9LXH
DOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006911 | biological_process | phagocytosis, engulfment |
| A | 0006915 | biological_process | apoptotic process |
| A | 0007015 | biological_process | actin filament organization |
| A | 0016020 | cellular_component | membrane |
| A | 0016601 | biological_process | Rac protein signal transduction |
| A | 0017124 | molecular_function | SH3 domain binding |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| A | 0048870 | biological_process | cell motility |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0160124 | molecular_function | guanyl nucleotide exchange factor activator activity |
| A | 2001212 | biological_process | regulation of vasculogenesis |
| B | 0002102 | cellular_component | podosome |
| B | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007520 | biological_process | myoblast fusion |
| B | 0010634 | biological_process | positive regulation of epithelial cell migration |
| B | 0016477 | biological_process | cell migration |
| B | 0016601 | biological_process | Rac protein signal transduction |
| B | 0031267 | molecular_function | small GTPase binding |
| B | 1900026 | biological_process | positive regulation of substrate adhesion-dependent cell spreading |
| B | 1904694 | biological_process | negative regulation of vascular associated smooth muscle contraction |
| B | 1904754 | biological_process | positive regulation of vascular associated smooth muscle cell migration |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0005829 | cellular_component | cytosol |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005925 | cellular_component | focal adhesion |
| C | 0007015 | biological_process | actin filament organization |
| C | 0007163 | biological_process | establishment or maintenance of cell polarity |
| C | 0007266 | biological_process | Rho protein signal transduction |
| C | 0008284 | biological_process | positive regulation of cell population proliferation |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0016601 | biological_process | Rac protein signal transduction |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0030036 | biological_process | actin cytoskeleton organization |
| C | 0030667 | cellular_component | secretory granule membrane |
| C | 0030865 | biological_process | cortical cytoskeleton organization |
| C | 0031410 | cellular_component | cytoplasmic vesicle |
| C | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| C | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| C | 0060326 | biological_process | cell chemotaxis |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0090630 | biological_process | activation of GTPase activity |
| C | 0098794 | cellular_component | postsynapse |
| C | 0098978 | cellular_component | glutamatergic synapse |
| C | 0150052 | biological_process | regulation of postsynapse assembly |
| C | 1903078 | biological_process | positive regulation of protein localization to plasma membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 173 |
| Details | Domain: {"description":"ELMO","evidences":[{"source":"PROSITE-ProRule","id":"PRU00664","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 121 |
| Details | Domain: {"description":"PH"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Motif: {"description":"SH3-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"Phosphotyrosine; by HCK","evidences":[{"source":"PubMed","id":"15952790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BPU7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 61 |
| Details | Domain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 184 |
| Details | Domain: {"description":"C2 DOCK-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00983","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylasparagine; by botulinum toxin","evidences":[{"source":"UniProtKB","id":"P61586","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate","evidences":[{"source":"PubMed","id":"24905543","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
