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Q9BRS2

- RIOK1_HUMAN

UniProt

Q9BRS2 - RIOK1_HUMAN

Protein

Serine/threonine-protein kinase RIO1

Gene

RIOK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei208 – 2081ATPBy similarity
    Active sitei324 – 3241Proton acceptorBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase RIO1 (EC:2.7.11.1)
    Alternative name(s):
    RIO kinase 1
    Gene namesi
    Name:RIOK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:18656. RIOK1.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134928236.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 568568Serine/threonine-protein kinase RIO1PRO_0000213526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei22 – 221Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BRS2.
    PaxDbiQ9BRS2.
    PRIDEiQ9BRS2.

    PTM databases

    PhosphoSiteiQ9BRS2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BRS2.
    BgeeiQ9BRS2.
    CleanExiHS_RIOK1.
    GenevestigatoriQ9BRS2.

    Organism-specific databases

    HPAiHPA017866.
    HPA051446.

    Interactioni

    Protein-protein interaction databases

    BioGridi123743. 11 interactions.
    IntActiQ9BRS2. 1 interaction.
    MINTiMINT-1630868.
    STRINGi9606.ENSP00000369162.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BRS2.
    SMRiQ9BRS2. Positions 145-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini180 – 479300Protein kinaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.Curated

    Phylogenomic databases

    eggNOGiCOG1718.
    HOGENOMiHOG000166501.
    HOVERGENiHBG056997.
    InParanoidiQ9BRS2.
    KOiK07178.
    OMAiVEPDHPR.
    OrthoDBiEOG7JT6W1.
    PhylomeDBiQ9BRS2.
    TreeFamiTF105831.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR018934. RIO-like_kinase.
    IPR000687. RIO_kinase.
    IPR018935. RIO_kinase_CS.
    IPR017407. Ser/Thr_kinase_Rio1.
    [Graphical view]
    PfamiPF01163. RIO1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038147. Ser/Thr_PK_RIO1. 1 hit.
    SMARTiSM00090. RIO. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01245. RIO1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BRS2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYRRLLMSR VVPGQFDDAD SSDSENRDLK TVKEKDDILF EDLQDNVNEN    50
    GEGEIEDEEE EGYDDDDDDW DWDEGVGKLA KGYVWNGGSN PQANRQTSDS 100
    SSAKMSTPAD KVLRKFENKI NLDKLNVTDS VINKVTEKSR QKEADMYRIK 150
    DKADRATVEQ VLDPRTRMIL FKMLTRGIIT EINGCISTGK EANVYHASTA 200
    NGESRAIKIY KTSILVFKDR DKYVSGEFRF RHGYCKGNPR KMVKTWAEKE 250
    MRNLIRLNTA EIPCPEPIML RSHVLVMSFI GKDDMPAPLL KNVQLSESKA 300
    RELYLQVIQY MRRMYQDARL VHADLSEFNM LYHGGGVYII DVSQSVEHDH 350
    PHALEFLRKD CANVNDFFMR HSVAVMTVRE LFEFVTDPSI THENMDAYLS 400
    KAMEIASQRT KEERSSQDHV DEEVFKRAYI PRTLNEVKNY ERDMDIIMKL 450
    KEEDMAMNAQ QDNILYQTVT GLKKDLSGVQ KVPALLENQV EERTCSDSED 500
    IGSSECSDTD SEEQGDHARP KKHTTDPDID KKERKKMVKE AQREKRKNKI 550
    PKHVKKRKEK TAKTKKGK 568
    Length:568
    Mass (Da):65,583
    Last modified:March 1, 2004 - v2
    Checksum:i5730BFC3798F5190
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti375 – 3751V → I.
    Corresponds to variant rs56067778 [ dbSNP | Ensembl ].
    VAR_061777

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4500.1.
    RefSeqiNP_113668.2. NM_031480.2.
    UniGeneiHs.437474.

    Genome annotation databases

    EnsembliENST00000379834; ENSP00000369162; ENSG00000124784.
    GeneIDi83732.
    KEGGihsa:83732.
    UCSCiuc003mxn.3. human.

    Polymorphism databases

    DMDMi56404949.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4500.1.
    RefSeqi NP_113668.2. NM_031480.2.
    UniGenei Hs.437474.

    3D structure databases

    ProteinModelPortali Q9BRS2.
    SMRi Q9BRS2. Positions 145-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123743. 11 interactions.
    IntActi Q9BRS2. 1 interaction.
    MINTi MINT-1630868.
    STRINGi 9606.ENSP00000369162.

    Chemistry

    BindingDBi Q9BRS2.
    ChEMBLi CHEMBL5975.
    GuidetoPHARMACOLOGYi 2186.

    PTM databases

    PhosphoSitei Q9BRS2.

    Polymorphism databases

    DMDMi 56404949.

    Proteomic databases

    MaxQBi Q9BRS2.
    PaxDbi Q9BRS2.
    PRIDEi Q9BRS2.

    Protocols and materials databases

    DNASUi 83732.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379834 ; ENSP00000369162 ; ENSG00000124784 .
    GeneIDi 83732.
    KEGGi hsa:83732.
    UCSCi uc003mxn.3. human.

    Organism-specific databases

    CTDi 83732.
    GeneCardsi GC06P007335.
    HGNCi HGNC:18656. RIOK1.
    HPAi HPA017866.
    HPA051446.
    neXtProti NX_Q9BRS2.
    PharmGKBi PA134928236.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1718.
    HOGENOMi HOG000166501.
    HOVERGENi HBG056997.
    InParanoidi Q9BRS2.
    KOi K07178.
    OMAi VEPDHPR.
    OrthoDBi EOG7JT6W1.
    PhylomeDBi Q9BRS2.
    TreeFami TF105831.

    Miscellaneous databases

    ChiTaRSi RIOK1. human.
    GenomeRNAii 83732.
    NextBioi 72727.
    PROi Q9BRS2.

    Gene expression databases

    ArrayExpressi Q9BRS2.
    Bgeei Q9BRS2.
    CleanExi HS_RIOK1.
    Genevestigatori Q9BRS2.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR018934. RIO-like_kinase.
    IPR000687. RIO_kinase.
    IPR018935. RIO_kinase_CS.
    IPR017407. Ser/Thr_kinase_Rio1.
    [Graphical view ]
    Pfami PF01163. RIO1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038147. Ser/Thr_PK_RIO1. 1 hit.
    SMARTi SM00090. RIO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01245. RIO1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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].

    Entry informationi

    Entry nameiRIOK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BRS2
    Secondary accession number(s): B2RB28, Q8NDC8, Q96NV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3