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Q9BVS4 (RIOK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase RIO2

EC=2.7.11.1
Alternative name(s):
RIO kinase 2
Gene names
Name:RIOK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Sequence similarities

Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.

Contains 1 protein kinase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BVS4-1)

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.
Isoform 2 (identifier: Q9BVS4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     467-552: DEENVGAMNQ...SLEAASFWGE → YRLLSIAF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Serine/threonine-protein kinase RIO2
PRO_0000213527

Regions

Domain271 – 552282Protein kinase

Sites

Active site2281Proton acceptor By similarity
Binding site1231ATP By similarity

Amino acid modifications

Modified residue3321Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11
Modified residue3351Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11
Modified residue3371Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.13
Modified residue3501Phosphoserine Ref.7
Modified residue3621Phosphoserine Ref.9
Modified residue3801Phosphoserine Ref.7 Ref.10
Modified residue3821Phosphoserine Ref.7 Ref.10
Modified residue3851Phosphoserine Ref.7 Ref.9 Ref.10
Modified residue3901Phosphoserine Ref.5 Ref.6 Ref.9 Ref.10
Modified residue4121Phosphoserine Ref.11
Modified residue4171Phosphoserine Ref.6
Modified residue4421Phosphoserine Ref.6 Ref.7 Ref.9
Modified residue4451Phosphotyrosine Ref.9

Natural variations

Alternative sequence467 – 55286DEENV…SFWGE → YRLLSIAF in isoform 2.
VSP_046388
Natural variant961S → C. Ref.15
Corresponds to variant rs2544773 [ dbSNP | Ensembl ].
VAR_042347
Natural variant1441H → R. Ref.15
Corresponds to variant rs35165987 [ dbSNP | Ensembl ].
VAR_042348
Natural variant1441H → Y. Ref.4
Corresponds to variant rs17849382 [ dbSNP | Ensembl ].
VAR_031597
Natural variant1551R → H. Ref.15
Corresponds to variant rs34916955 [ dbSNP | Ensembl ].
VAR_042349
Natural variant1751V → I. Ref.15
Corresponds to variant rs35713904 [ dbSNP | Ensembl ].
VAR_042350
Natural variant2161I → T in a renal clear cell carcinoma sample; somatic mutation. Ref.15
VAR_042351
Natural variant2441M → V. Ref.15
Corresponds to variant rs33996030 [ dbSNP | Ensembl ].
VAR_042352
Natural variant3491G → R. Ref.1 Ref.15
Corresponds to variant rs160632 [ dbSNP | Ensembl ].
VAR_031598
Natural variant3971N → S. Ref.15
Corresponds to variant rs12188395 [ dbSNP | Ensembl ].
VAR_031599
Natural variant4091E → D. Ref.15
Corresponds to variant rs35829000 [ dbSNP | Ensembl ].
VAR_042353
Natural variant5071R → H. Ref.15
Corresponds to variant rs34555783 [ dbSNP | Ensembl ].
VAR_042354

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 6EB260E72DDB78D7

FASTA55263,283
        10         20         30         40         50         60 
MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPGSLIAS IASLKHGGCN KVLRELVKHK 

        70         80         90        100        110        120 
LIAWERTKTV QGYRLTNAGY DYLALKTLSS RQVVESVGNQ MGVGKESDIY IVANEEGQQF 

       130        140        150        160        170        180 
ALKLHRLGRT SFRNLKNKRD YHKHRHNVSW LYLSRLSAMK EFAYMKALYE RKFPVPKPID 

       190        200        210        220        230        240 
YNRHAVVMEL INGYPLCQIH HVEDPASVYD EAMELIVKLA NHGLIHGDFN EFNLILDESD 

       250        260        270        280        290        300 
HITMIDFPQM VSTSHPNAEW YFDRDVKCIK DFFMKRFSYE SELFPTFKDI RREDTLDVEV 

       310        320        330        340        350        360 
SASGYTKEMQ ADDELLHPLG PDDKNIETKE GSEFSFSDGE VAEKAEVYGS ENESERNCLE 

       370        380        390        400        410        420 
ESEGCYCRSS GDPEQIKEDS LSEESADARS FEMTEFNQAL EEIKGQVVEN NSVTEFSEEK 

       430        440        450        460        470        480 
NRTENYNRQD GQRVQGGVPA GSDEYEDECP HLIALSSLNR EFRPFRDEEN VGAMNQYRTR 

       490        500        510        520        530        540 
TLSITSSGSA VSCSTIPPEL VKQKVKRQLT KQQKSAVRRR LQKGEANIFT KQRRENMQNI 

       550 
KSSLEAASFW GE 

« Hide

Isoform 2 [UniParc].

Checksum: 4B396021BE81BE84
Show »

FASTA47454,508

References

[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-349.
Tissue: Placenta.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hepatoma.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-144.
Tissue: Placenta.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337; SER-390; SER-417 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-380; SER-382; SER-385 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337; SER-362; SER-385; SER-390; SER-442 AND TYR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337; SER-380; SER-382; SER-385 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-96; ARG-144; HIS-155; ILE-175; THR-216; VAL-244; ARG-349; SER-397; ASP-409 AND HIS-507.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4089.1. [Q9BVS4-1]
CCDS54884.1. [Q9BVS4-2]
RefSeqNP_001153221.1. NM_001159749.1. [Q9BVS4-2]
NP_060813.2. NM_018343.2. [Q9BVS4-1]
UniGeneHs.27021.

3D structure databases

ProteinModelPortalQ9BVS4.
SMRQ9BVS4. Positions 3-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120896. 271 interactions.
IntActQ9BVS4. 18 interactions.
STRING9606.ENSP00000283109.

Chemistry

BindingDBQ9BVS4.
ChEMBLCHEMBL6000.
GuidetoPHARMACOLOGY2187.

PTM databases

PhosphoSiteQ9BVS4.

Polymorphism databases

DMDM143811448.

Proteomic databases

MaxQBQ9BVS4.
PaxDbQ9BVS4.
PRIDEQ9BVS4.

Protocols and materials databases

DNASU55781.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283109; ENSP00000283109; ENSG00000058729. [Q9BVS4-1]
ENST00000508447; ENSP00000420932; ENSG00000058729. [Q9BVS4-2]
GeneID55781.
KEGGhsa:55781.
UCSCuc003kmz.3. human. [Q9BVS4-1]

Organism-specific databases

CTD55781.
GeneCardsGC05M096496.
HGNCHGNC:18999. RIOK2.
HPAHPA005681.
neXtProtNX_Q9BVS4.
PharmGKBPA134885533.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0478.
HOGENOMHOG000225685.
HOVERGENHBG056045.
InParanoidQ9BVS4.
KOK07179.
OMAVAKLRYM.
OrthoDBEOG754HP9.
PhylomeDBQ9BVS4.
TreeFamTF321400.

Gene expression databases

ArrayExpressQ9BVS4.
BgeeQ9BVS4.
CleanExHS_RIOK2.
GenevestigatorQ9BVS4.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR015285. RIO2_kinase_winged_hlx_N.
IPR018935. RIO_kinase_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01163. RIO1. 1 hit.
PF09202. Rio2_N. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01245. RIO1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi55781.
NextBio60867.
PROQ9BVS4.

Entry information

Entry nameRIOK2_HUMAN
AccessionPrimary (citable) accession number: Q9BVS4
Secondary accession number(s): D6RDI3, Q9NUT0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM