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Q922Q2

- RIOK1_MOUSE

UniProt

Q922Q2 - RIOK1_MOUSE

Protein

Serine/threonine-protein kinase RIO1

Gene

Riok1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071ATPBy similarity
    Active sitei323 – 3231Proton 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1918590. Riok1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 567567Serine/threonine-protein kinase RIO1PRO_0000314490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei22 – 221PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ922Q2.

    PTM databases

    PhosphoSiteiQ922Q2.

    Expressioni

    Gene expression databases

    BgeeiQ922Q2.
    CleanExiMM_RIOK1.
    GenevestigatoriQ922Q2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ922Q2.
    SMRiQ922Q2. Positions 137-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini179 – 478300Protein kinaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.Curated

    Phylogenomic databases

    eggNOGiCOG1718.
    GeneTreeiENSGT00390000004370.
    HOGENOMiHOG000166501.
    HOVERGENiHBG056997.
    InParanoidiQ922Q2.
    KOiK07178.
    OMAiVEPDHPR.
    OrthoDBiEOG7JT6W1.
    PhylomeDBiQ922Q2.
    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.

    Q922Q2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDCSLDRMAS VVPGQFDDAD SSDSENKELQ PIHAEDGGVL LKSLQNAAAE    50
    VKGDAETDEE DDYDDDDDWY LDDATGKLTK GCTWNGGSNY QANRQTSNYN 100
    SAKMSTPIDK SLRKFENKIN LNKLNVTDSV TNKVTVKLRQ KEAESYRIKD 150
    KADRATVEQV LDPRTRMILF KLLHKDHISE IHGCISTGKE ANVYYASTPS 200
    GESRAIKIYK TSILMFKDRD KYVTGEFRFR RGYCKGNPRK MVRTWAEKEM 250
    RNLCRLKTAN IPCPEPIRLR SHVLLMGFIG KDDMPAPLLK NVQLSESKAR 300
    ELYLQVIQYM RKMYQDARLV HADLSEFNML YHGGDVYIID VSQSVEHDHP 350
    HALEFLRKDC TNVNDFFSKH AVAVMTVREL FDFVTDPSIT ADNMDAYLEK 400
    AMEIASQRTK EEKTSQDHVD EEVFKQAYIP RTLNEVKNYE RDVDIMMRLK 450
    EEDMALNTQQ DNILYQTVMG LKKDLSGVQK VPALLESEVK EETCFGSDDA 500
    GGSECSDTVS EEQEDQAGCR NHIADPDIDK KERKKMVKEA QREKRKNKIP 550
    KHVKKRKEKT AKAKKGK 567
    Length:567
    Mass (Da):64,910
    Last modified:January 15, 2008 - v2
    Checksum:iD2A1863DF0132366
    GO

    Sequence cautioni

    The sequence BAB29195.1 differs from that shown. Reason: Intron retention.
    The sequence BAB29195.1 differs from that shown. Reason: Frameshift at position 434.
    The sequence AAH02158.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB29195.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB30687.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti436 – 4361V → E in BAB29195. (PubMed:16141072)Curated
    Sequence conflicti492 – 4921E → K in BAB29195. (PubMed:16141072)Curated
    Sequence conflicti528 – 5281I → V in AAH02158. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014182 mRNA. Translation: BAB29195.1. Sequence problems.
    AK017312 mRNA. Translation: BAB30687.2. Different initiation.
    AK152707 mRNA. Translation: BAE31434.1.
    AC140331 Genomic DNA. No translation available.
    CT010477 Genomic DNA. No translation available.
    BC002158 mRNA. Translation: AAH02158.1. Different initiation.
    CCDSiCCDS26461.1.
    RefSeqiNP_077204.2. NM_024242.3.
    UniGeneiMm.297130.

    Genome annotation databases

    EnsembliENSMUST00000021866; ENSMUSP00000021866; ENSMUSG00000021428.
    GeneIDi71340.
    KEGGimmu:71340.
    UCSCiuc007qdi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014182 mRNA. Translation: BAB29195.1 . Sequence problems.
    AK017312 mRNA. Translation: BAB30687.2 . Different initiation.
    AK152707 mRNA. Translation: BAE31434.1 .
    AC140331 Genomic DNA. No translation available.
    CT010477 Genomic DNA. No translation available.
    BC002158 mRNA. Translation: AAH02158.1 . Different initiation.
    CCDSi CCDS26461.1.
    RefSeqi NP_077204.2. NM_024242.3.
    UniGenei Mm.297130.

    3D structure databases

    ProteinModelPortali Q922Q2.
    SMRi Q922Q2. Positions 137-372.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q922Q2.

    Proteomic databases

    PRIDEi Q922Q2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021866 ; ENSMUSP00000021866 ; ENSMUSG00000021428 .
    GeneIDi 71340.
    KEGGi mmu:71340.
    UCSCi uc007qdi.2. mouse.

    Organism-specific databases

    CTDi 83732.
    MGIi MGI:1918590. Riok1.

    Phylogenomic databases

    eggNOGi COG1718.
    GeneTreei ENSGT00390000004370.
    HOGENOMi HOG000166501.
    HOVERGENi HBG056997.
    InParanoidi Q922Q2.
    KOi K07178.
    OMAi VEPDHPR.
    OrthoDBi EOG7JT6W1.
    PhylomeDBi Q922Q2.
    TreeFami TF105831.

    Miscellaneous databases

    ChiTaRSi RIOK1. mouse.
    NextBioi 333585.
    PROi Q922Q2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q922Q2.
    CleanExi MM_RIOK1.
    Genevestigatori Q922Q2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage, Embryonic head and Head.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 192-567.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiRIOK1_MOUSE
    AccessioniPrimary (citable) accession number: Q922Q2
    Secondary accession number(s): Q3U7D5
    , Q99LZ1, Q9CU84, Q9CXN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3