Proteomics

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Quantification of highly homologous Major Urinary Proteins in wild house mice

ABSTRACT: Male house mice were housed under semi-natural conditions and their urinary proteins were quantified using MS1 and MS2 based label-free strategies. This dataset consists of 52 raw MS files, comprising 26 DIA (SWATH) and 26 IDA runs on a TripleTOF 5600. The composition of the dataset is described in the manuscript by Enk et al., titled: "Regulation of highly homologous Major Urinary Proteins in house mice quantified with label-free proteomic methods ", Molecular Biosystems, in review.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Urine

SUBMITTER: Viktoria Enk  

LAB HEAD: Ebrahim Razzazi-Fazeli

PROVIDER: PXD004642 | Pride | 2016-08-08

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Ionlibrary_MUP_database.mgf Mgf
Ionlibrary_MUP_database.mzIdentML Mzid
Ionlibrary_swissprot_mouse_unreviewed_MUPs.mgf Mgf
Ionlibrary_swissprot_mouse_unreviewed_MUPs.mzIdentML Mzid
MUP_01.wiff_centroid.mzML Mzml
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Publications

Regulation of highly homologous major urinary proteins in house mice quantified with label-free proteomic methods.

Enk Viktoria M VM   Baumann Christian C   Thoß Michaela M   Luzynski Kenneth C KC   Razzazi-Fazeli Ebrahim E   Penn Dustin J DJ  

Molecular bioSystems 20160728 10

Major urinary proteins (MUPs) are highly homologous proteoforms that function in binding, transporting and releasing pheromones in house mice. The main analytical challenge for studying variation in MUPs, even for state-of-the-art proteomics techniques, is their high degree of amino acid sequence homology. In this study we used unique peptides for proteoform-specific identification. We applied different search engines (ProteinPilot™vs. PEAKS®) and protein databases (MUP database vs. SwissProt +  ...[more]

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