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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8U3Z

Model of TTLL6 bound to microtubule from composite map

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003725molecular_functiondouble-stranded RNA binding
A0003924molecular_functionGTPase activity
A0005198molecular_functionstructural molecule activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005881cellular_componentcytoplasmic microtubule
A0005929cellular_componentcilium
A0007017biological_processmicrotubule-based process
A0015630cellular_componentmicrotubule cytoskeleton
A0016787molecular_functionhydrolase activity
A0030705biological_processcytoskeleton-dependent intracellular transport
A0031625molecular_functionubiquitin protein ligase binding
A0051301biological_processcell division
A0071353biological_processcellular response to interleukin-4
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005198molecular_functionstructural molecule activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005641cellular_componentnuclear envelope lumen
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0019904molecular_functionprotein domain specific binding
B0030705biological_processcytoskeleton-dependent intracellular transport
B0031625molecular_functionubiquitin protein ligase binding
B0032794molecular_functionGTPase activating protein binding
B0032991cellular_componentprotein-containing complex
B0035578cellular_componentazurophil granule lumen
B0036464cellular_componentcytoplasmic ribonucleoprotein granule
B0042267biological_processnatural killer cell mediated cytotoxicity
B0042288molecular_functionMHC class I protein binding
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0045171cellular_componentintercellular bridge
B0046872molecular_functionmetal ion binding
B0050807biological_processregulation of synapse organization
B0051225biological_processspindle assembly
B0051301biological_processcell division
B0070062cellular_componentextracellular exosome
B0071895biological_processodontoblast differentiation
B0072686cellular_componentmitotic spindle
E0000166molecular_functionnucleotide binding
E0000226biological_processmicrotubule cytoskeleton organization
E0000278biological_processmitotic cell cycle
E0003924molecular_functionGTPase activity
E0005198molecular_functionstructural molecule activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005641cellular_componentnuclear envelope lumen
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0007017biological_processmicrotubule-based process
E0015630cellular_componentmicrotubule cytoskeleton
E0019904molecular_functionprotein domain specific binding
E0030705biological_processcytoskeleton-dependent intracellular transport
E0031625molecular_functionubiquitin protein ligase binding
E0032794molecular_functionGTPase activating protein binding
E0032991cellular_componentprotein-containing complex
E0035578cellular_componentazurophil granule lumen
E0036464cellular_componentcytoplasmic ribonucleoprotein granule
E0042267biological_processnatural killer cell mediated cytotoxicity
E0042288molecular_functionMHC class I protein binding
E0044297cellular_componentcell body
E0044877molecular_functionprotein-containing complex binding
E0045121cellular_componentmembrane raft
E0045171cellular_componentintercellular bridge
E0046872molecular_functionmetal ion binding
E0050807biological_processregulation of synapse organization
E0051225biological_processspindle assembly
E0051301biological_processcell division
E0070062cellular_componentextracellular exosome
E0071895biological_processodontoblast differentiation
E0072686cellular_componentmitotic spindle
F0000166molecular_functionnucleotide binding
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0003725molecular_functiondouble-stranded RNA binding
F0003924molecular_functionGTPase activity
F0005198molecular_functionstructural molecule activity
F0005200molecular_functionstructural constituent of cytoskeleton
F0005515molecular_functionprotein binding
F0005525molecular_functionGTP binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005874cellular_componentmicrotubule
F0005881cellular_componentcytoplasmic microtubule
F0005929cellular_componentcilium
F0007017biological_processmicrotubule-based process
F0015630cellular_componentmicrotubule cytoskeleton
F0016787molecular_functionhydrolase activity
F0030705biological_processcytoskeleton-dependent intracellular transport
F0031625molecular_functionubiquitin protein ligase binding
F0051301biological_processcell division
F0071353biological_processcellular response to interleukin-4
N0000166molecular_functionnucleotide binding
N0001578biological_processmicrotubule bundle formation
N0003353biological_processpositive regulation of cilium movement
N0005515molecular_functionprotein binding
N0005524molecular_functionATP binding
N0005737cellular_componentcytoplasm
N0005856cellular_componentcytoskeleton
N0005874cellular_componentmicrotubule
N0005929cellular_componentcilium
N0015630cellular_componentmicrotubule cytoskeleton
N0015631molecular_functiontubulin binding
N0016874molecular_functionligase activity
N0018095biological_processprotein polyglutamylation
N0036064cellular_componentciliary basal body
N0036211biological_processprotein modification process
N0042995cellular_componentcell projection
N0046872molecular_functionmetal ion binding
N0051013biological_processmicrotubule severing
N0060296biological_processregulation of cilium beat frequency involved in ciliary motility
N0070739molecular_functionprotein-glutamic acid ligase activity
N0070740molecular_functiontubulin-glutamic acid ligase activity
N0097731cellular_component9+0 non-motile cilium
N0106437molecular_functionprotein-glutamic acid ligase activity, initiating
N0106438molecular_functionprotein-glutamic acid ligase activity, elongating
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
AGLY142-GLY148
BGLY140-GLY146
site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
BMET1-ILE4
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35482892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"16371510","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Campbell A.","Ozanne B.W.","Lourenco F.","Olson M.F."]}}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues343
DetailsDomain: {"description":"TTL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00568","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues79
DetailsRegion: {"description":"c-MTBD region","evidences":[{"source":"UniProtKB","id":"Q8N841","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VZT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6VZU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VZW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VZU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsSite: {"description":"Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity","evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsSite: {"description":"Important for specifying alpha-elongation versus initiation step of the polyglutamylase activity","evidences":[{"source":"PubMed","id":"32747782","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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