Proteomics

Dataset Information

0

Archael ubiquitin-like SAMP3 is isopeptide-linked to Proteins by an UbaA-dependent mechanism


ABSTRACT: FLAG-SAMP3ylated proteins were immunoprecipitated from Haloferax volcanii using anti-FLAG affinity agarose and separated using SDS-PAGE. The Coomassie-stained IP-bands represented FLAG-SAMP3ylated proteins harvested from the wild type and also from the ubaA mutant as negative control. The Coomassie-lanes from the IP samples were cut into 10 fractions and in-gel tryptic digested and the tryptic peptides measured using Orbitrap Velos LC-MS/MS.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Haloferax Volcanii (halobacterium Volcanii)

SUBMITTER: Haike Antelmann  

LAB HEAD: Haike Antelmann

PROVIDER: PXD000202 | Pride | 2020-07-02

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
110224_OV3_P3_BH_HA_SACO_1_1.raw Raw
110224_OV3_P3_BH_HA_SACO_1_10.raw Raw
110224_OV3_P3_BH_HA_SACO_1_2.raw Raw
110224_OV3_P3_BH_HA_SACO_1_3.raw Raw
110224_OV3_P3_BH_HA_SACO_1_4.raw Raw
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Publications


While many aspects of archaeal cell biology remain relatively unexplored, systems biology approaches like mass spectrometry (MS) based proteomics offer an opportunity for rapid advances. Unfortunately, the enormous amount of MS data generated often remains incompletely analyzed due to a lack of sophisticated bioinformatic tools and field-specific biological expertise for data interpretation. Here we present the initiation of the Archaeal Proteome Project (ArcPP), a community-based effort to comp  ...[more]

Publication: 1/2

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