4X1M
Structural basis for mutation-induced destabilization of Profilin 1 in ALS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000774 | molecular_function | adenyl-nucleotide exchange factor activity |
| A | 0001784 | molecular_function | phosphotyrosine residue binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003779 | molecular_function | actin binding |
| A | 0003785 | molecular_function | actin monomer binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005546 | molecular_function | phosphatidylinositol-4,5-bisphosphate binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0005938 | cellular_component | cell cortex |
| A | 0010634 | biological_process | positive regulation of epithelial cell migration |
| A | 0016020 | cellular_component | membrane |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0030833 | biological_process | regulation of actin filament polymerization |
| A | 0030838 | biological_process | positive regulation of actin filament polymerization |
| A | 0031267 | molecular_function | small GTPase binding |
| A | 0032232 | biological_process | negative regulation of actin filament bundle assembly |
| A | 0032233 | biological_process | positive regulation of actin filament bundle assembly |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0050804 | biological_process | modulation of chemical synaptic transmission |
| A | 0050821 | biological_process | protein stabilization |
| A | 0051497 | biological_process | negative regulation of stress fiber assembly |
| A | 0060074 | biological_process | synapse maturation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070064 | molecular_function | proline-rich region binding |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0098885 | biological_process | modification of postsynaptic actin cytoskeleton |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0110053 | biological_process | regulation of actin filament organization |
| A | 1900029 | biological_process | positive regulation of ruffle assembly |
Functional Information from PROSITE/UniProt
| site_id | PS00414 |
| Number of Residues | 9 |
| Details | PROFILIN Profilin signature. mAgWNaYiD |
| Chain | Residue | Details |
| A | MET1-ASP9 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62963","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by ROCK1","evidences":[{"source":"PubMed","id":"18573880","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"} |
| Chain | Residue | Details |
