Details of the Target

General Information of Target

Target ID LDTP13618
Target Name ATP-dependent RNA helicase DDX19B (DDX19B)
Gene Name DDX19B
Gene ID 11269
Synonyms
DBP5; DDX19; TDBP; ATP-dependent RNA helicase DDX19B; EC 3.6.4.13; DEAD box RNA helicase DEAD5; DEAD box protein 19B
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MLYSPGPSLPESAESLDGSQEDKPRGSCAEPTFTDTGMVAHINNSRLKAKGVGQHDNAQN
FGNQSFEELRAACLRKGELFEDPLFPAEPSSLGFKDLGPNSKNVQNISWQRPKDIINNPL
FIMDGISPTDICQGILGDCWLLAAIGSLTTCPKLLYRVVPRGQSFKKNYAGIFHFQIWQF
GQWVNVVVDDRLPTKNDKLVFVHSTERSEFWSALLEKAYAKLSGSYEALSGGSTMEGLED
FTGGVAQSFQLQRPPQNLLRLLRKAVERSSLMGCSIEVTSDSELESMTDKMLVRGHAYSV
TGLQDVHYRGKMETLIRVRNPWGRIEWNGAWSDSAREWEEVASDIQMQLLHKTEDGEFWM
SYQDFLNNFTLLEICNLTPDTLSGDYKSYWHTTFYEGSWRRGSSAGGCRNHPGTFWTNPQ
FKISLPEGDDPEDDAEGNVVVCTCLVALMQKNWRHARQQGAQLQTIGFVLYAVPKEFQNI
QDVHLKKEFFTKYQDHGFSEIFTNSREVSSQLRLPPGEYIIIPSTFEPHRDADFLLRVFT
EKHSESWELDEVNYAEQLQEEKVSEDDMDQDFLHLFKIVAGEGKEIGVYELQRLLNRMAI
KFKSFKTKGFGLDACRCMINLMDKDGSGKLGLLEFKILWKKLKKWMDIFRECDQDHSGTL
NSYEMRLVIEKAGIKLNNKVMQVLVARYADDDLIIDFDSFISCFLRLKTMFTFFLTMDPK
NTGHICLSLEQWLQMTMWG
Target Bioclass
Enzyme
Family
DEAD box helicase family, DDX19/DBP5 subfamily
Subcellular location
Cytoplasm
Function
ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.
Uniprot ID
Q9UMR2
Ensemble ID
ENST00000288071.11
HGNC ID
HGNC:2742

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
DOTC24510 SNV: p.Q322Ter DBIA    Probe Info 
LNCaP clone FGC SNV: p.P84S DBIA    Probe Info 
LS123 SNV: p.A346G DBIA    Probe Info 
LS180 Deletion: p.K385del DBIA    Probe Info 
NCIH1155 SNV: p.Q13Ter; p.V281M DBIA    Probe Info 
NCIH2170 SNV: p.G106R DBIA    Probe Info 
RL952 Substitution: p.H24_L25delinsQF DBIA    Probe Info 
SNU1196 SNV: p.E183Q DBIA    Probe Info 

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 18 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info  		C314(3.48); C393(3.04)  LDD3312  [1]
THZ1-DTB
 Probe Info  		C225(1.07)  LDD0460  [2]
BTD
 Probe Info  		C393(0.41)  LDD2089  [3]
AHL-Pu-1
 Probe Info  		C393(2.67)  LDD0168  [4]
HHS-475
 Probe Info  		Y89(0.83)  LDD0264  [5]
IA-alkyne
 Probe Info  		C393(0.00); C225(0.00)  LDD0032  [6]
ATP probe
 Probe Info  		N.A.  LDD0035  [7]
NAIA_4
 Probe Info  		N.A.  LDD2226  [8]
TFBX
 Probe Info  		N.A.  LDD0027  [9]
WYneN
 Probe Info  		C225(0.00); C393(0.00)  LDD0021  [10]
WYneO
 Probe Info  		N.A.  LDD0022  [10]
IPM
 Probe Info  		N.A.  LDD0005  [10]
NHS
 Probe Info  		N.A.  LDD0010  [10]
STPyne
 Probe Info  		N.A.  LDD0009  [10]
Phosphinate-6
 Probe Info  		N.A.  LDD0018  [11]
Ox-W18
 Probe Info  		N.A.  LDD2175  [12]
AOyne
 Probe Info  		10.30  LDD0443  [13]
HHS-465
 Probe Info  		K92(0.00); Y89(0.00)  LDD2240  [14]
PAL-AfBPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
STS-2
 Probe Info  		N.A.  LDD0138  [15]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0524  2-Cyano-N-(2-morpholin-4-yl-ethyl)-acetamide MDA-MB-231 C393(0.91)  LDD2117  [3]
 LDCM0558  2-Cyano-N-phenylacetamide MDA-MB-231 C393(0.91)  LDD2152  [3]
 LDCM0025  4SU-RNA HEK-293T C393(2.67)  LDD0168  [4]
 LDCM0026  4SU-RNA+native RNA HEK-293T C393(2.00)  LDD0169  [4]
 LDCM0545  Acetamide MDA-MB-231 C393(0.51)  LDD2138  [3]
 LDCM0520  AKOS000195272 MDA-MB-231 C393(0.99)  LDD2113  [3]
 LDCM0020  ARS-1620 HCC44 C393(0.96)  LDD2171  [16]
 LDCM0498  BS-3668 MDA-MB-231 C393(0.40)  LDD2091  [3]
 LDCM0630  CCW28-3 231MFP C393(1.44)  LDD2214  [17]
 LDCM0213  Electrophilic fragment 2 MDA-MB-231 C225(2.52)  LDD1702  [3]
 LDCM0116  HHS-0101 DM93 Y89(0.83)  LDD0264  [5]
 LDCM0117  HHS-0201 DM93 Y89(0.58)  LDD0265  [5]
 LDCM0118  HHS-0301 DM93 Y89(0.34)  LDD0266  [5]
 LDCM0119  HHS-0401 DM93 Y89(1.01)  LDD0267  [5]
 LDCM0120  HHS-0701 DM93 Y89(1.53)  LDD0268  [5]
 LDCM0022  KB02 22RV1 C314(1.52); C393(2.03)  LDD2243  [1]
 LDCM0023  KB03 MDA-MB-231 C393(6.86)  LDD1701  [3]
 LDCM0024  KB05 HMCB C314(3.48); C393(3.04)  LDD3312  [1]
 LDCM0528  N-(4-bromophenyl)-2-cyano-N-phenylacetamide MDA-MB-231 C393(0.50)  LDD2121  [3]
 LDCM0496  Nucleophilic fragment 11a MDA-MB-231 C393(0.41)  LDD2089  [3]
 LDCM0497  Nucleophilic fragment 11b MDA-MB-231 C393(1.17)  LDD2090  [3]
 LDCM0500  Nucleophilic fragment 13a MDA-MB-231 C393(0.89)  LDD2093  [3]
 LDCM0514  Nucleophilic fragment 20a MDA-MB-231 C393(0.94)  LDD2107  [3]
 LDCM0516  Nucleophilic fragment 21a MDA-MB-231 C393(0.52)  LDD2109  [3]
 LDCM0518  Nucleophilic fragment 22a MDA-MB-231 C393(0.86)  LDD2111  [3]
 LDCM0522  Nucleophilic fragment 24a MDA-MB-231 C393(0.92)  LDD2115  [3]
 LDCM0525  Nucleophilic fragment 25b MDA-MB-231 C393(0.67)  LDD2118  [3]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C393(1.08)  LDD2120  [3]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C393(0.73)  LDD2123  [3]
 LDCM0531  Nucleophilic fragment 28b MDA-MB-231 C393(0.66)  LDD2124  [3]
 LDCM0532  Nucleophilic fragment 29a MDA-MB-231 C393(0.59)  LDD2125  [3]
 LDCM0536  Nucleophilic fragment 31 MDA-MB-231 C393(0.91)  LDD2129  [3]
 LDCM0541  Nucleophilic fragment 36 MDA-MB-231 C393(0.65)  LDD2134  [3]
 LDCM0542  Nucleophilic fragment 37 MDA-MB-231 C393(1.04)  LDD2135  [3]
 LDCM0543  Nucleophilic fragment 38 MDA-MB-231 C393(1.02)  LDD2136  [3]
 LDCM0546  Nucleophilic fragment 40 MDA-MB-231 C393(0.55)  LDD2140  [3]
 LDCM0552  Nucleophilic fragment 6a MDA-MB-231 C393(0.80)  LDD2146  [3]
 LDCM0554  Nucleophilic fragment 7a MDA-MB-231 C393(0.49)  LDD2148  [3]
 LDCM0559  Nucleophilic fragment 9b MDA-MB-231 C393(1.14)  LDD2153  [3]
 LDCM0627  NUDT7-COV-1 HEK-293T C393(0.92)  LDD2206  [18]
 LDCM0628  OTUB2-COV-1 HEK-293T C393(0.76)  LDD2207  [18]
 LDCM0021  THZ1 HeLa S3 C225(1.07)  LDD0460  [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
TGF-beta receptor type-2 (TGFBR2) TKL Ser/Thr protein kinase family P37173
Other
Click To Hide/Show 3 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
MIF4G domain-containing protein (MIF4GD) MIF4GD family A9UHW6
Chromobox protein homolog 5 (CBX5) . P45973
Telomeric repeat-binding factor 1 (TERF1) . P54274

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 A Chemoproteomic Strategy for Direct and Proteome-Wide Covalent Inhibitor Target-Site Identification. J Am Chem Soc. 2019 Jan 9;141(1):191-203. doi: 10.1021/jacs.8b07911. Epub 2018 Dec 20.
3 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
4 Chemoproteomic capture of RNA binding activity in living cells. Nat Commun. 2023 Oct 7;14(1):6282. doi: 10.1038/s41467-023-41844-z.
Mass spectrometry data entry: PXD044625
5 Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2. Chembiochem. 2021 Jun 15;22(12):2134-2139. doi: 10.1002/cbic.202000879. Epub 2021 Apr 29.
6 SP3-FAIMS Chemoproteomics for High-Coverage Profiling of the Human Cysteinome*. Chembiochem. 2021 May 14;22(10):1841-1851. doi: 10.1002/cbic.202000870. Epub 2021 Feb 18.
Mass spectrometry data entry: PXD023056 , PXD023059 , PXD023058 , PXD023057 , PXD023060
7 Comparison of Quantitative Mass Spectrometry Platforms for Monitoring Kinase ATP Probe Uptake in Lung Cancer. J Proteome Res. 2018 Jan 5;17(1):63-75. doi: 10.1021/acs.jproteome.7b00329. Epub 2017 Nov 22.
Mass spectrometry data entry: PXD006095 , PXD006096
8 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
9 Chemoproteomic Profiling by Cysteine Fluoroalkylation Reveals Myrocin G as an Inhibitor of the Nonhomologous End Joining DNA Repair Pathway. J Am Chem Soc. 2021 Dec 8;143(48):20332-20342. doi: 10.1021/jacs.1c09724. Epub 2021 Nov 24.
Mass spectrometry data entry: PXD029255
10 A modification-centric assessment tool for the performance of chemoproteomic probes. Nat Chem Biol. 2022 Aug;18(8):904-912. doi: 10.1038/s41589-022-01074-8. Epub 2022 Jul 21.
Mass spectrometry data entry: PXD027758 , PXD027755 , PXD027760 , PXD027762 , PXD027756 , PXD027591 , PXD007149 , PXD030064 , PXD032392 , PXD027789 , PXD027767 , PXD027764
11 DFT-Guided Discovery of Ethynyl-Triazolyl-Phosphinates as Modular Electrophiles for Chemoselective Cysteine Bioconjugation and Profiling. Angew Chem Int Ed Engl. 2022 Oct 10;61(41):e202205348. doi: 10.1002/anie.202205348. Epub 2022 Aug 22.
Mass spectrometry data entry: PXD033004
12 Oxidative cyclization reagents reveal tryptophan cation- interactions. Nature. 2024 Mar;627(8004):680-687. doi: 10.1038/s41586-024-07140-6. Epub 2024 Mar 6.
Mass spectrometry data entry: PXD001377 , PXD005252
13 Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe. Redox Biol. 2017 Aug;12:712-718. doi: 10.1016/j.redox.2017.04.001. Epub 2017 Apr 5.
14 Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation. Cell Chem Biol. 2022 Dec 15;29(12):1709-1720.e7. doi: 10.1016/j.chembiol.2022.11.008. Epub 2022 Dec 6.
Mass spectrometry data entry: PXD038010
15 Design and synthesis of minimalist terminal alkyne-containing diazirine photo-crosslinkers and their incorporation into kinase inhibitors for cell- and tissue-based proteome profiling. Angew Chem Int Ed Engl. 2013 Aug 12;52(33):8551-6. doi: 10.1002/anie.201300683. Epub 2013 Jun 10.
16 Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries. Nat Biotechnol. 2021 May;39(5):630-641. doi: 10.1038/s41587-020-00778-3. Epub 2021 Jan 4.
17 Covalent Ligand Screening Uncovers a RNF4 E3 Ligase Recruiter for Targeted Protein Degradation Applications. ACS Chem Biol. 2019 Nov 15;14(11):2430-2440. doi: 10.1021/acschembio.8b01083. Epub 2019 May 13.
18 Rapid Covalent-Probe Discovery by Electrophile-Fragment Screening. J Am Chem Soc. 2019 Jun 5;141(22):8951-8968. doi: 10.1021/jacs.9b02822. Epub 2019 May 22.