7QJV

In vitro assembled tau filaments into Quadruple Helical Filaments type 1 (2c)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008017	molecular_function	microtubule binding
A	0015631	molecular_function	tubulin binding
B	0008017	molecular_function	microtubule binding
B	0015631	molecular_function	tubulin binding
C	0008017	molecular_function	microtubule binding
C	0015631	molecular_function	tubulin binding
D	0008017	molecular_function	microtubule binding
D	0015631	molecular_function	tubulin binding
E	0008017	molecular_function	microtubule binding
E	0015631	molecular_function	tubulin binding
F	0008017	molecular_function	microtubule binding
F	0015631	molecular_function	tubulin binding
G	0008017	molecular_function	microtubule binding
G	0015631	molecular_function	tubulin binding
H	0008017	molecular_function	microtubule binding
H	0015631	molecular_function	tubulin binding
I	0008017	molecular_function	microtubule binding
I	0015631	molecular_function	tubulin binding
J	0008017	molecular_function	microtubule binding
J	0015631	molecular_function	tubulin binding
K	0008017	molecular_function	microtubule binding
K	0015631	molecular_function	tubulin binding
L	0008017	molecular_function	microtubule binding
L	0015631	molecular_function	tubulin binding

Functional Information from PROSITE/UniProt

site_id	PS00229
Number of Residues	13
Details	TAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSteNlkHqPGGG

Chain	Residue	Details
A	GLY261-GLY273
A	GLY292-GLY304
A	GLY323-GLY335
A	GLY355-GLY367

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	84
Details	SITE: Not glycated => ECO:0000269|PubMed:9326300

Chain	Residue	Details
A	LYS24
A	LYS44
A	LYS67
A	ASN381
A	GLU391
A	ILE392
A	TYR394
F	LYS24
F	LYS44
F	LYS67
F	ASN381
F	GLU391
F	ILE392
F	TYR394
B	LYS24
B	LYS44
B	LYS67
B	ASN381
B	GLU391
B	ILE392
B	TYR394
C	LYS24
C	LYS44
C	LYS67
C	ASN381
C	GLU391
C	ILE392
C	TYR394
D	LYS24
D	LYS44
D	LYS67
D	ASN381
D	GLU391
D	ILE392
D	TYR394
E	LYS24
E	LYS44
E	LYS67
E	ASN381
E	GLU391
E	ILE392
E	TYR394
K	LYS24
K	LYS44
K	LYS67
K	ASN381
K	GLU391
K	ILE392
K	TYR394
G	LYS24
G	LYS44
G	LYS67
G	ASN381
G	GLU391
G	ILE392
G	TYR394
H	LYS24
H	LYS44
H	LYS67
H	ASN381
H	GLU391
H	ILE392
H	TYR394
I	LYS24
I	LYS44
I	LYS67
I	ASN381
I	GLU391
I	ILE392
I	TYR394
J	LYS24
J	LYS44
J	LYS67
J	ASN381
J	GLU391
J	ILE392
J	TYR394
L	LYS24
L	LYS44
L	LYS67
L	ASN381
L	GLU391
L	ILE392
L	TYR394

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244

Chain	Residue	Details
A	ALA2
F	ALA2
B	ALA2
C	ALA2
D	ALA2
E	ALA2
K	ALA2
G	ALA2
H	ALA2
I	ALA2
J	ALA2
L	ALA2

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081

Chain	Residue	Details
A	TYR18
F	TYR18
B	TYR18
C	TYR18
D	TYR18
E	TYR18
K	TYR18
G	TYR18
H	TYR18
I	TYR18
J	TYR18
L	TYR18

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637

Chain	Residue	Details
A	TYR29
F	TYR29
B	TYR29
C	TYR29
D	TYR29
E	TYR29
K	TYR29
G	TYR29
H	TYR29
I	TYR29
J	TYR29
L	TYR29

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332

Chain	Residue	Details
A	SER46
A	SER61
F	SER46
F	SER61
B	SER46
B	SER61
C	SER46
C	SER61
D	SER46
D	SER61
E	SER46
E	SER61
K	SER46
K	SER61
G	SER46
G	SER61
H	SER46
H	SER61
I	SER46
I	SER61
J	SER46
J	SER61
L	SER46
L	SER61

---

site_id	SWS_FT_FI6
Number of Residues	24
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637

Chain	Residue	Details
A	THR69
A	THR111
F	THR69
F	THR111
B	THR69
B	THR111
C	THR69
C	THR111
D	THR69
D	THR111
E	THR69
E	THR111
K	THR69
K	THR111
G	THR69
G	THR111
H	THR69
H	THR111
I	THR69
I	THR111
J	THR69
J	THR111
L	THR69
L	THR111

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332

Chain	Residue	Details
A	THR71
F	THR71
B	THR71
C	THR71
D	THR71
E	THR71
K	THR71
G	THR71
H	THR71
I	THR71
J	THR71
L	THR71

---

site_id	SWS_FT_FI8
Number of Residues	12
Details	MOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696

Chain	Residue	Details
A	SER214
F	SER214
B	SER214
C	SER214
D	SER214
E	SER214
K	SER214
G	SER214
H	SER214
I	SER214
J	SER214
L	SER214

---

site_id	SWS_FT_FI9
Number of Residues	12
Details	MOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488

Chain	Residue	Details
A	SER396
F	SER396
B	SER396
C	SER396
D	SER396
E	SER396
K	SER396
G	SER396
H	SER396
I	SER396
J	SER396
L	SER396

---

site_id	SWS_FT_FI10
Number of Residues	24
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300

Chain	Residue	Details
A	LYS87
A	LYS383
F	LYS87
F	LYS383
B	LYS87
B	LYS383
C	LYS87
C	LYS383
D	LYS87
D	LYS383
E	LYS87
E	LYS383
K	LYS87
K	LYS383
G	LYS87
G	LYS383
H	LYS87
H	LYS383
I	LYS87
I	LYS383
J	LYS87
J	LYS383
L	LYS87
L	LYS383

---

site_id	SWS_FT_FI11
Number of Residues	24
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637

Chain	Residue	Details
A	LYS44
F	LYS44
B	LYS44
C	LYS44
D	LYS44
E	LYS44
K	LYS44
G	LYS44
H	LYS44
I	LYS44
J	LYS44
L	LYS44

---