Details of the Target

General Information of Target

Target ID LDTP01047
Target Name Dolichol-phosphate mannosyltransferase subunit 1 (DPM1)
Gene Name DPM1
Gene ID 8813
Synonyms
Dolichol-phosphate mannosyltransferase subunit 1; EC 2.4.1.83; Dolichol-phosphate mannose synthase subunit 1; DPM synthase subunit 1; Dolichyl-phosphate beta-D-mannosyltransferase subunit 1; Mannose-P-dolichol synthase subunit 1; MPD synthase subunit 1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEI
IIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDAD
LSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGA
SDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESK
LGGNEIVSFLKGLLTLFATT
Target Bioclass
Enzyme
Family
Glycosyltransferase 2 family
Subcellular location
Endoplasmic reticulum
Function
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex.
Uniprot ID
O60762
Ensemble ID
ENST00000371588.10
HGNC ID
HGNC:3005

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 12 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
m-APA
 Probe Info  		9.74  LDD0402  [1]
CHEMBL5175495
 Probe Info  		6.88  LDD0196  [2]
BTD
 Probe Info  		C202(1.60)  LDD1700  [3]
EA-probe
 Probe Info  		N.A.  LDD0440  [4]
DBIA
 Probe Info  		C202(1.16)  LDD1507  [5]
ATP probe
 Probe Info  		K134(0.00); K136(0.00)  LDD0199  [6]
NHS
 Probe Info  		N.A.  LDD0010  [7]
STPyne
 Probe Info  		N.A.  LDD0009  [7]
AOyne
 Probe Info  		15.00  LDD0443  [8]
MPP-AC
 Probe Info  		N.A.  LDD0428  [9]
TER-AC
 Probe Info  		N.A.  LDD0426  [9]
TPP-AC
 Probe Info  		N.A.  LDD0427  [9]
PAL-AfBPP Probe
Click To Hide/Show 7 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C278
 Probe Info  		50.56  LDD1948  [10]
C350
 Probe Info  		23.92  LDD2011  [10]
FFF probe11
 Probe Info  		18.74  LDD0471  [11]
FFF probe3
 Probe Info  		13.54  LDD0464  [11]
STS-2
 Probe Info  		N.A.  LDD0138  [12]
DA-2
 Probe Info  		N.A.  LDD0072  [13]
OEA-DA
 Probe Info  		6.34  LDD0046  [14]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0548  1-(4-(Benzo[d][1,3]dioxol-5-ylmethyl)piperazin-1-yl)-2-nitroethan-1-one MDA-MB-231 C202(0.38)  LDD2142  [3]
 LDCM0519  1-(6-methoxy-3,4-dihydroquinolin-1(2H)-yl)-2-nitroethan-1-one MDA-MB-231 C202(0.55)  LDD2112  [3]
 LDCM0524  2-Cyano-N-(2-morpholin-4-yl-ethyl)-acetamide MDA-MB-231 C202(0.68)  LDD2117  [3]
 LDCM0214  AC1 HEK-293T C202(1.16)  LDD1507  [5]
 LDCM0276  AC17 HEK-293T C202(1.03)  LDD1515  [5]
 LDCM0285  AC25 HEK-293T C202(1.03)  LDD1524  [5]
 LDCM0294  AC33 HEK-293T C202(1.17)  LDD1533  [5]
 LDCM0303  AC41 HEK-293T C202(1.12)  LDD1542  [5]
 LDCM0311  AC49 HEK-293T C202(1.06)  LDD1550  [5]
 LDCM0320  AC57 HEK-293T C202(1.03)  LDD1559  [5]
 LDCM0356  AKOS034007680 HEK-293T C202(1.08)  LDD1570  [5]
 LDCM0156  Aniline NCI-H1299 11.78  LDD0403  [1]
 LDCM0498  BS-3668 MDA-MB-231 C202(0.29)  LDD2091  [3]
 LDCM0404  CL17 HEK-293T C202(0.99)  LDD1608  [5]
 LDCM0417  CL29 HEK-293T C202(1.14)  LDD1621  [5]
 LDCM0431  CL41 HEK-293T C202(1.05)  LDD1635  [5]
 LDCM0440  CL5 HEK-293T C202(1.20)  LDD1644  [5]
 LDCM0444  CL53 HEK-293T C202(1.12)  LDD1647  [5]
 LDCM0457  CL65 HEK-293T C202(1.09)  LDD1660  [5]
 LDCM0470  CL77 HEK-293T C202(1.06)  LDD1673  [5]
 LDCM0483  CL89 HEK-293T C202(1.09)  LDD1686  [5]
 LDCM0175  Ethacrynic acid HeLa N.A.  LDD0440  [4]
 LDCM0500  Nucleophilic fragment 13a MDA-MB-231 C202(0.98)  LDD2093  [3]
 LDCM0501  Nucleophilic fragment 13b MDA-MB-231 C202(1.20)  LDD2094  [3]
 LDCM0503  Nucleophilic fragment 14b MDA-MB-231 C202(0.19)  LDD2096  [3]
 LDCM0505  Nucleophilic fragment 15b MDA-MB-231 C202(0.58)  LDD2098  [3]
 LDCM0511  Nucleophilic fragment 18b MDA-MB-231 C202(0.51)  LDD2104  [3]
 LDCM0512  Nucleophilic fragment 19a MDA-MB-231 C202(1.39)  LDD2105  [3]
 LDCM0514  Nucleophilic fragment 20a MDA-MB-231 C202(0.98)  LDD2107  [3]
 LDCM0516  Nucleophilic fragment 21a MDA-MB-231 C202(0.37)  LDD2109  [3]
 LDCM0518  Nucleophilic fragment 22a MDA-MB-231 C202(0.80)  LDD2111  [3]
 LDCM0523  Nucleophilic fragment 24b MDA-MB-231 C202(0.49)  LDD2116  [3]
 LDCM0525  Nucleophilic fragment 25b MDA-MB-231 C202(0.52)  LDD2118  [3]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C202(0.50)  LDD2120  [3]
 LDCM0529  Nucleophilic fragment 27b MDA-MB-231 C202(0.29)  LDD2122  [3]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C202(0.61)  LDD2123  [3]
 LDCM0531  Nucleophilic fragment 28b MDA-MB-231 C202(0.31)  LDD2124  [3]
 LDCM0532  Nucleophilic fragment 29a MDA-MB-231 C202(0.53)  LDD2125  [3]
 LDCM0533  Nucleophilic fragment 29b MDA-MB-231 C202(0.27)  LDD2126  [3]
 LDCM0534  Nucleophilic fragment 30a MDA-MB-231 C202(0.81)  LDD2127  [3]
 LDCM0535  Nucleophilic fragment 30b MDA-MB-231 C202(0.68)  LDD2128  [3]
 LDCM0536  Nucleophilic fragment 31 MDA-MB-231 C202(1.00)  LDD2129  [3]
 LDCM0543  Nucleophilic fragment 38 MDA-MB-231 C202(0.82)  LDD2136  [3]
 LDCM0211  Nucleophilic fragment 3b MDA-MB-231 C202(1.60)  LDD1700  [3]
 LDCM0546  Nucleophilic fragment 40 MDA-MB-231 C202(0.59)  LDD2140  [3]
 LDCM0549  Nucleophilic fragment 43 MDA-MB-231 C202(0.51)  LDD2143  [3]
 LDCM0550  Nucleophilic fragment 5a MDA-MB-231 C202(2.25)  LDD2144  [3]
 LDCM0552  Nucleophilic fragment 6a MDA-MB-231 C202(0.63)  LDD2146  [3]
 LDCM0555  Nucleophilic fragment 7b MDA-MB-231 C202(0.35)  LDD2149  [3]
 LDCM0557  Nucleophilic fragment 8b MDA-MB-231 C202(0.30)  LDD2151  [3]
 LDCM0559  Nucleophilic fragment 9b MDA-MB-231 C202(1.62)  LDD2153  [3]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 2 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Dolichol-phosphate mannosyltransferase subunit 3 (DPM3) DPM3 family Q9P2X0
Tryptophan 2,3-dioxygenase (TDO2) Tryptophan 2,3-dioxygenase family P48775

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 Charting the Chemical Space of Acrylamide-Based Inhibitors of zDHHC20. ACS Med Chem Lett. 2022 Sep 26;13(10):1648-1654. doi: 10.1021/acsmedchemlett.2c00336. eCollection 2022 Oct 13.
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 Profiling Reveals Ethacrynic Acid Targets Adenine Nucleotide Translocases to Impair Mitochondrial Function. Mol Pharm. 2018 Jun 4;15(6):2413-2422. doi: 10.1021/acs.molpharmaceut.8b00250. Epub 2018 May 15.
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
6 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.
7 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
8 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.
9 Differently Tagged Probes for Protein Profiling of Mitochondria. Chembiochem. 2019 May 2;20(9):1155-1160. doi: 10.1002/cbic.201800735. Epub 2019 Mar 26.
10 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
11 Ligand and Target Discovery by Fragment-Based Screening in Human Cells. Cell. 2017 Jan 26;168(3):527-541.e29. doi: 10.1016/j.cell.2016.12.029. Epub 2017 Jan 19.
12 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.
13 Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes. J Am Chem Soc. 2012 Feb 15;134(6):3001-14. doi: 10.1021/ja208518u. Epub 2012 Feb 1.
14 Mapping Protein Targets of Bioactive Small Molecules Using Lipid-Based Chemical Proteomics. ACS Chem Biol. 2017 Oct 20;12(10):2671-2681. doi: 10.1021/acschembio.7b00581. Epub 2017 Sep 20.
Mass spectrometry data entry: PXD007570