OMIX009221

1Summary
Title TRIM21 orchestrates AKT K27-linked ubiquitination to counteract cancer chemotherapeutic resistance
Description Ubiquitin modifications play diverse and predominant roles in virous physiological and pathological processes. However, the impact of atypical ubiquitin modification on AKT and its potential role in tumorigenesis remain largely unclear. Although K48-linked ubiquitin-mediated degradation of phosphorylated AKT and K63-linked ubiquitin-mediated activation of AKT have been reported, whether and how AKT undergoes non-canonical types of ubiquitination in pathophysiological conditions have not been defined.Through systematic ubiquitin analyses, we have observed that AKT undergoes K27-linked ubiquitination to imply its negative regulation conditions.
Organism Homo sapiens
Data Type Proteomic Data by Mass Spectrometry (MS)
Data Accessibility Open-access
BioProject PRJCA036661
Release Date 2025-02-27
Submitter Jianping Guo (guojp6@mail.sysu.edu.cn)
Organization The First Affiliated Hospital, Sun Yat-sen University
Submission Date 2025-02-27
2Files & Download

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File ID File Title Number/Samples File Type File Size File Suffix Download
OMIX009221-01 TNF_EV 1 Proteomic Data by Mass Spectrometry (MS) 653.86 MB zip
OMIX009221-02 TNF_AKT 1 Proteomic Data by Mass Spectrometry (MS) 818.3 MB zip
OMIX009221-03 LPS_EV 1 Proteomic Data by Mass Spectrometry (MS) 546.16 MB zip
OMIX009221-04 LPS_AKT 1 Proteomic Data by Mass Spectrometry (MS) 551.57 MB zip
3Relevant Publications
Paper Title Journal Name Publish Time Accession Citing Type
TRIM21 and OTUD6A orchestrate AKT K27-linked atypical ubiquitination to modulate cancer chemoresistance Nature Structural & Molecular Biology 2025-11 OMIX009221 Deposit

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