Skip to main content
. Author manuscript; available in PMC: 2015 Aug 1.
Published in final edited form as: Free Radic Biol Med. 2014 Jun 9;73:411–420. doi: 10.1016/j.freeradbiomed.2014.06.002

Table 1.

Identification of 4-HNE and 4-ONE Modified Peptides on Human GRP78

Range Sequence Modified Residue Modification NaBH4 Type Scores Domain
75 – 96 R.LIGDAAK*NQLTSNPENTVFDAK.R K81 4-HNE M.A. X CID 35.6 (M:35.6) ATPase
75 – 96 R.LIGDAAK*NQLTSNPENTVFDAK.R K81 4-ONE S.B CID 25.5 (M:25.5) ATPase
164 – 181 K.K*VTH*AVVTVPAYFNDAQR.Q K164; H167 4-ONE M.A.; 4-ONE M.A. CID 42.5 (M:42.5) ATPase
164 – 181 K.K*VTHAVVTVPAYFNDAQR.Q K164 4-HNE M.A. X CID 38.8 (M:38.8) ATPase
164 – 181 K.K*VTHAVVTVPAYFNDAQR.Q K164 4-HNE S.B CID 48.7 (M:48.7) ATPase
165 – 181 K.VTH*AVVTVPAYFNDAQR.Q H167 4-HNE M.A. X ETD 76.0 (M:76.0) ATPase
165 – 181 K.VTH*AVVTVPAYFNDAQR.Q H167 4-HNE M.A. CID 65.7 (M:65.7) ATPase
165 – 181 K.VTH*AVVTVPAYFNDAQR.Q H167 4-HNE M.A. X ETD 71.2 (M:71.2) ATPase
198 – 214 R.IINEPTAAAIAYGLDK*R.E K213 4-HNE S.B ETD 20.1 (M:20.1) ATPase
198 – 214 R.IINEPTAAAIAYGLDK*R.E K213 4-ONE S.B CID 48.0 (M:48.0) ATPase
298 – 306 R.ALSSQH*QAR.I H303 4-HNE M.A. X CID 56.2 (M:56.2) ATPase
325 – 336 R.AK*FEELNmDLFR.S K326 4-HNE S.B ETD 24.9 (M:24.9) ATPase
353 – 367 K.K*SDIDEIVLVGGSTR.I K353 4-HNE S.B ETD 30.9 (M:30.9) ATPase
368 – 376 R.IPK*IQQLVK.E K370 4-HNE S.B ETD 27.2 (M:27.2) ATPase
368 – 376 R.IPK*IQQLVK.E K370 4-ONE M.A. CID 25.6 (M:25.6) ATPase
475 – 492 K.DNH*LLGTFDLTGIPPAPR.G H477 4-HNE M.A. X ETD 37.2 (M:37.2) Peptide-Binding
475 – 492 K.DNH*LLGTFDLTGIPPAPR.G H477 4-HNE M.A. CID 26.0 (M:26.0) Peptide-Binding
582 – 596 K.LGGK*LSSEDKETmEK.A K585 4-ONE S.B ETD 43.9 (M:43.9) Lid
602 – 617 K.IEWLESH*QDADIEDFK.A H608 4-HNE M.A. X ETD 42.1 (M:42.1) Lid
602 – 617 K.IEWLESH*QDADIEDFK.A H608 4-HNE M.A. CID 32.4 (M:32.4) Lid
602 – 617 K.IEWLESH*QDADIEDFK.A H608 4-HNE M.A. X CID 21.5 (M:21.5) Lid
621 – 633 K.K*ELEEIVQPIISK.L K621 4-HNE M.A. ETD 53.4 (M:53.4) Lid