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Protein

Serine/threonine-protein kinase RIO1

Gene

RIOK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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

BgeeiQ9BRS2.
CleanExiHS_RIOK1.
ExpressionAtlasiQ9BRS2. baseline and differential.
GenevestigatoriQ9BRS2.

Organism-specific databases

HPAiHPA017866.
HPA051446.

Interactioni

Protein-protein interaction databases

BioGridi123743. 18 interactions.
IntActiQ9BRS2. 1 interaction.
MINTiMINT-1630868.
STRINGi9606.ENSP00000369162.

Structurei

Secondary structure

1
568
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi166 – 17510Combined sources
Beta strandi181 – 1888Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi204 – 2107Combined sources
Helixi246 – 25914Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi274 – 2785Combined sources
Helixi290 – 2923Combined sources
Helixi297 – 31620Combined sources
Helixi327 – 3293Combined sources
Beta strandi330 – 3334Combined sources
Beta strandi336 – 3394Combined sources
Helixi353 – 36917Combined sources
Helixi378 – 3869Combined sources
Helixi395 – 40814Combined sources
Helixi411 – 42818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OTPX-ray2.70A143-494[»]
ProteinModelPortaliQ9BRS2.
SMRiQ9BRS2. Positions 163-430.
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.
GeneTreeiENSGT00390000004370.
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

        10         20         30         40         50
MDYRRLLMSR VVPGQFDDAD SSDSENRDLK TVKEKDDILF EDLQDNVNEN
60 70 80 90 100
GEGEIEDEEE EGYDDDDDDW DWDEGVGKLA KGYVWNGGSN PQANRQTSDS
110 120 130 140 150
SSAKMSTPAD KVLRKFENKI NLDKLNVTDS VINKVTEKSR QKEADMYRIK
160 170 180 190 200
DKADRATVEQ VLDPRTRMIL FKMLTRGIIT EINGCISTGK EANVYHASTA
210 220 230 240 250
NGESRAIKIY KTSILVFKDR DKYVSGEFRF RHGYCKGNPR KMVKTWAEKE
260 270 280 290 300
MRNLIRLNTA EIPCPEPIML RSHVLVMSFI GKDDMPAPLL KNVQLSESKA
310 320 330 340 350
RELYLQVIQY MRRMYQDARL VHADLSEFNM LYHGGGVYII DVSQSVEHDH
360 370 380 390 400
PHALEFLRKD CANVNDFFMR HSVAVMTVRE LFEFVTDPSI THENMDAYLS
410 420 430 440 450
KAMEIASQRT KEERSSQDHV DEEVFKRAYI PRTLNEVKNY ERDMDIIMKL
460 470 480 490 500
KEEDMAMNAQ QDNILYQTVT GLKKDLSGVQ KVPALLENQV EERTCSDSED
510 520 530 540 550
IGSSECSDTD SEEQGDHARP KKHTTDPDID KKERKKMVKE AQREKRKNKI
560
PKHVKKRKEK TAKTKKGK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OTPX-ray2.70A143-494[»]
ProteinModelPortaliQ9BRS2.
SMRiQ9BRS2. Positions 163-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123743. 18 interactions.
IntActiQ9BRS2. 1 interaction.
MINTiMINT-1630868.
STRINGi9606.ENSP00000369162.

Chemistry

BindingDBiQ9BRS2.
ChEMBLiCHEMBL5975.
GuidetoPHARMACOLOGYi2186.

PTM databases

PhosphoSiteiQ9BRS2.

Polymorphism databases

DMDMi56404949.

Proteomic databases

MaxQBiQ9BRS2.
PaxDbiQ9BRS2.
PRIDEiQ9BRS2.

Protocols and materials databases

DNASUi83732.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi83732.
GeneCardsiGC06P007335.
HGNCiHGNC:18656. RIOK1.
HPAiHPA017866.
HPA051446.
neXtProtiNX_Q9BRS2.
PharmGKBiPA134928236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1718.
GeneTreeiENSGT00390000004370.
HOGENOMiHOG000166501.
HOVERGENiHBG056997.
InParanoidiQ9BRS2.
KOiK07178.
OMAiVEPDHPR.
OrthoDBiEOG7JT6W1.
PhylomeDBiQ9BRS2.
TreeFamiTF105831.

Miscellaneous databases

ChiTaRSiRIOK1. human.
GenomeRNAii83732.
NextBioi72727.
PROiQ9BRS2.

Gene expression databases

BgeeiQ9BRS2.
CleanExiHS_RIOK1.
ExpressionAtlasiQ9BRS2. baseline and differential.
GenevestigatoriQ9BRS2.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 110 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.