ID   RIOK2_MOUSE             Reviewed;         547 AA.
AC   Q9CQS5; Q91XF3;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Serine/threonine-protein kinase RIO2;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BVS4};
DE   AltName: Full=RIO kinase 2;
GN   Name=Riok2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-437, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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).
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. May regulate the timing of the metaphase-
CC       anaphase transition during mitotic progression, and its
CC       phosphorylation, may regulate this function.
CC       {ECO:0000250|UniProtKB:Q9BVS4}.
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:0000250|UniProtKB:Q9BVS4};
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:0000250|UniProtKB:Q9BVS4};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Associated with late 40S pre-ribosomal particles. Interacts
CC       with PLK1 (via its N-terminus). {ECO:0000250|UniProtKB:Q9BVS4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVS4}.
CC   -!- PTM: Autophosphorylated (in vitro). Phosphorylation affects the timing
CC       of the metaphase-anaphase transition. {ECO:0000250|UniProtKB:Q9BVS4}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AK008385; BAB25639.1; -; mRNA.
DR   EMBL; AK008451; BAB25676.1; -; mRNA.
DR   EMBL; AK049232; BAC33625.1; -; mRNA.
DR   EMBL; BC010781; AAH10781.1; -; mRNA.
DR   CCDS; CCDS28417.1; -.
DR   RefSeq; NP_080210.1; NM_025934.2.
DR   AlphaFoldDB; Q9CQS5; -.
DR   SMR; Q9CQS5; -.
DR   BioGRID; 211899; 4.
DR   IntAct; Q9CQS5; 3.
DR   STRING; 10090.ENSMUSP00000024620; -.
DR   iPTMnet; Q9CQS5; -.
DR   PhosphoSitePlus; Q9CQS5; -.
DR   EPD; Q9CQS5; -.
DR   MaxQB; Q9CQS5; -.
DR   PeptideAtlas; Q9CQS5; -.
DR   ProteomicsDB; 255151; -.
DR   Pumba; Q9CQS5; -.
DR   Antibodypedia; 13276; 371 antibodies from 27 providers.
DR   DNASU; 67045; -.
DR   Ensembl; ENSMUST00000024620.8; ENSMUSP00000024620.7; ENSMUSG00000116564.2.
DR   GeneID; 67045; -.
DR   KEGG; mmu:67045; -.
DR   UCSC; uc008apd.2; mouse.
DR   AGR; MGI:1914295; -.
DR   CTD; 55781; -.
DR   MGI; MGI:1914295; Riok2.
DR   VEuPathDB; HostDB:ENSMUSG00000116564; -.
DR   GeneTree; ENSGT00390000003255; -.
DR   HOGENOM; CLU_018693_0_3_1; -.
DR   InParanoid; Q9CQS5; -.
DR   OMA; TSHHNAE; -.
DR   OrthoDB; 21899at2759; -.
DR   PhylomeDB; Q9CQS5; -.
DR   TreeFam; TF321400; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 67045; 13 hits in 33 CRISPR screens.
DR   ChiTaRS; Riok2; mouse.
DR   PRO; PR:Q9CQS5; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9CQS5; Protein.
DR   Bgee; ENSMUSG00000116564; Expressed in optic fissure and 263 other cell types or tissues.
DR   ExpressionAtlas; Q9CQS5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; ISO:MGI.
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:0030490; P:maturation of SSU-rRNA; ISO:MGI.
DR   GO; GO:2000208; P:positive regulation of ribosomal small subunit export from nucleus; ISO:MGI.
DR   GO; GO:2000234; P:positive regulation of rRNA processing; ISO:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:MGI.
DR   CDD; cd05144; RIO2_C; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR   PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR   Pfam; PF01163; RIO1; 1.
DR   Pfam; PF09202; Rio2_N; 1.
DR   SMART; SM00090; RIO; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01245; RIO1; 1.
DR   Genevisible; Q9CQS5; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..547
FT                   /note="Serine/threonine-protein kinase RIO2"
FT                   /id="PRO_0000213528"
FT   DOMAIN          97..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000305"
FT   REGION          352..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           399..408
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   COMPBIAS        404..426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BVS4"
FT   CONFLICT        369
FT                   /note="S -> L (in Ref. 2; AAH10781)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379..380
FT                   /note="GG -> DS (in Ref. 2; AAH10781)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="E -> D (in Ref. 2; AAH10781)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  62490 MW;  61A50648147B8850 CRC64;
     MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPCSLIAS IASLKHGGCN KILRELVKHK
     LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ MGVGKESDIY IVANEAGQQL
     ALKLHRLGRT SFRNLKNKRD YHKHRHNVSW LYLSRLSAMK EFAYMKALYE RKFPVPKPID
     YNRHAVIMEL INGYPLCQIH HVEDPASVYD EAMELIVKLG NHGLIHGDFN EFNLMLDKDD
     HITMIDFPQM VSTSHPNAEW YFDRDVKCIR EFFMKRFSYE SELYPTFSDI RKEDSLDVEV
     SASGYTKEMQ ADDELLHPVG PDDKITETEE DSDFTFSDEE MLEKAKVWRS ELEKEADPAD
     ESGGSWCCSS TDSKQIKDGG LPEESAHVSS FEVTALSQAV EEMERQVLPH RSVTEFSEES
     RRTENDGQPG QRSPAGSEDC DDEPPHLIAL SSVNREFRPF RDEESMSSVT RHRTRTLSVT
     SAGSALSCST IPPELVKQKV KRQLTRQQKA AARRRLQKGE ANVFTKQRRE NMQNIKSSLE
     AASFWGD
//