JPOST Repositoryapplication/xmlhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT%20R43L_TPD54-BirA_3.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT%20R43L_TPD54-BirA_1.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT_TPD54-BirA_1.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT_TPD54-BirA_3.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT%20R43L_TPD54-BirA_2.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT_TPD54-BirA_1.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT%20R43L_TPD54-BirA_3.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT_TPD54-BirA_3.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT%20R43L_TPD54-BirA_2.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT%20R43L_TPD54-BirA_4.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT_TPD54-BirA_2.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT_TPD54-BirA_2.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT%20R43L_TPD54-BirA_1.rawhttps://storage.jpostdb.org/JPST003761/files/Batch2_EcFMT_TPD54-BirA_4.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT%20R43L_TPD54-BirA_4.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_EcFMT_TPD54-BirA_4.rawhttps://storage.jpostdb.org/JPST003761/files/Batch1_BirA_LFQ_UNIPROT.BT.mgfhttps://storage.jpostdb.org/JPST003761/files/Batch2_BirA_LFQ_UNIPROT_BT.mgfhttps://storage.jpostdb.org/JPST003761/files/Batch1_BirA_LFQ_UNIPROT_BT.mzTabhttps://storage.jpostdb.org/JPST003761/files/Batch2_BirA_LFQ_UNIPROT_BT.mzTabprimaryOK200ProteomicsCheol-Sang HwangHomo Sapiens (human)https://repository.jpostdb.org/entry/JPST003761Korea universityjPOSTfalseN-terminal formylation-dependent protein interactions in human cellsN-terminal formylation of methionine is a unique protein modification found in prokaryotes, as well as in the mitochondria, chloroplasts, and even the cytosol of eukaryotic cells. Recent studies have revealed that human cells are capable of producing cytosolic proteins bearing N-terminal formylmethionine. This project aims to investigate N-terminal formylation-dependent interaction changes of the human tumor protein TPD54. Specifically, HeLa cells were transfected with TPD54-BirA*, along with either E. coli formyltransferase (EcFMT) or its catalytically inactive R43L mutant, to manipulate the formylation status.Thu Jun 04 00:00:00 BST 2026PXD0629089606