3P53
Structure of fascin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001725 | cellular_component | stress fiber |
| A | 0001726 | cellular_component | ruffle |
| A | 0002102 | cellular_component | podosome |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003779 | molecular_function | actin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005902 | cellular_component | microvillus |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0005938 | cellular_component | cell cortex |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007043 | biological_process | cell-cell junction assembly |
| A | 0007163 | biological_process | establishment or maintenance of cell polarity |
| A | 0008144 | molecular_function | obsolete drug binding |
| A | 0010592 | biological_process | positive regulation of lamellipodium assembly |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016477 | biological_process | cell migration |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030035 | biological_process | microspike assembly |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0030046 | biological_process | parallel actin filament bundle assembly |
| A | 0030175 | cellular_component | filopodium |
| A | 0030426 | cellular_component | growth cone |
| A | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| A | 0031252 | cellular_component | cell leading edge |
| A | 0031253 | cellular_component | cell projection membrane |
| A | 0032534 | biological_process | regulation of microvillus assembly |
| A | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| A | 0035089 | biological_process | establishment of apical/basal cell polarity |
| A | 0042995 | cellular_component | cell projection |
| A | 0044393 | cellular_component | microspike |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0048870 | biological_process | cell motility |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0051017 | biological_process | actin filament bundle assembly |
| A | 0051491 | biological_process | positive regulation of filopodium assembly |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070161 | cellular_component | anchoring junction |
| A | 0071803 | biological_process | positive regulation of podosome assembly |
| A | 0090091 | biological_process | positive regulation of extracellular matrix disassembly |
| B | 0001725 | cellular_component | stress fiber |
| B | 0001726 | cellular_component | ruffle |
| B | 0002102 | cellular_component | podosome |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003779 | molecular_function | actin binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005902 | cellular_component | microvillus |
| B | 0005911 | cellular_component | cell-cell junction |
| B | 0005938 | cellular_component | cell cortex |
| B | 0007015 | biological_process | actin filament organization |
| B | 0007043 | biological_process | cell-cell junction assembly |
| B | 0007163 | biological_process | establishment or maintenance of cell polarity |
| B | 0008144 | molecular_function | obsolete drug binding |
| B | 0010592 | biological_process | positive regulation of lamellipodium assembly |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016477 | biological_process | cell migration |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030035 | biological_process | microspike assembly |
| B | 0030036 | biological_process | actin cytoskeleton organization |
| B | 0030046 | biological_process | parallel actin filament bundle assembly |
| B | 0030175 | cellular_component | filopodium |
| B | 0030426 | cellular_component | growth cone |
| B | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| B | 0031252 | cellular_component | cell leading edge |
| B | 0031253 | cellular_component | cell projection membrane |
| B | 0032534 | biological_process | regulation of microvillus assembly |
| B | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| B | 0035089 | biological_process | establishment of apical/basal cell polarity |
| B | 0042995 | cellular_component | cell projection |
| B | 0044393 | cellular_component | microspike |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0048870 | biological_process | cell motility |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0051017 | biological_process | actin filament bundle assembly |
| B | 0051491 | biological_process | positive regulation of filopodium assembly |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070161 | cellular_component | anchoring junction |
| B | 0071803 | biological_process | positive regulation of podosome assembly |
| B | 0090091 | biological_process | positive regulation of extracellular matrix disassembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 494 |
| Chain | Residue |
| A | LEU380 |
| A | ILE381 |
| A | ASN382 |
| A | ARG383 |
| A | PRO384 |
| A | LEU416 |
| A | PHE418 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 495 |
| Chain | Residue |
| A | GLY421 |
| A | TYR423 |
| A | PHE452 |
| A | PHE453 |
| A | ASP342 |
| A | MET378 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 496 |
| Chain | Residue |
| A | LYS32 |
| A | VAL33 |
| A | VAL78 |
| A | ASP117 |
| A | ARG118 |
| A | LEU119 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 497 |
| Chain | Residue |
| A | LYS304 |
| A | ASP337 |
| A | ARG348 |
| A | ALA349 |
| A | SER350 |
| B | ASP446 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 12P A 498 |
| Chain | Residue |
| A | ILE17 |
| A | ASN18 |
| A | CYS19 |
| A | ASP98 |
| A | ARG100 |
| A | PRO128 |
| A | LYS131 |
| A | SER133 |
| A | PHE181 |
| A | ASP183 |
| A | GLN184 |
| A | ARG185 |
| A | TYR186 |
| A | HOH633 |
| B | PHE31 |
| B | ARG68 |
| B | GLU81 |
| B | GLU83 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 499 |
| Chain | Residue |
| A | THR318 |
| A | ALA319 |
| A | THR320 |
| A | ASN351 |
| A | LYS353 |
| A | SER366 |
| A | HOH658 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE A 500 |
| Chain | Residue |
| A | ARG389 |
| A | GLY390 |
| A | LYS460 |
| A | PRO487 |
| A | LEU490 |
| A | GLU492 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE A 501 |
| Chain | Residue |
| A | LEU40 |
| A | LYS42 |
| A | ILE45 |
| A | ALA137 |
| A | ARG389 |
| A | GLY390 |
| A | GLU391 |
| A | HIS392 |
| A | GLY393 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 495 |
| Chain | Residue |
| B | LEU380 |
| B | ILE381 |
| B | ASN382 |
| B | ARG383 |
| B | PRO384 |
| B | LEU416 |
| B | PHE418 |
| B | HOH591 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 496 |
| Chain | Residue |
| B | ASP342 |
| B | ARG343 |
| B | ARG344 |
| B | ILE345 |
| B | GLY421 |
| B | TYR423 |
| B | PHE452 |
| B | PHE453 |
| B | HOH533 |
| B | HOH557 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 497 |
| Chain | Residue |
| B | LYS32 |
| B | VAL33 |
| B | ASP117 |
| B | ARG118 |
| B | LEU119 |
| B | HOH614 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 498 |
| Chain | Residue |
| A | LYS74 |
| A | ASP75 |
| A | ARG110 |
| B | PRO448 |
| B | VAL449 |
| B | ASP450 |
| B | HOH556 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE B 494 |
| Chain | Residue |
| B | LYS460 |
| B | PRO487 |
| B | LEU490 |
| B | GLU492 |
| B | HOH663 |
| B | HOH667 |
| B | ARG389 |
| B | GLY390 |
| B | GLU391 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE B 499 |
| Chain | Residue |
| B | HIS135 |
| B | SER410 |
| B | HOH659 |
| B | HOH679 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG0 B 500 |
| Chain | Residue |
| B | LEU40 |
| B | LYS41 |
| B | ALA137 |
| B | ARG389 |
| B | HIS392 |
| B | PHE394 |
| B | ASN407 |
| B | ARG408 |
| B | SER409 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8999969","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22155786","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61553","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P85845","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
