6TJX

Cryo-EM structure of TypeII tau filaments extracted from the brains of individuals with Corticobasal degeneration

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

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	SITE: Not glycated => ECO:0000269|PubMed:9326300

Chain	Residue	Details
A	LYS24
B	LYS67
B	ASN381
B	GLU391
B	ILE392
B	TYR394
C	LYS24
C	LYS44
C	LYS67
C	ASN381
C	GLU391
A	LYS44
C	ILE392
C	TYR394
D	LYS24
D	LYS44
D	LYS67
D	ASN381
D	GLU391
D	ILE392
D	TYR394
E	LYS24
A	LYS67
E	LYS44
E	LYS67
E	ASN381
E	GLU391
E	ILE392
E	TYR394
F	LYS24
F	LYS44
F	LYS67
F	ASN381
A	ASN381
F	GLU391
F	ILE392
F	TYR394
A	GLU391
A	ILE392
A	TYR394
B	LYS24
B	LYS44

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2
E	ALA2
F	ALA2

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081

Chain	Residue	Details
A	TYR18
B	TYR18
C	TYR18
D	TYR18
E	TYR18
F	TYR18

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637

Chain	Residue	Details
A	TYR29
B	TYR29
C	TYR29
D	TYR29
E	TYR29
F	TYR29

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332

Chain	Residue	Details
A	SER46
E	SER61
F	SER46
F	SER61
A	SER61
B	SER46
B	SER61
C	SER46
C	SER61
D	SER46
D	SER61
E	SER46

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637

Chain	Residue	Details
A	THR69
E	THR111
F	THR69
F	THR111
A	THR111
B	THR69
B	THR111
C	THR69
C	THR111
D	THR69
D	THR111
E	THR69

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332

Chain	Residue	Details
A	THR71
B	THR71
C	THR71
D	THR71
E	THR71
F	THR71

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696

Chain	Residue	Details
A	SER214
B	SER214
C	SER214
D	SER214
E	SER214
F	SER214

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488

Chain	Residue	Details
A	SER396
B	SER396
C	SER396
D	SER396
E	SER396
F	SER396

---

site_id	SWS_FT_FI10
Number of Residues	12
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300

Chain	Residue	Details
A	LYS87
E	LYS383
F	LYS87
F	LYS383
A	LYS383
B	LYS87
B	LYS383
C	LYS87
C	LYS383
D	LYS87
D	LYS383
E	LYS87

---

site_id	SWS_FT_FI11
Number of Residues	12
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

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