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Protein Page:
Fascin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Fascin Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. Associates with beta-catenin. Ubiquitous. Belongs to the fascin family. Note: This description may include information from UniProtKB.
Protein type: Actin binding protein; Cytoskeletal protein; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 7p22
Cellular Component: cytoplasm; stress fiber; cytosol; cell junction; actin cytoskeleton; filopodium
Molecular Function: actin filament binding; protein binding, bridging; protein binding; drug binding; actin binding
Biological Process: actin filament bundle formation; cell proliferation; cell migration; cell motility involved in cell locomotion; actin cytoskeleton organization and biogenesis
Reference #:  Q16658 (UniProtKB)
Alt. Names/Synonyms: 55 kDa actin-bundling protein; actin bundling protein; FAN1; Fascin; fascin 1; fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus); FLJ38511; FSCN1; HSN; p55; Singed, drosophila, homolog-like; singed-like (fascin homolog, sea urchin); Singed-like protein; SNL
Gene Symbols: FSCN1
Molecular weight: 54,530 Da
Basal Isoelectric point: 6.84  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Fascin

Protein Structure Not Found.


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Sites Implicated In
cytoskeletal reorganization: S39‑p
molecular association, regulation: S39‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 Y23-p LINCGNKyLTAEAFG
0 2 S38-p FKVNASAssLkKkQI
8 3 S39-p KVNASAssLkKkQIW
0 18 K41-ac NASAssLkKkQIWTL
0 5 K41 NASAssLKKkQIWTL
0 1 K41-sc NASAssLkKkQIWTL
0 1 K42 ASAssLkKkQIWTLE
0 1 K43-ac SAssLkKkQIWTLEQ
0 9 K74-ac GRYLAADkDGNVTCE
0 8 K74 GRYLAADKDGNVTCE
0 1 K74-sc GRYLAADkDGNVTCE
0 2 S120-p GGTEDRLsCFAQTVs
0 3 S127-p sCFAQTVsPAEKWSV
0 2 Y145-p MHPQVNIysVtRKRY
0 1 S146-p HPQVNIysVtRKRYA
0 2 T148-p QVNIysVtRKRYAHL
0 1 K220 TLEFRSGKVAFRDCE
0 2 S234-p EGRYLAPsGPsGtLk
0 1 S237-p YLAPsGPsGtLkAGK
0 2 T239-p APsGPsGtLkAGKAT
0 9 K241-ub sGPsGtLkAGKATkV
0 1 K241-sc sGPsGtLkAGKATkV
0 1 K247-ub LkAGKATkVGkDELF
0 1 K250-ac GKATkVGkDELFALE
0 1 K304-ac EIDRDTKkCAFRTHT
0 1 Y314-p FRTHTGKyWTLTATG
0 1 S333-p TASSKNAsCYFDIEW
0 1 K353-m2 TLRASNGkFVTSKkN
0 1 K359-ub GkFVTSKkNGQLAAS
0 6 K399-ub HGFIGCRkVTGtLDA
0 2 T403-p GCRkVTGtLDANRSS
0 1 Y411-p LDANRSSyDVFQLEF
0 2 K464 DYNKVAIKVGGRYLk
0 1 K464-sc DYNKVAIkVGGRYLk
0 5 K471 kVGGRYLKGDHAGVL
0 1 K471-sc kVGGRYLkGDHAGVL
0 1 K471-ac kVGGRYLkGDHAGVL
0 1 K479-ub GDHAGVLkASAEtVD
0 1 T484-p VLkASAEtVDPASLW
  mouse

 
Y23 LISCGNKYLTAEAFG
S38 FKVNASASsLkkKQI
S39-p KVNASASsLkkKQIW
K41-ac NASASsLkkKQIWTL
K41-ub NASASsLkkKQIWTL
K41 NASASsLKkKQIWTL
K42-ub ASASsLkkKQIWTLE
K43 SASsLkkKQIWTLEQ
K74 GRYLAADKDGNVTCE
K74-ub GRYLAADkDGNVTCE
K74 GRYLAADKDGNVTCE
S120 GGTEDRLSCFAQSVS
S127 SCFAQSVSPAEKWSV
Y145 MHPQVNIYSVTRKRY
S146 HPQVNIYSVTRKRYA
T148 QVNIYSVTRKRYAHL
K220-ub TLEFRSGkVAFRDCE
S234 EGRYLAPSGPSGTLk
S237 YLAPSGPSGTLkAGK
T239 APSGPSGTLkAGKAT
K241-ub SGPSGTLkAGKATKV
K241 SGPSGTLKAGKATKV
K247 LkAGKATKVGKDELF
K250 GKATKVGKDELFALE
K304 EIDRDTRKCAFRTHT
Y314 FRTHTGKYWTLTATG
S333 TASTKNASCYFDIEW
K353 TLRASNGKFVTAKKN
K359 GKFVTAKKNGQLAAS
K399-ub HGFIGCRkVTGtLDA
T403-p GCRkVTGtLDANRSS
Y411 LDANRSSYDVFQLEF
K464-ub DYNKVALkVGGRYLk
K464 DYNKVALKVGGRYLk
K471-ub kVGGRYLkGDHAGVL
K471 kVGGRYLKGDHAGVL
K471 kVGGRYLKGDHAGVL
K479 GDHAGVLKACAETID
T484 VLKACAETIDPASLW
  rat

 
Y23 LISCGNKYLTAEAFG
S38 FKVNASASSLKKKQI
S39 KVNASASSLKKKQIW
K41 NASASSLKKKQIWTL
K41 NASASSLKKKQIWTL
K41 NASASSLKKKQIWTL
K42 ASASSLKKKQIWTLE
K43 SASSLKKKQIWTLEQ
K74 GPYLAADKDGNVTCE
K74 GPYLAADKDGNVTCE
K74 GPYLAADKDGNVTCE
S120 GGTEDRLSCFAQSVS
S127 SCFAQSVSPAEKWSV
Y145 MHPQVNIYSVTRKRY
S146 HPQVNIYSVTRKRYA
T148 QVNIYSVTRKRYAHL
K220 TLEFRSGKVAFRDCE
S234 EGRYLAPSGPSGTLK
S237 YLAPSGPSGTLKAGK
T239 APSGPSGTLKAGKAT
K241 SGPSGTLKAGKATKV
K241 SGPSGTLKAGKATKV
K247 LKAGKATKVGKDELF
K250 GKATKVGKDELFALE
K304 EIDRDTRKCAFRTHT
Y314 FRTHTGKYWTLTATG
S333 TASTKNASCYFDIEW
K353 TLRASNGKFVTAKKN
K359 GKFVTAKKNGQLAAT
K399 HGFIGCRKVTGtLDA
T403-p GCRKVTGtLDANRSS
Y411 LDANRSSYDVFQLEF
K464 DYNKVALKVGGRYLk
K464 DYNKVALKVGGRYLk
K471 KVGGRYLKGDHAGVL
K471 KVGGRYLKGDHAGVL
K471-ac KVGGRYLkGDHAGVL
K479 GDHAGVLKACAETID
T484 VLKACAETIDPATLW
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