3H2V
Human raver1 RRM1 domain in complex with human vinculin tail domain Vt
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003779 | molecular_function | actin binding |
A | 0007155 | biological_process | cell adhesion |
A | 0051015 | molecular_function | actin filament binding |
B | 0003779 | molecular_function | actin binding |
B | 0007155 | biological_process | cell adhesion |
B | 0051015 | molecular_function | actin filament binding |
C | 0003779 | molecular_function | actin binding |
C | 0007155 | biological_process | cell adhesion |
C | 0051015 | molecular_function | actin filament binding |
D | 0003779 | molecular_function | actin binding |
D | 0007155 | biological_process | cell adhesion |
D | 0051015 | molecular_function | actin filament binding |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0003723 | molecular_function | RNA binding |
F | 0003676 | molecular_function | nucleic acid binding |
F | 0003723 | molecular_function | RNA binding |
G | 0003676 | molecular_function | nucleic acid binding |
G | 0003723 | molecular_function | RNA binding |
H | 0003676 | molecular_function | nucleic acid binding |
H | 0003723 | molecular_function | RNA binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by SRC-type Tyr-kinases => ECO:0000269|PubMed:15229287 |
Chain | Residue | Details |