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Omics score: 0

Identify UFM1 targeted protein

ABSTRACT: we want to identify UFM1 target protein in human cells

OTHER RELATED OMICS DATASETS IN: GSE126451

INSTRUMENT(S): LTQ

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Bo Qin

LAB HEAD: Zhenkun Lou

PROVIDER: PXD012729 | Pride | 2019-04-02

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	GFY_21583_sequest.params	Other
	GFY_22726_sequest1.params	Other
	UFM1.tgz	Other
	Vector.tgz	Other
	ufm1.raw	Raw

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Publications

UFL1 promotes histone H4 ufmylation and ATM activation.

Qin Bo B Yu Jia J Nowsheen Somaira S Wang Minghui M Tu Xinyi X Liu Tongzheng T Li Honglin H Wang Liewei L Lou Zhenkun Z

Nature communications 20190318 1

The ataxia-telangiectasia mutated (ATM) kinase, an upstream kinase of the DNA damage response (DDR), is rapidly activated following DNA damage, and phosphorylates its downstream targets to launch DDR signaling. However, the mechanism of ATM activation is still not completely understood. Here we report that UFM1 specific ligase 1 (UFL1), an ufmylation E3 ligase, is important for ATM activation. UFL1 is recruited to double strand breaks by the MRE11/RAD50/NBS1 complex, and monoufmylates histone H4 ...[more]

PMID: 30886146

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The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction

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2018-10-22 | PXD008644 | Pride

LC-MS/MS analysis of ribosome UFMylation in vitro

Project description:UFMylation, is a Ubiquitin-like modification occurring on RPL26, a ribosomal subunit, upon ribosome stalling at the ER membrane. This modification is achieved by a pool of enzymes commonly referred to as E1-activating, E2-conjugating and E3-ligase enzymes. The UFM1 E3 ligase comprises of three proteins: UFL1, UFBP1 and CDK5RAP3, referred to as UFM1 Ribosome E3 Ligase (UREL) complex. While UFL1 and UFBP1 are sufficient for E3 ligase activity in vitro, CDK5RAP3 is indispensable for ribosome UFMylation in vivo. In this work, we characterize in vitro UFMylation reaction of purified 60S ribosomes in the presence and absence of CDK5RAP3 using LC-MS/MS. Specifically, we analyse sites of UFMylation, linkage type and quantify monoUFMylation and diUFMylation on RPL26. Interestingly, we find UFMylation to occur on a specific lysine residue, K134, in the presence of UFL1/UFBP1 alone and in complex with CDK5RAP3. In addition, we also provide quantitative information on relative abundances of RPL26 mono- and di-UFMylation under these conditions.

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Mechanism of 60S ribosomal subunit recognition and UFMylation by the UFM1 E3 ligase complex

Project description:During co-translational translocation at the endoplasmic reticulum (ER), ribosomes can stall and become covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit RPL26 (uL24). This process, known as UFMylation, is mediated by the UFM1 Ribosome E3 Ligase (UREL) complex, comprised of UFL1, UFBP1, and CDK5RAP3. However, the functional consequences of UFMylation and catalytic mechanisms of UREL are unknown. Here, we present crosslinking-mass spectrometry (XL-MS) data of UREL bound to 60S ribosomes.

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NSUN3 and ABH1 modify the wobble position of mt-tRNAMet to expand codon recognition in mitochondrial translation

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Identification of UFBP1 interacting proteins

Project description: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.

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Phase separation and stress granule association of SARS-CoV-2 Nucleocapsid protein

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Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and C53-mediated autophagy

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