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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VA2

Symmetry expanded map of 2 gamma-tubulins bound to 2 alpha tubulins in gamma tubulin ring complex capped microtubule end.

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
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
b0030705biological_processcytoskeleton-dependent intracellular transport
b0031625molecular_functionubiquitin protein ligase binding
b0051301biological_processcell division
b0071353biological_processcellular response to interleukin-4
g0000070biological_processmitotic sister chromatid segregation
g0000166molecular_functionnucleotide binding
g0000212biological_processmeiotic spindle organization
g0000226biological_processmicrotubule cytoskeleton organization
g0000242cellular_componentpericentriolar material
g0000278biological_processmitotic cell cycle
g0000794cellular_componentcondensed nuclear chromosome
g0000930cellular_componentgamma-tubulin complex
g0000931cellular_componentgamma-tubulin ring complex
g0005200molecular_functionstructural constituent of cytoskeleton
g0005515molecular_functionprotein binding
g0005525molecular_functionGTP binding
g0005634cellular_componentnucleus
g0005737cellular_componentcytoplasm
g0005813cellular_componentcentrosome
g0005814cellular_componentcentriole
g0005819cellular_componentspindle
g0005827cellular_componentpolar microtubule
g0005829cellular_componentcytosol
g0005856cellular_componentcytoskeleton
g0005874cellular_componentmicrotubule
g0005876cellular_componentspindle microtubule
g0005881cellular_componentcytoplasmic microtubule
g0005929cellular_componentcilium
g0007017biological_processmicrotubule-based process
g0007020biological_processmicrotubule nucleation
g0007052biological_processmitotic spindle organization
g0015630cellular_componentmicrotubule cytoskeleton
g0031122biological_processcytoplasmic microtubule organization
g0031252cellular_componentcell leading edge
g0036064cellular_componentciliary basal body
g0042802molecular_functionidentical protein binding
g0043005cellular_componentneuron projection
g0045177cellular_componentapical part of cell
g0055037cellular_componentrecycling endosome
g0097730cellular_componentnon-motile cilium
g0140490molecular_functionmicrotubule nucleator activity
g1990498cellular_componentmitotic spindle microtubule
h0000070biological_processmitotic sister chromatid segregation
h0000166molecular_functionnucleotide binding
h0000212biological_processmeiotic spindle organization
h0000226biological_processmicrotubule cytoskeleton organization
h0000242cellular_componentpericentriolar material
h0000278biological_processmitotic cell cycle
h0000794cellular_componentcondensed nuclear chromosome
h0000930cellular_componentgamma-tubulin complex
h0000931cellular_componentgamma-tubulin ring complex
h0005200molecular_functionstructural constituent of cytoskeleton
h0005515molecular_functionprotein binding
h0005525molecular_functionGTP binding
h0005634cellular_componentnucleus
h0005737cellular_componentcytoplasm
h0005813cellular_componentcentrosome
h0005814cellular_componentcentriole
h0005819cellular_componentspindle
h0005827cellular_componentpolar microtubule
h0005829cellular_componentcytosol
h0005856cellular_componentcytoskeleton
h0005874cellular_componentmicrotubule
h0005876cellular_componentspindle microtubule
h0005881cellular_componentcytoplasmic microtubule
h0005929cellular_componentcilium
h0007017biological_processmicrotubule-based process
h0007020biological_processmicrotubule nucleation
h0007052biological_processmitotic spindle organization
h0015630cellular_componentmicrotubule cytoskeleton
h0031122biological_processcytoplasmic microtubule organization
h0031252cellular_componentcell leading edge
h0036064cellular_componentciliary basal body
h0042802molecular_functionidentical protein binding
h0043005cellular_componentneuron projection
h0045177cellular_componentapical part of cell
h0055037cellular_componentrecycling endosome
h0097730cellular_componentnon-motile cilium
h0140490molecular_functionmicrotubule nucleator activity
h1990498cellular_componentmitotic spindle microtubule
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. AGGTGSG
ChainResidueDetails
gALA142-GLY148
aGLY142-GLY148
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
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_FI4
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_FI5
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
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_FI7
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by BRSK1","evidences":[{"source":"UniProtKB","id":"P83887","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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