eF-site ID 3uiv-AH
PDB Code 3uiv
Chain A, H

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Title Human serum albumin-myristate-amantadine hydrochloride complex
Classification LIPID BINDING PROTEIN
Compound Serum albumin
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKL
VNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDV
MCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCAS
LQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKP
LLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCA
AADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPE
AKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQ
IKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKAD
DKETCFAEEGKKLVAASQAALG
H:  HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKL
VNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDV
MCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCAS
LQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKP
LLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCA
AADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPE
AKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQ
IKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKAD
DKETCFAEEGKKLVAASQAALG
Description


Functional site
1) chain A
residue 117
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1001
source : AC1
2) chain A
residue 123
type
sequence M
description BINDING SITE FOR RESIDUE MYR A 1001
source : AC1
3) chain A
residue 138
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1001
source : AC1
4) chain A
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1001
source : AC1
5) chain A
residue 161
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1001
source : AC1
6) chain A
residue 22
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
7) chain A
residue 23
type
sequence V
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
8) chain A
residue 66
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
9) chain A
residue 150
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
10) chain A
residue 152
type
sequence P
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
11) chain A
residue 251
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
12) chain A
residue 254
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
13) chain A
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
14) chain A
residue 258
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
15) chain A
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC2
16) chain A
residue 342
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
17) chain A
residue 344
type
sequence V
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
18) chain A
residue 348
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
19) chain A
residue 388
type
sequence I
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
20) chain A
residue 446
type
sequence M
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
21) chain A
residue 485
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC3
22) chain A
residue 387
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC4
23) chain A
residue 411
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC4
24) chain A
residue 460
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC4
25) chain A
residue 489
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC4
26) chain A
residue 401
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
27) chain A
residue 405
type
sequence N
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
28) chain A
residue 507
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
29) chain A
residue 525
type
sequence K
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
30) chain A
residue 532
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
31) chain A
residue 547
type
sequence V
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
32) chain A
residue 548
type
sequence M
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
33) chain A
residue 551
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC5
34) chain A
residue 196
type
sequence Q
description BINDING SITE FOR RESIDUE MYR A 1006
source : AC6
35) chain A
residue 238
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1006
source : AC6
36) chain A
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE MYR A 1006
source : AC6
37) chain A
residue 245
type
sequence C
description BINDING SITE FOR RESIDUE MYR A 1006
source : AC6
38) chain A
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1006
source : AC6
39) chain H
residue 117
type
sequence R
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
40) chain H
residue 123
type
sequence M
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
41) chain H
residue 138
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
42) chain H
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
43) chain H
residue 161
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
44) chain H
residue 165
type
sequence F
description BINDING SITE FOR RESIDUE MYR H 1001
source : AC7
45) chain H
residue 150
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1002
source : AC8
46) chain H
residue 254
type
sequence A
description BINDING SITE FOR RESIDUE MYR H 1002
source : AC8
47) chain H
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE MYR H 1002
source : AC8
48) chain H
residue 258
type
sequence A
description BINDING SITE FOR RESIDUE MYR H 1002
source : AC8
49) chain H
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE MYR H 1002
source : AC8
50) chain H
residue 342
type
sequence S
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
51) chain H
residue 344
type
sequence V
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
52) chain H
residue 348
type
sequence R
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
53) chain H
residue 388
type
sequence I
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
54) chain H
residue 391
type
sequence N
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
55) chain H
residue 446
type
sequence M
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
56) chain H
residue 485
type
sequence R
description BINDING SITE FOR RESIDUE MYR H 1003
source : AC9
57) chain H
residue 387
type
sequence L
description BINDING SITE FOR RESIDUE MYR H 1004
source : BC1
58) chain H
residue 411
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1004
source : BC1
59) chain H
residue 415
type
sequence V
description BINDING SITE FOR RESIDUE MYR H 1004
source : BC1
60) chain H
residue 489
type
sequence S
description BINDING SITE FOR RESIDUE MYR H 1004
source : BC1
61) chain H
residue 401
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
62) chain H
residue 405
type
sequence N
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
63) chain H
residue 507
type
sequence F
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
64) chain H
residue 525
type
sequence K
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
65) chain H
residue 528
type
sequence A
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
66) chain H
residue 579
type
sequence S
description BINDING SITE FOR RESIDUE MYR H 1005
source : BC2
67) chain H
residue 199
type
sequence K
description BINDING SITE FOR RESIDUE MYR H 1006
source : BC3
68) chain H
residue 211
type
sequence F
description BINDING SITE FOR RESIDUE MYR H 1006
source : BC3
69) chain H
residue 214
type
sequence W
description BINDING SITE FOR RESIDUE MYR H 1006
source : BC3
70) chain H
residue 238
type
sequence L
description BINDING SITE FOR RESIDUE MYR H 1006
source : BC3
71) chain H
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE MYR H 1006
source : BC3
72) chain H
residue 150
type
sequence Y
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
73) chain H
residue 153
type
sequence E
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
74) chain H
residue 192
type
sequence S
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
75) chain H
residue 196
type
sequence Q
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
76) chain H
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
77) chain H
residue 245
type
sequence C
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
78) chain H
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE MYR H 1007
source : BC4
79) chain H
residue 238
type
sequence L
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
80) chain H
residue 260
type
sequence L
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
81) chain H
residue 264
type
sequence I
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
82) chain H
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
83) chain H
residue 290
type
sequence I
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
84) chain H
residue 291
type
sequence A
description BINDING SITE FOR RESIDUE 308 H 1008
source : BC5
85) chain A
residue 161-185
type prosite
sequence YKAAFTECCQAADKAACLLPKLDEL
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
86) chain A
residue 353-377
type prosite
sequence YETTLEKCCAAADPHECYAKVFDEF
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
87) chain A
residue 551-575
type prosite
sequence FAAFVEKCCKADDKETCFAEEGKKL
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
88) chain A
residue 3
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P02770
source Swiss-Prot : SWS_FT_FI1
89) chain H
residue 3
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P02770
source Swiss-Prot : SWS_FT_FI1
90) chain A
residue 83
type MOD_RES
sequence T
description Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI10
91) chain H
residue 83
type MOD_RES
sequence T
description Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI10
92) chain A
residue 519
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
93) chain A
residue 564
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
94) chain H
residue 205
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
95) chain H
residue 436
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
96) chain H
residue 519
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
97) chain H
residue 564
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
98) chain A
residue 205
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
99) chain A
residue 436
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
100) chain A
residue 273
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI12
101) chain H
residue 273
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI12
102) chain A
residue 419
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI13
103) chain H
residue 419
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI13
104) chain A
residue 420
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
105) chain A
residue 422
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
106) chain H
residue 420
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
107) chain H
residue 422
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
108) chain A
residue 489
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI15
109) chain H
residue 489
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI15
110) chain A
residue 534
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI16
111) chain H
residue 534
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI16
112) chain H
residue 12
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
113) chain H
residue 281
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
114) chain H
residue 317
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
115) chain H
residue 439
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
116) chain A
residue 12
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
117) chain A
residue 281
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
118) chain A
residue 317
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
119) chain A
residue 439
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
120) chain A
residue 444
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
121) chain A
residue 536
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
122) chain A
residue 545
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
123) chain A
residue 573
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
124) chain H
residue 51
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
125) chain H
residue 137
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
126) chain H
residue 162
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
127) chain H
residue 225
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
128) chain H
residue 276
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
129) chain H
residue 313
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
130) chain H
residue 323
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
131) chain H
residue 378
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
132) chain H
residue 413
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
133) chain H
residue 444
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
134) chain H
residue 536
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
135) chain H
residue 545
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
136) chain H
residue 573
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
137) chain A
residue 162
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
138) chain A
residue 225
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
139) chain A
residue 276
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
140) chain A
residue 313
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
141) chain A
residue 323
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
142) chain A
residue 378
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
143) chain A
residue 413
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
144) chain A
residue 51
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
145) chain A
residue 137
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
146) chain A
residue 199
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI19
147) chain H
residue 199
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI19
148) chain A
residue 6
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
149) chain H
residue 252
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
150) chain H
residue 255
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
151) chain H
residue 259
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
152) chain H
residue 6
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
153) chain H
residue 13
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
154) chain H
residue 244
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
155) chain A
residue 13
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
156) chain A
residue 244
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
157) chain A
residue 252
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
158) chain A
residue 255
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
159) chain A
residue 259
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
160) chain A
residue 233
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
161) chain A
residue 351
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
162) chain H
residue 233
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
163) chain H
residue 351
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
164) chain A
residue 318
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine; in variant Redhill
source Swiss-Prot : SWS_FT_FI21
165) chain H
residue 318
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine; in variant Redhill
source Swiss-Prot : SWS_FT_FI21
166) chain A
residue 494
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine; in variant Casebrook
source Swiss-Prot : SWS_FT_FI22
167) chain H
residue 494
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine; in variant Casebrook
source Swiss-Prot : SWS_FT_FI22
168) chain A
residue 525
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI23
169) chain H
residue 525
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI23
170) chain A
residue 534
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI24
171) chain H
residue 534
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI24
172) chain A
residue 67
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
173) chain A
residue 247
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
174) chain A
residue 249
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
175) chain H
residue 67
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
176) chain H
residue 247
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
177) chain H
residue 249
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
178) chain A
residue 240
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:656055
source Swiss-Prot : SWS_FT_FI4
179) chain H
residue 240
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:656055
source Swiss-Prot : SWS_FT_FI4
180) chain A
residue 174
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
181) chain A
residue 181
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
182) chain A
residue 190
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
183) chain A
residue 195
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
184) chain A
residue 205
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
185) chain A
residue 212
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
186) chain A
residue 240
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
187) chain A
residue 262
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
188) chain A
residue 274
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
189) chain A
residue 286
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
190) chain A
residue 359
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
191) chain A
residue 372
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
192) chain A
residue 389
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
193) chain A
residue 402
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
194) chain A
residue 414
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
195) chain A
residue 432
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
196) chain A
residue 436
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
197) chain A
residue 466
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
198) chain A
residue 475
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
199) chain A
residue 500
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
200) chain A
residue 41
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
201) chain A
residue 519
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
202) chain A
residue 524
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
203) chain A
residue 538
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
204) chain A
residue 541
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
205) chain A
residue 557
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
206) chain A
residue 560
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
207) chain A
residue 564
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
208) chain A
residue 574
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
209) chain H
residue 4
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
210) chain H
residue 20
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
211) chain A
residue 64
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
212) chain H
residue 41
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
213) chain H
residue 64
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
214) chain H
residue 73
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
215) chain H
residue 93
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
216) chain H
residue 106
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
217) chain H
residue 136
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
218) chain H
residue 159
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
219) chain H
residue 174
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
220) chain H
residue 181
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
221) chain H
residue 190
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
222) chain A
residue 73
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
223) chain H
residue 195
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
224) chain H
residue 205
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
225) chain H
residue 212
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
226) chain H
residue 240
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
227) chain H
residue 262
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
228) chain H
residue 274
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
229) chain H
residue 286
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
230) chain H
residue 359
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
231) chain H
residue 372
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
232) chain H
residue 389
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
233) chain A
residue 93
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
234) chain H
residue 402
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
235) chain H
residue 414
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
236) chain H
residue 432
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
237) chain H
residue 436
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
238) chain H
residue 466
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
239) chain H
residue 475
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
240) chain H
residue 500
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
241) chain H
residue 519
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
242) chain H
residue 524
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
243) chain H
residue 538
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
244) chain A
residue 106
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
245) chain H
residue 541
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
246) chain H
residue 557
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
247) chain H
residue 560
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
248) chain H
residue 564
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
249) chain H
residue 574
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
250) chain A
residue 136
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
251) chain A
residue 159
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
252) chain A
residue 4
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
253) chain A
residue 20
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
254) chain A
residue 199
type SITE
sequence K
description Aspirin-acetylated lysine
source Swiss-Prot : SWS_FT_FI6
255) chain H
residue 199
type SITE
sequence K
description Aspirin-acetylated lysine
source Swiss-Prot : SWS_FT_FI6
256) chain A
residue 5
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI7
257) chain H
residue 5
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI7
258) chain A
residue 58
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8
259) chain H
residue 58
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8
260) chain A
residue 65
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
261) chain H
residue 65
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

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