<%@ Page Language="C#" AutoEventWireup="true" CodeFile="Default.aspx.cs" Inherits="lkem_mtalpd_Default" %> <%@ Register Src="~/templates/LKEMmtalpdHeader.ascx" TagName="Header" TagPrefix="uc2" %> <%@ Register Src="~/templates/Footer.ascx" TagName="Footer" TagPrefix="uc1" %> mTAL Phosphoproteome Database. LKEM, DIR, NHLBI, NIH
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The mTAL Phosphoproteome Database (mTAL-PD) contains phosphoprotein mass spectrometry data from native renal medullary thick ascending limb (mTAL) enriched tubule suspensions.

Experiment description:
Large-scale quantitative phosphoproteomic profiling was performed on paired vehicle- and hormone-treated mTAL-enriched suspensions. The samples were analyzed on an LTQ-Orbitrap mass spectrometer and the resulting MS spectra were searched using three search algorithms: SEQUEST, InsPecT, and OMSSA. In all cases, a target-decoy analysis approach was undertaken to limit the false discovery rate to < 2%. Phosphorylation site assignment was carried out using the following scoring algorithms: Ascore and PhosphoScore for SEQUEST data, and Phosphate Localization Score for InsPecT data. In order to assign a phosphorylation site correctly, at least one score had to pass the given threshold (Ascore = 19, PhosphoScore was "Passed" or "OneChoice" PLS score = 8). Final assignment of phosphorylation sites was performed using the in-house programs, NHLBI Promatch and Phosphosite. Quantification of phosphopeptide abundance (area under the curve of the reconstructed ion chromatogram elution profile) was achieved using QUOIL, an in-house software program designed for quantification of label-free peptides by LC-MS (NHLBI Proteomics Core Facility). As a result, 654 unique phosphopeptides corresponding to 374 unique phosphoproteins were identified.

Description of data format:
The peptide sequence, phosphorylation site(s), and the corresponding protein name, gene symbol, and RefSeq accession number are reported for each phosphopeptide identified in either of three independent experiments. For those phosphopeptides that could be quantified in all three experiments, the mean Log2 (Hormone/Vehicle) abundance ratio and corresponding standard error are also reported.

Peptide Sequence column: * = phosphorylated residue

Site(s) column: ^ = ambiguously assigned phosphorylation site

Log2(H/V) Mean and SE columns: H = hormone-treated, V = vehicle-treated, n/a = peptide not observable in all 3 replicates

Sig. column: * = significantly changed Log2(H/V), p<0.05; ‡= |Log2(H/V)|>0.58

The mTAL-PD was created by Ruwan Gunaratne, Guozhong Ma, Trairak Pisitkun, and Mark A. Knepper. Contact us with questions or comments at knepperm@nhlbi.nih.gov.

Reference:
Gunaratne R, Braucht DW, Rinschen MM, Chou CL, Hoffert JD, Pisitkun T, Knepper MA. Quantitative phosphoproteomic analysis reveals cAMP/vasopressin-dependent signaling pathways in native renal thick ascending limb cells. Proc Natl Acad Sci U S A. 2010 Aug 16. [Epub ahead of print]

Click here to download data in Excel formatExcel File (File size: 201 KB).

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