Details of the Target

General Information of Target

Target ID LDTP14534
Target Name Arginyl-tRNA--protein transferase 1 (ATE1)
Gene Name ATE1
Gene ID 11101
Synonyms
Arginyl-tRNA--protein transferase 1; Arginyltransferase 1; R-transferase 1; EC 2.3.2.8; Arginine-tRNA--protein transferase 1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MGIFPGIILIFLRVKFATAAVIVSGHQKSTTVSHEMSGLNWKPFVYGGLASIVAEFGTFP
VDLTKTRLQVQGQSIDARFKEIKYRGMFHALFRICKEEGVLALYSGIAPALLRQASYGTI
KIGIYQSLKRLFVERLEDETLLINMICGVVSGVISSTIANPTDVLKIRMQAQGSLFQGSM
IGSFIDIYQQEGTRGLWRGVVPTAQRAAIVVGVELPVYDITKKHLILSGMMGDTILTHFV
SSFTCGLAGALASNPVDVVRTRMMNQRAIVGHVDLYKGTVDGILKMWKHEGFFALYKGFW
PNWLRLGPWNIIFFITYEQLKRLQI
Target Bioclass
Enzyme
Family
R-transferase family
Subcellular location
Cytoplasm; Nucleus
Function
Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues.
Uniprot ID
O95260
Ensemble ID
ENST00000224652.12
HGNC ID
HGNC:782

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
22RV1 SNV: p.R56Q .
HCT15 SNV: p.S150R DBIA    Probe Info 
HT115 SNV: p.I147N .
HUH7 SNV: p.N35H DBIA    Probe Info 
IM95 SNV: p.L385P DBIA    Probe Info 
MM1S SNV: p.R452C .
NCIH1793 SNV: p.Y344Ter DBIA    Probe Info 
NCIH1993 SNV: p.G7S .
SUPT1 Deletion: p.G7VfsTer36 DBIA    Probe Info 
TE1 SNV: p.D113G DBIA    Probe Info 

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 17 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
m-APA
 Probe Info  		14.90  LDD0402  [1]
BTD
 Probe Info  		C138(1.32)  LDD1699  [2]
IPM
 Probe Info  		C138(0.00); C205(0.00); C79(0.00); C71(0.00)  LDD0241  [3]
Probe 1
 Probe Info  		Y501(7.84)  LDD3495  [4]
HHS-475
 Probe Info  		Y63(0.65)  LDD0264  [5]
DBIA
 Probe Info  		C71(1.14); C72(1.14)  LDD0078  [6]
4-Iodoacetamidophenylacetylene
 Probe Info  		N.A.  LDD0038  [7]
IA-alkyne
 Probe Info  		C79(0.00); C205(0.00); C429(0.00); C441(0.00)  LDD0036  [7]
Lodoacetamide azide
 Probe Info  		C79(0.00); C429(0.00); C138(0.00); C205(0.00)  LDD0037  [7]
WYneN
 Probe Info  		N.A.  LDD0021  [8]
WYneO
 Probe Info  		N.A.  LDD0022  [8]
TFBX
 Probe Info  		N.A.  LDD0148  [9]
VSF
 Probe Info  		N.A.  LDD0007  [8]
W1
 Probe Info  		C138(0.00); C205(0.00)  LDD0236  [3]
AOyne
 Probe Info  		11.50  LDD0443  [10]
NAIA_5
 Probe Info  		N.A.  LDD2223  [11]
HHS-482
 Probe Info  		Y63(0.46)  LDD2239  [12]
PAL-AfBPP Probe
Click To Hide/Show 4 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C087
 Probe Info  		8.22  LDD1779  [13]
C129
 Probe Info  		5.17  LDD1811  [13]
C165
 Probe Info  		22.47  LDD1845  [13]
C166
 Probe Info  		9.58  LDD1846  [13]

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 C205(0.93)  LDD2117  [2]
 LDCM0156  Aniline NCI-H1299 14.37  LDD0403  [1]
 LDCM0020  ARS-1620 HCC44 C71(1.14); C72(1.14)  LDD0078  [6]
 LDCM0498  BS-3668 MDA-MB-231 C205(1.18)  LDD2091  [2]
 LDCM0213  Electrophilic fragment 2 MDA-MB-231 C205(1.02)  LDD1702  [2]
 LDCM0116  HHS-0101 DM93 Y63(0.65)  LDD0264  [5]
 LDCM0118  HHS-0301 DM93 Y63(0.79)  LDD0266  [5]
 LDCM0119  HHS-0401 DM93 Y63(6.35)  LDD0267  [5]
 LDCM0120  HHS-0701 DM93 Y63(6.33)  LDD0268  [5]
 LDCM0022  KB02 42-MG-BA C310(1.41)  LDD2244  [14]
 LDCM0023  KB03 MDA-MB-231 C205(1.32)  LDD1701  [2]
 LDCM0024  KB05 G361 C79(1.67); C72(0.91)  LDD3311  [14]
 LDCM0528  N-(4-bromophenyl)-2-cyano-N-phenylacetamide MDA-MB-231 C205(0.41)  LDD2121  [2]
 LDCM0505  Nucleophilic fragment 15b MDA-MB-231 C205(0.69)  LDD2098  [2]
 LDCM0512  Nucleophilic fragment 19a MDA-MB-231 C205(1.15)  LDD2105  [2]
 LDCM0514  Nucleophilic fragment 20a MDA-MB-231 C138(1.42)  LDD2107  [2]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C205(0.91)  LDD2120  [2]
 LDCM0529  Nucleophilic fragment 27b MDA-MB-231 C205(1.06)  LDD2122  [2]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C205(1.31)  LDD2123  [2]
 LDCM0534  Nucleophilic fragment 30a MDA-MB-231 C205(0.76)  LDD2127  [2]
 LDCM0535  Nucleophilic fragment 30b MDA-MB-231 C205(1.11)  LDD2128  [2]
 LDCM0211  Nucleophilic fragment 3b MDA-MB-231 C205(0.81)  LDD1700  [2]
 LDCM0552  Nucleophilic fragment 6a MDA-MB-231 C205(0.71)  LDD2146  [2]
 LDCM0556  Nucleophilic fragment 8a MDA-MB-231 C205(0.31)  LDD2150  [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
Histone-lysine N-methyltransferase SUV39H1 (SUV39H1) Histone-lysine methyltransferase family O43463

References

1 Quantitative and Site-Specific Chemoproteomic Profiling of Targets of Acrolein. Chem Res Toxicol. 2019 Mar 18;32(3):467-473. doi: 10.1021/acs.chemrestox.8b00343. Epub 2019 Jan 15.
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 Oxidant-Induced Bioconjugation for Protein Labeling in Live Cells. ACS Chem Biol. 2023 Jan 20;18(1):112-122. doi: 10.1021/acschembio.2c00740. Epub 2022 Dec 21.
4 An Azo Coupling-Based Chemoproteomic Approach to Systematically Profile the Tyrosine Reactivity in the Human Proteome. Anal Chem. 2021 Jul 27;93(29):10334-10342. doi: 10.1021/acs.analchem.1c01935. Epub 2021 Jul 12.
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 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.
7 Enhancing Cysteine Chemoproteomic Coverage through Systematic Assessment of Click Chemistry Product Fragmentation. Anal Chem. 2022 Mar 8;94(9):3800-3810. doi: 10.1021/acs.analchem.1c04402. Epub 2022 Feb 23.
Mass spectrometry data entry: PXD028853
8 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
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 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.
11 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
12 Global targeting of functional tyrosines using sulfur-triazole exchange chemistry. Nat Chem Biol. 2020 Feb;16(2):150-159. doi: 10.1038/s41589-019-0404-5. Epub 2019 Nov 25.
13 Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells. Science. 2024 Apr 26;384(6694):eadk5864. doi: 10.1126/science.adk5864. Epub 2024 Apr 26.
Mass spectrometry data entry: PXD041587
14 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