RIOK1_MOUSE
ID RIOK1_MOUSE Reviewed; 567 AA.
AC Q922Q2; Q3U7D5; Q99LZ1; Q9CU84; Q9CXN9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine/threonine-protein kinase RIO1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BRS2};
DE EC=3.6.3.-;
DE AltName: Full=RIO kinase 1;
GN Name=Riok1;
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=Bone marrow macrophage, Embryonic head, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-567.
RC TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and 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: Involved in the final steps of cytoplasmic maturation of the
CC 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the
CC mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the
CC late 40S precursor (By similarity). The association with the very late
CC 40S subunit intermediate may involve a translation-like checkpoint
CC point cycle preceeding the binding to the 60S ribosomal subunit (By
CC similarity). Despite the protein kinase domain is proposed to act
CC predominantly as an ATPase (By similarity). The catalytic activity
CC regulates its dynamic association with the 40S subunit (By similarity).
CC In addition to its role in ribosomal biogenesis acts as an adapter
CC protein by recruiting NCL/nucleolin the to PRMT5 complex for its
CC symmetrical methylation (By similarity). {ECO:0000250|UniProtKB:G0S3J5,
CC ECO:0000250|UniProtKB:Q12196, ECO:0000250|UniProtKB:Q9BRS2}.
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:Q9BRS2};
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:Q9BRS2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BRS2, ECO:0000305};
CC -!- SUBUNIT: Associates with the precursor of the 40S ribosome subunit.
CC Interacts (via its N-terminus) with PRMT5 (via its N-terminus).
CC Interacts with WDR77 (By similarity). Found in a PRMT5 complex composed
CC of PRMT5, WDR77 and RIOK1 (By similarity). Interacts (via its C-
CC terminus) with NCL; this interaction targets NCL for PRTM5 methylation
CC (By similarity). {ECO:0000250|UniProtKB:Q9BRS2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BRS2}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29195.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB29195.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB29195.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB30687.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014182; BAB29195.1; ALT_SEQ; mRNA.
DR EMBL; AK017312; BAB30687.2; ALT_INIT; mRNA.
DR EMBL; AK152707; BAE31434.1; -; mRNA.
DR EMBL; AC140331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002158; AAH02158.1; ALT_INIT; mRNA.
DR CCDS; CCDS26461.1; -.
DR RefSeq; NP_077204.2; NM_024242.3.
DR AlphaFoldDB; Q922Q2; -.
DR SMR; Q922Q2; -.
DR BioGRID; 214650; 9.
DR IntAct; Q922Q2; 2.
DR MINT; Q922Q2; -.
DR STRING; 10090.ENSMUSP00000021866; -.
DR iPTMnet; Q922Q2; -.
DR PhosphoSitePlus; Q922Q2; -.
DR EPD; Q922Q2; -.
DR jPOST; Q922Q2; -.
DR MaxQB; Q922Q2; -.
DR PaxDb; Q922Q2; -.
DR PeptideAtlas; Q922Q2; -.
DR PRIDE; Q922Q2; -.
DR ProteomicsDB; 253290; -.
DR Antibodypedia; 24663; 208 antibodies from 30 providers.
DR DNASU; 71340; -.
DR Ensembl; ENSMUST00000021866; ENSMUSP00000021866; ENSMUSG00000021428.
DR GeneID; 71340; -.
DR KEGG; mmu:71340; -.
DR UCSC; uc007qdi.2; mouse.
DR CTD; 83732; -.
DR MGI; MGI:1918590; Riok1.
DR VEuPathDB; HostDB:ENSMUSG00000021428; -.
DR eggNOG; KOG2270; Eukaryota.
DR GeneTree; ENSGT00940000157075; -.
DR HOGENOM; CLU_018693_4_3_1; -.
DR InParanoid; Q922Q2; -.
DR OMA; QEINGCI; -.
DR OrthoDB; 1238900at2759; -.
DR PhylomeDB; Q922Q2; -.
DR TreeFam; TF105831; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 71340; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Riok1; mouse.
DR PRO; PR:Q922Q2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q922Q2; protein.
DR Bgee; ENSMUSG00000021428; Expressed in animal zygote and 255 other tissues.
DR ExpressionAtlas; Q922Q2; baseline and differential.
DR Genevisible; Q922Q2; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0034708; C:methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0030688; C:preribosome, small subunit precursor; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
DR PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrolase; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..567
FT /note="Serine/threonine-protein kinase RIO1"
FT /id="PRO_0000314490"
FT DOMAIN 179..478
FT /note="Protein kinase"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT ACT_SITE 340
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 436
FT /note="V -> E (in Ref. 1; BAB29195)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="E -> K (in Ref. 1; BAB29195)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="I -> V (in Ref. 3; AAH02158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 64910 MW; D2A1863DF0132366 CRC64;
MDCSLDRMAS VVPGQFDDAD SSDSENKELQ PIHAEDGGVL LKSLQNAAAE VKGDAETDEE
DDYDDDDDWY LDDATGKLTK GCTWNGGSNY QANRQTSNYN SAKMSTPIDK SLRKFENKIN
LNKLNVTDSV TNKVTVKLRQ KEAESYRIKD KADRATVEQV LDPRTRMILF KLLHKDHISE
IHGCISTGKE ANVYYASTPS GESRAIKIYK TSILMFKDRD KYVTGEFRFR RGYCKGNPRK
MVRTWAEKEM RNLCRLKTAN IPCPEPIRLR SHVLLMGFIG KDDMPAPLLK NVQLSESKAR
ELYLQVIQYM RKMYQDARLV HADLSEFNML YHGGDVYIID VSQSVEHDHP HALEFLRKDC
TNVNDFFSKH AVAVMTVREL FDFVTDPSIT ADNMDAYLEK AMEIASQRTK EEKTSQDHVD
EEVFKQAYIP RTLNEVKNYE RDVDIMMRLK EEDMALNTQQ DNILYQTVMG LKKDLSGVQK
VPALLESEVK EETCFGSDDA GGSECSDTVS EEQEDQAGCR NHIADPDIDK KERKKMVKEA
QREKRKNKIP KHVKKRKEKT AKAKKGK
