Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9M1I

Cryo-EM structure of the TBC-D-Arl2-beta-tubulin complex

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
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
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 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 Residues15
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsMotif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
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

PDB statisticsPDBj update infoContact PDBjnumon