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Q922Q2 (RIOK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 caution

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 BAB29195.1 differs from that shown. Reason: Frameshift at position 434.

The sequence BAB29195.1 differs from that shown. Reason: Intron retention.

The sequence BAB30687.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Serine/threonine-protein kinase RIO1
PRO_0000314490

Regions

Domain179 – 478300Protein kinase

Sites

Active site3231Proton acceptor By similarity
Binding site2071ATP By similarity

Amino acid modifications

Modified residue211Phosphoserine By similarity
Modified residue221Phosphoserine By similarity

Experimental info

Sequence conflict4361V → E in BAB29195. Ref.1
Sequence conflict4921E → K in BAB29195. Ref.1
Sequence conflict5281I → V in AAH02158. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q922Q2 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: D2A1863DF0132366

FASTA56764,910
        10         20         30         40         50         60 
MDCSLDRMAS VVPGQFDDAD SSDSENKELQ PIHAEDGGVL LKSLQNAAAE VKGDAETDEE 

        70         80         90        100        110        120 
DDYDDDDDWY LDDATGKLTK GCTWNGGSNY QANRQTSNYN SAKMSTPIDK SLRKFENKIN 

       130        140        150        160        170        180 
LNKLNVTDSV TNKVTVKLRQ KEAESYRIKD KADRATVEQV LDPRTRMILF KLLHKDHISE 

       190        200        210        220        230        240 
IHGCISTGKE ANVYYASTPS GESRAIKIYK TSILMFKDRD KYVTGEFRFR RGYCKGNPRK 

       250        260        270        280        290        300 
MVRTWAEKEM RNLCRLKTAN IPCPEPIRLR SHVLLMGFIG KDDMPAPLLK NVQLSESKAR 

       310        320        330        340        350        360 
ELYLQVIQYM RKMYQDARLV HADLSEFNML YHGGDVYIID VSQSVEHDHP HALEFLRKDC 

       370        380        390        400        410        420 
TNVNDFFSKH AVAVMTVREL FDFVTDPSIT ADNMDAYLEK AMEIASQRTK EEKTSQDHVD 

       430        440        450        460        470        480 
EEVFKQAYIP RTLNEVKNYE RDVDIMMRLK EEDMALNTQQ DNILYQTVMG LKKDLSGVQK 

       490        500        510        520        530        540 
VPALLESEVK EETCFGSDDA GGSECSDTVS EEQEDQAGCR NHIADPDIDK KERKKMVKEA 

       550        560 
QREKRKNKIP KHVKKRKEKT AKAKKGK 

« Hide

References

[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_077204.2. NM_024242.3.
UniGeneMm.297130.

3D structure databases

ProteinModelPortalQ922Q2.
SMRQ922Q2. Positions 137-372.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ922Q2.

Proteomic databases

PRIDEQ922Q2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021866; ENSMUSP00000021866; ENSMUSG00000021428.
GeneID71340.
KEGGmmu:71340.
UCSCuc007qdi.2. mouse.

Organism-specific databases

CTD83732.
MGIMGI:1918590. Riok1.

Phylogenomic databases

eggNOGCOG1718.
GeneTreeENSGT00390000004370.
HOGENOMHOG000166501.
HOVERGENHBG056997.
InParanoidQ922Q2.
KOK07178.
OMAVEPDHPR.
OrthoDBEOG7JT6W1.
TreeFamTF105831.

Gene expression databases

BgeeQ922Q2.
CleanExMM_RIOK1.
GenevestigatorQ922Q2.

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. mouse.
NextBio333585.
PROQ922Q2.
SOURCESearch...

Entry information

Entry nameRIOK1_MOUSE
AccessionPrimary (citable) accession number: Q922Q2
Secondary accession number(s): Q3U7D5 expand/collapse secondary AC list , Q99LZ1, Q9CU84, Q9CXN9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot