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Table 2 The background information and their distribution of differentially acetylated sites at lysines in proteins

From: Protein acetylation in mitochondria plays critical functions in the pathogenesis of fatty liver disease

Protein accession numberProtein nameNumber of potential modification sitesNumber of differentially acetylated sitesPositionModified sequenceaAverage fold change of acetylated level by FL/NormMaximum P valueb
Q3SZ00HADHA2314516MQLLEIITTEK(1)TSK1.50 ± 0.49 (n = 14)≤0.0469
P79134ANXA61713306SLYSMIK(1)NDTSGEYK0.59 ± 0.11 (n = 13)≤0.0473
F1ML89CPS13511875LTSIDK(1)WFLYK1.31 ± 0.25 (n = 11)≤0.0179
P12344GOT2161190K(1)AEAQIAAK(1)NLDK1.31 ± 0.25 (n = 11)≤0.0354
Q2KIE6HMGCS21311350LEDTYTNK(1)DVDK(1)AFLK1.96 ± 0.82 (n = 11)≤0.0496
Q29RZ0ACAT11410197IHMGNCAENTAK(1)K1.86 ± 0.38 (n = 10)≤0.0169
A0A140T871GLUD1189460LTFK(1)YER1.42 ± 0.30 (n = 9)≤0.0495
F1N7K8ALDH6A1109333K(1)WLPELVER1.34 ± 0.30 (n = 9)≤0.0246
F1MQV8ACSS3138124HIENGK(1)GDK1.68 ± 0.24 (n = 8)≤0.0083
Q3ZCH0HSPA9108612LK(1)EEISK1.41 ± 0.43 (n = 8)≤0.0302
Q3T0R7ACAA2117240QTMQVDEHPRPQTTMEQLNK(1)LPPVFK(1)K1.47 ± 0.41 (n = 7)≤0.0416
F1MV74SCP297189NHK(1)HSVNNPYSQFQK0.37 ± 0.07 (n = 7)≤0.0017
Q5E9F8H3F3A8728K(1)SAPSTGGVK(0.857)K(0.143)PHR0.58 ± 0.06 (n = 7)≤0.0426
Q32LG3MDH2146328ASIK(1)K(1)GEEFVK1.53 ± 0.21 (n = 6)≤0.0017
F1N206DLD126159ITGK(1)NQVTATK1.26 ± 0.36 (n = 6)≤0.0191
P05307P4HB116387NFEEVAFDEK(1)K0.56 ± 0.06 (n = 6)≤0.0151
P20000ALDH2116371TEQGPQVDETQFK(1)K1.26 ± 0.29 (n = 6))≤0.0176
O46629HADHB106189MMLDLNK(1)AK(1)TLAQR1.43 ± 0.34 (n = 6)≤0.0350
Q0VCM4PYGL96465IHSDIVK(1)TQVFK0.61 ± 0.08 (n = 6)≤0.0433
F1MZP8_76348LVTDFMAK(1)K0.70 ± 0.06 (n = 6)≤0.0358
P52898_76161DAGLTK(1)SIGVSNFNHK0.63 ± 0.09 (n = 6)≤0.0217
  1. a Shown is the distribution range of P-values of all the aceltylated sites in this protein by picking up the ultimate value
  2. b Identified peptide sequence containing acetylated modification sites marked with localization and probabilities