Proteomics

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Mass spectrometry identification data for the interactomics of SMYD3

ABSTRACT: SMYD3, a member of the SET and MYND domain-containing (SMYD) family, is a histone methyltransferase (HMT) and transcription factor that plays an important role in transcriptional regulation in human carcinogenesis.In an effort to better understanding the mechanistic role of SMYD3, affinity purification and mass spectrometry assays were used to identify proteins associated with SMYD3 in vivo. In these experiments, FLAG-tagged SMYD3 or an empty vector was stably expressed in LM3 cells. Cellular extracts were prepared and subjected to affinity purification using an anti-FLAG affinity gel. Immunocomplexed proteins were separated using SDS–PAGE and silver stained. Immunoprecipitated proteins in specific bands in comparison to the vector were gel extracted, trypsin digested and identified using liquid chromatography tandem mass spectrometry.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Liver

SUBMITTER: Yang Yang  

LAB HEAD: Ji Jiansong

PROVIDER: PXD031971 | Pride | 2023-03-11

REPOSITORIES: Pride

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20P02370001.mgf Mgf
20P02370001.raw Raw
20P02370002.mgf Mgf
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Publications

SMYD3 associates with the NuRD (MTA1/2) complex to regulate transcription and promote proliferation and invasiveness in hepatocellular carcinoma cells.

Yang Yang Y   Qiu Rongfang R   Zhao Siyu S   Shen Lin L   Tang Bufu B   Weng Qiaoyou Q   Xu Ziwei Z   Zheng Liyun L   Chen Weiqian W   Shu Gaofeng G   Wang Yajie Y   Zhao Zhongwei Z   Chen Minjiang M   Ji Jiansong J  

BMC biology 20221227 1

<h4>Background</h4>SMYD3, a member of the SET and MYND domain-containing (SMYD) family, is a histone methyltransferase (HMT) and transcription factor that plays an important role in transcriptional regulation in human carcinogenesis.<h4>Results</h4>Using affinity purification and mass spectrometry assays to identify SMYD3-associated proteins in hepatocellular carcinoma (HCC) cells, we found several previously undiscovered SMYD3-interacting proteins, including the NuRD (MTA1/2) complex, the METTL  ...[more]

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