eF-site ID 4byf-ABCD
PDB Code 4byf
Chain A, B, C, D

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Title Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state
Classification HYDROLASE
Compound UNCONVENTIONAL MYOSIN-IC
Source Homo sapiens (Human) (CALM_HUMAN)
Sequence A:  DRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPV
LVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTV
YRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPA
PERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMD
VQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQL
LEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSD
WKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANE
NAQVTTENQLKYLTRLLSVEGSTLREALTHRKIELLSPLN
LEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPS
WRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFI
ELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGI
ISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLAD
RKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKET
MCSSKNPIMSQCFDRSEKRPETVATQFKMSLLQLVEILQS
KEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRV
RRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVL
VRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSL
ATKIQAAWRGFHWRQKFL
B:  MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSL
GQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDT
DSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTA
C:  RVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVL
VSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVY
RALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAP
ERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDV
QFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLL
EGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDW
KVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEN
AQVTTENQLKYLTRLLSVEGSTLREALTHRKIELLSPLNL
EQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSW
RSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIE
LTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGII
SILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADR
KSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETM
CSSKNPIMSQCFDRSKRPETVATQFKMSLLQLVEILQSKE
PAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRR
AGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVR
HLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSLAT
KIQAAWRGFHWRQKFL
D:  ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK
Description


Functional site
1) chain A
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE MG A 1000
source : AC1
2) chain A
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE MG A 1000
source : AC1
3) chain A
residue 53
type
sequence N
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
4) chain A
residue 56
type
sequence R
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
5) chain A
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
6) chain A
residue 106
type
sequence E
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
7) chain A
residue 107
type
sequence S
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
8) chain A
residue 108
type
sequence G
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
9) chain A
residue 109
type
sequence A
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
10) chain A
residue 110
type
sequence G
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
11) chain A
residue 111
type
sequence K
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
12) chain A
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
13) chain A
residue 113
type
sequence E
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
14) chain A
residue 157
type
sequence N
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
15) chain A
residue 159
type
sequence N
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
16) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
17) chain A
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
18) chain A
residue 388
type
sequence Y
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
19) chain A
residue 389
type
sequence G
description BINDING SITE FOR RESIDUE AOV A 1001
source : AC2
20) chain C
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE MG C 1000
source : AC3
21) chain C
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE MG C 1000
source : AC3
22) chain C
residue 53
type
sequence N
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
23) chain C
residue 56
type
sequence R
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
24) chain C
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
25) chain C
residue 106
type
sequence E
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
26) chain C
residue 107
type
sequence S
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
27) chain C
residue 108
type
sequence G
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
28) chain C
residue 109
type
sequence A
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
29) chain C
residue 110
type
sequence G
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
30) chain C
residue 111
type
sequence K
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
31) chain C
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
32) chain C
residue 113
type
sequence E
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
33) chain C
residue 157
type
sequence N
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
34) chain C
residue 159
type
sequence N
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
35) chain C
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
36) chain C
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
37) chain C
residue 388
type
sequence Y
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
38) chain C
residue 389
type
sequence G
description BINDING SITE FOR RESIDUE AOV C 1001
source : AC4
39) chain D
residue 94
type
sequence D
description BINDING SITE FOR RESIDUE MG D 1000
source : AC5
40) chain D
residue 96
type
sequence D
description BINDING SITE FOR RESIDUE MG D 1000
source : AC5
41) chain D
residue 98
type
sequence N
description BINDING SITE FOR RESIDUE MG D 1000
source : AC5
42) chain D
residue 100
type
sequence Y
description BINDING SITE FOR RESIDUE MG D 1000
source : AC5
43) chain B
residue 21-33
type prosite
sequence DKDGDGTITTKEL
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
44) chain B
residue 57-69
type prosite
sequence DADGNGTIDFPEF
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
45) chain B
residue 94-106
type prosite
sequence DKDGNGYISAAEL
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
46) chain B
residue 130-142
type prosite
sequence DIDGDGQVNYEEF
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
47) chain B
residue 21
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
48) chain B
residue 68
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
49) chain D
residue 21
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
50) chain D
residue 23
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
51) chain D
residue 25
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
52) chain D
residue 27
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
53) chain D
residue 32
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
54) chain D
residue 57
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
55) chain D
residue 59
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
56) chain D
residue 61
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
57) chain D
residue 63
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
58) chain B
residue 23
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
59) chain D
residue 68
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
60) chain B
residue 25
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
61) chain B
residue 27
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
62) chain B
residue 32
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
63) chain B
residue 57
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
64) chain B
residue 59
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
65) chain B
residue 61
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
66) chain B
residue 63
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1
67) chain B
residue 111
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10
68) chain D
residue 111
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10
69) chain B
residue 116
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI11
70) chain D
residue 116
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI11
71) chain B
residue 139
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI12
72) chain D
residue 139
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI12
73) chain B
residue 22
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
source Swiss-Prot : SWS_FT_FI13
74) chain D
residue 22
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
source Swiss-Prot : SWS_FT_FI13
75) chain B
residue 94
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
76) chain B
residue 141
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
77) chain D
residue 94
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
78) chain D
residue 96
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
79) chain D
residue 98
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
80) chain D
residue 100
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
81) chain D
residue 105
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
82) chain D
residue 130
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
83) chain D
residue 132
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
84) chain D
residue 134
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
85) chain D
residue 136
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
86) chain B
residue 96
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
87) chain D
residue 141
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
88) chain B
residue 98
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
89) chain B
residue 100
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
90) chain B
residue 105
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
91) chain B
residue 130
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
92) chain B
residue 132
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
93) chain B
residue 134
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
94) chain B
residue 136
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2
95) chain B
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3
96) chain D
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3
97) chain B
residue 22
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4
98) chain D
residue 22
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4
99) chain B
residue 45
type MOD_RES
sequence T
description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
source Swiss-Prot : SWS_FT_FI5
100) chain D
residue 45
type MOD_RES
sequence T
description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
source Swiss-Prot : SWS_FT_FI5
101) chain B
residue 82
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6
102) chain D
residue 82
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6
103) chain B
residue 95
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7
104) chain D
residue 95
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7
105) chain B
residue 100
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8
106) chain D
residue 100
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8
107) chain B
residue 102
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
108) chain D
residue 102
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

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