General Information of Target

Target ID LDTP11903
Target Name Ribokinase (RBKS)
Gene Name RBKS
Gene ID 64080
Synonyms
RBSK; Ribokinase; RK; EC 2.7.1.15
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MEPPMEPSGGEQEPGAVRFLDLPWEDVLLPHVLNRVPLRQLLRLQRVSRAFRSLVQLHLA
GLRRFDAAQVGPQIPRAALARLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVA
LGGCGQLSRRALGALAEGCPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLK
DEAIVYLAQRRGAGLRSLSLAVNANVGDAAVQELARNCPELHHLDLTGCLRVGSDGVRTL
AEYCPVLRSLRVRHCHHVAESSLSRLRKRGVDIDVEPPLHQALVLLQDMAGFAPFVNLQV
Target Bioclass
Enzyme
Family
Carbohydrate kinase PfkB family, Ribokinase subfamily
Subcellular location
Cytoplasm
Function
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. {|HAMAP-Rule:MF_03215}.
Uniprot ID
Q9H477
Ensemble ID
ENST00000302188.8
HGNC ID
HGNC:30325

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
IGR37 SNV: p.E288K .
IGR39 SNV: p.E288K .
MEWO SNV: p.E154K .
RBE SNV: p.T133M .
SNU5 Deletion: p.Q188HfsTer19
SNV: p.Q188K
.

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 4 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info 
C59(1.75)  LDD3378  [1]
BTD
 Probe Info 
C59(1.35)  LDD2090  [2]
ATP probe
 Probe Info 
N.A.  LDD0199  [3]
NAIA_5
 Probe Info 
C59(0.00); C24(0.00)  LDD2223  [4]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0214  AC1 HEK-293T C59(1.25)  LDD1507  [5]
 LDCM0276  AC17 HEK-293T C59(1.04)  LDD1515  [5]
 LDCM0281  AC21 HEK-293T C59(1.22)  LDD1520  [5]
 LDCM0285  AC25 HEK-293T C59(0.76)  LDD1524  [5]
 LDCM0289  AC29 HEK-293T C59(1.20)  LDD1528  [5]
 LDCM0294  AC33 HEK-293T C59(1.29)  LDD1533  [5]
 LDCM0298  AC37 HEK-293T C59(0.96)  LDD1537  [5]
 LDCM0303  AC41 HEK-293T C59(1.61)  LDD1542  [5]
 LDCM0307  AC45 HEK-293T C59(1.31)  LDD1546  [5]
 LDCM0311  AC49 HEK-293T C59(0.95)  LDD1550  [5]
 LDCM0312  AC5 HEK-293T C59(0.71)  LDD1551  [5]
 LDCM0316  AC53 HEK-293T C59(0.97)  LDD1555  [5]
 LDCM0320  AC57 HEK-293T C59(1.27)  LDD1559  [5]
 LDCM0325  AC61 HEK-293T C59(1.12)  LDD1564  [5]
 LDCM0248  AKOS034007472 HEK-293T C59(1.02)  LDD1511  [5]
 LDCM0356  AKOS034007680 HEK-293T C59(1.46)  LDD1570  [5]
 LDCM0404  CL17 HEK-293T C59(1.16)  LDD1608  [5]
 LDCM0409  CL21 HEK-293T C59(1.06)  LDD1613  [5]
 LDCM0417  CL29 HEK-293T C59(1.07)  LDD1621  [5]
 LDCM0422  CL33 HEK-293T C59(0.76)  LDD1626  [5]
 LDCM0431  CL41 HEK-293T C59(0.96)  LDD1635  [5]
 LDCM0435  CL45 HEK-293T C59(1.01)  LDD1639  [5]
 LDCM0440  CL5 HEK-293T C59(1.07)  LDD1644  [5]
 LDCM0444  CL53 HEK-293T C59(0.80)  LDD1647  [5]
 LDCM0448  CL57 HEK-293T C59(1.14)  LDD1651  [5]
 LDCM0457  CL65 HEK-293T C59(0.92)  LDD1660  [5]
 LDCM0461  CL69 HEK-293T C59(0.95)  LDD1664  [5]
 LDCM0470  CL77 HEK-293T C59(0.96)  LDD1673  [5]
 LDCM0475  CL81 HEK-293T C59(1.22)  LDD1678  [5]
 LDCM0483  CL89 HEK-293T C59(0.72)  LDD1686  [5]
 LDCM0484  CL9 HEK-293T C59(0.97)  LDD1687  [5]
 LDCM0488  CL93 HEK-293T C59(1.04)  LDD1691  [5]
 LDCM0022  KB02 769-P C59(1.77)  LDD2246  [1]
 LDCM0023  KB03 769-P C59(2.24)  LDD2663  [1]
 LDCM0024  KB05 OS-RC-2 C59(1.75)  LDD3378  [1]
 LDCM0497  Nucleophilic fragment 11b MDA-MB-231 C59(1.35)  LDD2090  [2]
 LDCM0503  Nucleophilic fragment 14b MDA-MB-231 C59(0.31)  LDD2096  [2]
 LDCM0507  Nucleophilic fragment 16b MDA-MB-231 C59(0.42)  LDD2100  [2]
 LDCM0512  Nucleophilic fragment 19a MDA-MB-231 C59(1.28)  LDD2105  [2]
 LDCM0513  Nucleophilic fragment 19b MDA-MB-231 C59(0.50)  LDD2106  [2]
 LDCM0522  Nucleophilic fragment 24a MDA-MB-231 C59(0.54)  LDD2115  [2]
 LDCM0525  Nucleophilic fragment 25b MDA-MB-231 C59(0.81)  LDD2118  [2]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C59(0.93)  LDD2120  [2]
 LDCM0529  Nucleophilic fragment 27b MDA-MB-231 C59(0.61)  LDD2122  [2]
 LDCM0531  Nucleophilic fragment 28b MDA-MB-231 C59(0.58)  LDD2124  [2]
 LDCM0533  Nucleophilic fragment 29b MDA-MB-231 C59(0.56)  LDD2126  [2]
 LDCM0551  Nucleophilic fragment 5b MDA-MB-231 C59(0.69)  LDD2145  [2]
 LDCM0554  Nucleophilic fragment 7a MDA-MB-231 C59(0.47)  LDD2148  [2]
 LDCM0555  Nucleophilic fragment 7b MDA-MB-231 C59(0.75)  LDD2149  [2]
 LDCM0557  Nucleophilic fragment 8b MDA-MB-231 C59(0.66)  LDD2151  [2]
 LDCM0559  Nucleophilic fragment 9b MDA-MB-231 C59(1.27)  LDD2153  [2]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Ribokinase (RBKS) Carbohydrate kinase PfkB family Q9H477
Other
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Adrenocortical dysplasia protein homolog (ACD) . Q96AP0

References

1 DrugMap: A quantitative pan-cancer analysis of cysteine ligandability. Cell. 2024 May 9;187(10):2536-2556.e30. doi: 10.1016/j.cell.2024.03.027. Epub 2024 Apr 22.
Mass spectrometry data entry: PXD047840
2 Nucleophilic covalent ligand discovery for the cysteine redoxome. Nat Chem Biol. 2023 Nov;19(11):1309-1319. doi: 10.1038/s41589-023-01330-5. Epub 2023 May 29.
Mass spectrometry data entry: PXD039908 , PXD029761
3 Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases. J Proteome Res. 2022 Aug 5;21(8):2063-2070. doi: 10.1021/acs.jproteome.2c00225. Epub 2022 Jul 12.
4 N-Acryloylindole-alkyne (NAIA) enables imaging and profiling new ligandable cysteines and oxidized thiols by chemoproteomics. Nat Commun. 2023 Jun 15;14(1):3564. doi: 10.1038/s41467-023-39268-w.
Mass spectrometry data entry: PXD041264
5 Accelerating multiplexed profiling of protein-ligand interactions: High-throughput plate-based reactive cysteine profiling with minimal input. Cell Chem Biol. 2024 Mar 21;31(3):565-576.e4. doi: 10.1016/j.chembiol.2023.11.015. Epub 2023 Dec 19.
Mass spectrometry data entry: PXD044402