Proteomics

Dataset Information

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N-terminal acetyaltion of Human JunB in yeast expressing all N-terminal acetyltransferases, no NatA enzyme or no NatB enzyne


ABSTRACT: Define the N-terminal status of overexpressed human JUNB in WT yeast strain, NAA10 Δ strain and NAA20 Δ strain.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Malin Lundekvam  

LAB HEAD: Thomas Arnesen

PROVIDER: PXD047612 | Pride | 2024-07-03

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
10_1.mzML Mzml
10_1.mzid.gz Mzid
10_1.raw Raw
10_2.mzML Mzml
10_2.mzid.gz Mzid
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Publications

N-terminal cysteine acetylation and oxidation patterns may define protein stability.

Heathcote Karen C KC   Keeley Thomas P TP   Myllykoski Matti M   Lundekvam Malin M   McTiernan Nina N   Akter Salma S   Masson Norma N   Ratcliffe Peter J PJ   Arnesen Thomas T   Flashman Emily E  

Nature communications 20240625 1


Oxygen homeostasis is maintained in plants and animals by O<sub>2</sub>-sensing enzymes initiating adaptive responses to low O<sub>2</sub> (hypoxia). Recently, the O<sub>2</sub>-sensitive enzyme ADO was shown to initiate degradation of target proteins RGS4/5 and IL32 via the Cysteine/Arginine N-degron pathway. ADO functions by catalysing oxidation of N-terminal cysteine residues, but despite multiple proteins in the human proteome having an N-terminal cysteine, other endogenous ADO substrates ha  ...[more]

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