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Protein

Serine/threonine-protein kinase RIO2

Gene

RIOK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123ATPBy similarity1
Active sitei228Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • maturation of SSU-rRNA Source: UniProtKB
  • positive regulation of ribosomal small subunit export from nucleus Source: UniProtKB
  • positive regulation of rRNA processing Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of mitotic metaphase/anaphase transition Source: UniProtKB
  • ribosomal small subunit biogenesis Source: UniProtKB
  • rRNA processing Source: Reactome

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Ribosome biogenesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RIO2 (EC:2.7.11.12 Publications)
Alternative name(s):
RIO kinase 2
Gene namesi
Name:RIOK2Imported
Synonyms:RIO21 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000058729.10.
HGNCiHGNC:18999. RIOK2.
MIMi617754. gene.
neXtProtiNX_Q9BVS4.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123K → A: Abolishes autophosphorylation; impairs release of pre-40S trans-acting factors and rRNA processing; when associated with A-246. 1 Publication1
Mutagenesisi246D → A: Abolishes autophosphorylation; impairs release of pre-40S trans-acting factors and rRNA processing; when associated with A-123. 1 Publication1
Mutagenesisi335S → A: Does not affect autophosphorylation activity; when associated with A-380 and A-548. Does not affect the timing of metaphase-anaphase transition; when associated with A-380 and A-548. 1 Publication1
Mutagenesisi335S → D: Increases time spent in metaphase; when associated with D-380 and D-548. 1 Publication1
Mutagenesisi380S → A: Does not affect autophosphorylation activity; when associated with A-335 and A-548. Does not affect the timing of metaphase-anaphase transition; when associated with A-335 and A-548. 1 Publication1
Mutagenesisi380S → D: Increases time spent in metaphase; when associated with D-335 and D-548. 1 Publication1
Mutagenesisi400L → A: Nuclear relocalization; when associated with A-403. 1 Publication1
Mutagenesisi403I → A: Nuclear relocalization; when associated with A-400. 1 Publication1
Mutagenesisi548S → A: Does not affect autophosphorylation activity; when associated with A-335 and A-380. Does not affect the timing of metaphase-anaphase transition; when associated with A-335 and A-380. 1 Publication1
Mutagenesisi548S → D: Increases time spent in metaphase; when associated with D-335 and D-380. 1 Publication1

Organism-specific databases

DisGeNETi55781.
OpenTargetsiENSG00000058729.
PharmGKBiPA134885533.

Chemistry databases

ChEMBLiCHEMBL6000.
GuidetoPHARMACOLOGYi2187.

Polymorphism and mutation databases

BioMutaiRIOK2.
DMDMi143811448.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002135271 – 552Serine/threonine-protein kinase RIO2Add BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei332PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1 Publication1
Modified residuei337PhosphoserineCombined sources1
Modified residuei350PhosphoserineCombined sources1
Modified residuei362PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1 Publication1
Modified residuei382PhosphoserineCombined sources1
Modified residuei385PhosphoserineCombined sources1
Modified residuei390PhosphoserineCombined sources1
Modified residuei412PhosphoserineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei442PhosphoserineCombined sources1
Modified residuei445PhosphotyrosineCombined sources1
Modified residuei548Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylated (in vitro) (PubMed:19564402, PubMed:21880710). Phosphorylation at Ser-335, Ser-380, Ser-548 by PLK1 affects the timing of the metaphase-anaphase transition (PubMed:21880710).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BVS4.
MaxQBiQ9BVS4.
PaxDbiQ9BVS4.
PeptideAtlasiQ9BVS4.
PRIDEiQ9BVS4.

PTM databases

iPTMnetiQ9BVS4.
PhosphoSitePlusiQ9BVS4.

Expressioni

Gene expression databases

BgeeiENSG00000058729.
CleanExiHS_RIOK2.
ExpressionAtlasiQ9BVS4. baseline and differential.
GenevisibleiQ9BVS4. HS.

Organism-specific databases

HPAiHPA005681.

Interactioni

Subunit structurei

Associated with late 40S pre-ribosomal particles (PubMed:16037817, PubMed:21081503). Interacts with PLK1 (via its N-terminus) (PubMed:21880710).2 Publications

Protein-protein interaction databases

BioGridi120896. 31 interactors.
IntActiQ9BVS4. 24 interactors.
STRINGi9606.ENSP00000283109.

Chemistry databases

BindingDBiQ9BVS4.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi394 – 400Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DHFX-ray2.29D389-403[»]
ProteinModelPortaliQ9BVS4.
SMRiQ9BVS4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini97 – 272Protein kinaseCuratedAdd BLAST176

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi399 – 408Nuclear export signal1 Publication10

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2268. Eukaryota.
COG0478. LUCA.
GeneTreeiENSGT00390000003255.
HOGENOMiHOG000225685.
HOVERGENiHBG056045.
InParanoidiQ9BVS4.
KOiK07179.
OMAiVDYNRHA.
OrthoDBiEOG091G06ON.
PhylomeDBiQ9BVS4.
TreeFamiTF321400.

Family and domain databases

CDDicd05144. RIO2_C. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom_sf.
IPR030484. Rio2.
IPR015285. RIO2_wHTH_N.
IPR000687. RIO_kinase.
IPR018935. RIO_kinase_CS.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF09202. Rio2_N. 1 hit.
SMARTiView protein in SMART
SM00090. RIO. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS01245. RIO1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BVS4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPGSLIAS IASLKHGGCN
60 70 80 90 100
KVLRELVKHK LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ
110 120 130 140 150
MGVGKESDIY IVANEEGQQF ALKLHRLGRT SFRNLKNKRD YHKHRHNVSW
160 170 180 190 200
LYLSRLSAMK EFAYMKALYE RKFPVPKPID YNRHAVVMEL INGYPLCQIH
210 220 230 240 250
HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDESD HITMIDFPQM
260 270 280 290 300
VSTSHPNAEW YFDRDVKCIK DFFMKRFSYE SELFPTFKDI RREDTLDVEV
310 320 330 340 350
SASGYTKEMQ ADDELLHPLG PDDKNIETKE GSEFSFSDGE VAEKAEVYGS
360 370 380 390 400
ENESERNCLE ESEGCYCRSS GDPEQIKEDS LSEESADARS FEMTEFNQAL
410 420 430 440 450
EEIKGQVVEN NSVTEFSEEK NRTENYNRQD GQRVQGGVPA GSDEYEDECP
460 470 480 490 500
HLIALSSLNR EFRPFRDEEN VGAMNQYRTR TLSITSSGSA VSCSTIPPEL
510 520 530 540 550
VKQKVKRQLT KQQKSAVRRR LQKGEANIFT KQRRENMQNI KSSLEAASFW

GE
Length:552
Mass (Da):63,283
Last modified:April 3, 2007 - v2
Checksum:i6EB260E72DDB78D7
GO
Isoform 2 (identifier: Q9BVS4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     467-552: DEENVGAMNQ...SLEAASFWGE → YRLLSIAF

Note: No experimental confirmation available.
Show »
Length:474
Mass (Da):54,508
Checksum:i4B396021BE81BE84
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04234796S → C1 PublicationCorresponds to variant dbSNP:rs2544773Ensembl.1
Natural variantiVAR_042348144H → R1 PublicationCorresponds to variant dbSNP:rs35165987Ensembl.1
Natural variantiVAR_031597144H → Y1 PublicationCorresponds to variant dbSNP:rs17849382Ensembl.1
Natural variantiVAR_042349155R → H1 PublicationCorresponds to variant dbSNP:rs34916955Ensembl.1
Natural variantiVAR_042350175V → I1 PublicationCorresponds to variant dbSNP:rs35713904Ensembl.1
Natural variantiVAR_042351216I → T in a renal clear cell carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs147608663Ensembl.1
Natural variantiVAR_042352244M → V1 PublicationCorresponds to variant dbSNP:rs33996030Ensembl.1
Natural variantiVAR_031598349G → R2 PublicationsCorresponds to variant dbSNP:rs160632Ensembl.1
Natural variantiVAR_031599397N → S1 PublicationCorresponds to variant dbSNP:rs12188395Ensembl.1
Natural variantiVAR_042353409E → D1 PublicationCorresponds to variant dbSNP:rs35829000Ensembl.1
Natural variantiVAR_042354507R → H1 PublicationCorresponds to variant dbSNP:rs34555783Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046388467 – 552DEENV…SFWGE → YRLLSIAF in isoform 2. 1 PublicationAdd BLAST86

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002021 mRNA. Translation: BAA92040.1.
AK225348 mRNA. No translation available.
AC008865 Genomic DNA. No translation available.
AC008883 Genomic DNA. No translation available.
BC000953 mRNA. Translation: AAH00953.1.
CCDSiCCDS4089.1. [Q9BVS4-1]
CCDS54884.1. [Q9BVS4-2]
RefSeqiNP_001153221.1. NM_001159749.1. [Q9BVS4-2]
NP_060813.2. NM_018343.2. [Q9BVS4-1]
UniGeneiHs.27021.

Genome annotation databases

EnsembliENST00000283109; ENSP00000283109; ENSG00000058729. [Q9BVS4-1]
ENST00000508447; ENSP00000420932; ENSG00000058729. [Q9BVS4-2]
GeneIDi55781.
KEGGihsa:55781.
UCSCiuc003kmz.4. human. [Q9BVS4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRIOK2_HUMAN
AccessioniPrimary (citable) accession number: Q9BVS4
Secondary accession number(s): D6RDI3, Q9NUT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: April 3, 2007
Last modified: February 28, 2018
This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome