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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7PQC

tau-microtubule structural ensemble based on CryoEM data

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0001764biological_processneuron migration
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0001764biological_processneuron migration
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0003924molecular_functionGTPase activity
D0005200molecular_functionstructural constituent of cytoskeleton
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0007017biological_processmicrotubule-based process
D0015630cellular_componentmicrotubule cytoskeleton
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0001764biological_processneuron migration
E0003924molecular_functionGTPase activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0007017biological_processmicrotubule-based process
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0003924molecular_functionGTPase activity
F0005200molecular_functionstructural constituent of cytoskeleton
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005874cellular_componentmicrotubule
F0007017biological_processmicrotubule-based process
F0015630cellular_componentmicrotubule cytoskeleton
F0016787molecular_functionhydrolase activity
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0000226biological_processmicrotubule cytoskeleton organization
G0000278biological_processmitotic cell cycle
G0001764biological_processneuron migration
G0003924molecular_functionGTPase activity
G0005200molecular_functionstructural constituent of cytoskeleton
G0005515molecular_functionprotein binding
G0005525molecular_functionGTP binding
G0005737cellular_componentcytoplasm
G0005856cellular_componentcytoskeleton
G0005874cellular_componentmicrotubule
G0007017biological_processmicrotubule-based process
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0000226biological_processmicrotubule cytoskeleton organization
H0000278biological_processmitotic cell cycle
H0003924molecular_functionGTPase activity
H0005200molecular_functionstructural constituent of cytoskeleton
H0005525molecular_functionGTP binding
H0005737cellular_componentcytoplasm
H0005856cellular_componentcytoskeleton
H0005874cellular_componentmicrotubule
H0007017biological_processmicrotubule-based process
H0015630cellular_componentmicrotubule cytoskeleton
H0016787molecular_functionhydrolase activity
H0046872molecular_functionmetal ion binding
I0000166molecular_functionnucleotide binding
I0000226biological_processmicrotubule cytoskeleton organization
I0000278biological_processmitotic cell cycle
I0001764biological_processneuron migration
I0003924molecular_functionGTPase activity
I0005200molecular_functionstructural constituent of cytoskeleton
I0005515molecular_functionprotein binding
I0005525molecular_functionGTP binding
I0005737cellular_componentcytoplasm
I0005856cellular_componentcytoskeleton
I0005874cellular_componentmicrotubule
I0007017biological_processmicrotubule-based process
I0046872molecular_functionmetal ion binding
J0000166molecular_functionnucleotide binding
J0000226biological_processmicrotubule cytoskeleton organization
J0000278biological_processmitotic cell cycle
J0003924molecular_functionGTPase activity
J0005200molecular_functionstructural constituent of cytoskeleton
J0005525molecular_functionGTP binding
J0005737cellular_componentcytoplasm
J0005856cellular_componentcytoskeleton
J0005874cellular_componentmicrotubule
J0007017biological_processmicrotubule-based process
J0015630cellular_componentmicrotubule cytoskeleton
J0016787molecular_functionhydrolase activity
J0046872molecular_functionmetal ion binding
K0000166molecular_functionnucleotide binding
K0000226biological_processmicrotubule cytoskeleton organization
K0000278biological_processmitotic cell cycle
K0001764biological_processneuron migration
K0003924molecular_functionGTPase activity
K0005200molecular_functionstructural constituent of cytoskeleton
K0005515molecular_functionprotein binding
K0005525molecular_functionGTP binding
K0005737cellular_componentcytoplasm
K0005856cellular_componentcytoskeleton
K0005874cellular_componentmicrotubule
K0007017biological_processmicrotubule-based process
K0046872molecular_functionmetal ion binding
L0000166molecular_functionnucleotide binding
L0000226biological_processmicrotubule cytoskeleton organization
L0000278biological_processmitotic cell cycle
L0003924molecular_functionGTPase activity
L0005200molecular_functionstructural constituent of cytoskeleton
L0005525molecular_functionGTP binding
L0005737cellular_componentcytoplasm
L0005856cellular_componentcytoskeleton
L0005874cellular_componentmicrotubule
L0007017biological_processmicrotubule-based process
L0015630cellular_componentmicrotubule cytoskeleton
L0016787molecular_functionhydrolase activity
L0046872molecular_functionmetal ion binding
M0000166molecular_functionnucleotide binding
M0000226biological_processmicrotubule cytoskeleton organization
M0000278biological_processmitotic cell cycle
M0001764biological_processneuron migration
M0003924molecular_functionGTPase activity
M0005200molecular_functionstructural constituent of cytoskeleton
M0005515molecular_functionprotein binding
M0005525molecular_functionGTP binding
M0005737cellular_componentcytoplasm
M0005856cellular_componentcytoskeleton
M0005874cellular_componentmicrotubule
M0007017biological_processmicrotubule-based process
M0046872molecular_functionmetal ion binding
N0000166molecular_functionnucleotide binding
N0000226biological_processmicrotubule cytoskeleton organization
N0000278biological_processmitotic cell cycle
N0003924molecular_functionGTPase activity
N0005200molecular_functionstructural constituent of cytoskeleton
N0005525molecular_functionGTP binding
N0005737cellular_componentcytoplasm
N0005856cellular_componentcytoskeleton
N0005874cellular_componentmicrotubule
N0007017biological_processmicrotubule-based process
N0015630cellular_componentmicrotubule cytoskeleton
N0016787molecular_functionhydrolase activity
N0046872molecular_functionmetal ion binding
O0008017molecular_functionmicrotubule binding
O0015631molecular_functiontubulin binding
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY142-GLY148
AGLY140-GLY146
site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
AMET1-ILE4
site_idPS00229
Number of Residues13
DetailsTAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSteNlkHqPGGG
ChainResidueDetails
OGLY261-GLY273
OGLY292-GLY304
OGLY323-GLY335
OGLY355-GLY367
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues280
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues21
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues112
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues49
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues126
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues7
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q13885","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues14
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsModified residue: {"description":"5-glutamyl polyglutamate","evidences":[{"source":"UniProtKB","id":"Q2T9S0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues7
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues14
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues21
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues7
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues7
DetailsSite: {"description":"Involved in polymerization","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues7
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues14
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues7
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues7
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues7
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues7
DetailsModified residue: {"description":"5-glutamyl polyglutamate","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues7
DetailsModified residue: {"description":"5-glutamyl polyglutamate","evidences":[{"source":"UniProtKB","id":"P68369","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues7
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q71U36","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues21
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues30
DetailsRepeat: {"description":"Tau/MAP 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues30
DetailsRepeat: {"description":"Tau/MAP 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues30
DetailsRepeat: {"description":"Tau/MAP 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues31
DetailsRepeat: {"description":"Tau/MAP 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00824","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues124
DetailsRegion: {"description":"Microtubule-binding domain","evidences":[{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues20
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"9326300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CK1, PDPK1 and TTBK1","evidences":[{"source":"PubMed","id":"14761950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16923168","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21327254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9614189","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CK1 and PDPK1","evidences":[{"source":"PubMed","id":"14761950","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1","evidences":[{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18599021","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21985311","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9614189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9614189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by GSK3-beta and PDPK1","evidences":[{"source":"PubMed","id":"14690523","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PDPK1","evidences":[{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9614189","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PHK","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8999860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK","evidences":[{"source":"PubMed","id":"15546861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19451179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21985311","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23666762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8999860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9614189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues1
DetailsModified residue: {"description":"Deamidated asparagine; in tau and PHF-tau; partial","evidences":[{"source":"PubMed","id":"1512244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues10
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PHK","evidences":[{"source":"PubMed","id":"8999860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PHK","evidences":[{"source":"PubMed","id":"7706316","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8999860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"21327254","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro","evidences":[{"source":"PubMed","id":"9326300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues11
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI54
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P10637","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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