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. 2010 Apr 28;299(1):F77–F90. doi: 10.1152/ajprenal.00581.2009

Table 2.

Identification of Na-K-ATPase phosphorylated peptides from ouabain-treated HKC-11 cells

Peptide m/z Putative Modifications Start Sequence End Sequence Missed Cleavages Peptide Amino Acid Sequence
2,554.157 1Phospho 662 683 1 (K)ACVVHGSDLKDMTSEQLDDILK(Y)
1Met-ox
2,093.914 3Phospho 608 625 1 (R)SAGIKVIMVTGDHPITAK (A)
1,139.453 2Phospho 256 264 0 (R)GIVVYTGDR(T)
1,453.528 2Phospho 10 21 0 (K)YEPAAVSEQGDK(K)
2,537.037 3Phospho 75 94 1 (R)DGPNALTPPPTTPEWIKFCR(Q)

Table shows peptide mass, phosphorylation site, and putative peptide sequences from the immunoprecipitated 100-kDa band. The peptide sequences that showed homology with the Na-K-ATPase α1-subunit are shown. Peptide 4 shows the known tyrosine phosphorylation of the Na-K-ATPase α1-subunit (Tyr-10). The other 4 peptides show putative unique serine/tyrosine phosphorylation sites in ouabain-treated samples. These peptides were not identified in control samples.