QKI_HUMAN
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 03-AUG-2022, entry version 174.
DE RecName: Full=Protein quaking;
DE Short=Hqk;
DE Short=HqkI;
GN Name=QKI; Synonyms=HKQ;
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 1; 4 AND 5).
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 1 AND 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-341 (ISOFORM 6).
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 1).
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 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 [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 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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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-binding protein that plays a central role in
CC myelinization (PubMed:16641098). Binds to the 5'-NACUAAY-N(1,20)-UAAY-
CC 3' RNA core sequence. Regulates target mRNA stability
CC (PubMed:23630077). In addition, acts by regulating pre-mRNA splicing,
CC mRNA export and protein translation. Required to protect and promote
CC stability of mRNAs such as MBP and CDKN1B. Regulator of oligodendrocyte
CC differentiation and maturation in the brain that may play a role in
CC myelin and oligodendrocyte dysfunction in schizophrenia
CC (PubMed:16641098). Participates in mRNA transport by regulating the
CC nuclear export of MBP mRNA. Also involved in regulation of mRNA
CC splicing of MAG pre-mRNA. Acts as a translational repressor (By
CC similarity). {ECO:0000250|UniProtKB:Q9QYS9,
CC ECO:0000269|PubMed:16641098, ECO:0000269|PubMed:23630077}.
CC -!- SUBUNIT: Homodimer (PubMed:23630077). Does not require RNA to
CC homodimerize. Able to heterodimerize with BICC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QYS9, ECO:0000269|PubMed:23630077}.
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:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; 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=4; Synonyms=HQK-7;
CC IsoId=Q96PU8-6; Sequence=VSP_019190;
CC Name=5; Synonyms=HQK-7B;
CC IsoId=Q96PU8-8; Sequence=VSP_019191;
CC Name=6;
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 -!- 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}.
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}.
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};
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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. [Q96PU8-5]
DR PDB; 4JVH; X-ray; 3.50 A; A=7-214.
DR PDBsum; 4JVH; -.
DR AlphaFoldDB; Q96PU8; -.
DR SMR; Q96PU8; -.
DR BioGRID; 114834; 173.
DR IntAct; Q96PU8; 66.
DR MINT; Q96PU8; -.
DR STRING; 9606.ENSP00000355094; -.
DR GlyGen; Q96PU8; 1 site, 1 O-linked glycan (1 site).
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; Q96PU8; -.
DR PeptideAtlas; Q96PU8; -.
DR PRIDE; 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 ABCD; Q96PU8; 5 sequenced antibodies.
DR Antibodypedia; 20048; 448 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 CTD; 9444; -.
DR DisGeNET; 9444; -.
DR GeneCards; QKI; -.
DR HGNC; HGNC:21100; QKI.
DR HPA; ENSG00000112531; Tissue enhanced (brain).
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; PPCSCEC; -.
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; 32 hits in 1088 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 207 other tissues.
DR ExpressionAtlas; Q96PU8; baseline and differential.
DR Genevisible; Q96PU8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
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_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"
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 4)"
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 -> GKFFSPWG (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11856480"
FT /id="VSP_019191"
FT VAR_SEQ 312..341
FT /note="GAVATKVRRHDMRVHPYQRIVTADRAATGN -> GMAFPTKG (in
FT isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019189"
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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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
