eF-site/Summary 4jpz-I

eF-site ID	4jpz-I
PDB Code	4jpz
Chain	I

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Title	Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin
Classification	TRANSPORT PROTEIN
Compound	Fibroblast growth factor 13
Source	Homo sapiens (Human) (CALM_HUMAN)

Sequence	I:	EEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTE AELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI REAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMI READIDGDGQVNYEEFVQMMTAK

Description

Functional site


1)	chain	I
	residue	21
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 201
	source	: AC5

2)	chain	I
	residue	23
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 201
	source	: AC5

3)	chain	I
	residue	25
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 201
	source	: AC5

4)	chain	I
	residue	27
	type
	sequence	T
	description	BINDING SITE FOR RESIDUE CA I 201
	source	: AC5

5)	chain	I
	residue	32
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE CA I 201
	source	: AC5

6)	chain	I
	residue	57
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 202
	source	: AC6

7)	chain	I
	residue	59
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 202
	source	: AC6

8)	chain	I
	residue	61
	type
	sequence	N
	description	BINDING SITE FOR RESIDUE CA I 202
	source	: AC6

9)	chain	I
	residue	63
	type
	sequence	T
	description	BINDING SITE FOR RESIDUE CA I 202
	source	: AC6

10)	chain	I
	residue	68
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE CA I 202
	source	: AC6

11)	chain	I
	residue	94
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 203
	source	: AC7

12)	chain	I
	residue	96
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 203
	source	: AC7

13)	chain	I
	residue	98
	type
	sequence	N
	description	BINDING SITE FOR RESIDUE CA I 203
	source	: AC7

14)	chain	I
	residue	100
	type
	sequence	Y
	description	BINDING SITE FOR RESIDUE CA I 203
	source	: AC7

15)	chain	I
	residue	130
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 204
	source	: AC8

16)	chain	I
	residue	132
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 204
	source	: AC8

17)	chain	I
	residue	134
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE CA I 204
	source	: AC8

18)	chain	I
	residue	136
	type
	sequence	Q
	description	BINDING SITE FOR RESIDUE CA I 204
	source	: AC8

19)	chain	I
	residue	45
	type	MOD_RES
	sequence	T
	description	Phosphothreonine; by CaMK4 => ECO:0000250\|UniProtKB:P0DP29
	source	Swiss-Prot : SWS_FT_FI5

20)	chain	I
	residue	95
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI7

21)	chain	I
	residue	100
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332
	source	Swiss-Prot : SWS_FT_FI8

22)	chain	I
	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

23)	chain	I
	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

24)	chain	I
	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

25)	chain	I
	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

26)	chain	I
	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

27)	chain	I
	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

28)	chain	I
	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

29)	chain	I
	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

30)	chain	I
	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

31)	chain	I
	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

32)	chain	I
	residue	111
	type	MOD_RES
	sequence	T
	description	Phosphothreonine => ECO:0007744\|PubMed:24275569
	source	Swiss-Prot : SWS_FT_FI10

33)	chain	I
	residue	116
	type	MOD_RES
	sequence	K
	description	N6-methyllysine; alternate => ECO:0007744\|PubMed:24129315
	source	Swiss-Prot : SWS_FT_FI11

34)	chain	I
	residue	139
	type	MOD_RES
	sequence	Y
	description	Phosphotyrosine => ECO:0007744\|PubMed:19690332
	source	Swiss-Prot : SWS_FT_FI12

35)	chain	I
	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

36)	chain	I
	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

37)	chain	I
	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

38)	chain	I
	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

39)	chain	I
	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

40)	chain	I
	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

41)	chain	I
	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

42)	chain	I
	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

43)	chain	I
	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

44)	chain	I
	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

45)	chain	I
	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

46)	chain	I
	residue	22
	type	MOD_RES
	sequence	K
	description	N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861
	source	Swiss-Prot : SWS_FT_FI4

47)	chain	I
	residue	82
	type	MOD_RES
	sequence	S
	description	Phosphoserine => ECO:0007744\|PubMed:23186163
	source	Swiss-Prot : SWS_FT_FI6

48)	chain	I
	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