General Information of Target

Target ID LDTP04908
Target Name DNA-directed RNA polymerases I, II, and III subunit RPABC2 (POLR2F)
Gene Name POLR2F
Gene ID 5435
Synonyms
POLRF; DNA-directed RNA polymerases I, II, and III subunit RPABC2; RNA polymerases I, II, and III subunit ABC2; DNA-directed RNA polymerase II subunit F; DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide; RPABC14.4; RPB14.4; RPB6 homolog; RPC15
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MSDNEDNFDGDDFDDVEEDEGLDDLENAEEEGQENVEILPSGERPQANQKRITTPYMTKY
ERARVLGTRALQIAMCAPVMVELEGETDPLLIAMKELKARKIPIIIRRYLPDGSYEDWGV
DELIITD
Target Bioclass
Enzyme
Family
Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family
Subcellular location
Nucleus
Function
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPABC2 is part of the clamp element and together with parts of POLR2A/RPB1 and POLR2B/RPB2 forms a pocket to which the POLR2D/RPB4-POLR2G/RPB7 subcomplex binds.
Uniprot ID
P61218
Ensemble ID
ENST00000442738.7
HGNC ID
HGNC:9193

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 6 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
Probe 1
 Probe Info 
Y56(12.01)  LDD3495  [1]
DBIA
 Probe Info 
C76(1.01)  LDD3312  [2]
JW-RF-010
 Probe Info 
N.A.  LDD0026  [3]
NAIA_4
 Probe Info 
N.A.  LDD2226  [4]
Phosphinate-6
 Probe Info 
N.A.  LDD0018  [5]
NAIA_5
 Probe Info 
N.A.  LDD2223  [4]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0259  AC14 HEK-293T C76(1.28)  LDD1512  [6]
 LDCM0282  AC22 HEK-293T C76(0.99)  LDD1521  [6]
 LDCM0291  AC30 HEK-293T C76(1.23)  LDD1530  [6]
 LDCM0299  AC38 HEK-293T C76(0.99)  LDD1538  [6]
 LDCM0308  AC46 HEK-293T C76(1.57)  LDD1547  [6]
 LDCM0317  AC54 HEK-293T C76(0.94)  LDD1556  [6]
 LDCM0323  AC6 HEK-293T C76(0.80)  LDD1562  [6]
 LDCM0326  AC62 HEK-293T C76(1.02)  LDD1565  [6]
 LDCM0368  CL10 HEK-293T C76(0.26)  LDD1572  [6]
 LDCM0410  CL22 HEK-293T C76(0.51)  LDD1614  [6]
 LDCM0423  CL34 HEK-293T C76(0.48)  LDD1627  [6]
 LDCM0436  CL46 HEK-293T C76(0.68)  LDD1640  [6]
 LDCM0449  CL58 HEK-293T C76(0.59)  LDD1652  [6]
 LDCM0463  CL70 HEK-293T C76(0.46)  LDD1666  [6]
 LDCM0476  CL82 HEK-293T C76(0.43)  LDD1679  [6]
 LDCM0489  CL94 HEK-293T C76(0.74)  LDD1692  [6]
 LDCM0022  KB02 22RV1 C76(0.67)  LDD2243  [2]
 LDCM0023  KB03 22RV1 C76(0.61)  LDD2660  [2]
 LDCM0024  KB05 HMCB C76(1.01)  LDD3312  [2]

References

1 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.
2 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
3 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
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 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
6 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