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Phosphoproteome of filamentous fungus Aspergillus nidulans

ABSTRACT: We describe thephosphoproteome of filamentous fungus Aspergillus nidulans. Phosphopeptides were enriched using affinity enrichment using titanium dioxide and separated using a convenient ultralong gradient separations on c18 reverse phase columns. Over 1637 phosphopeptides corresponding to 647 phosphoproteins were identified using using a “high-high” strategy using HCD on the novel Q-exactive platform

INSTRUMENT(S): Q Exactive

ORGANISM(S): Emericella Nidulans (strain Fgsc A4 / Atcc 38163 / Cbs 112.46 / Nrrl 194 / M139) (aspergillus Nidulans)

SUBMITTER: Nikhil Ramsubramaniam

LAB HEAD: Mark Marten

PROVIDER: PXD000715 | Pride | 2014-11-18

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Inchorus_Peaks_Sequest_OMSSA_peptides.xml	Xml
	TiO2_720MinutesQErep2.raw	Raw
	TiO2_720Minutes_QErep1.raw	Raw
	uniprot-Aspergillusnidulans.fasta	Fasta

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Publications

The phosphoproteome of Aspergillus nidulans reveals functional association with cellular processes involved in morphology and secretion.

Ramsubramaniam Nikhil N Harris Steven D SD Marten Mark R MR

Proteomics 20141008 21-22

We describe the first phosphoproteome of the model filamentous fungus Aspergillus nidulans. Phosphopeptides were enriched using titanium dioxide, separated using a convenient ultra-long reverse phase gradient, and identified using a "high-high" strategy (high mass accuracy on the parent and fragment ions) with higher-energy collisional dissociation. Using this approach 1801 phosphosites, from 1637 unique phosphopeptides, were identified. Functional classification revealed phosphoproteins were ov ...[more]

PMID: 25116090

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