RIOK2_HUMAN
ID RIOK2_HUMAN Reviewed; 552 AA.
AC Q9BVS4; D6RDI3; Q9NUT0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase RIO2;
DE EC=2.7.11.1 {ECO:0000269|PubMed:19564402, ECO:0000269|PubMed:21880710};
DE AltName: Full=RIO kinase 2;
GN Name=RIOK2 {ECO:0000312|HGNC:HGNC:18999};
GN Synonyms=RIO2 {ECO:0000303|PubMed:21880710};
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-349.
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hepatoma;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-144.
RC TISSUE=Placenta;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16037817; DOI=10.1038/sj.emboj.7600752;
RA Rouquette J., Choesmel V., Gleizes P.E.;
RT "Nuclear export and cytoplasmic processing of precursors to the 40S
RT ribosomal subunits in mammalian cells.";
RL EMBO J. 24:2862-2872(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;
RP SER-390; SER-417 AND SER-442, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-380; SER-382;
RP SER-385 AND SER-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL,
RP PHOSPHORYLATION, AND MUTAGENESIS OF LYS-123; ASP-246; LEU-400 AND ILE-403.
RX PubMed=19564402; DOI=10.1083/jcb.200904048;
RA Zemp I., Wild T., O'Donohue M.F., Wandrey F., Widmann B., Gleizes P.E.,
RA Kutay U.;
RT "Distinct cytoplasmic maturation steps of 40S ribosomal subunit precursors
RT require hRio2.";
RL J. Cell Biol. 185:1167-1180(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;
RP SER-362; SER-385; SER-390; SER-442 AND TYR-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;
RP SER-380; SER-382; SER-385 AND SER-390, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337 AND
RP SER-412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP SUBUNIT.
RX PubMed=21081503; DOI=10.1074/jbc.m110.148486;
RA Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K.,
RA Fischer U., Grimmler M.;
RT "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5),
RT competes with pICln for binding and modulates PRMT5 complex composition and
RT substrate specificity.";
RL J. Biol. Chem. 286:1976-1986(2011).
RN [16]
RP PHOSPHORYLATION AT SER-335; SER-380 AND SER-548 BY PLK1, FUNCTION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF SER-335; SER-380 AND SER-548, AND
RP INTERACTION WITH PLK1.
RX PubMed=21880710; DOI=10.1074/jbc.m111.250175;
RA Liu T., Deng M., Li J., Tong X., Wei Q., Ye X.;
RT "Phosphorylation of right open reading frame 2 (Rio2) protein kinase by
RT polo-like kinase 1 regulates mitotic progression.";
RL J. Biol. Chem. 286:36352-36360(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;
RP SER-350; SER-380; SER-382; SER-390; SER-412 AND SER-442, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-96; ARG-144; HIS-155; ILE-175; THR-216;
RP VAL-244; ARG-349; SER-397; ASP-409 AND HIS-507.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the final steps
CC of cytoplasmic maturation of the 40S ribosomal subunit. Involved in
CC export of the 40S pre-ribosome particles (pre-40S) from the nucleus to
CC the cytoplasm. Its kinase activity is required for the release of NOB1,
CC PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-
CC rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of
CC the metaphase-anaphase transition during mitotic progression, and its
CC phosphorylation, most likely by PLK1, regulates this function
CC (PubMed:21880710). {ECO:0000269|PubMed:16037817,
CC ECO:0000269|PubMed:19564402, ECO:0000269|PubMed:21880710}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:19564402, ECO:0000269|PubMed:21880710};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:19564402,
CC ECO:0000269|PubMed:21880710};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Associated with late 40S pre-ribosomal particles
CC (PubMed:16037817, PubMed:21081503). Interacts with PLK1 (via its N-
CC terminus) (PubMed:21880710). {ECO:0000269|PubMed:16037817,
CC ECO:0000269|PubMed:21880710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16037817,
CC ECO:0000269|PubMed:19564402}. Note=Exported out of the nucleus via its
CC NES in a XPO1-dependent manner. {ECO:0000269|PubMed:19564402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVS4-2; Sequence=VSP_046388;
CC -!- PTM: Autophosphorylated (in vitro) (PubMed:19564402, PubMed:21880710).
CC Phosphorylation at Ser-335, Ser-380, Ser-548 by PLK1 affects the timing
CC of the metaphase-anaphase transition (PubMed:21880710).
CC {ECO:0000269|PubMed:19564402, ECO:0000269|PubMed:21880710}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; AK002021; BAA92040.1; -; mRNA.
DR EMBL; AK225348; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000953; AAH00953.1; -; mRNA.
DR CCDS; CCDS4089.1; -. [Q9BVS4-1]
DR CCDS; CCDS54884.1; -. [Q9BVS4-2]
DR RefSeq; NP_001153221.1; NM_001159749.1. [Q9BVS4-2]
DR RefSeq; NP_060813.2; NM_018343.2. [Q9BVS4-1]
DR PDB; 5DHF; X-ray; 2.29 A; D=389-403.
DR PDB; 6FDM; X-ray; 2.10 A; A/B/C/D=1-313.
DR PDB; 6FDN; X-ray; 2.90 A; A/B=1-320.
DR PDB; 6FDO; X-ray; 2.60 A; A/B=1-353.
DR PDB; 6G18; EM; 3.60 A; v=1-552.
DR PDB; 6G51; EM; 4.10 A; v=1-552.
DR PDB; 6HK6; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I/J=1-329.
DR PDBsum; 5DHF; -.
DR PDBsum; 6FDM; -.
DR PDBsum; 6FDN; -.
DR PDBsum; 6FDO; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6HK6; -.
DR AlphaFoldDB; Q9BVS4; -.
DR SMR; Q9BVS4; -.
DR BioGRID; 120896; 88.
DR IntAct; Q9BVS4; 41.
DR STRING; 9606.ENSP00000283109; -.
DR BindingDB; Q9BVS4; -.
DR ChEMBL; CHEMBL6000; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9BVS4; -.
DR GlyGen; Q9BVS4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVS4; -.
DR PhosphoSitePlus; Q9BVS4; -.
DR BioMuta; RIOK2; -.
DR DMDM; 143811448; -.
DR EPD; Q9BVS4; -.
DR jPOST; Q9BVS4; -.
DR MassIVE; Q9BVS4; -.
DR MaxQB; Q9BVS4; -.
DR PaxDb; Q9BVS4; -.
DR PeptideAtlas; Q9BVS4; -.
DR PRIDE; Q9BVS4; -.
DR ProteomicsDB; 14107; -.
DR ProteomicsDB; 79230; -. [Q9BVS4-1]
DR Antibodypedia; 13276; 345 antibodies from 27 providers.
DR DNASU; 55781; -.
DR Ensembl; ENST00000283109.8; ENSP00000283109.3; ENSG00000058729.11. [Q9BVS4-1]
DR Ensembl; ENST00000508447.1; ENSP00000420932.1; ENSG00000058729.11. [Q9BVS4-2]
DR GeneID; 55781; -.
DR KEGG; hsa:55781; -.
DR MANE-Select; ENST00000283109.8; ENSP00000283109.3; NM_018343.3; NP_060813.2.
DR UCSC; uc003kmz.4; human. [Q9BVS4-1]
DR CTD; 55781; -.
DR DisGeNET; 55781; -.
DR GeneCards; RIOK2; -.
DR HGNC; HGNC:18999; RIOK2.
DR HPA; ENSG00000058729; Low tissue specificity.
DR MIM; 617754; gene.
DR neXtProt; NX_Q9BVS4; -.
DR OpenTargets; ENSG00000058729; -.
DR PharmGKB; PA134885533; -.
DR VEuPathDB; HostDB:ENSG00000058729; -.
DR eggNOG; KOG2268; Eukaryota.
DR GeneTree; ENSGT00390000003255; -.
DR HOGENOM; CLU_018693_0_3_1; -.
DR InParanoid; Q9BVS4; -.
DR OMA; FEMTEFS; -.
DR OrthoDB; 1010730at2759; -.
DR PhylomeDB; Q9BVS4; -.
DR TreeFam; TF321400; -.
DR PathwayCommons; Q9BVS4; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9BVS4; -.
DR SIGNOR; Q9BVS4; -.
DR BioGRID-ORCS; 55781; 775 hits in 1123 CRISPR screens.
DR ChiTaRS; RIOK2; human.
DR GenomeRNAi; 55781; -.
DR Pharos; Q9BVS4; Tbio.
DR PRO; PR:Q9BVS4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BVS4; protein.
DR Bgee; ENSG00000058729; Expressed in oocyte and 179 other tissues.
DR ExpressionAtlas; Q9BVS4; baseline and differential.
DR Genevisible; Q9BVS4; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP:UniProtKB.
DR GO; GO:2000208; P:positive regulation of ribosomal small subunit export from nucleus; IMP:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR CDD; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..552
FT /note="Serine/threonine-protein kinase RIO2"
FT /id="PRO_0000213527"
FT DOMAIN 97..272
FT /note="Protein kinase"
FT /evidence="ECO:0000305"
FT MOTIF 399..408
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:19564402"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21880710,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21880710,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21880710"
FT VAR_SEQ 467..552
FT /note="DEENVGAMNQYRTRTLSITSSGSAVSCSTIPPELVKQKVKRQLTKQQKSAVR
FT RRLQKGEANIFTKQRRENMQNIKSSLEAASFWGE -> YRLLSIAF (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_046388"
FT VARIANT 96
FT /note="S -> C (in dbSNP:rs2544773)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042347"
FT VARIANT 144
FT /note="H -> R (in dbSNP:rs35165987)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042348"
FT VARIANT 144
FT /note="H -> Y (in dbSNP:rs17849382)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031597"
FT VARIANT 155
FT /note="R -> H (in dbSNP:rs34916955)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042349"
FT VARIANT 175
FT /note="V -> I (in dbSNP:rs35713904)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042350"
FT VARIANT 216
FT /note="I -> T (in a renal clear cell carcinoma sample;
FT somatic mutation; dbSNP:rs147608663)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042351"
FT VARIANT 244
FT /note="M -> V (in dbSNP:rs33996030)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042352"
FT VARIANT 349
FT /note="G -> R (in dbSNP:rs160632)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_031598"
FT VARIANT 397
FT /note="N -> S (in dbSNP:rs12188395)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_031599"
FT VARIANT 409
FT /note="E -> D (in dbSNP:rs35829000)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042353"
FT VARIANT 507
FT /note="R -> H (in dbSNP:rs34555783)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042354"
FT MUTAGEN 123
FT /note="K->A: Abolishes autophosphorylation; impairs release
FT of pre-40S trans-acting factors and rRNA processing; when
FT associated with A-246."
FT /evidence="ECO:0000269|PubMed:19564402"
FT MUTAGEN 246
FT /note="D->A: Abolishes autophosphorylation; impairs release
FT of pre-40S trans-acting factors and rRNA processing; when
FT associated with A-123."
FT /evidence="ECO:0000269|PubMed:19564402"
FT MUTAGEN 335
FT /note="S->A: Does not affect autophosphorylation activity;
FT when associated with A-380 and A-548. Does not affect the
FT timing of metaphase-anaphase transition; when associated
FT with A-380 and A-548."
FT /evidence="ECO:0000269|PubMed:21880710"
FT MUTAGEN 335
FT /note="S->D: Increases time spent in metaphase; when
FT associated with D-380 and D-548."
FT /evidence="ECO:0000269|PubMed:21880710"
FT MUTAGEN 380
FT /note="S->A: Does not affect autophosphorylation activity;
FT when associated with A-335 and A-548. Does not affect the
FT timing of metaphase-anaphase transition; when associated
FT with A-335 and A-548."
FT /evidence="ECO:0000269|PubMed:21880710"
FT MUTAGEN 380
FT /note="S->D: Increases time spent in metaphase; when
FT associated with D-335 and D-548."
FT /evidence="ECO:0000269|PubMed:21880710"
FT MUTAGEN 400
FT /note="L->A: Nuclear relocalization; when associated with
FT A-403."
FT /evidence="ECO:0000269|PubMed:19564402"
FT MUTAGEN 403
FT /note="I->A: Nuclear relocalization; when associated with
FT A-400."
FT /evidence="ECO:0000269|PubMed:19564402"
FT MUTAGEN 548
FT /note="S->A: Does not affect autophosphorylation activity;
FT when associated with A-335 and A-380. Does not affect the
FT timing of metaphase-anaphase transition; when associated
FT with A-335 and A-380."
FT /evidence="ECO:0000269|PubMed:21880710"
FT MUTAGEN 548
FT /note="S->D: Increases time spent in metaphase; when
FT associated with D-335 and D-380."
FT /evidence="ECO:0000269|PubMed:21880710"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:6FDM"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6HK6"
FT HELIX 147..170
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:6FDM"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:6FDM"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:5DHF"
SQ SEQUENCE 552 AA; 63283 MW; 6EB260E72DDB78D7 CRC64;
MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPGSLIAS IASLKHGGCN KVLRELVKHK
LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ MGVGKESDIY IVANEEGQQF
ALKLHRLGRT SFRNLKNKRD YHKHRHNVSW LYLSRLSAMK EFAYMKALYE RKFPVPKPID
YNRHAVVMEL INGYPLCQIH HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDESD
HITMIDFPQM VSTSHPNAEW YFDRDVKCIK DFFMKRFSYE SELFPTFKDI RREDTLDVEV
SASGYTKEMQ ADDELLHPLG PDDKNIETKE GSEFSFSDGE VAEKAEVYGS ENESERNCLE
ESEGCYCRSS GDPEQIKEDS LSEESADARS FEMTEFNQAL EEIKGQVVEN NSVTEFSEEK
NRTENYNRQD GQRVQGGVPA GSDEYEDECP HLIALSSLNR EFRPFRDEEN VGAMNQYRTR
TLSITSSGSA VSCSTIPPEL VKQKVKRQLT KQQKSAVRRR LQKGEANIFT KQRRENMQNI
KSSLEAASFW GE
