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Protein

Ribokinase

Gene

Rbks

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.UniRule annotation

Catalytic activityi

ATP + D-ribose = ADP + D-ribose 5-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.UniRule annotation

Enzyme regulationi

Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity. Competitively inhibited by phosphonoacetic acid, etidronate, 2-carboxethylphosphonic acid, N-(phosphonomethyl)glycine, N-(phosphonomethyl)iminodiacetic acid and clodronate (By similarity).UniRule annotationBy similarity

Pathwayi: D-ribose degradation

This protein is involved in step 2 of the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Ribokinase (Rbks)
This subpathway is part of the pathway D-ribose degradation, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose, the pathway D-ribose degradation and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateUniRule annotation
Binding sitei200 – 2001ATPUniRule annotation
Binding sitei257 – 2571ATPUniRule annotation
Metal bindingi264 – 2641PotassiumUniRule annotation
Metal bindingi266 – 2661Potassium; via carbonyl oxygenUniRule annotation
Active sitei270 – 2701Proton acceptorUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Binding sitei296 – 2961ATPUniRule annotation
Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi311 – 3111PotassiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi236 – 2416ATPUniRule annotation
Nucleotide bindingi269 – 2702ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

UniPathwayiUPA00916; UER00889.

Names & Taxonomyi

Protein namesi
Recommended name:
RibokinaseUniRule annotationImported (EC:2.7.1.15UniRule annotation)
Short name:
RKUniRule annotation
Gene namesi
Name:RbksUniRule annotationImported
Synonyms:RbskBy similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1918586. Rbks.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323RibokinasePRO_0000375977Add
BLAST

Proteomic databases

EPDiQ8R1Q9.
MaxQBiQ8R1Q9.
PaxDbiQ8R1Q9.
PeptideAtlasiQ8R1Q9.
PRIDEiQ8R1Q9.

PTM databases

iPTMnetiQ8R1Q9.
PhosphoSiteiQ8R1Q9.

Expressioni

Gene expression databases

BgeeiQ8R1Q9.
GenevisibleiQ8R1Q9. MM.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031018.

Structurei

3D structure databases

ProteinModelPortaliQ8R1Q9.
SMRiQ8R1Q9. Positions 17-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 283Substrate bindingUniRule annotation
Regioni54 – 585Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2855. Eukaryota.
COG0524. LUCA.
GeneTreeiENSGT00390000005743.
HOGENOMiHOG000235950.
InParanoidiQ8R1Q9.
KOiK00852.
OMAiANQACAI.
OrthoDBiEOG715Q4W.
PhylomeDBiQ8R1Q9.
TreeFamiTF105770.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011877. D_ribokin.
IPR011611. PfkB_dom.
IPR002139. Ribo/fructo_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSiPR00990. RIBOKINASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR02152. D_ribokin_bact. 1 hit.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R1Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAACGEPGRP WQEEEAAAVV VVGSCMTDLV SLTSRLPKTG ETIHGHEFFI
60 70 80 90 100
GFGGKGANQC VQAARLGAKA AIVCKVGNDS FGNDYIENLK QNHISTEFTY
110 120 130 140 150
QTRDAATGTA SIIVNNEGQN IIVIVAGANL FLNSEDLKKA ASVISRAKVM
160 170 180 190 200
ICQLEISPAA SLEALTMARR SGVKTLFNPA PAMADLDPQF YTLSSIFCCN
210 220 230 240 250
ESEAEILTGH AVSDPTTAGK AAMILLERGC QVVVITLGAS GCVILSQAEP
260 270 280 290 300
VPKHIPTEAV KAVDTTGAGD SFVGALAFYL AYYPNLSLEE MLKRSNFIAA
310 320
VSVQATGTQS SYPYKKDLPL ALF
Length:323
Mass (Da):34,119
Last modified:June 1, 2002 - v1
Checksum:i65A93A8372651F60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138939 mRNA. Translation: BAE23825.1.
BC023339 mRNA. Translation: AAH23339.1.
CCDSiCCDS19187.1.
RefSeqiNP_694876.1. NM_153196.1.
UniGeneiMm.22519.

Genome annotation databases

EnsembliENSMUST00000031018; ENSMUSP00000031018; ENSMUSG00000029136.
GeneIDi71336.
KEGGimmu:71336.
UCSCiuc008wyv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138939 mRNA. Translation: BAE23825.1.
BC023339 mRNA. Translation: AAH23339.1.
CCDSiCCDS19187.1.
RefSeqiNP_694876.1. NM_153196.1.
UniGeneiMm.22519.

3D structure databases

ProteinModelPortaliQ8R1Q9.
SMRiQ8R1Q9. Positions 17-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031018.

PTM databases

iPTMnetiQ8R1Q9.
PhosphoSiteiQ8R1Q9.

Proteomic databases

EPDiQ8R1Q9.
MaxQBiQ8R1Q9.
PaxDbiQ8R1Q9.
PeptideAtlasiQ8R1Q9.
PRIDEiQ8R1Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031018; ENSMUSP00000031018; ENSMUSG00000029136.
GeneIDi71336.
KEGGimmu:71336.
UCSCiuc008wyv.1. mouse.

Organism-specific databases

CTDi64080.
MGIiMGI:1918586. Rbks.

Phylogenomic databases

eggNOGiKOG2855. Eukaryota.
COG0524. LUCA.
GeneTreeiENSGT00390000005743.
HOGENOMiHOG000235950.
InParanoidiQ8R1Q9.
KOiK00852.
OMAiANQACAI.
OrthoDBiEOG715Q4W.
PhylomeDBiQ8R1Q9.
TreeFamiTF105770.

Enzyme and pathway databases

UniPathwayiUPA00916; UER00889.

Miscellaneous databases

PROiQ8R1Q9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R1Q9.
GenevisibleiQ8R1Q9. MM.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011877. D_ribokin.
IPR011611. PfkB_dom.
IPR002139. Ribo/fructo_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSiPR00990. RIBOKINASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR02152. D_ribokin_bact. 1 hit.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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/6JImported.
    Tissue: AortaImported.
  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].
    Tissue: Mammary tumorImported.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver and Spleen.

Entry informationi

Entry nameiRBSK_MOUSE
AccessioniPrimary (citable) accession number: Q8R1Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 109 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.