FSCN1
entrez
6624
canonical
uniprot
Q16658
canonical
ensembl
ENSG00000075618
resolver
ensp
ENSP00000371798
resolver
enst
ENST00000382361
resolver
genesymbol
FSCN1
resolver
genesymbol_syn
FAN1
resolver
genesymbol_syn
HSN
resolver
genesymbol_syn
SNL
resolver
hgnc
HGNC:11148
resolver
uniprot
A0A384MEG1
resolver
uniprot
A6NI89
resolver
uniprot
B2RE97
resolver
uniprot
B3KTA3
resolver
uniprot
Q96IC5
resolver
uniprot
Q96IH1
resolver
uniprot
Q9BRF1
resolver
uniprot_entry
A0A384MEG1_HUMAN
resolver
uniprot_entry
B3KTA3_HUMAN
resolver
uniprot_entry
FSCN1_HUMAN
resolver
uniprot_sec
A6NI89
resolver
uniprot_sec
B2RE97
resolver
uniprot_sec
Q96IC5
resolver
uniprot_sec
Q96IH1
resolver
uniprot_sec
Q9BRF1
resolver
amino_acid_sequence
MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY
uniprot
proteins
function
FUNCTION: Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:20393565, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:23184945, ECO:0000269|PubMed:9362073, ECO:0000269|PubMed:9571235}.
uniprot
proteins
mass_dalton
54530
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="K->E: Decreased actin-binding and loss of actin-bundling activity; when associated with E-43 and E-398. Decreased actin-binding and loss of actin-bundling activity; when associated with E-43; E-100 and E-109."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 29; /note="F->A: Strongly decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 36..39; /note="SASS->AAAA: Abolishes axon growth cone collapse in response to NGF."; /evidence="ECO:0000269|PubMed:22155786"; MUTAGEN 39; /note="S->A: Loss of phosphorylation."; /evidence="ECO:0000269|PubMed:8999969"; MUTAGEN 39; /note="S->D: Phosphomimetic mutant that strongly decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 43; /note="K->E: Decreased actin-binding and loss of actin-bundling activity; when associated with E-22 and E-398. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-100 and E-109."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 49; /note="E->A: Strongly decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 100; /note="R->E: Mildly decreased actin-binding and actin-bundling activity; when associated with E-109 and E-247. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-43 and E-109."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 109; /note="R->E: Mildly decreased actin-binding and actin-bundling activity; when associated with E-100 and E-247. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-43 and E-100."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 149..151; /note="RKR->AAA: Strongly decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 150..151; /note="KR->EE: No significant effect on actin-binding and actin-bundling activity; when associated with E-313."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 247..250; /note="KVGK->AVGA: Decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 247; /note="K->E: Mildly decreased actin-binding and actin-bundling activity; when associated with E-100 and E-109."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 271; /note="R->E: Decreased actin-binding and actin-bundling activity; when associated with E-353 and E-358."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 313; /note="K->E: No significant effect on actin-binding and actin-bundling activity; when associated with 150-E-E-151."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 341; /note="R->E: No significant effect on actin-binding and actin-bundling activity; when associated with E-348 and Q-464."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 348; /note="R->E: No significant effect on actin-binding and actin-bundling activity; when associated with E-341 and Q-464."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 353; /note="K->E: Decreased actin-binding and actin-bundling activity; when associated with E-271 and E-358."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 358; /note="K->A: Strongly decreases actin-bundling activity."; /evidence="ECO:0000269|PubMed:23184945"; MUTAGEN 358; /note="K->E: Decreased actin-binding and actin-bundling activity; when associated with E-271 and E-353."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 392; /note="H->A: Decreased actin-bundling activity."; /evidence="ECO:0000269|PubMed:20393565"; MUTAGEN 398; /note="R->E: Decreased actin-binding and loss of actin-bundling activity; when associated with E-22 and E-43."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 464; /note="K->Q: No significant effect on actin-binding and actin-bundling activity; when associated with E-341 and E-348."; /evidence="ECO:0000269|PubMed:21685497"; MUTAGEN 471; /note="K->A: Decreased actin-bundling activity."; /evidence="ECO:0000269|PubMed:20393565"; MUTAGEN 488; /note="A->W: Decreased actin-bundling activity."; /evidence="ECO:0000269|PubMed:20393565
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-39 inhibits actin-binding (PubMed:8647875, PubMed:8999969). Phosphorylation is required for the reorganization of the actin cytoskeleton in response to NGF (PubMed:22155786). {ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:8647875, ECO:0000269|PubMed:8999969}.
uniprot
proteins
protein_family
Fascin family
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20137952
uniprot
proteins
pubmed
20393565
uniprot
proteins
pubmed
20434460
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21685497
uniprot
proteins
pubmed
21706053
uniprot
proteins
pubmed
22155786
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23184945
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
3525578
uniprot
proteins
pubmed
7933116
uniprot
proteins
pubmed
8068206
uniprot
proteins
pubmed
8647875
uniprot
proteins
pubmed
8999969
uniprot
proteins
pubmed
9362073
uniprot
proteins
pubmed
9571235
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21706053, ECO:0000269|PubMed:9571235}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21685497}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:3525578, ECO:0000269|PubMed:9571235}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:21706053}. Cell projection, filopodium {ECO:0000269|PubMed:20137952, ECO:0000269|PubMed:21685497, ECO:0000269|PubMed:3525578}. Cell projection, invadopodium {ECO:0000269|PubMed:20137952}. Cell projection, microvillus {ECO:0000269|PubMed:9571235}. Cell junction {ECO:0000269|PubMed:9571235}. Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone. Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone (By similarity). {ECO:0000250|UniProtKB:Q61553, ECO:0000269|PubMed:21706053}.
uniprot
proteins