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9BBL

THF filament generated from 4E-Tau(297-407) under neutral Mg2+ condition

Functional Information from GO Data
ChainGOidnamespacecontents
A0008017molecular_functionmicrotubule binding
A0015631molecular_functiontubulin binding
B0008017molecular_functionmicrotubule binding
B0015631molecular_functiontubulin binding
C0008017molecular_functionmicrotubule binding
C0015631molecular_functiontubulin binding
D0008017molecular_functionmicrotubule binding
D0015631molecular_functiontubulin binding
E0008017molecular_functionmicrotubule binding
E0015631molecular_functiontubulin binding
F0008017molecular_functionmicrotubule binding
F0015631molecular_functiontubulin binding
G0008017molecular_functionmicrotubule binding
G0015631molecular_functiontubulin binding
H0008017molecular_functionmicrotubule binding
H0015631molecular_functiontubulin binding
I0008017molecular_functionmicrotubule binding
I0015631molecular_functiontubulin binding
Functional Information from PROSITE/UniProt
site_idPS00229
Number of Residues13
DetailsTAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSteNlkHqPGGG
ChainResidueDetails
AGLY261-GLY273
AGLY292-GLY304
AGLY323-GLY335
AGLY355-GLY367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS24
BLYS67
BASN381
BGLU391
BILE392
BTYR394
CLYS24
CLYS44
CLYS67
CASN381
CGLU391
ALYS44
CILE392
CTYR394
DLYS24
DLYS44
DLYS67
DASN381
DGLU391
DILE392
DTYR394
ELYS24
ALYS67
ELYS44
ELYS67
EASN381
EGLU391
EILE392
ETYR394
FLYS24
FLYS44
FLYS67
FASN381
AASN381
FGLU391
FILE392
FTYR394
GLYS24
GLYS44
GLYS67
GASN381
GGLU391
GILE392
GTYR394
AGLU391
HLYS24
HLYS44
HLYS67
HASN381
HGLU391
HILE392
HTYR394
ILYS24
ILYS44
ILYS67
AILE392
IASN381
IGLU391
IILE392
ITYR394
ATYR394
BLYS24
BLYS44

site_idSWS_FT_FI2
Number of Residues9
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2
EALA2
FALA2
GALA2
HALA2
IALA2

site_idSWS_FT_FI3
Number of Residues9
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
ATYR18
BTYR18
CTYR18
DTYR18
ETYR18
FTYR18
GTYR18
HTYR18
ITYR18

site_idSWS_FT_FI4
Number of Residues9
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATYR29
BTYR29
CTYR29
DTYR29
ETYR29
FTYR29
GTYR29
HTYR29
ITYR29

site_idSWS_FT_FI5
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ASER46
ESER61
FSER46
FSER61
GSER46
GSER61
HSER46
HSER61
ISER46
ISER61
ASER61
BSER46
BSER61
CSER46
CSER61
DSER46
DSER61
ESER46

site_idSWS_FT_FI6
Number of Residues18
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATHR69
ETHR111
FTHR69
FTHR111
GTHR69
GTHR111
HTHR69
HTHR111
ITHR69
ITHR111
ATHR111
BTHR69
BTHR111
CTHR69
CTHR111
DTHR69
DTHR111
ETHR69

site_idSWS_FT_FI7
Number of Residues9
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ATHR71
BTHR71
CTHR71
DTHR71
ETHR71
FTHR71
GTHR71
HTHR71
ITHR71

site_idSWS_FT_FI8
Number of Residues9
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
ASER214
BSER214
CSER214
DSER214
ESER214
FSER214
GSER214
HSER214
ISER214

site_idSWS_FT_FI9
Number of Residues9
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
AGLU396
BGLU396
CGLU396
DGLU396
EGLU396
FGLU396
GGLU396
HGLU396
IGLU396

site_idSWS_FT_FI10
Number of Residues18
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS87
ELYS383
FLYS87
FLYS383
GLYS87
GLYS383
HLYS87
HLYS383
ILYS87
ILYS383
ALYS383
BLYS87
BLYS383
CLYS87
CLYS383
DLYS87
DLYS383
ELYS87

site_idSWS_FT_FI11
Number of Residues18
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ALYS44
FLYS44
GLYS44
HLYS44
ILYS44
BLYS44
CLYS44
DLYS44
ELYS44

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PDB entries from 2024-10-30

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