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9M1M

Cryo-EM structure of the TBC-DEC-Arl2-alpha-beta-tubulin complex with GDP-AlFx

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
a0005525molecular_functionGTP binding
a0005737cellular_componentcytoplasm
a0005856cellular_componentcytoskeleton
a0005874cellular_componentmicrotubule
a0015630cellular_componentmicrotubule cytoskeleton
a0016787molecular_functionhydrolase activity
a0030182biological_processneuron differentiation
a0046872molecular_functionmetal ion binding
b0000166molecular_functionnucleotide binding
b0000226biological_processmicrotubule cytoskeleton organization
b0000278biological_processmitotic cell cycle
b0005200molecular_functionstructural constituent of cytoskeleton
b0005515molecular_functionprotein binding
b0005525molecular_functionGTP binding
b0005634cellular_componentnucleus
b0005641cellular_componentnuclear envelope lumen
b0005737cellular_componentcytoplasm
b0005856cellular_componentcytoskeleton
b0005874cellular_componentmicrotubule
b0005929cellular_componentcilium
b0015630cellular_componentmicrotubule cytoskeleton
b0031625molecular_functionubiquitin protein ligase binding
b0036464cellular_componentcytoplasmic ribonucleoprotein granule
b0042288molecular_functionMHC class I protein binding
b0044297cellular_componentcell body
b0045171cellular_componentintercellular bridge
b0046872molecular_functionmetal ion binding
b0050807biological_processregulation of synapse organization
b0072686cellular_componentmitotic spindle
b0097228cellular_componentsperm principal piece
b0097229cellular_componentsperm end piece
b0097542cellular_componentciliary tip
C0003924molecular_functionGTPase activity
C0005096molecular_functionGTPase activator activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0006457biological_processprotein folding
C0007021biological_processtubulin complex assembly
C0007023biological_processpost-chaperonin tubulin folding pathway
C0032391cellular_componentphotoreceptor connecting cilium
C0051087molecular_functionprotein-folding chaperone binding
D0000226biological_processmicrotubule cytoskeleton organization
D0000278biological_processmitotic cell cycle
D0005096molecular_functionGTPase activator activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005874cellular_componentmicrotubule
D0005912cellular_componentadherens junction
D0005923cellular_componentbicellular tight junction
D0006457biological_processprotein folding
D0007021biological_processtubulin complex assembly
D0007023biological_processpost-chaperonin tubulin folding pathway
D0010812biological_processnegative regulation of cell-substrate adhesion
D0016328cellular_componentlateral plasma membrane
D0031115biological_processnegative regulation of microtubule polymerization
D0034333biological_processadherens junction assembly
D0048487molecular_functionbeta-tubulin binding
D0048667biological_processcell morphogenesis involved in neuron differentiation
D0051087molecular_functionprotein-folding chaperone binding
D0070830biological_processbicellular tight junction assembly
E0000226biological_processmicrotubule cytoskeleton organization
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005874cellular_componentmicrotubule
E0006457biological_processprotein folding
E0007021biological_processtubulin complex assembly
E0007023biological_processpost-chaperonin tubulin folding pathway
E0007052biological_processmitotic spindle organization
E0043014molecular_functionalpha-tubulin binding
E0051087molecular_functionprotein-folding chaperone binding
G0000166molecular_functionnucleotide binding
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005525molecular_functionGTP binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005730cellular_componentnucleolus
G0005737cellular_componentcytoplasm
G0005739cellular_componentmitochondrion
G0005758cellular_componentmitochondrial intermembrane space
G0005759cellular_componentmitochondrial matrix
G0005813cellular_componentcentrosome
G0005829cellular_componentcytosol
G0005929cellular_componentcilium
G0006110biological_processregulation of glycolytic process
G0006457biological_processprotein folding
G0007098biological_processcentrosome cycle
G0010811biological_processpositive regulation of cell-substrate adhesion
G0015630cellular_componentmicrotubule cytoskeleton
G0016328cellular_componentlateral plasma membrane
G0019003molecular_functionGDP binding
G0031113biological_processregulation of microtubule polymerization
G0031116biological_processpositive regulation of microtubule polymerization
G0034260biological_processnegative regulation of GTPase activity
G0051457biological_processmaintenance of protein location in nucleus
G0070830biological_processbicellular tight junction assembly
G1903715biological_processregulation of aerobic respiration
Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
bGLY140-GLY146
aGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
bMET1-ILE4

site_idPS00845
Number of Residues33
DetailsCAP_GLY_1 CAP-Gly domain signature. Gvvppvagp..WlGVewDnper...GKHdGSheGtvYF
ChainResidueDetails
EGLY27-PHE59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues37
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues44
DetailsDomain: {"description":"CAP-Gly","evidences":[{"source":"PROSITE-ProRule","id":"PRU00045","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues42
DetailsDomain: {"description":"LRRCT"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9D0J4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues3
DetailsMotif: {"description":"MREC motif","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues3
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_FI28
Number of Residues3
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues1
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_FI36
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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