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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5O3L

Paired helical filament in Alzheimer's disease brain

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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY323-GLY335
A	GLY355-GLY367

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	SITE: Not glycated => ECO:0000269\|PubMed:9326300

Chain	Residue	Details
A	LYS311
B	LYS317
B	LYS321
B	LYS331
B	LYS340
B	LYS343
B	LYS370
B	LYS375
C	LYS311
C	LYS317
C	LYS321
A	LYS317
C	LYS331
C	LYS340
C	LYS343
C	LYS370
C	LYS375
D	LYS311
D	LYS317
D	LYS321
D	LYS331
D	LYS340
A	LYS321
D	LYS343
D	LYS370
D	LYS375
E	LYS311
E	LYS317
E	LYS321
E	LYS331
E	LYS340
E	LYS343
E	LYS370
A	LYS331
E	LYS375
F	LYS311
F	LYS317
F	LYS321
F	LYS331
F	LYS340
F	LYS343
F	LYS370
F	LYS375
G	LYS311
A	LYS340
G	LYS317
G	LYS321
G	LYS331
G	LYS340
G	LYS343
G	LYS370
G	LYS375
H	LYS311
H	LYS317
H	LYS321
A	LYS343
H	LYS331
H	LYS340
H	LYS343
H	LYS370
H	LYS375
I	LYS311
I	LYS317
I	LYS321
I	LYS331
I	LYS340
A	LYS370
I	LYS343
I	LYS370
I	LYS375
J	LYS311
J	LYS317
J	LYS321
J	LYS331
J	LYS340
J	LYS343
J	LYS370
A	LYS375
J	LYS375
B	LYS311

site_id	SWS_FT_FI2
Number of Residues	70
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P10637

Chain	Residue	Details
A	LYS311
B	LYS321
B	LYS331
B	LYS343
B	LYS347
B	LYS369
C	LYS311
C	LYS317
C	LYS321
C	LYS331
C	LYS343
A	LYS317
C	LYS347
C	LYS369
D	LYS311
D	LYS317
D	LYS321
D	LYS331
D	LYS343
D	LYS347
D	LYS369
E	LYS311
A	LYS321
E	LYS317
E	LYS321
E	LYS331
E	LYS343
E	LYS347
E	LYS369
F	LYS311
F	LYS317
F	LYS321
F	LYS331
A	LYS331
F	LYS343
F	LYS347
F	LYS369
G	LYS311
G	LYS317
G	LYS321
G	LYS331
G	LYS343
G	LYS347
G	LYS369
A	LYS343
H	LYS311
H	LYS317
H	LYS321
H	LYS331
H	LYS343
H	LYS347
H	LYS369
I	LYS311
I	LYS317
I	LYS321
A	LYS347
I	LYS331
I	LYS343
I	LYS347
I	LYS369
J	LYS311
J	LYS317
J	LYS321
J	LYS331
J	LYS343
J	LYS347
A	LYS369
J	LYS369
B	LYS311
B	LYS317

site_id	SWS_FT_FI3
Number of Residues	20
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:7706316

Chain	Residue	Details
A	SER324
E	SER356
F	SER324
F	SER356
G	SER324
G	SER356
H	SER324
H	SER356
I	SER324
I	SER356
J	SER324
A	SER356
J	SER356
B	SER324
B	SER356
C	SER324
C	SER356
D	SER324
D	SER356
E	SER324

site_id	SWS_FT_FI4
Number of Residues	10
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:P10637

Chain	Residue	Details
A	ARG349
J	ARG349
B	ARG349
C	ARG349
D	ARG349
E	ARG349
F	ARG349
G	ARG349
H	ARG349
I	ARG349

site_id	SWS_FT_FI5
Number of Residues	10
Details	MOD_RES: Phosphoserine; by PHK => ECO:0000269\|PubMed:8999860

Chain	Residue	Details
A	SER352
J	SER352
B	SER352
C	SER352
D	SER352
E	SER352
F	SER352
G	SER352
H	SER352
I	SER352

site_id	SWS_FT_FI6
Number of Residues	30
Details	CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269\|PubMed:9326300

Chain	Residue	Details
A	LYS347
D	LYS347
D	LYS353
D	LYS369
E	LYS347
E	LYS353
E	LYS369
F	LYS347
F	LYS353
F	LYS369
G	LYS347
A	LYS353
G	LYS353
G	LYS369
H	LYS347
H	LYS353
H	LYS369
I	LYS347
I	LYS353
I	LYS369
J	LYS347
J	LYS353
A	LYS369
J	LYS369
B	LYS347
B	LYS353
B	LYS369
C	LYS347
C	LYS353
C	LYS369

site_id	SWS_FT_FI7
Number of Residues	20
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269\|PubMed:16443603

Chain	Residue	Details
A	LYS311
E	LYS353
F	LYS311
F	LYS353
G	LYS311
G	LYS353
H	LYS311
H	LYS353
I	LYS311
I	LYS353
J	LYS311
A	LYS353
J	LYS353
B	LYS311
B	LYS353
C	LYS311
C	LYS353
D	LYS311
D	LYS353
E	LYS311

site_id	SWS_FT_FI8
Number of Residues	20
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P10637

Chain	Residue	Details
E	LYS375
F	LYS375
G	LYS375
H	LYS375
I	LYS375
A	LYS375
J	LYS375
B	LYS375
C	LYS375
D	LYS375

site_id	SWS_FT_FI9
Number of Residues	60
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P10637

Chain	Residue	Details
A	LYS317
B	LYS343
B	LYS347
B	LYS369
C	LYS317
C	LYS321
C	LYS331
C	LYS343
C	LYS347
C	LYS369
D	LYS317
A	LYS321
D	LYS321
D	LYS331
D	LYS343
D	LYS347
D	LYS369
E	LYS317
E	LYS321
E	LYS331
E	LYS343
E	LYS347
A	LYS331
E	LYS369
F	LYS317
F	LYS321
F	LYS331
F	LYS343
F	LYS347
F	LYS369
G	LYS317
G	LYS321
G	LYS331
A	LYS343
G	LYS343
G	LYS347
G	LYS369
H	LYS317
H	LYS321
H	LYS331
H	LYS343
H	LYS347
H	LYS369
I	LYS317
A	LYS347
I	LYS321
I	LYS331
I	LYS343
I	LYS347
I	LYS369
J	LYS317
J	LYS321
J	LYS331
J	LYS343
J	LYS347
A	LYS369
J	LYS369
B	LYS317
B	LYS321
B	LYS331

226707

PDB entries from 2024-10-30

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