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Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,

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Presentation on theme: "Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,"— Presentation transcript:

1 Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides, phosphorylation events, and a breakdown of the types of phosphorylation sites found are shown. Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides, phosphorylation events, and a breakdown of the types of phosphorylation sites found are shown. B, the distribution of the number of phosphorylation events per phosphopeptide shows that the majority of phosphopeptides were singly and doubly phosphorylated peptides, but good coverage of highly phosphorylated peptides was also achieved. Mark O. Collins et al. Mol Cell Proteomics 2008;7: © 2008 The American Society for Biochemistry and Molecular Biology

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14-3-3 binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for 14-3-3 binding. 50 of these correspond.

binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.
Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.

Quantification of C-terminal phosphorylation of AtPIP2;1 upon NaCl (A) and H2O2 (B) treatments.A, plants were either untreated (white bars) or treated.
Sequence alignment of C-terminal phosphorylated plant aquaporins

Sequence alignment of C-terminal phosphorylated plant aquaporins
Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.

Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.
MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.

MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z 1188.53).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).
Distribution of disorder in the cytosolic phosphoproteome

Distribution of disorder in the cytosolic phosphoproteome
Experimental overview A sequential protein and peptide IMAC enrichment was analyzed by four different LC-MS/MS strategies. Experimental overview A sequential.

Experimental overview A sequential protein and peptide IMAC enrichment was analyzed by four different LC-MS/MS strategies. Experimental overview A sequential.
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z 1617.55).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
Fast protein LC IMAC purification of cytosolic phosphoproteins

Fast protein LC IMAC purification of cytosolic phosphoproteins
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z 1217.53).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z ).
Phosphopeptides identified harboring minimal binding motifs

Phosphopeptides identified harboring minimal binding motifs
Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.

Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Novel phosphorylation sites on H+-ATPase proteins

Novel phosphorylation sites on H+-ATPase proteins
Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.

Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.
Phosphorylation reduces peptide solution charge state and alters SCX elution at low pH.A, at pH 2.7, a theoretical tryptic peptide without histidine residues.

Phosphorylation reduces peptide solution charge state and alters SCX elution at low pH.A, at pH 2.7, a theoretical tryptic peptide without histidine residues.
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,

Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.

Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.
Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.

Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.

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