QKI_MOUSE
ID QKI_MOUSE Reviewed; 341 AA.
AC Q9QYS9; O88972; Q61110; Q78ZE4; Q78ZE5; Q8K4X9; Q8K4Y0; Q9CW34; Q9QUH4;
AC Q9R2A8; Q9Z246;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein quaking;
DE Short=MqkI;
DE Short=qkI;
GN Name=Qki; Synonyms=Qk, Qk1, Qka1;
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 [MRNA] (ISOFORM 3), INVOLVEMENT IN QKV, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLU-48.
RX PubMed=8589716; DOI=10.1038/ng0396-260;
RA Ebersole T.A., Chen Q., Justice M.J., Artzt K.;
RT "The quaking gene product necessary in embryogenesis and myelination
RT combines features of RNA binding and signal transduction proteins.";
RL Nat. Genet. 12:260-265(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 3; 4 AND 7), AND
RP ALTERNATIVE SPLICING (ISOFORM 1).
RC STRAIN=129/J;
RX PubMed=10384037; DOI=10.1007/s003359901068;
RA Kondo T., Furuta T., Mitsunaga K., Ebersole T.A., Shichiri M., Wu J.,
RA Artzt K., Yamamura K., Abe K.;
RT "Genomic organization and expression analysis of the mouse qkI locus.";
RL Mamm. Genome 10:662-669(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-341 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [GENOMIC DNA] OF 49-341, ALTERNATIVE SPLICING (ISOFORMS
RP 1; 3; 4 AND 8), AND MUTAGENESIS OF VAL-157.
RX PubMed=10328999; DOI=10.1006/geno.1999.5804;
RA Cox R.D., Hugill A., Shedlovsky A., Noveroske J.K., Best S., Justice M.J.,
RA Lehrach H., Dove W.F.;
RT "Contrasting effects of ENU induced embryonic lethal mutations of the
RT quaking gene.";
RL Genomics 57:333-341(1999).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8987822; DOI=10.1523/jneurosci.16-24-07941.1996;
RA Hardy R.J., Loushin C.L., Friedrich V.L. Jr., Chen Q., Ebersole T.A.,
RA Lazzarini R.A., Artzt K.;
RT "Neural cell type-specific expression of QKI proteins is altered in
RT quakingviable mutant mice.";
RL J. Neurosci. 16:7941-7949(1996).
RN [8]
RP SUBUNIT, AND INTERACTION WITH BICC1.
RX PubMed=9315629; DOI=10.1128/mcb.17.10.5707;
RA Chen T., Damaj B.B., Herrera C., Lasko P., Richard S.;
RT "Self-association of the single-KH-domain family members Sam68, GRP33, GLD-
RT 1, and Qk1: role of the KH domain.";
RL Mol. Cell. Biol. 17:5707-5718(1997).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=9778149;
RX DOI=10.1002/(sici)1097-4547(19981001)54:1<46::aid-jnr6>3.0.co;2-h;
RA Hardy R.J.;
RT "QKI expression is regulated during neuron-glial cell fate decisions.";
RL J. Neurosci. Res. 54:46-57(1998).
RN [10]
RP SUBUNIT, AND MUTAGENESIS OF GLU-48.
RX PubMed=9671495; DOI=10.1128/mcb.18.8.4863;
RA Chen T., Richard S.;
RT "Structure-function analysis of Qk1: a lethal point mutation in mouse
RT quaking prevents homodimerization.";
RL Mol. Cell. Biol. 18:4863-4871(1998).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-48; ARG-324; TYR-328
RP AND ARG-330.
RX PubMed=10506177; DOI=10.1074/jbc.274.41.29202;
RA Wu J., Zhou L., Tonissen K., Tee R., Artzt K.;
RT "The quaking I-5 protein (QKI-5) has a novel nuclear localization signal
RT and shuttles between the nucleus and the cytoplasm.";
RL J. Biol. Chem. 274:29202-29210(1999).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10535969; DOI=10.1073/pnas.96.22.12605;
RA Saccomanno L., Loushin C., Jan E., Punkay E., Artzt K., Goodwin E.B.;
RT "The STAR protein QKI-6 is a translational repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12605-12610(1999).
RN [13]
RP FUNCTION.
RX PubMed=10864952; DOI=10.1523/jneurosci.20-13-04944.2000;
RA Li Z., Zhang Y., Li D., Feng Y.;
RT "Destabilization and mislocalization of myelin basic protein mRNAs in
RT quaking dysmyelination lacking the QKI RNA-binding proteins.";
RL J. Neurosci. 20:4944-4953(2000).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11297509; DOI=10.1101/gad.860301;
RA Pilotte J., Larocque D., Richard S.;
RT "Nuclear translocation controlled by alternatively spliced isoforms
RT inactivates the QUAKING apoptotic inducer.";
RL Genes Dev. 15:845-858(2001).
RN [15]
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF VAL-157.
RX PubMed=12467586; DOI=10.1016/s0896-6273(02)01055-3;
RA Larocque D., Pilotte J., Chen T., Cloutier F., Massie B., Pedraza L.,
RA Couture R., Lasko P., Almazan G., Richard S.;
RT "Nuclear retention of MBP mRNAs in the quaking viable mice.";
RL Neuron 36:815-829(2002).
RN [16]
RP FUNCTION.
RX PubMed=11917126; DOI=10.1073/pnas.072090399;
RA Wu J.I., Reed R.B., Grabowski P.J., Artzt K.;
RT "Function of quaking in myelination: regulation of alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4233-4238(2002).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF VAL-157.
RX PubMed=11892011; DOI=10.1002/gene.10060;
RA Noveroske J.K., Lai L., Gaussin V., Northrop J.L., Nakamura H.,
RA Hirschi K.K., Justice M.J.;
RT "Quaking is essential for blood vessel development.";
RL Genesis 32:218-230(2002).
RN [18]
RP PHOSPHORYLATION, AND MUTAGENESIS OF 276-PRO--PRO-279; TYR-285; TYR-288;
RP TYR-290; TYR-292 AND TYR-303.
RX PubMed=12682013; DOI=10.1093/emboj/cdg171;
RA Zhang Y., Lu Z., Ku L., Chen Y., Wang H., Feng Y.;
RT "Tyrosine phosphorylation of QKI mediates developmental signals to regulate
RT mRNA metabolism.";
RL EMBO J. 22:1801-1810(2003).
RN [19]
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 [20]
RP INVOLVEMENT IN QKV.
RX PubMed=12888522; DOI=10.1093/nar/gkg635;
RA Lu Z., Zhang Y., Ku L., Wang H., Ahmadian A., Feng Y.;
RT "The quakingviable mutation affects qkI mRNA expression specifically in
RT myelin-producing cells of the nervous system.";
RL Nucleic Acids Res. 31:4616-4624(2003).
RN [21]
RP INVOLVEMENT IN QKV.
RX PubMed=15014970; DOI=10.1007/s00335-003-2333-5;
RA Lorenzetti D., Antalffy B., Vogel H., Noveroske J., Armstrong D.,
RA Justice M.;
RT "The neurological mutant quaking(viable) is Parkin deficient.";
RL Mamm. Genome 15:210-217(2004).
RN [22]
RP FUNCTION.
RX PubMed=16198329; DOI=10.1016/j.ydbio.2005.08.038;
RA Lakiza O., Frater L., Yoo Y., Villavicencio E., Walterhouse D.,
RA Goodwin E.B., Iannaccone P.;
RT "STAR proteins quaking-6 and GLD-1 regulate translation of the homologues
RT GLI1 and tra-1 through a conserved RNA 3'UTR-based mechanism.";
RL Dev. Biol. 287:98-110(2005).
RN [23]
RP FUNCTION.
RX PubMed=14706070; DOI=10.1111/j.1440-169x.2003.00712.x;
RA Li Z., Takakura N., Oike Y., Imanaka T., Araki K., Suda T., Kaname T.,
RA Kondo T., Abe K., Yamamura K.;
RT "Defective smooth muscle development in qkI-deficient mice.";
RL Dev. Growth Differ. 45:449-462(2003).
RN [24]
RP PHOSPHORYLATION.
RX PubMed=15528192; DOI=10.1074/jbc.m405973200;
RA Lu Z., Ku L., Chen Y., Feng Y.;
RT "Developmental abnormalities of myelin basic protein expression in fyn
RT knock-out brain reveal a role of Fyn in posttranscriptional regulation.";
RL J. Biol. Chem. 280:389-395(2005).
RN [25]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15568022; DOI=10.1038/nn1359;
RA Larocque D., Galarneau A., Liu H.-N., Scott M., Almazan G., Richard S.;
RT "Protection of p27(Kip1) mRNA by quaking RNA binding proteins promotes
RT oligodendrocyte differentiation.";
RL Nat. Neurosci. 8:27-33(2005).
RN [26]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=16041388; DOI=10.1038/nsmb963;
RA Galarneau A., Richard S.;
RT "Target RNA motif and target mRNAs of the Quaking STAR protein.";
RL Nat. Struct. Mol. Biol. 12:691-698(2005).
RN [27]
RP FUNCTION.
RX PubMed=16470614; DOI=10.1002/gene.20189;
RA Bohnsack B.L., Lai L., Northrop J.L., Justice M.J., Hirschi K.K.;
RT "Visceral endoderm function is regulated by quaking and required for
RT vascular development.";
RL Genesis 44:93-104(2006).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [29]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-227; ARG-242 AND ARG-256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: RNA-binding protein that plays a central role in
CC myelinization (PubMed:10864952, PubMed:11917126). Also required for
CC visceral endoderm function and blood vessel development
CC (PubMed:11892011, PubMed:16470614). Binds to the 5'-NACUAAY-N(1,20)-
CC UAAY-3' RNA core sequence (PubMed:16041388). Acts by regulating pre-
CC mRNA splicing, mRNA export, mRNA stability and protein translation, as
CC well as cellular processes including apoptosis, cell cycle, glial cell
CC fate and development (PubMed:10535969, PubMed:12467586,
CC PubMed:11297509, PubMed:11917126, PubMed:15568022). Required to protect
CC and promote stability of mRNAs such as MBP and CDKN1B which promotes
CC oligodendrocyte differentiation (PubMed:10535969, PubMed:15568022).
CC Participates in mRNA transport by regulating the nuclear export of MBP
CC mRNA (PubMed:12467586). May also play a role in smooth muscle
CC development (PubMed:14706070). {ECO:0000269|PubMed:10535969,
CC ECO:0000269|PubMed:10864952, ECO:0000269|PubMed:11297509,
CC ECO:0000269|PubMed:11892011, ECO:0000269|PubMed:11917126,
CC ECO:0000269|PubMed:12467586, ECO:0000269|PubMed:14706070,
CC ECO:0000269|PubMed:15568022, ECO:0000269|PubMed:16041388,
CC ECO:0000269|PubMed:16470614}.
CC -!- FUNCTION: Isoform 1 is involved in regulation of mRNA splicing of MAG
CC pre-mRNA by acting as a negative regulator of MAG exon 12 alternative
CC splicing. {ECO:0000269|PubMed:11917126}.
CC -!- FUNCTION: Isoform 3 can induce apoptosis, while heterodimerization with
CC other isoforms results in nuclear translocation of isoform 3 and
CC suppression of apoptosis. {ECO:0000269|PubMed:11297509}.
CC -!- FUNCTION: Isoform 4 acts as a translational repressor for GLI1.
CC {ECO:0000269|PubMed:16198329}.
CC -!- SUBUNIT: Homodimer. Does not require RNA to homodimerize
CC (PubMed:10506177, PubMed:11297509, PubMed:9671495). Able to
CC heterodimerize with BICC1 (PubMed:9315629).
CC {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:11297509,
CC ECO:0000269|PubMed:9315629, ECO:0000269|PubMed:9671495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. Note=Isoform 1
CC localizes predominantly in the nucleus and at lower levels in
CC cytoplasm. It shuttles between the cytoplasm and the nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus. Note=Isoform 3
CC localizes predominantly in the cytoplasm and at much lower levels in
CC nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=Isoform 4
CC localizes both in the cytoplasm and nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=QKI-5;
CC IsoId=Q9QYS9-1; Sequence=Displayed;
CC Name=2; Synonyms=QKI-7B;
CC IsoId=Q9QYS9-2; Sequence=VSP_019195;
CC Name=3; Synonyms=QkI-7;
CC IsoId=Q9QYS9-3; Sequence=VSP_019196;
CC Name=4; Synonyms=QKI-6, QKI-5B;
CC IsoId=Q9QYS9-4; Sequence=VSP_019197;
CC Name=5; Synonyms=D;
CC IsoId=Q9QYS9-5; Sequence=VSP_019192, VSP_019193;
CC Name=6; Synonyms=QKI-7B;
CC IsoId=Q9QYS9-6; Sequence=VSP_019194, VSP_019195;
CC Name=7; Synonyms=QKI-5A;
CC IsoId=Q9QYS9-7; Sequence=VSP_019199;
CC Name=8; Synonyms=QKI-G;
CC IsoId=Q9QYS9-8; Sequence=VSP_019198;
CC -!- TISSUE SPECIFICITY: Highly expressed in myelin-forming cells. Expressed
CC in oligodendrocytes and astrocytes in the central nervous system as
CC well as Schwann cells in the peripheral nervous system. Also expressed
CC in the yolk sac endoderm, adjacent to the mesodermal site of developing
CC blood islands, where the differentiation of blood and endothelial cells
CC first occurs (at protein level). Expressed in brain, lung, heart and
CC testis. {ECO:0000269|PubMed:8589716, ECO:0000269|PubMed:8987822,
CC ECO:0000269|PubMed:9778149}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neural progenitors of the ventricular
CC zone (vz) during CNS development, but that expression is down-regulated
CC during neuronal differentiation. By contrast, neural progenitors
CC located in specific subdomains of the vz maintain expression as they
CC differentiate and migrate away into the emerging nervous system. These
CC have characteristics consistent with the acquisition of a glial rather
CC than neuronal fate (at protein level) First detected in the
CC neuroepithelium of the head folds at 7.5 dpc. Expression is strongly
CC present ventrally in the nascent brain and neural tube of 8.5 dpc and
CC 9.5 dpc and in the heart of 8.5 dpc. Isoform 1 is expressed in early
CC embryos, while isoform 3 and isoform 4 are found in late development
CC when myelination begins.
CC -!- DOMAIN: The KH domain and the Qua2 region are involved in RNA binding.
CC {ECO:0000250|UniProtKB:Q96PU8}.
CC -!- PTM: Methylated by PRMT1. {ECO:0000269|PubMed:12529443}.
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. The level of Tyr
CC phosphorylation in the developing myelin is highest in the first
CC postnatal week (P7). During the vigorous accumulation of MBP mRNA
CC between P7 and P20, phosphorylation in the developing myelin
CC drastically declines. By the end of the fourth postnatal week (P28),
CC phosphorylation is reduced approximately 90%.
CC {ECO:0000269|PubMed:12682013, ECO:0000269|PubMed:15528192}.
CC -!- DISEASE: Note=Defects in Qki are the cause of quakingviable (qkv). Qkv
CC is a spontaneous mutation resulting in hypomyelinization of the central
CC and peripheral nervous systems. Mutant mice develop normally until
CC postnatal day 10 when they display rapid tremors or 'quaking' that is
CC especially pronounced in hindlimbs and experience convulsive tonic-
CC clonic seizures as they mature (PubMed:8589716). Mice with qkv
CC specifically lack isoform 3 and isoform 4 in myelin-forming cells,
CC while isoform 1 is lacking in oligodendrocytes of severely affected
CC tracts (PubMed:12888522). Mice with qkv also lack the PRKN gene
CC product, suggesting that the absence of PRKN may also affect the
CC phenotype (PubMed:15014970). {ECO:0000269|PubMed:12888522,
CC ECO:0000269|PubMed:15014970, ECO:0000269|PubMed:8589716}.
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DR EMBL; U44940; AAC52491.1; -; mRNA.
DR EMBL; AF090402; AAC99452.1; -; mRNA.
DR EMBL; AF090403; AAC99453.1; -; mRNA.
DR EMBL; AF090404; AAC99454.1; -; mRNA.
DR EMBL; AF091047; AAC63042.1; -; mRNA.
DR EMBL; AF090401; AAD53329.1; -; Genomic_DNA.
DR EMBL; AF090392; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090393; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090394; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090395; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090396; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090397; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090400; AAD53329.1; JOINED; Genomic_DNA.
DR EMBL; AF090397; AAD53330.1; -; Genomic_DNA.
DR EMBL; AF090392; AAD53330.1; JOINED; Genomic_DNA.
DR EMBL; AF090393; AAD53330.1; JOINED; Genomic_DNA.
DR EMBL; AF090394; AAD53330.1; JOINED; Genomic_DNA.
DR EMBL; AF090395; AAD53330.1; JOINED; Genomic_DNA.
DR EMBL; AF090396; AAD53330.1; JOINED; Genomic_DNA.
DR EMBL; AF090397; AAD53331.1; -; Genomic_DNA.
DR EMBL; AF090392; AAD53331.1; JOINED; Genomic_DNA.
DR EMBL; AF090393; AAD53331.1; JOINED; Genomic_DNA.
DR EMBL; AF090395; AAD53331.1; JOINED; Genomic_DNA.
DR EMBL; AF090396; AAD53331.1; JOINED; Genomic_DNA.
DR EMBL; AF090394; AAD53331.1; JOINED; Genomic_DNA.
DR EMBL; AF090396; AAD53332.1; -; Genomic_DNA.
DR EMBL; AF090392; AAD53332.1; JOINED; Genomic_DNA.
DR EMBL; AF090393; AAD53332.1; JOINED; Genomic_DNA.
DR EMBL; AF090394; AAD53332.1; JOINED; Genomic_DNA.
DR EMBL; AF090395; AAD53332.1; JOINED; Genomic_DNA.
DR EMBL; AF467890; AAM21006.1; -; Genomic_DNA.
DR EMBL; AF467890; AAM21007.1; -; Genomic_DNA.
DR EMBL; AF467890; AAM21008.1; -; Genomic_DNA.
DR EMBL; AF467890; AAM21009.1; -; Genomic_DNA.
DR EMBL; AF467890; AAM21010.1; -; Genomic_DNA.
DR EMBL; AK005169; BAB23859.1; -; mRNA.
DR EMBL; AK132303; BAE21091.1; -; mRNA.
DR EMBL; BC053426; AAH53426.1; -; mRNA.
DR EMBL; BC056346; AAH56346.1; -; mRNA.
DR EMBL; AJ012812; CAB37614.1; -; Genomic_DNA.
DR EMBL; AJ012813; CAB37614.1; JOINED; Genomic_DNA.
DR EMBL; AJ012814; CAB37614.1; JOINED; Genomic_DNA.
DR EMBL; AJ012816; CAB37614.1; JOINED; Genomic_DNA.
DR EMBL; AJ012817; CAB37614.1; JOINED; Genomic_DNA.
DR EMBL; AJ012815; CAB37614.1; JOINED; Genomic_DNA.
DR EMBL; AJ012812; CAB37615.1; -; Genomic_DNA.
DR EMBL; AJ012813; CAB37615.1; JOINED; Genomic_DNA.
DR EMBL; AJ012814; CAB37615.1; JOINED; Genomic_DNA.
DR EMBL; AJ012818; CAB37615.1; JOINED; Genomic_DNA.
DR EMBL; AJ012816; CAB37615.1; JOINED; Genomic_DNA.
DR EMBL; AJ012815; CAB37615.1; JOINED; Genomic_DNA.
DR EMBL; AJ012812; CAB37616.1; -; Genomic_DNA.
DR EMBL; AJ012813; CAB37616.1; JOINED; Genomic_DNA.
DR EMBL; AJ012814; CAB37616.1; JOINED; Genomic_DNA.
DR EMBL; AJ012816; CAB37616.1; JOINED; Genomic_DNA.
DR EMBL; AJ012820; CAB37616.1; JOINED; Genomic_DNA.
DR EMBL; AJ012819; CAB37616.1; JOINED; Genomic_DNA.
DR EMBL; AJ012815; CAB37616.1; JOINED; Genomic_DNA.
DR CCDS; CCDS28387.1; -. [Q9QYS9-3]
DR CCDS; CCDS49947.1; -. [Q9QYS9-1]
DR CCDS; CCDS88989.1; -. [Q9QYS9-4]
DR RefSeq; NP_001152988.1; NM_001159516.1. [Q9QYS9-4]
DR RefSeq; NP_001152989.1; NM_001159517.1. [Q9QYS9-1]
DR RefSeq; NP_068681.1; NM_021881.2. [Q9QYS9-3]
DR PDB; 4DNN; X-ray; 2.10 A; A/B=14-67.
DR PDBsum; 4DNN; -.
DR AlphaFoldDB; Q9QYS9; -.
DR SMR; Q9QYS9; -.
DR BioGRID; 202529; 16.
DR IntAct; Q9QYS9; 2.
DR MINT; Q9QYS9; -.
DR STRING; 10090.ENSMUSP00000095025; -.
DR iPTMnet; Q9QYS9; -.
DR PhosphoSitePlus; Q9QYS9; -.
DR EPD; Q9QYS9; -.
DR jPOST; Q9QYS9; -.
DR MaxQB; Q9QYS9; -.
DR PaxDb; Q9QYS9; -.
DR PeptideAtlas; Q9QYS9; -.
DR PRIDE; Q9QYS9; -.
DR ProteomicsDB; 301842; -. [Q9QYS9-1]
DR ProteomicsDB; 301843; -. [Q9QYS9-2]
DR ProteomicsDB; 301844; -. [Q9QYS9-3]
DR ProteomicsDB; 301845; -. [Q9QYS9-4]
DR ProteomicsDB; 301846; -. [Q9QYS9-5]
DR ProteomicsDB; 301847; -. [Q9QYS9-6]
DR ProteomicsDB; 301848; -. [Q9QYS9-7]
DR ProteomicsDB; 301849; -. [Q9QYS9-8]
DR ABCD; Q9QYS9; 1 sequenced antibody.
DR Antibodypedia; 20048; 448 antibodies from 43 providers.
DR DNASU; 19317; -.
DR Ensembl; ENSMUST00000042296; ENSMUSP00000046740; ENSMUSG00000062078. [Q9QYS9-3]
DR Ensembl; ENSMUST00000097414; ENSMUSP00000095025; ENSMUSG00000062078. [Q9QYS9-4]
DR Ensembl; ENSMUST00000233645; ENSMUSP00000156511; ENSMUSG00000062078. [Q9QYS9-1]
DR Ensembl; ENSMUST00000233828; ENSMUSP00000156665; ENSMUSG00000062078. [Q9QYS9-4]
DR GeneID; 19317; -.
DR KEGG; mmu:19317; -.
DR UCSC; uc008akb.2; mouse. [Q9QYS9-1]
DR UCSC; uc008ake.2; mouse. [Q9QYS9-4]
DR UCSC; uc012ajv.1; mouse. [Q9QYS9-3]
DR CTD; 19317; -.
DR MGI; MGI:97837; Qk.
DR VEuPathDB; HostDB:ENSMUSG00000062078; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000155310; -.
DR HOGENOM; CLU_046595_2_0_1; -.
DR InParanoid; Q9QYS9; -.
DR OMA; PPCSCEC; -.
DR OrthoDB; 1565749at2759; -.
DR PhylomeDB; Q9QYS9; -.
DR TreeFam; TF314878; -.
DR BioGRID-ORCS; 19317; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Qk; mouse.
DR PRO; PR:Q9QYS9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QYS9; protein.
DR Bgee; ENSMUSG00000062078; Expressed in gonadal ridge and 277 other tissues.
DR ExpressionAtlas; Q9QYS9; baseline and differential.
DR Genevisible; Q9QYS9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; TAS:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008366; P:axon ensheathment; IMP:MGI.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; IGI:MGI.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR Gene3D; 3.30.1370.10; -; 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; PTHR11208; 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; SSF54791; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Methylation; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW SH3-binding; Translation regulation; Transport.
FT CHAIN 1..341
FT /note="Protein quaking"
FT /id="PRO_0000239374"
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:0000250|UniProtKB:Q96PU8"
FT MOTIF 276..279
FT /note="SH3-binding"
FT MOTIF 324..330
FT /note="Nuclear localization signal"
FT SITE 97
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 120
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 124
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 130
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 190
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 193
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
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:0000250|UniProtKB:Q96PU8"
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:0007744|PubMed:24129315"
FT VAR_SEQ 183..187
FT /note="AEGED -> VSKFS (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_019192"
FT VAR_SEQ 188..341
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_019193"
FT VAR_SEQ 213..220
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_019194"
FT VAR_SEQ 312..341
FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> VWLSQRKAKNSRTVLTEP
FT SSDLNLTNA (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10384037"
FT /id="VSP_019195"
FT VAR_SEQ 312..341
FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> EWIEMPVMPDISAH (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10384037,
FT ECO:0000303|PubMed:8589716"
FT /id="VSP_019196"
FT VAR_SEQ 312..341
FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> GMAFPTKG (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10384037"
FT /id="VSP_019197"
FT VAR_SEQ 312..341
FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> GKYDSCTM (in
FT isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_019198"
FT VAR_SEQ 341
FT /note="N -> NVNW (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10384037"
FT /id="VSP_019199"
FT MUTAGEN 48
FT /note="E->G: In qk-Kt4; induces embryonic lethality
FT possibly due to its inability to homodimerize."
FT /evidence="ECO:0000269|PubMed:10506177,
FT ECO:0000269|PubMed:8589716, ECO:0000269|PubMed:9671495"
FT MUTAGEN 157
FT /note="V->E: In qk-k24; induces embryonic lethality
FT possibly due to blood vessel defects; prevents RNA-binding
FT but not homodimerization."
FT /evidence="ECO:0000269|PubMed:10328999,
FT ECO:0000269|PubMed:11892011, ECO:0000269|PubMed:12467586"
FT MUTAGEN 276..279
FT /note="PPGP->AAGA: Strongly impairs phosphorylation."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 285
FT /note="Y->F: Abolishes phosphorylation and RNA-binding;
FT when associated with F-288; F-290; F-292 and F-303."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 288
FT /note="Y->F: Abolishes phosphorylation and RNA-binding;
FT when associated with F-285; F-290; F-292 and F-303."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 290
FT /note="Y->F: Abolishes phosphorylation and RNA-binding;
FT when associated with F-285; F-288; F-292 and F-303."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 292
FT /note="Y->F: Abolishes phosphorylation and RNA-binding;
FT when associated with F-285; F-288; F-290 and F-303."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 303
FT /note="Y->F: Abolishes phosphorylation and RNA-binding;
FT when associated with F-285; F-288; F-290 and F-292."
FT /evidence="ECO:0000269|PubMed:12682013"
FT MUTAGEN 324
FT /note="R->A: Abolishes nuclear localization; when
FT associated with A-330."
FT /evidence="ECO:0000269|PubMed:10506177"
FT MUTAGEN 328
FT /note="Y->F: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:10506177"
FT MUTAGEN 330
FT /note="R->A: Abolishes nuclear localization; when
FT associated with A-324."
FT /evidence="ECO:0000269|PubMed:10506177"
FT CONFLICT 276
FT /note="P -> A (in Ref. 4; BAB23859)"
FT /evidence="ECO:0000305"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:4DNN"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4DNN"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:4DNN"
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
