PRELID3A

Last update 08 May 2025

Basic Info

Synonyms

C18orf43, FLJ31484, HFL-EDDG1

+ [5]

Introduction

In vitro, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space. Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane.

100 Clinical Results associated with PRELID3A

100 Translational Medicine associated with PRELID3A

0 Patents (Medical) associated with PRELID3A

Literatures (Medical) associated with PRELID3A

04 Sep 2015·Journal of Proteome ResearchQ2 · BIOLOGY

PPLine: An Automated Pipeline for SNP, SAP, and Splice Variant Detection in the Context of Proteogenomics

Q2 · BIOLOGY

Article

Author: Kudryavtseva, Anna Viktorovna ; Uroshlev, Leonid Andreevich ; Karpov, Dmitry Sergeevich ; Krasnov, George Sergeevich ; Ponomarenko, Elena Alexandrovna ; Shargunov, Alexander Valerievich ; Archakov, Alexander Ivanovich ; Blinov, Vladimir Mikhailovich ; Poverennaya, Ekaterina Vladimirovna ; Melnikova, Natalya Vladimirovna ; Lisitsa, Andrey Valerievich ; Dmitriev, Alexey Alexandrovich

The fundamental mission of the Chromosome-Centric Human Proteome Project (C-HPP) is the research of human proteome diversity, including rare variants. Liver tissues, HepG2 cells, and plasma were selected as one of the major objects for C-HPP studies. The proteogenomic approach, a recently introduced technique, is a powerful method for predicting and validating proteoforms coming from alternative splicing, mutations, and transcript editing. We developed PPLine, a Python-based proteogenomic pipeline providing automated single-amino-acid polymorphism (SAP), indel, and alternative-spliced-variants discovery based on raw transcriptome and exome sequence data, single-nucleotide polymorphism (SNP) annotation and filtration, and the prediction of proteotypic peptides (available at https://sourceforge.net/projects/ppline). In this work, we performed deep transcriptome sequencing of HepG2 cells and liver tissues using two platforms: Illumina HiSeq and Applied Biosystems SOLiD. Using PPLine, we revealed 7756 SAP and indels for HepG2 cells and liver (including 659 variants nonannotated in dbSNP). We found 17 indels in transcripts associated with the translation of alternate reading frames (ARF) longer than 300 bp. The ARF products of two genes, SLMO1 and TMEM8A, demonstrate signatures of caspase-binding domain and Gcn5-related N-acetyltransferase. Alternative splicing analysis predicted novel proteoforms encoded by 203 (liver) and 475 (HepG2) genes according to both Illumina and SOLiD data. The results of the present work represent a basis for subsequent proteomic studies by the C-HPP consortium.

01 Jul 2015·EMBO reportsQ1 · BIOLOGY

Structural insight into the TRIAP 1/ PRELI ‐like domain family of mitochondrial phospholipid transfer complexes

Q1 · BIOLOGY

Article

Author: Tatsuta, Takashi ; Yague, Ernesto ; Langer, Thomas ; Baldie, Heather ; Matthews, Stephen ; Abid Ali, Ferdos ; Simpson, Peter ; Pérez‐Dorado, Inmaculada ; Miliara, Xeni ; Garnett, James A

The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.

Frontiers in MedicineQ3 · MEDICINE

Identification TRIM46 as a Potential Biomarker and Therapeutic Target for Clear Cell Renal Cell Carcinoma Through Comprehensive Bioinformatics Analyses

Q3 · MEDICINE

ArticleOA

Author: Jiang, Shao-Bo ; Zhao, Jing ; Guo, Xu-Dong ; Xiang, Yu-Zhu ; Liang, Xue-Feng ; Ren, Xiang-Bin

Background: Tripartite motif containing 46 was initially identified as the oncogene in several human tumors. However, the clinical value and potential functions of tripartite motif containing 46 (TRIM46) in clear cell renal cell carcinoma (ccRCC) remained largely unclear.Methods: The expressing patterns, clinical involvement, and prognostic values of TRIM46 were analyzed using the data obtained from TCGA and GEO databases. A nomogram was constructed to examine the outcome of patients with ccRCC. We estimated the association between TRIM46 with tumor immunity in ccRCC.Results: Tripartite motif containing 46 was highly expressed in ccRCC, and its upregulation revealed an unfavorable prognosis. A nomogram based on TRIM46 expressions and other independent prognostic factors could robustly predict the overall survival of tumor patients. TRIM46 has a strong positive correlation with NUMBL, CACNB1, THBS3, ROBO3, MAP3K12, ANKRD13D, PIF1, PRELID3A, ANKRD13B, and PCNX2. Mechanically, TRIM46 displayed regulatory functions in ccRCC progression via several tumor-associated pathways. Besides, we observed that TRIM46 was distinctly related to tumor immunity in ccRCC.Conclusions: Our findings provide a novel tumor promotive role regarding TRIM46 function in the malignant progression of ccRCC.

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PRELID3A

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