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Human EDEM2 proteomics and glycoproteomics datasets

ABSTRACT: The endoplasmic reticulum (ER) homeostasis is maintained by redirecting misfolded or unfolded polypeptide products towards the endoplasmic reticulum associated degradation (ERAD), where proteins are sent to degradation in the ubiquitin-proteasome system. One active–player in this process, is EDEM2 (ER degradation-enhancing alpha-mannosidase-like protein 2), presumably to be one of the first ER mannosidases to act in the early steps of ERAD. Here, we provide a full data set encoding a proteomic, affinity-proteomic and glycoproteomic analysis of melanoma cells with altered expression level of EDEM2. Our affinity-proteomics data are complemented by molecular mass separation of the identified complexes in sucrose fractionation experiments, while the glycoproteomic results allowed the identification of new glycosylation sites regulated by EDEM2 altered expression level. These results were also validated by alternative biochemical methods.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Melanocyte

DISEASE(S): Melanoma

SUBMITTER: Cristian Munteanu

LAB HEAD: Ștefana M. Petrescu

PROVIDER: PXD025881 | Pride | 2021-07-30

REPOSITORIES: Pride

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			Action	DRS
	01A375E2DIG_FullLane.msf	Msf
	01A375E2DIG_frA_run01.raw	Raw
	01A375E2DIG_frB_run03.raw	Raw
	01A375E2DIG_frC_run01.raw	Raw
	01A375E2DIG_frD_run01.raw	Raw

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Human EDEM2 proteomics and glycoproteomics datasets

Project description:The endoplasmic reticulum (ER) homeostasis is maintained by redirecting misfolded or unfolded polypeptide products towards the endoplasmic reticulum associated degradation (ERAD), where proteins are sent to degradation in the ubiquitin-proteasome system. One active–player in this process, is EDEM2 (ER degradation-enhancing alpha-mannosidase-like protein 2), presumably to be one of the first ER mannosidases to act in the early steps of ERAD. Here, we provide a full data set encoding a proteomic, affinity-proteomic and glycoproteomic analysis of melanoma cells with altered expression level of EDEM2. Our affinity-proteomics data are complemented by molecular mass separation of the identified complexes in sucrose fractionation experiments, while the glycoproteomic results allowed the identification of new glycosylation sites regulated by EDEM2 altered expression level. These results were also validated by alternative biochemical methods.

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