Oxidative modification of proteins ubiquitously present in samples irrespective of storage. Modifications labeled with Ox or C represent either peptide oxidation or peptide carbonylation, respectively.
Accession
Description
Sequence
Modification
Day 0
Day 14
Day 35
A0A0K2BMD8
Mutant hemoglobin alpha 2 globin chain
VADALTNAVAHVDDMPNALSALSDLHAHK
Ox
Ox
P00558
Phosphoglycerate kinase 1
AHSSMVGVNLPQK
Ox
IQLINNMLDK
Ox
Ox
SVVLMSHLGRPDGVPMPDK
Ox
VNEMIIGGGMAFTFLK
Ox
P02042
Hemoglobin subunit delta
EFTPQMQAAYQK
Ox
P02549
Spectrin alpha chain, erythrocytic 1
ADMEAEAPTFQALEDFSAELIDSGHHASPEIEK
Ox, C
Ox
Ox
EKMEILDNNWTALLELWDER
Ox
Ox
FSSDFDELSGWMNEK
Ox
Ox, C
Ox
LTLSHPSDAPQIQEMKEDLVSSWEHIR
Ox, C
SDDKSSLDSLEALMK
Ox
Ox
P02730
Band 3 anion transport protein
GLDLNGGPDDPLQQTGQLFGGLVR
C
YTQEIFSFLISLIFIYETFSKLIKIFQDHPLQK
C
PQGPLPNTALLSLVLMAGTFFFAMMLR
Ox
Ox
RYQSSPAKPDSSFYK
Ox
P04075
Fructose-bisphosphate aldolase A
IGEHTPSALAIMENANVLAR
Ox
P04406
Glyceraldehyde-3-phosphate dehydrogenase
WGDAGAEYVVESTGVFTTMEK
Ox
P11166
Solute carrier family 2, facilitated glucose transporter member 1
QGGASQSDKTPEELFHPLGADSQV
C
SFEMLILGR
Ox
P11171
Protein 4.1
SMTPAQADLEFLENAK
Ox
Ox
P11277
Spectrin beta chain, erythrocytic
DEEGAIVMLK
Ox
Ox
DGLNEMWADLLELIDTR
Ox
Ox
DLEDETLWVEER
C
C
ESQQLMDSHPEQK
Ox
GLDAHLEQIFQEAHGMVAR
Ox
Ox
HQAFVAELASHEGWLENIDAEGK
C
KEELGELFAQVPSMGEEGGDADLSIEK
Ox, C
LWSYLQELLQSR
Ox
Ox
QLMDEKPQFTALVSQK
C
C
Ox, C
VISDEIPKDEEGAIVMLK
Ox
P16157
Ankyrin-1
DIEVLEGMSLFAELSGNLVPVKK
Ox
EGQNANMENLYTALQSIDR
Ox
GFTPLYMAAQENHLEVVK
Ox
HGVMVDATTR
Ox
Ox
MGYTPLHVASHYGNIKLVK
Ox, C
SLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSK
Ox, C
TGASIDAVTESGLTPLHVASFMGHLPIVK
Ox
Ox
VETPLHMAAR
Ox
P27105
Erythrocyte band 7 integral membrane protein
EEIAHNMQSTLDDATDAWGIK
Ox
NLSQILSDREEIAHNMQSTLDDATDAWGIK
Ox
Ox
P52209-2
Isoform 2 of 6-phosphogluconate dehydrogenase, decarboxylating
