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ProteomicsPRMT6 substrate specificity analysis
Protein arginine methyltransferase 6 (PRMT6) catalyses the asymmetric dimethylation of arginines on numerous substrate proteins within the human cell. In particular, PRMT6 methylates histone H3 arginine 2 (H3R2) which affects both gene repression and activation. However, the substrate specificity of...
ORGANISM(S): Homo Sapiens 
PXD016711 | panorama
GenomicsStructural basis for substrate recognition and chemical inhibition of oncogenic MAGE ubiquitin ligases
Structural basis for substrate recognition and chemical inhibition of oncogenic MAGE ubiquitin ligases
PRJNA624321 | ENA
UnknownElectrostatic recognition in substrate binding to serine proteases.
Not available
S-EPMC6175425 | biostudies-literature
TranscriptomicsStructural basis for substrate recognition and chemical inhibition of oncogenic MAGE ubiquitin ligases
Testis-restricted melanoma antigen (MAGE) proteins are frequently hijacked in cancer and play a critical role in tumorigenesis. MAGEs assemble with E3 ubiquitin ligases and function as substrate adaptors that direct the ubiquitination of novel targets, including key tumor suppressors. However, how M...
ORGANISM(S): Homo sapiens 
2020-08-15 | GSE148458 | GEO
TranscriptomicsThe tumor antigen PRAME is a substrate recognition subunit of a Cul2-based ubiquitin ligase and is associated with active NFY promoters
The human tumor antigen PRAME (Preferentially expressed antigen of melanoma) is frequently overexpressed in tumors. High PRAME levels correlate with poor clinical outcome of several cancers, but the mechanisms by which PRAME could be involved in tumorigenesis remain largely elusive. We applied prote...
ORGANISM(S): Homo sapiens 
2011-07-29 | E-GEOD-26439 | biostudies-arrayexpress
ProteomicsDecoding isozyme-specific substrate recognition in protein arginine deiminases by in vitro proteome-wide citrullination mapping
Protein arginine deiminases (PADs) convert arginine to citrulline, altering protein structure and function. Of the five human isozymes, PAD1–4 are catalytically active with distinct tissue-specificities, yet isozyme-specific substrate recognition remains poorly defined. Here, we provide a systematic...
ORGANISM(S): Homo sapiens (Human) 
2026-04-22 | PXD071247 | Pride
TranscriptomicsFunctional signature for the recognition of specific target mRNAs by human staufen1 protein
Cellular mRNAs are permanently associated to proteins in the form of ribonucleoprotein particles. In addition to the hnRNP and SR protein families, the double-stranded RNA-binding (DRB) proteins play important roles in mRNA synthesis, modification, activity and decay (Dreyfuss et al, 2002; Stutz & I...
ORGANISM(S): Homo sapiens 
2014-02-06 | E-GEOD-47226 | biostudies-arrayexpress
TranscriptomicsCotranslational signal independent SRP preloading during membrane targeting
Cotranslational targeting into the endoplasmic reticulum (ER) by the Signal Recognition Particle (SRP) is a key event determining polypeptide fate in eukaryotic cells. Here, we globally define the principles and mechanisms of SRP binding and ER targeting in vivo. Cotranslational targeting through SR...
ORGANISM(S): Saccharomyces cerevisiae 
2016-08-03 | E-GEOD-74393 | biostudies-arrayexpress
UnknownHIV-1 Protease and Substrate Coevolution Validates the Substrate Envelope As the Substrate Recognition Pattern.
Not available
S-EPMC3862175 | biostudies-literature
TranscriptomicsDual regulation of Fbw7 function and oncogenic transformation by Usp28
Fbw7, the substrate recognition subunit of SCF(Fbw7) ubiquitin ligase, mediates turnover of multiple proto-oncoproteins and promotes its own degradation. Fbw7-mediated substrate degradation is antagonized by the Usp28 deubiquitinase. We now show, using knockout mice, that Usp28 preferentially deubiq...
ORGANISM(S): Mus musculus 
2015-05-01 | E-GEOD-59354 | biostudies-arrayexpress
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