Proteins > Lethal(3)malignant brain tumor-like protein 3
Page last updated: 2024-08-08 00:09:21
Lethal(3)malignant brain tumor-like protein 3
A lethal(3)malignant brain tumor-like protein 3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q96JM7]
Synonyms
H-l(3)mbt-like protein 3;
L(3)mbt-like protein 3;
L3mbt-like 3;
MBT-1
Research
Bioassay Publications (5)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 5 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Compounds (5)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
entecavir | Homo sapiens (human) | Kd | 0.1200 | 3 | 2 |
The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.MedChemComm, , Volume: 4, Issue:11, 2013
Small-molecule ligands of methyl-lysine binding proteins: optimization of selectivity for L3MBTL3.Journal of medicinal chemistry, , Sep-26, Volume: 56, Issue:18, 2013
Small-molecule ligands of methyl-lysine binding proteins.Journal of medicinal chemistry, , Apr-14, Volume: 54, Issue:7, 2011
Discovery of a Potent and Selective Fragment-like Inhibitor of Methyllysine Reader Protein Spindlin 1 (SPIN1).Journal of medicinal chemistry, , 10-24, Volume: 62, Issue:20, 2019
The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.MedChemComm, , Volume: 4, Issue:11, 2013
Small-molecule ligands of methyl-lysine binding proteins: optimization of selectivity for L3MBTL3.Journal of medicinal chemistry, , Sep-26, Volume: 56, Issue:18, 2013
[no title available],
Enables
This protein enables 6 target(s):
Target | Category | Definition |
chromatin binding | molecular function | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. [GOC:jl, ISBN:0198506732, PMID:20404130] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
methylation-dependent protein binding | molecular function | Binding to a protein upon methylation of the target protein. [PMID:26060076] |
histone binding | molecular function | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. [GOC:jl, PMID:16209651, PMID:30212449, PMID:9305837] |
Located In
This protein is located in 2 target(s):
Target | Category | Definition |
nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
nucleolus | cellular component | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732] |
Active In
This protein is active in 1 target(s):
Target | Category | Definition |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
Involved In
This protein is involved in 7 target(s):
Target | Category | Definition |
chromatin organization | biological process | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. [PMID:20404130] |
macrophage differentiation | biological process | The process in which a relatively unspecialized monocyte acquires the specialized features of a macrophage. [GOC:add, ISBN:0781735149] |
granulocyte differentiation | biological process | The process in which a myeloid precursor cell acquires the specialized features of a granulocyte. Granulocytes are a class of leukocytes characterized by the presence of granules in their cytoplasm. These cells are active in allergic immune reactions such as arthritic inflammation and rashes. This class includes basophils, eosinophils and neutrophils. [GOC:ecd, http://life.nthu.edu.tw/~g864204/dict-search1.htm] |
erythrocyte maturation | biological process | A developmental process, independent of morphogenetic (shape) change, that is required for an erythrocyte to attain its fully functional state. [GOC:devbiol, GOC:jl] |
negative regulation of DNA-templated transcription | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
regulation of DNA methylation-dependent heterochromatin formation | biological process | Any process that modulates the rate, frequency, or extent of DNA methylation-dependent heterochromatin formation. [GOC:BHF] |
positive regulation of ubiquitin-dependent protein catabolic process | biological process | Any process that activates or increases the frequency, rate or extent of ubiquitin-dependent protein catabolic process. [GOC:BHF] |