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8XM7

Cryo-EM structure of the RhoG/DOCK5/ELMO1/Rac1 complex: RhoG/DOCK5/ELMO1 focused map

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
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005096molecular_functionGTPase activator activity
B0007264biological_processsmall GTPase-mediated signal transduction
B0016477biological_processcell migration
D0000166molecular_functionnucleotide binding
D0003924molecular_functionGTPase activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005789cellular_componentendoplasmic reticulum membrane
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0007015biological_processactin filament organization
D0007163biological_processestablishment or maintenance of cell polarity
D0007264biological_processsmall GTPase-mediated signal transduction
D0007266biological_processRho protein signal transduction
D0008284biological_processpositive regulation of cell population proliferation
D0008360biological_processregulation of cell shape
D0016601biological_processRac protein signal transduction
D0019901molecular_functionprotein kinase binding
D0030036biological_processactin cytoskeleton organization
D0030667cellular_componentsecretory granule membrane
D0030865biological_processcortical cytoskeleton organization
D0031410cellular_componentcytoplasmic vesicle
D0032956biological_processregulation of actin cytoskeleton organization
D0042995cellular_componentcell projection
D0045893biological_processpositive regulation of DNA-templated transcription
D0060326biological_processcell chemotaxis
D0070062cellular_componentextracellular exosome
D0090630biological_processactivation of GTPase activity
D0098794cellular_componentpostsynapse
D0098978cellular_componentglutamatergic synapse
D0150052biological_processregulation of postsynapse assembly
D1903078biological_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

247536

PDB entries from 2026-01-14

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