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 Genevisible; Q9CQS5; MM.
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.
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
//
