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0RIOK1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRIOK1
DescriptionSerine/threonine-protein kinase rio1 (ec 2.7.1.37) (rio kinase 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
RIO kinases exhibit little sequence similarity with eukaryotic protein kinases.nd are classified as atypical protein kinases . The conformation of ATP when bound to the RIO kinases is unique when compared with ePKs.uch as serine/threonine kinases or the insulin receptor tyrosine kinase.uggesting that the detailed mechanism by which the catalytic aspartate of RIO kinases participates in phosphoryl transfer may not be identical to that employed in known serine/threonine ePKs. Representatives of the RIO family are present in organisms varying from Archaea to humans.lthough the RIO3 proteins have only been identified in multicellular eukaryotes.o date. Yeast Rio1 and Rio2 proteins are required for proper cell cycle progression and chromosome maintenance.nd are necessary for survival of the cells. These proteins are involved in the processing of 20 S pre-rRNA via late 18 S rRNA processing.
  IPR000687:RIO kinase
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
IPR000687:RIO 
Evalue:-136.602059991328 
Location:151-387IPR000719:PROTEIN_KINASE_DOM 
Evalue:0 
Location:0-0
SequencesProtein: RIOK1_HUMAN (568 aa)
mRNA: NM_031480
Local Annotation
Synapse Ontology
?
sdb:0297 NMDA receptor  (Evidence:keywords)
KO assignmentK07178
  Level 3 annotation:
    RIO-type serine/threonine protein kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 82 residues, 7335060-7335305Exon2: 70 residues, 7338330-7338535Exon3: 32 residues, 7340284-7340375Exon4: 25 residues, 7341934-7342004Exon5: 16 residues, 7343929-7343972Exon6: 33 residues, 7346189-7346282Exon7: 39 residues, 7347834-7347947Exon8: 29 residues, 7348048-7348129Exon9: 31 residues, 7349172-7349259Exon10: 48 residues, 7349649-7349787Exon11: 36 residues, 7350149-7350253Exon12: 37 residues, 7350480-7350587Exon13: 24 residues, 7355617-7355683Exon14: 42 residues, 7356563-7356683Exon15: 20 residues, 7358120-7358174Exon16: 53 residues, 7359469-7359622Exon17: 237 residues, 7362562-7363267Exon18: 2 residues, -Jump to RIOK1_HUMAN  
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Loci Cluster (Details)Loci: 3520 7486868-7531945 ~-45K 30281(DSP)(+)Loci: 3519 7335060-7363267 ~-28K 30277(RIOK1)(+)Link out to UCSC