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Identification of UFBP1 interacting proteins

ABSTRACT: UFBP1 (UFM1-binding and PCI domain-containing protein 1, also called DDRGK domain-containing protein 1, Dashurin, or C20orf116) is a protein that also participates in the ufmylation conjugating systems besides the E1 ubiquitin-like modifier-activating enzyme 5 (UBA5), the E2, UFM1-conjugating enzyme 1 (UFC1), and the E3, UFM1-protein ligase 1 (UFL1). Although this protein play important roles in the ufmylation, its other biological functions have not been explored. To identify the UFBP1 interacting proteins, we expressed GFP (control sample) and FLAG-UFBP1 (experimental sample) in HEK293T cells and purified UFBP1 and its interacting proteins for MS analysis.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Embryonic Stem Cell, Kidney

DISEASE(S): Breast Cancer

SUBMITTER: Dan Li

LAB HEAD: Guoqiang Xu

PROVIDER: PXD009051 | Pride | 2018-05-08

REPOSITORIES: Pride

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			Action	DRS
	20151014Ctrl1Rep1.msf	Msf
	20151014Ctrl1Rep1.raw	Raw
	20151014Ctrl2Rep1.msf	Msf
	20151014Ctrl2Rep1.raw	Raw
	20151014Ctrl3Rep1.msf	Msf

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Publications

Proteomic and Biochemical Analyses Reveal a Novel Mechanism for Promoting Protein Ubiquitination and Degradation by UFBP1, a Key Component of Ufmylation.

Zhu Ying Y Lei Qing Q Li Dan D Zhang Yang Y Jiang Xiaogang X Hu Zhanhong Z Xu Guoqiang G

Journal of proteome research 20180322 4

Protein post-translational modification by ubiquitin-fold modifier 1, UFM1, regulates many biological processes such as response to endoplasmic reticulum stress and regulation of tumor progression. A recent study has indicated that the UFM1-binding and PCI domain-containing protein 1 (UFBP1) is required for the conjugation of UFM1 to a substrate. However, other biological functions of UFBP1 have not been explored. Here, we use immunoprecipitation and label-free quantitative proteomics to identif ...[more]

PMID: 29533670

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