GenomeNet

Database: UniProt
Entry: Q8R1Q9
LinkDB: Q8R1Q9
Original site: Q8R1Q9 
ID   RBSK_MOUSE              Reviewed;         323 AA.
AC   Q8R1Q9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000312|EMBL:AAH23339.1};
DE            Short=RK {ECO:0000255|HAMAP-Rule:MF_03215};
DE            EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_03215};
GN   Name=Rbks {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000312|EMBL:AAH23339.1,
GN   ECO:0000312|MGI:MGI:1918586}; Synonyms=Rbsk {ECO:0000250|UniProtKB:Q9H477};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:BAE23825.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23825.1};
RC   TISSUE=Aorta {ECO:0000312|EMBL:BAE23825.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000312|EMBL:AAH23339.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH23339.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC       requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC       then be used either for sythesis of nucleotides, histidine, and
CC       tryptophan, or as a component of the pentose phosphate pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_03215}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC         EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_03215};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03215};
CC       Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC       electrophilic catalyst to aid phosphoryl group transfer. It is the
CC       chelate of the metal and the nucleotide that is the actual substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_03215};
CC   -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC       but not in, the active site. The most likely occupant of the site in
CC       vivo is potassium. Ion binding induces a conformational change that may
CC       alter substrate affinity. Competitively inhibited by phosphonoacetic
CC       acid, etidronate, 2-carboxethylphosphonic acid, N-
CC       (phosphonomethyl)glycine, N-(phosphonomethyl)iminodiacetic acid and
CC       clodronate (By similarity). {ECO:0000250|UniProtKB:Q9H477,
CC       ECO:0000255|HAMAP-Rule:MF_03215}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_03215}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03215}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03215}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03215}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK138939; BAE23825.1; -; mRNA.
DR   EMBL; BC023339; AAH23339.1; -; mRNA.
DR   CCDS; CCDS19187.1; -.
DR   RefSeq; NP_694876.1; NM_153196.1.
DR   AlphaFoldDB; Q8R1Q9; -.
DR   SMR; Q8R1Q9; -.
DR   BioGRID; 214646; 1.
DR   STRING; 10090.ENSMUSP00000031018; -.
DR   iPTMnet; Q8R1Q9; -.
DR   PhosphoSitePlus; Q8R1Q9; -.
DR   SwissPalm; Q8R1Q9; -.
DR   EPD; Q8R1Q9; -.
DR   MaxQB; Q8R1Q9; -.
DR   PaxDb; 10090-ENSMUSP00000031018; -.
DR   PeptideAtlas; Q8R1Q9; -.
DR   ProteomicsDB; 255162; -.
DR   Antibodypedia; 13898; 158 antibodies from 22 providers.
DR   DNASU; 71336; -.
DR   Ensembl; ENSMUST00000031018.10; ENSMUSP00000031018.8; ENSMUSG00000029136.10.
DR   GeneID; 71336; -.
DR   KEGG; mmu:71336; -.
DR   UCSC; uc008wyv.1; mouse.
DR   AGR; MGI:1918586; -.
DR   CTD; 64080; -.
DR   MGI; MGI:1918586; Rbks.
DR   VEuPathDB; HostDB:ENSMUSG00000029136; -.
DR   eggNOG; KOG2855; Eukaryota.
DR   GeneTree; ENSGT00390000005743; -.
DR   HOGENOM; CLU_027634_2_3_1; -.
DR   InParanoid; Q8R1Q9; -.
DR   OMA; DIVLIQQ; -.
DR   OrthoDB; 1217765at2759; -.
DR   PhylomeDB; Q8R1Q9; -.
DR   TreeFam; TF105770; -.
DR   Reactome; R-MMU-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00916; UER00889.
DR   BioGRID-ORCS; 71336; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Rbks; mouse.
DR   PRO; PR:Q8R1Q9; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8R1Q9; Protein.
DR   Bgee; ENSMUSG00000029136; Expressed in lumbar dorsal root ganglion and 129 other cell types or tissues.
DR   Genevisible; Q8R1Q9; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004747; F:ribokinase activity; IMP:MGI.
DR   GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI.
DR   CDD; cd01174; ribokinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01987; Ribokinase; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011877; D_ribokin.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR02152; D_ribokin_bact; 1.
DR   PANTHER; PTHR10584:SF166; RIBOKINASE; 1.
DR   PANTHER; PTHR10584; SUGAR KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Potassium; Reference proteome;
KW   Transferase.
FT   CHAIN           1..323
FT                   /note="Ribokinase"
FT                   /id="PRO_0000375977"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         54..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         236..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         257
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         264
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         266
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         269..270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         302
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         305
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         307
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
FT   BINDING         311
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03215"
SQ   SEQUENCE   323 AA;  34119 MW;  65A93A8372651F60 CRC64;
     MAACGEPGRP WQEEEAAAVV VVGSCMTDLV SLTSRLPKTG ETIHGHEFFI GFGGKGANQC
     VQAARLGAKA AIVCKVGNDS FGNDYIENLK QNHISTEFTY QTRDAATGTA SIIVNNEGQN
     IIVIVAGANL FLNSEDLKKA ASVISRAKVM ICQLEISPAA SLEALTMARR SGVKTLFNPA
     PAMADLDPQF YTLSSIFCCN ESEAEILTGH AVSDPTTAGK AAMILLERGC QVVVITLGAS
     GCVILSQAEP VPKHIPTEAV KAVDTTGAGD SFVGALAFYL AYYPNLSLEE MLKRSNFIAA
     VSVQATGTQS SYPYKKDLPL ALF
//
DBGET integrated database retrieval system