB; 76105at2759; -.
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; 81 hits in 332 CRISPR screens.
DR   BioGRID-ORCS; 10432; 792 hits in 1137 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q96PK6; baseline and differential.
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; IEA:Ensembl.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:1990935; F:splicing factor binding; IEA:Ensembl.
DR   GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR   GO; GO:0007369; P:gastrulation; IEA:Ensembl.
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:1902151; P:regulation of response to DNA integrity checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; TAS:UniProtKB.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IPI:UniProtKB.
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   PANTHER; PTHR48025; OS02G0815200 PROTEIN; 1.
DR   PANTHER; PTHR48025:SF21; RNA-BINDING PROTEIN 14; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   Genevisible; Q96PK6; HS.
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
//