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Q9BRS2 (RIOK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase RIO1

EC=2.7.11.1
Alternative name(s):
RIO kinase 1
Gene names
Name:RIOK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length568 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Serine/threonine-protein kinase RIO1
PRO_0000213526

Regions

Domain180 – 479300Protein kinase

Sites

Active site3241Proton acceptor By similarity
Binding site2081ATP By similarity

Amino acid modifications

Modified residue211Phosphoserine Ref.8
Modified residue221Phosphoserine Ref.8

Natural variations

Natural variant3751V → I.
Corresponds to variant rs56067778 [ dbSNP | Ensembl ].
VAR_061777

Sequences

Sequence LengthMass (Da)Tools
Q9BRS2 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 5730BFC3798F5190

FASTA56865,583
        10         20         30         40         50         60 
MDYRRLLMSR VVPGQFDDAD SSDSENRDLK TVKEKDDILF EDLQDNVNEN GEGEIEDEEE 

        70         80         90        100        110        120 
EGYDDDDDDW DWDEGVGKLA KGYVWNGGSN PQANRQTSDS SSAKMSTPAD KVLRKFENKI 

       130        140        150        160        170        180 
NLDKLNVTDS VINKVTEKSR QKEADMYRIK DKADRATVEQ VLDPRTRMIL FKMLTRGIIT 

       190        200        210        220        230        240 
EINGCISTGK EANVYHASTA NGESRAIKIY KTSILVFKDR DKYVSGEFRF RHGYCKGNPR 

       250        260        270        280        290        300 
KMVKTWAEKE MRNLIRLNTA EIPCPEPIML RSHVLVMSFI GKDDMPAPLL KNVQLSESKA 

       310        320        330        340        350        360 
RELYLQVIQY MRRMYQDARL VHADLSEFNM LYHGGGVYII DVSQSVEHDH PHALEFLRKD 

       370        380        390        400        410        420 
CANVNDFFMR HSVAVMTVRE LFEFVTDPSI THENMDAYLS KAMEIASQRT KEERSSQDHV 

       430        440        450        460        470        480 
DEEVFKRAYI PRTLNEVKNY ERDMDIIMKL KEEDMAMNAQ QDNILYQTVT GLKKDLSGVQ 

       490        500        510        520        530        540 
KVPALLENQV EERTCSDSED IGSSECSDTD SEEQGDHARP KKHTTDPDID KKERKKMVKE 

       550        560 
AQREKRKNKI PKHVKKRKEK TAKTKKGK 

« Hide

References

« Hide 'large scale' 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].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Lung.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-568.
Tissue: Brain.
[5]Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 156-165; 191-205; 212-218; 380-401 AND 482-493, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Lung carcinoma.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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].
[8]"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-21 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK054568 mRNA. Translation: BAB70761.1.
AK314467 mRNA. Translation: BAG37075.1.
CH471087 Genomic DNA. Translation: EAW55210.1.
BC006104 mRNA. Translation: AAH06104.2.
AL834277 mRNA. Translation: CAD38952.1.
RefSeqNP_113668.2. NM_031480.2.
UniGeneHs.437474.

3D structure databases

ProteinModelPortalQ9BRS2.
SMRQ9BRS2. Positions 145-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123743. 11 interactions.
IntActQ9BRS2. 1 interaction.
MINTMINT-1630868.
STRING9606.ENSP00000369162.

Chemistry

BindingDBQ9BRS2.
ChEMBLCHEMBL5975.
GuidetoPHARMACOLOGY2186.

PTM databases

PhosphoSiteQ9BRS2.

Polymorphism databases

DMDM56404949.

Proteomic databases

PaxDbQ9BRS2.
PRIDEQ9BRS2.

Protocols and materials databases

DNASU83732.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379834; ENSP00000369162; ENSG00000124784.
GeneID83732.
KEGGhsa:83732.
UCSCuc003mxn.3. human.

Organism-specific databases

CTD83732.
GeneCardsGC06P007335.
HGNCHGNC:18656. RIOK1.
HPAHPA017866.
HPA051446.
neXtProtNX_Q9BRS2.
PharmGKBPA134928236.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1718.
HOGENOMHOG000166501.
HOVERGENHBG056997.
InParanoidQ9BRS2.
KOK07178.
OMAVEPDHPR.
OrthoDBEOG7JT6W1.
PhylomeDBQ9BRS2.
TreeFamTF105831.

Gene expression databases

ArrayExpressQ9BRS2.
BgeeQ9BRS2.
CleanExHS_RIOK1.
GenevestigatorQ9BRS2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR018934. RIO-like_kinase.
IPR000687. RIO_kinase.
IPR018935. RIO_kinase_CS.
IPR017407. Ser/Thr_kinase_Rio1.
[Graphical view]
PfamPF01163. RIO1. 1 hit.
[Graphical view]
PIRSFPIRSF038147. Ser/Thr_PK_RIO1. 1 hit.
SMARTSM00090. RIO. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01245. RIO1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRIOK1. human.
GenomeRNAi83732.
NextBio72727.
PROQ9BRS2.

Entry information

Entry nameRIOK1_HUMAN
AccessionPrimary (citable) accession number: Q9BRS2
Secondary accession number(s): B2RB28, Q8NDC8, Q96NV9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2004
Last modified: April 16, 2014
This is version 104 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 6

Human chromosome 6: entries, gene names and cross-references to MIM