RIOK1_HUMAN
ID RIOK1_HUMAN Reviewed; 568 AA.
AC Q9BRS2; B2RB28; Q8NDC8; Q96NV9;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase RIO1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:22072790};
DE EC=3.6.3.-;
DE AltName: Full=RIO kinase 1;
GN Name=RIOK1 {ECO:0000312|HGNC:HGNC:18656}; Synonyms=RIO1;
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].
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-568.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PROTEIN SEQUENCE OF 156-165; 191-205; 212-218; 380-401 AND 482-493, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-22, AND
RP IDENTIFICATION BY MASS 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 [9]
RP 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 [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 SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRMT5 AND NCL,
RP IDENTIFICATION IN A COMPLEX WITH PRTM5; WDR77 AND RIOK1, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND FUNCTION.
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 [12]
RP IDENTIFICATION BY 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 [13]
RP FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF ASP-324.
RX PubMed=22072790; DOI=10.1091/mbc.e11-07-0639;
RA Widmann B., Wandrey F., Badertscher L., Wyler E., Pfannstiel J., Zemp I.,
RA Kutay U.;
RT "The kinase activity of human Rio1 is required for final steps of
RT cytoplasmic maturation of 40S subunits.";
RL Mol. Biol. Cell 23:22-35(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 143-494 IN COMPLEX WITH ADP, AND
RP COFACTOR.
RX PubMed=24948609; DOI=10.1093/nar/gku542;
RA Ferreira-Cerca S., Kiburu I., Thomson E., LaRonde N., Hurt E.;
RT "Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-
RT 40S biogenesis factors in 80S-like ribosomes.";
RL Nucleic Acids Res. 42:8635-8647(2014).
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 (PubMed:22072790). The association with the very
CC late 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 (PubMed:21081503).
CC {ECO:0000250|UniProtKB:G0S3J5, ECO:0000250|UniProtKB:Q12196,
CC ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:22072790}.
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:22072790};
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:22072790};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24948609, 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 (PubMed:22072790, PubMed:21081503). Interacts with WDR77
CC (PubMed:22072790). Found in a PRMT5 complex composed of PRMT5, WDR77
CC and RIOK1 (PubMed:21081503). Interacts (via its C-terminus) with NCL;
CC this interaction targets NCL for PRTM5 methylation (PubMed:21081503).
CC {ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:22072790}.
CC -!- INTERACTION:
CC Q9BRS2; O14744: PRMT5; NbExp=5; IntAct=EBI-7307838, EBI-351098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21081503}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; AK054568; BAB70761.1; -; mRNA.
DR EMBL; AK314467; BAG37075.1; -; mRNA.
DR EMBL; CH471087; EAW55210.1; -; Genomic_DNA.
DR EMBL; BC006104; AAH06104.2; -; mRNA.
DR EMBL; AL834277; CAD38952.1; -; mRNA.
DR CCDS; CCDS4500.1; -.
DR RefSeq; NP_113668.2; NM_031480.2.
DR PDB; 4OTP; X-ray; 2.70 A; A=143-494.
DR PDB; 6G5I; EM; 3.50 A; z=1-568.
DR PDB; 6V0N; X-ray; 2.11 A; C=11-23.
DR PDB; 6ZV6; EM; 2.90 A; h=1-568.
DR PDB; 6ZXD; EM; 3.20 A; z=1-568.
DR PDB; 6ZXE; EM; 3.00 A; z=1-568.
DR PDB; 6ZXF; EM; 3.70 A; z=1-568.
DR PDB; 6ZXG; EM; 2.60 A; z=1-568.
DR PDB; 6ZXH; EM; 2.70 A; z=1-568.
DR PDB; 7BOC; X-ray; 2.55 A; B=9-23.
DR PDBsum; 4OTP; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6V0N; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7BOC; -.
DR AlphaFoldDB; Q9BRS2; -.
DR SMR; Q9BRS2; -.
DR BioGRID; 123743; 518.
DR IntAct; Q9BRS2; 42.
DR MINT; Q9BRS2; -.
DR STRING; 9606.ENSP00000369162; -.
DR BindingDB; Q9BRS2; -.
DR ChEMBL; CHEMBL5975; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9BRS2; -.
DR iPTMnet; Q9BRS2; -.
DR MetOSite; Q9BRS2; -.
DR PhosphoSitePlus; Q9BRS2; -.
DR BioMuta; RIOK1; -.
DR DMDM; 56404949; -.
DR EPD; Q9BRS2; -.
DR jPOST; Q9BRS2; -.
DR MassIVE; Q9BRS2; -.
DR MaxQB; Q9BRS2; -.
DR PaxDb; Q9BRS2; -.
DR PeptideAtlas; Q9BRS2; -.
DR PRIDE; Q9BRS2; -.
DR ProteomicsDB; 78823; -.
DR Antibodypedia; 24663; 208 antibodies from 30 providers.
DR DNASU; 83732; -.
DR Ensembl; ENST00000379834.7; ENSP00000369162.2; ENSG00000124784.9.
DR GeneID; 83732; -.
DR KEGG; hsa:83732; -.
DR MANE-Select; ENST00000379834.7; ENSP00000369162.2; NM_031480.3; NP_113668.2.
DR UCSC; uc003mxn.4; human.
DR CTD; 83732; -.
DR DisGeNET; 83732; -.
DR GeneCards; RIOK1; -.
DR HGNC; HGNC:18656; RIOK1.
DR HPA; ENSG00000124784; Low tissue specificity.
DR MIM; 617753; gene.
DR neXtProt; NX_Q9BRS2; -.
DR OpenTargets; ENSG00000124784; -.
DR PharmGKB; PA134928236; -.
DR VEuPathDB; HostDB:ENSG00000124784; -.
DR eggNOG; KOG2270; Eukaryota.
DR GeneTree; ENSGT00940000157075; -.
DR HOGENOM; CLU_018693_4_3_1; -.
DR InParanoid; Q9BRS2; -.
DR OMA; QEINGCI; -.
DR OrthoDB; 1238900at2759; -.
DR PhylomeDB; Q9BRS2; -.
DR TreeFam; TF105831; -.
DR PathwayCommons; Q9BRS2; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9BRS2; -.
DR BioGRID-ORCS; 83732; 778 hits in 1114 CRISPR screens.
DR ChiTaRS; RIOK1; human.
DR GenomeRNAi; 83732; -.
DR Pharos; Q9BRS2; Tchem.
DR PRO; PR:Q9BRS2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BRS2; protein.
DR Bgee; ENSG00000124784; Expressed in epithelial cell of pancreas and 164 other tissues.
DR ExpressionAtlas; Q9BRS2; baseline and differential.
DR Genevisible; Q9BRS2; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034708; C:methyltransferase complex; IMP:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
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 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..568
FT /note="Serine/threonine-protein kinase RIO1"
FT /id="PRO_0000213526"
FT DOMAIN 180..479
FT /note="Protein kinase"
FT REGION 14..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..568
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:22072790,
FT ECO:0000305|PubMed:24948609"
FT ACT_SITE 341
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24948609,
FT ECO:0007744|PDB:4OTP"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 375
FT /note="V -> I (in dbSNP:rs56067778)"
FT /id="VAR_061777"
FT MUTAGEN 324
FT /note="D->A: Abolishes autophosphorylation activity;
FT enhances association with pre-40S ribosomal subunits;
FT inhibits processing of 18S-E pre-rRNA to the mature 18S
FT rRNA."
FT /evidence="ECO:0000269|PubMed:22072790"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:6V0N"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6ZXD"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:6ZXD"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6ZXH"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 239..259
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 297..316
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 552..558
FT /evidence="ECO:0007829|PDB:6ZXG"
SQ SEQUENCE 568 AA; 65583 MW; 5730BFC3798F5190 CRC64;
MDYRRLLMSR VVPGQFDDAD SSDSENRDLK TVKEKDDILF EDLQDNVNEN GEGEIEDEEE
EGYDDDDDDW DWDEGVGKLA KGYVWNGGSN PQANRQTSDS SSAKMSTPAD KVLRKFENKI
NLDKLNVTDS VINKVTEKSR QKEADMYRIK DKADRATVEQ VLDPRTRMIL FKMLTRGIIT
EINGCISTGK EANVYHASTA NGESRAIKIY KTSILVFKDR DKYVSGEFRF RHGYCKGNPR
KMVKTWAEKE MRNLIRLNTA EIPCPEPIML RSHVLVMSFI GKDDMPAPLL KNVQLSESKA
RELYLQVIQY MRRMYQDARL VHADLSEFNM LYHGGGVYII DVSQSVEHDH PHALEFLRKD
CANVNDFFMR HSVAVMTVRE LFEFVTDPSI THENMDAYLS KAMEIASQRT KEERSSQDHV
DEEVFKRAYI PRTLNEVKNY ERDMDIIMKL KEEDMAMNAQ QDNILYQTVT GLKKDLSGVQ
KVPALLENQV EERTCSDSED IGSSECSDTD SEEQGDHARP KKHTTDPDID KKERKKMVKE
AQREKRKNKI PKHVKKRKEK TAKTKKGK
