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7SP1

RNA-induced tau amyloid fibril

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
J0008017molecular_functionmicrotubule binding
J0015631molecular_functiontubulin binding
K0008017molecular_functionmicrotubule binding
K0015631molecular_functiontubulin binding
L0008017molecular_functionmicrotubule binding
L0015631molecular_functiontubulin binding
M0008017molecular_functionmicrotubule binding
M0015631molecular_functiontubulin binding
N0008017molecular_functionmicrotubule binding
N0015631molecular_functiontubulin binding
O0008017molecular_functionmicrotubule binding
O0015631molecular_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 Residues465
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS24
DTYR394
ELYS24
ELYS44
ELYS67
EASN381
EGLU391
EILE392
ETYR394
FLYS24
FLYS44
FLYS67
FASN381
FGLU391
FILE392
FTYR394
GLYS24
GLYS44
GLYS67
GASN381
GGLU391
GILE392
GTYR394
ALYS44
HLYS24
HLYS44
HLYS67
HASN381
HGLU391
HILE392
HTYR394
ILYS24
ILYS44
ILYS67
IASN381
IGLU391
IILE392
ITYR394
JLYS24
JLYS44
JLYS67
JASN381
JGLU391
JILE392
JTYR394
ALYS67
KLYS24
KLYS44
KLYS67
KASN381
KGLU391
KILE392
KTYR394
BLYS24
BLYS44
BLYS67
LLYS24
LLYS44
LLYS67
LASN381
LGLU391
LILE392
LTYR394
BASN381
BGLU391
BILE392
MLYS24
MLYS44
MLYS67
MASN381
MGLU391
MILE392
MTYR394
BTYR394
AASN381
NLYS24
NLYS44
NLYS67
NASN381
NGLU391
NILE392
NTYR394
OLYS24
OLYS44
OLYS67
OASN381
OGLU391
OILE392
OTYR394
AGLU391
AILE392
CLYS24
CLYS44
CLYS67
CASN381
CGLU391
CILE392
CTYR394
ATYR394
DLYS24
DLYS44
DLYS67
DASN381
DGLU391
DILE392

site_idSWS_FT_FI2
Number of Residues15
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
AALA2
JALA2
KALA2
LALA2
MALA2
NALA2
OALA2
BALA2
CALA2
DALA2
EALA2
FALA2
GALA2
HALA2
IALA2

site_idSWS_FT_FI3
Number of Residues15
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
ATYR18
JTYR18
KTYR18
LTYR18
MTYR18
NTYR18
OTYR18
BTYR18
CTYR18
DTYR18
ETYR18
FTYR18
GTYR18
HTYR18
ITYR18

site_idSWS_FT_FI4
Number of Residues30
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATYR29
FTYR29
GTYR29
HTYR29
ITYR29
JTYR29
KTYR29
LTYR29
MTYR29
NTYR29
OTYR29
BTYR29
CTYR29
DTYR29
ETYR29

site_idSWS_FT_FI5
Number of Residues30
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ASER46
ESER61
FSER46
FSER61
GSER46
GSER61
HSER46
HSER61
ISER46
ISER61
JSER46
ASER61
JSER61
KSER46
KSER61
LSER46
LSER61
MSER46
MSER61
NSER46
NSER61
OSER46
BSER46
OSER61
BSER61
CSER46
CSER61
DSER46
DSER61
ESER46

site_idSWS_FT_FI6
Number of Residues75
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATHR69
CTHR69
CTHR111
DTHR69
DTHR111
ATHR111
ETHR69
ETHR111
FTHR69
FTHR111
GTHR69
GTHR111
HTHR69
HTHR111
ITHR69
ITHR111
JTHR69
JTHR111
KTHR69
KTHR111
LTHR69
LTHR111
BTHR69
MTHR69
MTHR111
NTHR69
NTHR111
BTHR111
OTHR69
OTHR111

site_idSWS_FT_FI7
Number of Residues15
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ATHR71
JTHR71
KTHR71
LTHR71
MTHR71
NTHR71
OTHR71
BTHR71
CTHR71
DTHR71
ETHR71
FTHR71
GTHR71
HTHR71
ITHR71

site_idSWS_FT_FI8
Number of Residues15
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
ASER214
JSER214
KSER214
LSER214
MSER214
NSER214
OSER214
BSER214
CSER214
DSER214
ESER214
FSER214
GSER214
HSER214
ISER214

site_idSWS_FT_FI9
Number of Residues15
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
ASER396
JSER396
KSER396
LSER396
MSER396
NSER396
OSER396
BSER396
CSER396
DSER396
ESER396
FSER396
GSER396
HSER396
ISER396

site_idSWS_FT_FI10
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues30
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues165
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues30
DetailsMOD_RES: Deamidated asparagine; in tau and PHF-tau; partial => ECO:0000269|PubMed:1512244
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:15546861
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues45
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues15
DetailsMOD_RES: Phosphotyrosine; by TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues15
DetailsMOD_RES: Phosphoserine; by CK1, PDPK1 and TTBK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues30
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:8999860
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues15
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues15
DetailsMOD_RES: Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues30
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues45
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues15
DetailsMOD_RES: Phosphoserine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues15
DetailsMOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:19690332
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues15
DetailsMOD_RES: Phosphoserine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues15
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15546861, ECO:0007744|PubMed:19690332
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues15
DetailsMOD_RES: Phosphoserine; by CaMK2 and TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues15
DetailsMOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues15
DetailsMOD_RES: Phosphothreonine; by TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues195
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS87
ILYS87
ILYS383
JLYS87
JLYS383
KLYS87
KLYS383
BLYS87
LLYS87
LLYS383
BLYS383
MLYS87
MLYS383
NLYS87
NLYS383
OLYS87
OLYS383
ALYS383
CLYS87
CLYS383
DLYS87
DLYS383
ELYS87
ELYS383
FLYS87
FLYS383
GLYS87
GLYS383
HLYS87
HLYS383

site_idSWS_FT_FI41
Number of Residues30
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:21327254
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues15
DetailsCARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000269|PubMed:21327254
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues45
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ALYS44
DLYS44
ELYS44
FLYS44
GLYS44
HLYS44
ILYS44
JLYS44
KLYS44
LLYS44
MLYS44
BLYS44
NLYS44
OLYS44
CLYS44

site_idSWS_FT_FI44
Number of Residues165
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues45
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603
ChainResidueDetails

227111

PDB entries from 2024-11-06

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