Table 1.

Ace2 phosphorylation sites

Site Local sequence No. identified peptides No. quantified peptides No. replicates quantified Average ratio SD 
S122 SHKRGLSGTAIFG 2.51 0.72 
T135 FLGHNKTLSISSL 2.41 ND 
S137 GHNKTLSISSLQQ ND ND 
S140 KTLSISSLQQSIL ND ND 
T245 KLVSGATNSNSKP 2.44 ND 
S249 GATNSNSKPGSPV 0.93 0.02 
S253 SNSKPGSPVILKT 1.43 0.73 
S709 KKSLLDSPHDTSP 1.54 0.29 
T713 LDSPHDTSPVKET 1.62 0.24 
S714 DSPHDTSPVKETI 1.27 0.05 
Site Local sequence No. identified peptides No. quantified peptides No. replicates quantified Average ratio SD 
S122 SHKRGLSGTAIFG 2.51 0.72 
T135 FLGHNKTLSISSL 2.41 ND 
S137 GHNKTLSISSLQQ ND ND 
S140 KTLSISSLQQSIL ND ND 
T245 KLVSGATNSNSKP 2.44 ND 
S249 GATNSNSKPGSPV 0.93 0.02 
S253 SNSKPGSPVILKT 1.43 0.73 
S709 KKSLLDSPHDTSP 1.54 0.29 
T713 LDSPHDTSPVKET 1.62 0.24 
S714 DSPHDTSPVKETI 1.27 0.05 

The table shows all identified and quantified phosphosites in Ace2. The phosphorylated residue is shown in bold in the context of its flanking sequence. Six sites were identified in two out of three biological replicates, and out of those six, four showed increased phosphorylation above the log2 threshold: S122, S253, S709, and T713.

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