Proteomics

Dataset Information

0

Nt-propionylation in yeast - Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo


ABSTRACT: a yNatA N-terminal proteome (WT) was differentialy compared with either a yNatA delta or a yNatA delta/hNatA expressing N-terminal proteome

INSTRUMENT(S): LTQ Orbitrap, instrument model

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

SUBMITTER: Petra Van Damme  

PROVIDER: PRD000673 | Pride | 2013-02-27

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
PRIDE_Exp_Complete_Ac_22438.pride.mgf.gz Mgf
PRIDE_Exp_Complete_Ac_22438.xml.gz Xml
Items per page:
1 - 2 of 2
altmetric image

Publications

Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.

Foyn Håvard H   Van Damme Petra P   Støve Svein I SI   Glomnes Nina N   Evjenth Rune R   Gevaert Kris K   Arnesen Thomas T  

Molecular & cellular proteomics : MCP 20121004 1


N-terminal acetylation (Nt-acetylation) is a highly abundant protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), which transfer an acetyl group from acetyl coenzyme A to the alpha amino group of a nascent polypeptide. Nt-acetylation has emerged as an important protein modifier, steering protein degradation, protein complex formation and protein localization. Very recently, it was reported that some human proteins could carry a propionyl group at their N-terminus  ...[more]

Similar Datasets

| S-EPMC3536908 | biostudies-literature
2024-07-03 | PXD047612 | Pride
2020-12-15 | PXD015217 | Pride
2016-08-02 | E-GEOD-71993 | biostudies-arrayexpress
2015-10-23 | E-GEOD-74279 | biostudies-arrayexpress
| S-EPMC5118915 | biostudies-literature
| S-EPMC2573080 | biostudies-literature
2015-10-23 | GSE74279 | GEO
| S-EPMC6884420 | biostudies-literature
| S-EPMC2688859 | biostudies-other