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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9LXH

DOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane

Functional Information from GO Data
ChainGOidnamespacecontents
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006909biological_processphagocytosis
A0006911biological_processphagocytosis, engulfment
A0006915biological_processapoptotic process
A0007015biological_processactin filament organization
A0016020cellular_componentmembrane
A0016601biological_processRac protein signal transduction
A0017124molecular_functionSH3 domain binding
A0030036biological_processactin cytoskeleton organization
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0048870biological_processcell motility
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0150052biological_processregulation of postsynapse assembly
A0160124molecular_functionguanyl nucleotide exchange factor activator activity
A2001212biological_processregulation of vasculogenesis
B0002102cellular_componentpodosome
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007520biological_processmyoblast fusion
B0010634biological_processpositive regulation of epithelial cell migration
B0016477biological_processcell migration
B0016601biological_processRac protein signal transduction
B0031267molecular_functionsmall GTPase binding
B1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
B1904694biological_processnegative regulation of vascular associated smooth muscle contraction
B1904754biological_processpositive regulation of vascular associated smooth muscle cell migration
C0000166molecular_functionnucleotide binding
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0007015biological_processactin filament organization
C0007163biological_processestablishment or maintenance of cell polarity
C0007266biological_processRho protein signal transduction
C0008284biological_processpositive regulation of cell population proliferation
C0008360biological_processregulation of cell shape
C0016601biological_processRac protein signal transduction
C0019901molecular_functionprotein kinase binding
C0030036biological_processactin cytoskeleton organization
C0030667cellular_componentsecretory granule membrane
C0030865biological_processcortical cytoskeleton organization
C0031410cellular_componentcytoplasmic vesicle
C0032956biological_processregulation of actin cytoskeleton organization
C0042995cellular_componentcell projection
C0045893biological_processpositive regulation of DNA-templated transcription
C0060326biological_processcell chemotaxis
C0070062cellular_componentextracellular exosome
C0090630biological_processactivation of GTPase activity
C0098794cellular_componentpostsynapse
C0098978cellular_componentglutamatergic synapse
C0150052biological_processregulation of postsynapse assembly
C1903078biological_processpositive regulation of protein localization to plasma membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues173
DetailsDomain: {"description":"ELMO","evidences":[{"source":"PROSITE-ProRule","id":"PRU00664","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues121
DetailsDomain: {"description":"PH"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsMotif: {"description":"SH3-binding"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues5
DetailsModified residue: {"description":"Phosphotyrosine; by HCK","evidences":[{"source":"PubMed","id":"15952790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BPU7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues61
DetailsDomain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues184
DetailsDomain: {"description":"C2 DOCK-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00983","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate","evidences":[{"source":"PubMed","id":"24905543","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-01-21

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