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. 2013 Mar;1828(3):956–966. doi: 10.1016/j.bbamem.2012.11.030

Table 1.

Identified sites containing EGS-derived modifications.

Protein Position Peptide Structural feature Identification (#)a (% of total counts)
Stomatin 9–25 DSEAQRLPDSFKDSPSK N-terminus 1 (1%)
15–25 LPDSFKDSPSK N-terminus 24 (25%)
56–62 IIKEYER CRAC motif b 5 (5%)
196–205 DVKLPVQLQR β6c 2 (2%)
219–232 AKVIAAGEMNASR α5c 64 (67%)
Band 3 346–360 RYQSSPAKPDSSFYK N-terminal domain 2 (9%)
347–360 YQSSPAKPDSSFYK N-terminal domain 12 (52%)
591–600 FKNSSYFPGK Loop TM6–7 3 (13%)
593–602 NSSYFPGKLR Loop TM6–7 2 (9%)
731–743 SVTHANALTVMGK Loop TM9–10 3 (13%)
818–827 YHPDVPYVKR Loop TM11–12 1 (4%)
GLUT1 224–229 AKSVLK Loop TM6–7 3 (30%)
224–230 AKSVLKK Loop TM6–7 6 (60%)
226–232 SVLKKLR Loop TM6–7 1 (10%)
UT1 362–374 MPLSKVTYPEENR C-terminus 1
375–382 IFYLQAKK C-terminus 1
Flot1 169–177 TAQVQKDAR α5-equivalentc 1 (20%)
178–185 IGEAEAKR α5-equivalentc 3 (60%)
245–253 TKQQIEEQR Coiled-coil 1 (20%)
Flot2 278–287 TDKELIATVR Coiled-coil 1
RhCE 2–7 SSKYPR N-terminus 2
a

Signal counts of identified peptides.

b

Cholesterol recognition/interaction amino acid consensus.

c

Refers to P. horikoshii stomatin structure [21].