CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007278
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase RIO2 
Protein Synonyms/Alias
  
Gene Name
 RIO2 
Gene Synonyms/Alias
 YNL207W; N1342 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
69ISKMRNVKYDGYRLTacetylation[1]
86GIDYLALKTMLNRDTubiquitination[2]
175MLYSKGFKVPEPFDNubiquitination[2]
415SSGVENLKMDKLGNYubiquitination[2]
418VENLKMDKLGNYILEacetylation[1]
418VENLKMDKLGNYILEubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Required for the final endonucleolytic cleavage of 20S pre-rRNA at site D in the cytoplasm, converting it into the mature 18S rRNA. Involved in normal export of the pre-40S particles from the nucleus to the cytoplasm. No longer associates with pre-40S subunits in RPS19 disruptions, suggesting it acts after the ribosomal protein in 18S rRNA maturation. 
Sequence Annotation
 DOMAIN 95 257 Protein kinase.
 ACT_SITE 229 229 Proton acceptor (By similarity).
 BINDING 123 123 ATP (By similarity).
 MOD_RES 346 346 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 425 AA 
Protein Sequence
MKLDTSHMRY LTTDDFRVLQ AVEQGSRSHE VVPTPLIHQI SGMRSQSGTN RAISDLAKLS 60
LISKMRNVKY DGYRLTYNGI DYLALKTMLN RDTVYSVGNT IGVGKESDIY KVSDKNGNPR 120
VMKIHRLGRT SFHSVRNNRD YLKKSNQGAN WMHLSRLAAN KEYQFMSMLY SKGFKVPEPF 180
DNSRHIVVME LIEGYPMRRL RKHKNIPKLY SDLMCFIVDL ANSGLIHCDF NEFNIMIKDK 240
LEDENDCGFV VIDFPQCISI QHQDADYYFQ RDVDCIRRFF KKKLKYEPKP DSSMLDTEGF 300
GDGYKYAYPD FKRDVKRTDN LDELVQASGF SKKHPGDRGL ETAVESMRNA VYNSDDDMSN 360
DEAEEENGEG DYSEEDEYYD SELDNESSED DSEDAQEEEN ERIIEALSSG VENLKMDKLG 420
NYILE 425 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005487; F:nucleocytoplasmic transporter activity; IGI:SGD.
 GO:0004672; F:protein kinase activity; IDA:SGD.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
 GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR018934; RIO-like_kinase.
 IPR015285; RIO2_kinase_winged_hlx_N.
 IPR000687; RIO_kinase.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01163; RIO1
 PF09202; Rio2_N 
SMART
 SM00090; RIO 
PROSITE
 PS50011; PROTEIN_KINASE_DOM
 PS01245; RIO1 
PRINTS