RBM14_MOUSE
ID RBM14_MOUSE Reviewed; 669 AA.
AC Q8C2Q3; Q3TJB6; Q91Z21; Q9DBI6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RNA-binding protein 14;
DE AltName: Full=RNA-binding motif protein 14;
GN Name=Rbm14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206 AND SER-618, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP FUNCTION.
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).
CC -!- FUNCTION: May function as a nuclear receptor coactivator, enhancing
CC transcription through other coactivators such as NCOA6 and CITED1 (By
CC similarity). Regulates centriole biogenesis by suppressing the
CC formation of aberrant centriolar protein complexes in the cytoplasm and
CC thus preserving mitotic spindle integrity (PubMed:25385835). 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 (By similarity). 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. {ECO:0000250|UniProtKB:Q96PK6,
CC ECO:0000269|PubMed:25385835}.
CC -!- SUBUNIT: Interacts with NCOA6, CITED1 and XRCC5/KU86. Interacts with
CC SS18. Interacts with STIL and interferes with its interaction with
CC CENPJ. Interacts with gamma-tubulin. 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:Q96PK6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PK6}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q96PK6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96PK6}. Note=In punctate subnuclear structures
CC often located adjacent to splicing speckles, called paraspeckles.
CC Cytoplasmic localization is crucial for its function in suppressing the
CC formation of aberrant centriolar protein complexes.
CC {ECO:0000250|UniProtKB:Q96PK6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C2Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C2Q3-2; Sequence=VSP_015080;
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DR EMBL; AK004928; BAB23678.1; -; mRNA.
DR EMBL; AK088201; BAC40206.1; -; mRNA.
DR EMBL; AK167503; BAE39579.1; -; mRNA.
DR EMBL; BC010294; AAH10294.1; -; mRNA.
DR CCDS; CCDS29437.1; -. [Q8C2Q3-1]
DR RefSeq; NP_063922.2; NM_019869.3. [Q8C2Q3-1]
DR AlphaFoldDB; Q8C2Q3; -.
DR SMR; Q8C2Q3; -.
DR BioGRID; 207870; 114.
DR DIP; DIP-58946N; -.
DR IntAct; Q8C2Q3; 9.
DR MINT; Q8C2Q3; -.
DR STRING; 10090.ENSMUSP00000006625; -.
DR iPTMnet; Q8C2Q3; -.
DR PhosphoSitePlus; Q8C2Q3; -.
DR EPD; Q8C2Q3; -.
DR jPOST; Q8C2Q3; -.
DR MaxQB; Q8C2Q3; -.
DR PaxDb; Q8C2Q3; -.
DR PeptideAtlas; Q8C2Q3; -.
DR PRIDE; Q8C2Q3; -.
DR ProteomicsDB; 254998; -. [Q8C2Q3-1]
DR ProteomicsDB; 254999; -. [Q8C2Q3-2]
DR Antibodypedia; 34813; 230 antibodies from 27 providers.
DR DNASU; 56275; -.
DR Ensembl; ENSMUST00000006625; ENSMUSP00000006625; ENSMUSG00000006456. [Q8C2Q3-1]
DR GeneID; 56275; -.
DR KEGG; mmu:56275; -.
DR UCSC; uc008gaz.2; mouse. [Q8C2Q3-1]
DR CTD; 10432; -.
DR MGI; MGI:1929092; Rbm14.
DR VEuPathDB; HostDB:ENSMUSG00000006456; -.
DR eggNOG; ENOG502R6FF; Eukaryota.
DR GeneTree; ENSGT00940000157436; -.
DR HOGENOM; CLU_473775_0_0_1; -.
DR InParanoid; Q8C2Q3; -.
DR OMA; YRHSPTK; -.
DR OrthoDB; 1563362at2759; -.
DR PhylomeDB; Q8C2Q3; -.
DR TreeFam; TF320661; -.
DR Reactome; R-MMU-8941326; RUNX2 regulates bone development.
DR BioGRID-ORCS; 56275; 24 hits in 78 CRISPR screens.
DR PRO; PR:Q8C2Q3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C2Q3; protein.
DR Bgee; ENSMUSG00000006456; Expressed in internal carotid artery and 262 other tissues.
DR ExpressionAtlas; Q8C2Q3; baseline and differential.
DR Genevisible; Q8C2Q3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; IEA:Ensembl.
DR GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; ISS: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; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
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 Acetylation; Alternative splicing; Cytoplasm; Immunity; Innate immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..669
FT /note="RNA-binding protein 14"
FT /id="PRO_0000081775"
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 148..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 307..354
FT /note="TRBP-interacting domain; interaction with STIL"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 164
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT CROSSLNK 600
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96PK6"
FT VAR_SEQ 603..669
FT /note="GSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHSDYARYSGSYND
FT YLRAAQMHSGYQRRM -> CMPPRLSPQLGLRARG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015080"
FT CONFLICT 124
FT /note="D -> Y (in Ref. 1; BAB23678)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="E -> G (in Ref. 1; BAB23678)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> F (in Ref. 1; BAB23678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 69449 MW; 5B913852B06C87FA CRC64;
MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGAVR AIEALHGHEL
RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME
KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPALAIQ SGDKTKKPGA GDTAFPGTGG
FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ
PSVSLGAAYR AQPSASLGVG YRTQPMAAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS
SLGPYGGVQP SASALSTYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA
AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYSAQPSASY SAQSAPYAAQ
QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASI
GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY
RGQPGSAYDG TGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK
RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ
MHSGYQRRM
