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Q9CQS5 (RIOK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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
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 RIO2
EC=2.7.11.1
Alternative name(s):
RIO kinase 2
Gene names
Name:Riok2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length547 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 – 547547Serine/threonine-protein kinase RIO2
PRO_0000213528

Regions

Domain271 – 547277Protein kinase

Sites

Active site2281Proton acceptor By similarity
Binding site1231ATP By similarity

Amino acid modifications

Modified residue3321Phosphoserine By similarity
Modified residue3371Phosphoserine By similarity
Modified residue3501Phosphoserine By similarity
Modified residue3621Phosphoserine By similarity
Modified residue3851Phosphoserine By similarity
Modified residue3901Phosphoserine By similarity
Modified residue4121Phosphoserine Ref.3
Modified residue4171Phosphoserine By similarity
Modified residue4371Phosphoserine By similarity

Experimental info

Sequence conflict3691S → L in AAH10781. Ref.2
Sequence conflict379 – 3802GG → DS in AAH10781. Ref.2
Sequence conflict4021E → D in AAH10781. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CQS5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 61A50648147B8850

FASTA54762,490
        10         20         30         40         50         60 
MGKVNVAKLR YMSRDDFRVL TAVEMGMKNH EIVPCSLIAS IASLKHGGCN KILRELVKHK 

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

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

       190        200        210        220        230        240 
YNRHAVIMEL INGYPLCQIH HVEDPASVYD EAMELIVKLG NHGLIHGDFN EFNLMLDKDD 

       250        260        270        280        290        300 
HITMIDFPQM VSTSHPNAEW YFDRDVKCIR EFFMKRFSYE SELYPTFSDI RKEDSLDVEV 

       310        320        330        340        350        360 
SASGYTKEMQ ADDELLHPVG PDDKITETEE DSDFTFSDEE MLEKAKVWRS ELEKEADPAD 

       370        380        390        400        410        420 
ESGGSWCCSS TDSKQIKDGG LPEESAHVSS FEVTALSQAV EEMERQVLPH RSVTEFSEES 

       430        440        450        460        470        480 
RRTENDGQPG QRSPAGSEDC DDEPPHLIAL SSVNREFRPF RDEESMSSVT RHRTRTLSVT 

       490        500        510        520        530        540 
SAGSALSCST IPPELVKQKV KRQLTRQQKA AARRRLQKGE ANVFTKQRRE NMQNIKSSLE 


AASFWGD

« 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: Small intestine.
[2]"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].
Strain: FVB/N.
Tissue: Colon.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK008385 mRNA. Translation: BAB25639.1.
AK008451 mRNA. Translation: BAB25676.1.
AK049232 mRNA. Translation: BAC33625.1.
BC010781 mRNA. Translation: AAH10781.1.
IPIIPI00471148.
RefSeqNP_080210.1. NM_025934.2.
UniGeneMm.35117.

3D structure databases

ProteinModelPortalQ9CQS5.
SMRQ9CQS5. Positions 3-314.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9CQS5. 1 interaction.

PTM databases

PhosphoSiteQ9CQS5.

Proteomic databases

PaxDbQ9CQS5.
PRIDEQ9CQS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024620; ENSMUSP00000024620; ENSMUSG00000023846.
GeneID67045.
KEGGmmu:67045.
UCSCuc008apd.2. mouse.

Organism-specific databases

CTD55781.
MGIMGI:1914295. Riok2.

Phylogenomic databases

eggNOGCOG0478.
GeneTreeENSGT00390000003255.
HOGENOMHOG000225685.
HOVERGENHBG056045.
InParanoidQ9CQS5.
KOK07179.
OMADECPDLV.
OrthoDBEOG4W6NVN.

Gene expression databases

BgeeQ9CQS5.
CleanExMM_RIOK2.
GenevestigatorQ9CQS5.
GermOnlineENSMUSG00000023846. Mus musculus.

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. Kinase_like. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. False negative.
PS01245. RIO1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio323412.
SOURCESearch...

Entry information

Entry nameRIOK2_MOUSE
AccessionPrimary (citable) accession number: Q9CQS5
Secondary accession number(s): Q91XF3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

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