ID QKI_HUMAN Reviewed; 341 AA. AC Q96PU8; Q2I375; Q5MJQ1; Q969L9; Q96EJ3; Q96KA3; Q96PU6; Q96PU7; Q9P0X6; AC Q9P0X7; Q9P0X8; Q9P0X9; Q9P0Y0; Q9P0Y1; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 183. DE RecName: Full=KH domain-containing RNA-binding protein QKI {ECO:0000305}; DE AltName: Full=Protein quaking {ECO:0000303|PubMed:11856480}; DE Short=Hqk {ECO:0000303|PubMed:11856480}; DE Short=HqkI; GN Name=QKI {ECO:0000303|PubMed:16342280, ECO:0000312|HGNC:HGNC:21100}; GN Synonyms=HKQ {ECO:0000303|PubMed:11856480}; 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 [GENOMIC DNA / MRNA] (ISOFORMS QKI5; QKI7 AND QKI7B). RC TISSUE=Brain; RX PubMed=11856480; DOI=10.1111/j.1349-7006.2002.tb01255.x; RA Li Z.Z., Kondo T., Murata T., Ebersole T.A., Nishi T., Tada K., Ushio Y., RA Yamamura K., Abe K.; RT "Expression of Hqk encoding a KH RNA binding protein is altered in human RT glioma."; RL Jpn. J. Cancer Res. 93:167-177(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS QKI5 AND QKI7), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 5-341 (ISOFORM QKI6). RA Xia J.-H., Xiao J.-F., He Y.-G., Yu K.-P., Pan Q., Dai H.-P.; RT "Molecular cloning of human QUAKING gene."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 5-341 (ISOFORM 3). RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Liang M., Tang Z., RA Huang B., Lin L., Yang S.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM QKI5). RC TISSUE=Placenta, and 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 15-341 (ISOFORM QKI5). 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 [7] RP METHYLATION. RX PubMed=12529443; DOI=10.1091/mbc.e02-08-0484; RA Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.; RT "Sam68 RNA binding protein is an in vivo substrate for protein arginine N- RT methyltransferase 1."; RL Mol. Biol. Cell 14:274-287(2003). RN [8] RP TISSUE SPECIFICITY. RX PubMed=16342280; DOI=10.1002/ajmg.b.30243; RA Aeberg K., Saetre P., Lindholm E., Ekholm B., Pettersson U., Adolfsson R., RA Jazin E.; RT "Human QKI, a new candidate gene for schizophrenia involved in RT myelination."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 141:84-90(2006). RN [9] RP FUNCTION AS REGULATOR OF OLIGODENDROCYTE DIFFERENTIATION. RX PubMed=16641098; DOI=10.1073/pnas.0601213103; RA Aberg K., Saetre P., Jareborg N., Jazin E.; RT "Human QKI, a potential regulator of mRNA expression of human RT oligodendrocyte-related genes involved in schizophrenia."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7482-7487(2006). RN [10] 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 [11] RP FUNCTION (ISOFORM QKI5), AND INDUCTION (ISOFORM QKI5). RX PubMed=22398723; DOI=10.1091/mbc.e11-05-0412; RA Fu H., Yang G., Wei M., Liu L., Jin L., Lu X., Wang L., Shen L., Zhang J., RA Lu H., Yao L., Lu Z.; RT "The RNA-binding protein QKI5 is a direct target of C/EBPalpha and delays RT macrophage differentiation."; RL Mol. Biol. Cell 23:1628-1635(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, 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 [13] RP METHYLATION AT ARG-242 BY CARM1. RX PubMed=23455924; DOI=10.1038/nmeth.2397; RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D., RA Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.; RT "A Y2H-seq approach defines the human protein methyltransferase RT interactome."; RL Nat. Methods 10:339-342(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-227 AND ARG-242, AND RP IDENTIFICATION BY MASS 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 (ISOFORM QKI5). RX PubMed=25768908; DOI=10.1016/j.cell.2015.02.014; RA Conn S.J., Pillman K.A., Toubia J., Conn V.M., Salmanidis M., RA Phillips C.A., Roslan S., Schreiber A.W., Gregory P.A., Goodall G.J.; RT "The RNA binding protein quaking regulates formation of circRNAs."; RL Cell 160:1125-1134(2015). RN [17] RP FUNCTION. RX PubMed=27029405; DOI=10.1038/ncomms10846; RA de Bruin R.G., Shiue L., Prins J., de Boer H.C., Singh A., Fagg W.S., RA van Gils J.M., Duijs J.M., Katzman S., Kraaijeveld A.O., Boehringer S., RA Leung W.Y., Kielbasa S.M., Donahue J.P., van der Zande P.H., Sijbom R., RA van Alem C.M., Bot I., van Kooten C., Jukema J.W., Van Esch H., RA Rabelink T.J., Kazan H., Biessen E.A., Ares M. Jr., van Zonneveld A.J., RA van der Veer E.P.; RT "Quaking promotes monocyte differentiation into pro-atherogenic macrophages RT by controlling pre-mRNA splicing and gene expression."; RL Nat. Commun. 7:10846-10846(2016). RN [18] RP FUNCTION. RX PubMed=31331967; DOI=10.1242/jcs.230276; RA Caines R., Cochrane A., Kelaini S., Vila-Gonzalez M., Yang C., RA Eleftheriadou M., Moez A., Stitt A.W., Zeng L., Grieve D.J., Margariti A.; RT "The RNA-binding protein QKI controls alternative splicing in vascular RT cells, producing an effective model for therapy."; RL J. Cell Sci. 132:0-0(2019). RN [19] RP FUNCTION (ISOFORM QKI7), AND INTERACTION WITH TENT2 (ISOFORM QKI7). RX PubMed=31792053; DOI=10.1074/jbc.ra119.011617; RA Hojo H., Yashiro Y., Noda Y., Ogami K., Yamagishi R., Okada S., RA Hoshino S.I., Suzuki T.; RT "The RNA-binding protein QKI-7 recruits the poly(A) polymerase GLD-2 for 3' RT adenylation and selective stabilization of microRNA-122."; RL J. Biol. Chem. 295:390-402(2020). RN [20] RP FUNCTION (ISOFORM QKI7). RX PubMed=32732889; DOI=10.1038/s41467-020-17468-y; RA Yang C., Eleftheriadou M., Kelaini S., Morrison T., Gonzalez M.V., RA Caines R., Edwards N., Yacoub A., Edgar K., Moez A., Ivetic A., RA Zampetaki A., Zeng L., Wilkinson F.L., Lois N., Stitt A.W., Grieve D.J., RA Margariti A.; RT "Targeting QKI-7 in vivo restores endothelial cell function in diabetes."; RL Nat. Commun. 11:3812-3812(2020). RN [21] RP FUNCTION (ISOFORM QKI5). RX PubMed=31829086; DOI=10.1080/15476286.2019.1703069; RA Liao K.C., Chuo V., Fagg W.S., Bradrick S.S., Pompon J., RA Garcia-Blanco M.A.; RT "The RNA binding protein Quaking represses host interferon response by RT downregulating MAVS."; RL RNA Biol. 17:366-380(2020). RN [22] RP FUNCTION. RX PubMed=34428287; DOI=10.1093/nar/gkab732; RA Liao K.C., Chuo V., Fagg W.S., Modahl C.M., Widen S., Garcia-Blanco M.A.; RT "The RNA binding protein Quaking represses splicing of the Fibronectin EDA RT exon and downregulates the interferon response."; RL Nucleic Acids Res. 49:10034-10045(2021). RN [23] RP FUNCTION (ISOFORMS QKI6 AND QKI7), SUBCELLULAR LOCATION (ISOFORMS QKI5; RP QKI6 AND QKI7), AND INTERACTION WITH G3BP1 (ISOFORM QKI7). RX PubMed=37379838; DOI=10.1016/j.cell.2023.05.047; RA Zhao Z., Qing Y., Dong L., Han L., Wu D., Li Y., Li W., Xue J., Zhou K., RA Sun M., Tan B., Chen Z., Shen C., Gao L., Small A., Wang K., Leung K., RA Zhang Z., Qin X., Deng X., Xia Q., Su R., Chen J.; RT "QKI shuttles internal m7G-modified transcripts into stress granules and RT modulates mRNA metabolism."; RL Cell 0:0-0(2023). RN [24] RP VARIANT [LARGE SCALE ANALYSIS] GLN-336. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [25] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 7-204 IN COMPLEX WITH RNA, RP RNA-BINDING, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASN-97; LYS-120; RP ARG-124; ARG-130; LYS-190 AND GLN-193. RX PubMed=23630077; DOI=10.1101/gad.216531.113; RA Teplova M., Hafner M., Teplov D., Essig K., Tuschl T., Patel D.J.; RT "Structure-function studies of STAR family Quaking proteins bound to their RT in vivo RNA target sites."; RL Genes Dev. 27:928-940(2013). CC -!- FUNCTION: RNA reader protein, which recognizes and binds specific RNAs, CC thereby regulating RNA metabolic processes, such as pre-mRNA splicing, CC circular RNA (circRNA) formation, mRNA export, mRNA stability and/or CC translation (PubMed:22398723, PubMed:25768908, PubMed:27029405, CC PubMed:31331967, PubMed:23630077, PubMed:37379838). Involved in various CC cellular processes, such as mRNA storage into stress granules, CC apoptosis, lipid deposition, interferon response, glial cell fate and CC development (PubMed:25768908, PubMed:31829086, PubMed:34428287, CC PubMed:37379838). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core CC sequence (PubMed:23630077). Acts as a mRNA modification reader that CC specifically recognizes and binds mRNA transcripts modified by internal CC N(7)-methylguanine (m7G) (PubMed:37379838). Promotes the formation of CC circular RNAs (circRNAs) during the epithelial to mesenchymal CC transition and in cardiomyocytes: acts by binding to sites flanking CC circRNA-forming exons (PubMed:25768908). CircRNAs are produced by back- CC splicing circularization of pre-mRNAs (PubMed:25768908). Plays a CC central role in myelinization via 3 distinct mechanisms CC (PubMed:16641098). First, acts by protecting and promoting stability of CC target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes CC oligodendrocyte differentiation (By similarity). Second, participates CC in mRNA transport by regulating the nuclear export of MBP mRNA (By CC similarity). Finally, indirectly regulates mRNA splicing of MAG pre- CC mRNA during oligodendrocyte differentiation by acting as a negative CC regulator of MAG exon 12 alternative splicing: acts by binding to CC HNRNPA1 mRNA splicing factor, preventing its translation (By CC similarity). Involved in microglia differentiation and remyelination by CC regulating microexon alternative splicing of the Rho GTPase pathway (By CC similarity). Involved in macrophage differentiation: promotes monocyte CC differentiation by regulating pre-mRNA splicing in naive peripheral CC blood monocytes (PubMed:27029405). Acts as an important regulator of CC muscle development: required for the contractile function of CC cardiomyocytes by regulating alternative splicing of cardiomyocyte CC transcripts (By similarity). Acts as a negative regulator of CC thermogenesis by decreasing stability, nuclear export and translation CC of mRNAs encoding PPARGC1A and UCP1 (By similarity). Also required for CC visceral endoderm function and blood vessel development (By CC similarity). May also play a role in smooth muscle development CC (PubMed:31331967). In addition to its RNA-binding activity, also acts CC as a nuclear transcription coactivator for SREBF2/SREBP2 (By CC similarity). {ECO:0000250|UniProtKB:Q9QYS9, CC ECO:0000269|PubMed:16641098, ECO:0000269|PubMed:22398723, CC ECO:0000269|PubMed:23630077, ECO:0000269|PubMed:25768908, CC ECO:0000269|PubMed:27029405, ECO:0000269|PubMed:31331967, CC ECO:0000269|PubMed:31829086, ECO:0000269|PubMed:34428287, CC ECO:0000269|PubMed:37379838}. CC -!- FUNCTION: [Isoform QKI5]: Nuclear isoform that acts as an indirect CC regulator of mRNA splicing (By similarity). Regulates mRNA splicing of CC MAG pre-mRNA by inhibiting translation of HNRNPA1 mRNA, thereby CC preventing MAG exon 12 alternative splicing (By similarity). Involved CC in oligodendrocyte differentiation by promoting stabilization of SIRT2 CC mRNA (By similarity). Acts as a negative regulator of the interferon CC response by binding to MAVS mRNA, downregulating its expression CC (PubMed:31829086). Also inhibits the interferon response by binding to CC fibrinectin FN1 pre-mRNA, repressing EDA exon inclusion in FN1 CC (PubMed:34428287). Delays macrophage differentiation by binding to CC CSF1R mRNA, promoting its degradation (PubMed:22398723). In addition to CC its RNA-binding activity, also acts as a nuclear transcription CC coactivator for SREBF2/SREBP2, promoting SREBF2/SREBP2-dependent CC cholesterol biosynthesis (By similarity). SREBF2/SREBP2-dependent CC cholesterol biosynthesis participates to myelinization and is required CC for eye lens transparency (By similarity). CC {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:22398723, CC ECO:0000269|PubMed:31829086, ECO:0000269|PubMed:34428287}. CC -!- FUNCTION: [Isoform QKI6]: Cytosolic isoform that specifically CC recognizes and binds mRNA transcripts modified by internal N(7)- CC methylguanine (m7G) (PubMed:37379838). Interaction with G3BP1 promotes CC localization of m7G-containing mRNAs into stress granules in response CC to stress, thereby suppressing their translation (PubMed:37379838). CC Acts as a translational repressor for HNRNPA1 and GLI1 (By similarity). CC Translation inhibition of HNRNPA1 during oligodendrocyte CC differentiation prevents inclusion of exon 12 in MAG pre-mRNA splicing CC (By similarity). Involved in astrocyte differentiation by regulating CC translation of target mRNAs (By similarity). CC {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:37379838}. CC -!- FUNCTION: [Isoform QKI7]: Cytosolic isoform that specifically CC recognizes and binds mRNA transcripts modified by internal N(7)- CC methylguanine (m7G) (PubMed:37379838). Interaction with G3BP1 promotes CC localization of m7G-containing mRNAs into stress granules in response CC to stress, thereby suppressing their translation (PubMed:37379838). CC Acts as a negative regulator of angiogenesis by binding to mRNAs CC encoding CDH5, NLGN1 and TNFAIP6, promoting their degradation CC (PubMed:32732889). Can also induce apoptosis in the cytoplasm (By CC similarity). Heterodimerization with other isoforms results in nuclear CC translocation of isoform QKI7 and suppression of apoptosis (By CC similarity). Also binds some microRNAs: promotes stabilitation of miR- CC 122 by mediating recruitment of poly(A) RNA polymerase TENT2, leading CC to 3' adenylation and stabilization of miR-122 (PubMed:31792053). CC {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:31792053, CC ECO:0000269|PubMed:32732889, ECO:0000269|PubMed:37379838}. CC -!- SUBUNIT: Homodimer; does not require RNA to homodimerize CC (PubMed:23630077). Able to heterodimerize with BICC1 (By similarity). CC {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:23630077}. CC -!- SUBUNIT: [Isoform QKI6]: Interacts with G3BP1; directing N(7)- CC methylguanine (m7G)-containing mRNAs to stress granules to suppress CC mRNA translation. {ECO:0000269|PubMed:37379838}. CC -!- SUBUNIT: [Isoform QKI7]: Interacts with G3BP1; directing N(7)- CC methylguanine (m7G)-containing mRNAs to stress granules to suppress CC mRNA translation (PubMed:37379838). Interacts with TENT2; promoting CC stabilization of miR-122 (PubMed:31792053). CC {ECO:0000269|PubMed:31792053, ECO:0000269|PubMed:37379838}. CC -!- INTERACTION: CC Q96PU8; Q86X55: CARM1; NbExp=2; IntAct=EBI-945792, EBI-2339854; CC Q96PU8; Q96I24: FUBP3; NbExp=4; IntAct=EBI-945792, EBI-954200; CC Q96PU8; P61978: HNRNPK; NbExp=7; IntAct=EBI-945792, EBI-304185; CC Q96PU8; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-945792, EBI-7060731; CC Q96PU8; Q8WVV9: HNRNPLL; NbExp=3; IntAct=EBI-945792, EBI-535849; CC Q96PU8; Q9UDY8: MALT1; NbExp=2; IntAct=EBI-945792, EBI-1047372; CC Q96PU8; Q96AH0: NABP1; NbExp=3; IntAct=EBI-945792, EBI-2889252; CC Q96PU8; Q96CV9: OPTN; NbExp=3; IntAct=EBI-945792, EBI-748974; CC Q96PU8; Q15365: PCBP1; NbExp=2; IntAct=EBI-945792, EBI-946095; CC Q96PU8; O43741: PRKAB2; NbExp=3; IntAct=EBI-945792, EBI-1053424; CC Q96PU8; P26599: PTBP1; NbExp=3; IntAct=EBI-945792, EBI-350540; CC Q96PU8; Q9NWB1: RBFOX1; NbExp=2; IntAct=EBI-945792, EBI-945906; CC Q96PU8; O43251: RBFOX2; NbExp=3; IntAct=EBI-945792, EBI-746056; CC Q96PU8; P57052: RBM11; NbExp=3; IntAct=EBI-945792, EBI-741332; CC Q96PU8; Q93062: RBPMS; NbExp=5; IntAct=EBI-945792, EBI-740322; CC Q96PU8; P09012: SNRPA; NbExp=3; IntAct=EBI-945792, EBI-607085; CC Q96PU8; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-945792, EBI-11064654; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37379838}. Cytoplasm CC {ECO:0000269|PubMed:37379838}. CC -!- SUBCELLULAR LOCATION: [Isoform QKI5]: Nucleus CC {ECO:0000269|PubMed:37379838}. Cytoplasm {ECO:0000269|PubMed:37379838}. CC Note=Localizes predominantly in the nucleus and at lower levels in CC cytoplasm (PubMed:37379838). It shuttles between the cytoplasm and the CC nucleus (By similarity). {ECO:0000250|UniProtKB:Q9QYS9, CC ECO:0000269|PubMed:37379838}. CC -!- SUBCELLULAR LOCATION: [Isoform QKI6]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:37379838}. Nucleus {ECO:0000269|PubMed:37379838}. CC Note=Localizes predominantly in the cytoplasm and at lower levels in CC nucleus. {ECO:0000269|PubMed:37379838}. CC -!- SUBCELLULAR LOCATION: [Isoform QKI7]: Cytoplasm, cytosol CC {ECO:0000269|PubMed:37379838}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:37379838}. Nucleus {ECO:0000269|PubMed:37379838}. CC Note=Localizes predominantly in the cytoplasm and at much lower levels CC in nucleus (PubMed:37379838). Shuttles between the cytosol and stress CC granules in response to stress (PubMed:37379838). CC {ECO:0000269|PubMed:37379838}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=QKI5 {ECO:0000303|PubMed:37379838}; Synonyms=HQK-5, QKI-5; CC IsoId=Q96PU8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96PU8-3; Sequence=VSP_019188; CC Name=3; CC IsoId=Q96PU8-5; Sequence=VSP_019188, VSP_019190; CC Name=QKI7 {ECO:0000303|PubMed:37379838}; Synonyms=HQK-7, QKI-7 CC {ECO:0000303|PubMed:32732889}; CC IsoId=Q96PU8-6; Sequence=VSP_019190; CC Name=QKI7B; Synonyms=HQK-7B; CC IsoId=Q96PU8-8; Sequence=VSP_019191; CC Name=QKI6 {ECO:0000303|PubMed:37379838}; Synonyms=QKI-6 CC {ECO:0000303|PubMed:31331967}; CC IsoId=Q96PU8-9; Sequence=VSP_019189; CC -!- TISSUE SPECIFICITY: Expressed in the frontal cortex of brain. Down- CC regulated in the brain of schizophrenic patients. CC {ECO:0000269|PubMed:16342280}. CC -!- INDUCTION: [Isoform QKI5]: Expression is activated by CEBPA furing CC macrophage differentiation. {ECO:0000269|PubMed:22398723}. CC -!- DOMAIN: The KH domain and the Qua2 region are involved in RNA binding. CC {ECO:0000269|PubMed:23630077}. CC -!- PTM: Methylated by PRMT1. {ECO:0000250|UniProtKB:Q9QYS9}. CC -!- PTM: Tyrosine phosphorylated at its C-terminus, probably by FYN. CC Phosphorylation leads to decreased mRNA-binding affinity, affecting CC transport and/or stabilization of MBP mRNA (By similarity). CC {ECO:0000250|UniProtKB:Q9QYS9}. CC -!- PTM: Ubiquitinated by RNF6 in macrophages, leading to its degradation. CC {ECO:0000250|UniProtKB:Q9QYS9}. CC -!- SIMILARITY: Belongs to the quaking family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF63412.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; CC Sequence=AAF63413.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63413.1; Type=Miscellaneous discrepancy; Note=Cloning artifact in N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63414.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63414.1; Type=Miscellaneous discrepancy; Note=Cloning artifact in N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63415.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; CC Sequence=AAF63416.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305}; CC Sequence=AAF63417.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63417.1; Type=Miscellaneous discrepancy; Note=Cloning artifact in N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB067798; BAB69496.1; -; mRNA. DR EMBL; AB067799; BAB69497.1; -; mRNA. DR EMBL; AB067800; BAB69498.1; -; mRNA. DR EMBL; AB067801; BAB69499.1; -; mRNA. DR EMBL; AB067808; BAB69681.1; -; Genomic_DNA. DR EMBL; AF142417; AAF63412.1; ALT_SEQ; mRNA. DR EMBL; AF142418; AAF63413.1; ALT_SEQ; mRNA. DR EMBL; AF142419; AAF63414.1; ALT_SEQ; mRNA. DR EMBL; AF142420; AAF63415.1; ALT_SEQ; mRNA. DR EMBL; AF142421; AAF63416.1; ALT_SEQ; mRNA. DR EMBL; AF142422; AAF63417.1; ALT_SEQ; mRNA. DR EMBL; AY780788; AAV98358.1; -; mRNA. DR EMBL; DQ323998; ABC88600.1; -; mRNA. DR EMBL; AL356119; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031781; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012222; AAH12222.1; -; mRNA. DR EMBL; BC019917; AAH19917.1; -; mRNA. DR EMBL; AK027309; BAB55032.1; ALT_INIT; mRNA. DR CCDS; CCDS43525.1; -. [Q96PU8-8] DR CCDS; CCDS5285.1; -. [Q96PU8-1] DR CCDS; CCDS5286.1; -. [Q96PU8-9] DR CCDS; CCDS5287.1; -. [Q96PU8-6] DR CCDS; CCDS75546.1; -. [Q96PU8-3] DR RefSeq; NP_001288014.1; NM_001301085.1. [Q96PU8-3] DR RefSeq; NP_006766.1; NM_006775.2. [Q96PU8-1] DR RefSeq; NP_996735.1; NM_206853.2. [Q96PU8-9] DR RefSeq; NP_996736.1; NM_206854.2. [Q96PU8-6] DR RefSeq; NP_996737.1; NM_206855.2. [Q96PU8-8] DR RefSeq; XP_011534561.1; XM_011536259.2. DR PDB; 4JVH; X-ray; 3.50 A; A=7-214. DR PDBsum; 4JVH; -. DR AlphaFoldDB; Q96PU8; -. DR SMR; Q96PU8; -. DR BioGRID; 114834; 195. DR IntAct; Q96PU8; 70. DR MINT; Q96PU8; -. DR STRING; 9606.ENSP00000355094; -. DR GlyCosmos; Q96PU8; 1 site, 1 glycan. DR GlyGen; Q96PU8; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q96PU8; -. DR PhosphoSitePlus; Q96PU8; -. DR SwissPalm; Q96PU8; -. DR BioMuta; QKI; -. DR DMDM; 74761039; -. DR EPD; Q96PU8; -. DR jPOST; Q96PU8; -. DR MassIVE; Q96PU8; -. DR MaxQB; Q96PU8; -. DR PaxDb; 9606-ENSP00000355094; -. DR PeptideAtlas; Q96PU8; -. DR ProteomicsDB; 77761; -. [Q96PU8-1] DR ProteomicsDB; 77762; -. [Q96PU8-3] DR ProteomicsDB; 77763; -. [Q96PU8-5] DR ProteomicsDB; 77764; -. [Q96PU8-6] DR ProteomicsDB; 77765; -. [Q96PU8-8] DR ProteomicsDB; 77766; -. [Q96PU8-9] DR Pumba; Q96PU8; -. DR ABCD; Q96PU8; 5 sequenced antibodies. DR Antibodypedia; 20048; 505 antibodies from 43 providers. DR DNASU; 9444; -. DR Ensembl; ENST00000275262.11; ENSP00000275262.7; ENSG00000112531.17. [Q96PU8-6] DR Ensembl; ENST00000361195.6; ENSP00000354867.2; ENSG00000112531.17. [Q96PU8-3] DR Ensembl; ENST00000361752.8; ENSP00000355094.3; ENSG00000112531.17. [Q96PU8-1] DR Ensembl; ENST00000361758.8; ENSP00000354951.4; ENSG00000112531.17. [Q96PU8-9] DR Ensembl; ENST00000392127.6; ENSP00000375973.2; ENSG00000112531.17. [Q96PU8-8] DR Ensembl; ENST00000424802.7; ENSP00000408382.3; ENSG00000112531.17. [Q96PU8-5] DR Ensembl; ENST00000453779.6; ENSP00000408775.2; ENSG00000112531.17. [Q96PU8-9] DR GeneID; 9444; -. DR KEGG; hsa:9444; -. DR MANE-Select; ENST00000361752.8; ENSP00000355094.3; NM_006775.3; NP_006766.1. DR UCSC; uc003que.4; human. [Q96PU8-1] DR AGR; HGNC:21100; -. DR CTD; 9444; -. DR DisGeNET; 9444; -. DR GeneCards; QKI; -. DR HGNC; HGNC:21100; QKI. DR HPA; ENSG00000112531; Tissue enhanced (brain, tongue). DR MalaCards; QKI; -. DR MIM; 609590; gene. DR neXtProt; NX_Q96PU8; -. DR OpenTargets; ENSG00000112531; -. DR Orphanet; 251671; Angiocentric glioma. DR PharmGKB; PA134912180; -. DR VEuPathDB; HostDB:ENSG00000112531; -. DR eggNOG; KOG1588; Eukaryota. DR GeneTree; ENSGT00940000155310; -. DR HOGENOM; CLU_046595_2_0_1; -. DR InParanoid; Q96PU8; -. DR OMA; WICAEIS; -. DR OrthoDB; 1397at2759; -. DR PhylomeDB; Q96PU8; -. DR TreeFam; TF314878; -. DR PathwayCommons; Q96PU8; -. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR SignaLink; Q96PU8; -. DR BioGRID-ORCS; 9444; 34 hits in 1168 CRISPR screens. DR ChiTaRS; QKI; human. DR GeneWiki; QKI; -. DR GenomeRNAi; 9444; -. DR Pharos; Q96PU8; Tbio. DR PRO; PR:Q96PU8; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96PU8; Protein. DR Bgee; ENSG00000112531; Expressed in endothelial cell and 209 other cell types or tissues. DR ExpressionAtlas; Q96PU8; baseline and differential. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0160089; F:internal N(7)-methylguanine-containing RNA reader activity; IDA:UniProt. DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0008298; P:intracellular mRNA localization; IDA:UniProtKB. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl. DR GO; GO:0014004; P:microglia differentiation; ISS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IDA:UniProt. DR GO; GO:0042552; P:myelination; IEA:Ensembl. DR GO; GO:1990764; P:myofibroblast contraction; IEA:Ensembl. DR GO; GO:1905869; P:negative regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:UniProtKB. DR GO; GO:0045650; P:negative regulation of macrophage differentiation; IDA:UniProtKB. DR GO; GO:2000626; P:negative regulation of miRNA catabolic process; IDA:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB. DR GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProtKB. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB. DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0048710; P:regulation of astrocyte differentiation; ISS:UniProtKB. DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IDA:UniProtKB. DR GO; GO:0045649; P:regulation of macrophage differentiation; IDA:UniProtKB. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IDA:UniProtKB. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR CDD; cd22465; KH-I_Hqk; 1. DR Gene3D; 1.20.5.4010; -; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR InterPro; IPR045071; BBP-like. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR032367; Quaking_NLS. DR InterPro; IPR032377; STAR_dimer. DR PANTHER; PTHR11208:SF125; PROTEIN QUAKING; 1. DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF16551; Quaking_NLS; 1. DR Pfam; PF16544; STAR_dimer; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR Genevisible; Q96PU8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein; KW Differentiation; DNA-binding; Methylation; mRNA processing; mRNA splicing; KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; KW SH3-binding; Translation regulation; Transport; Ubl conjugation. FT CHAIN 1..341 FT /note="KH domain-containing RNA-binding protein QKI" FT /id="PRO_0000239373" FT DOMAIN 87..153 FT /note="KH" FT REGION 11..82 FT /note="Qua1 domain; involved in homodimerization" FT /evidence="ECO:0000250|UniProtKB:Q17339" FT REGION 182..213 FT /note="Qua2 domain; involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT MOTIF 276..279 FT /note="SH3-binding" FT MOTIF 324..330 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:Q9QYS9" FT SITE 97 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT SITE 120 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT SITE 124 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT SITE 130 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT SITE 190 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT SITE 193 FT /note="Involved in RNA binding" FT /evidence="ECO:0000269|PubMed:23630077" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 227 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 242 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000269|PubMed:23455924" FT MOD_RES 242 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 256 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9QYS9" FT VAR_SEQ 213..220 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_019188" FT VAR_SEQ 312..341 FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> EWIEMPVMPDISAH (in FT isoform 3 and isoform QKI7)" FT /evidence="ECO:0000303|PubMed:11856480, ECO:0000303|Ref.2, FT ECO:0000303|Ref.3" FT /id="VSP_019190" FT VAR_SEQ 312..341 FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> GMAFPTKG (in FT isoform QKI6)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_019189" FT VAR_SEQ 312..341 FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> GKFFSPWG (in FT isoform QKI7B)" FT /evidence="ECO:0000303|PubMed:11856480" FT /id="VSP_019191" FT VARIANT 336 FT /note="R -> Q (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1258390251)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036051" FT MUTAGEN 97 FT /note="N->A: Decrease in target mRNA abundance and 10-fold FT decrease in RNA binding affinity; when associated with FT A-130." FT /evidence="ECO:0000269|PubMed:23630077" FT MUTAGEN 120 FT /note="K->A: Decrease in target mRNA abundance and 20-fold FT decrease in RNA binding affinity; when associated with FT A-124." FT /evidence="ECO:0000269|PubMed:23630077" FT MUTAGEN 124 FT /note="R->A: Decrease in target mRNA abundance and 20-fold FT decrease in RNA binding affinity; when associated with FT A-120." FT /evidence="ECO:0000269|PubMed:23630077" FT MUTAGEN 130 FT /note="R->A: Decrease in target mRNA abundance and 10-fold FT decrease in RNA binding affinity; when associated with FT A-97." FT /evidence="ECO:0000269|PubMed:23630077" FT MUTAGEN 190 FT /note="K->A: Decrease in target mRNA abundance and 124-fold FT decrease in RNA binding affinity; when associated with FT A-193." FT /evidence="ECO:0000269|PubMed:23630077" FT MUTAGEN 193 FT /note="Q->A: Decrease in target mRNA abundance and 124-fold FT decrease in RNA binding affinity; when associated with FT A-190." FT /evidence="ECO:0000269|PubMed:23630077" FT CONFLICT 30 FT /note="S -> G (in Ref. 3; ABC88600)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="N -> D (in Ref. 5; AAH12222)" FT /evidence="ECO:0000305" SQ SEQUENCE 341 AA; 37671 MW; 43E7F3A426A494C4 CRC64; MVGEMETKEK PKPTPDYLMQ LMNDKKLMSS LPNFCGIFNH LERLLDEEIS RVRKDMYNDT LNGSTEKRSA ELPDAVGPIV QLQEKLYVPV KEYPDFNFVG RILGPRGLTA KQLEAETGCK IMVRGKGSMR DKKKEEQNRG KPNWEHLNED LHVLITVEDA QNRAEIKLKR AVEEVKKLLV PAAEGEDSLK KMQLMELAIL NGTYRDANIK SPALAFSLAA TAQAAPRIIT GPAPVLPPAA LRTPTPAGPT IMPLIRQIQT AVMPNGTPHP TAAIVPPGPE AGLIYTPYEY PYTLAPATSI LEYPIEPSGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N //