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8VT7

Structure of the gamma tubulin ring complex nucleated microtubule protofilament.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005929cellular_componentcilium
A0007017biological_processmicrotubule-based process
A0007411biological_processaxon guidance
A0015630cellular_componentmicrotubule cytoskeleton
A0030027cellular_componentlamellipodium
A0030175cellular_componentfilopodium
A0030182biological_processneuron differentiation
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0030426cellular_componentgrowth cone
A0038007biological_processnetrin-activated signaling pathway
A0042277molecular_functionpeptide binding
A0043025cellular_componentneuronal cell body
A0045171cellular_componentintercellular bridge
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0071944cellular_componentcell periphery
A0072686cellular_componentmitotic spindle
A0097228cellular_componentsperm principal piece
A0097229cellular_componentsperm end piece
A0097542cellular_componentciliary tip
A1990791biological_processdorsal root ganglion development
A1990890molecular_functionnetrin receptor binding
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003725molecular_functiondouble-stranded RNA binding
B0003924molecular_functionGTPase activity
B0005198molecular_functionstructural molecule activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0005881cellular_componentcytoplasmic microtubule
B0005929cellular_componentcilium
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0016787molecular_functionhydrolase activity
B0030182biological_processneuron differentiation
B0030705biological_processcytoskeleton-dependent intracellular transport
B0031625molecular_functionubiquitin protein ligase binding
B0051301biological_processcell division
F0000166molecular_functionnucleotide binding
F0000226biological_processmicrotubule cytoskeleton organization
F0000278biological_processmitotic cell cycle
F0003924molecular_functionGTPase activity
F0005200molecular_functionstructural constituent of cytoskeleton
F0005515molecular_functionprotein binding
F0005525molecular_functionGTP binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005874cellular_componentmicrotubule
F0005929cellular_componentcilium
F0007017biological_processmicrotubule-based process
F0007411biological_processaxon guidance
F0015630cellular_componentmicrotubule cytoskeleton
F0030027cellular_componentlamellipodium
F0030175cellular_componentfilopodium
F0030182biological_processneuron differentiation
F0030424cellular_componentaxon
F0030425cellular_componentdendrite
F0030426cellular_componentgrowth cone
F0038007biological_processnetrin-activated signaling pathway
F0042277molecular_functionpeptide binding
F0043025cellular_componentneuronal cell body
F0045171cellular_componentintercellular bridge
F0046872molecular_functionmetal ion binding
F0070062cellular_componentextracellular exosome
F0071944cellular_componentcell periphery
F0072686cellular_componentmitotic spindle
F0097228cellular_componentsperm principal piece
F0097229cellular_componentsperm end piece
F0097542cellular_componentciliary tip
F1990791biological_processdorsal root ganglion development
F1990890molecular_functionnetrin receptor binding
J0000166molecular_functionnucleotide binding
J0000226biological_processmicrotubule cytoskeleton organization
J0000278biological_processmitotic cell cycle
J0003725molecular_functiondouble-stranded RNA binding
J0003924molecular_functionGTPase activity
J0005198molecular_functionstructural molecule activity
J0005200molecular_functionstructural constituent of cytoskeleton
J0005515molecular_functionprotein binding
J0005525molecular_functionGTP binding
J0005737cellular_componentcytoplasm
J0005856cellular_componentcytoskeleton
J0005874cellular_componentmicrotubule
J0005881cellular_componentcytoplasmic microtubule
J0005929cellular_componentcilium
J0007017biological_processmicrotubule-based process
J0015630cellular_componentmicrotubule cytoskeleton
J0016787molecular_functionhydrolase activity
J0030182biological_processneuron differentiation
J0030705biological_processcytoskeleton-dependent intracellular transport
J0031625molecular_functionubiquitin protein ligase binding
J0051301biological_processcell division
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
FGLY140-GLY146
JGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
FMET1-ILE4

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35482892","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z6S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"16371510","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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_FI10
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_FI11
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
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_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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