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Protein

Fascin

Gene

FSCN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • drug binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament bundle assembly Source: UniProtKB
  • anatomical structure morphogenesis Source: GO_Central
  • cell-cell junction assembly Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell motility Source: UniProtKB
  • cell proliferation Source: ProtInc
  • establishment of apical/basal cell polarity Source: UniProtKB
  • microspike assembly Source: UniProtKB
  • positive regulation of extracellular matrix disassembly Source: UniProtKB
  • positive regulation of filopodium assembly Source: UniProtKB
  • positive regulation of lamellipodium assembly Source: UniProtKB
  • positive regulation of podosome assembly Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of microvillus assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000075618-MONOMER.
SIGNORiQ16658.

Names & Taxonomyi

Protein namesi
Recommended name:
Fascin
Alternative name(s):
55 kDa actin-bundling protein
Singed-like protein
p55
Gene namesi
Name:FSCN1
Synonyms:FAN1, HSN, SNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:11148. FSCN1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell junction Source: UniProtKB
  • cell projection membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • filamentous actin Source: GO_Central
  • filopodium Source: UniProtKB
  • growth cone Source: UniProtKB
  • invadopodium Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • microspike Source: UniProtKB
  • microvillus Source: UniProtKB
  • myelin sheath Source: Ensembl
  • podosome Source: UniProtKB
  • ruffle Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39S → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi392H → A: Decreased actin-bundling activity. 1 Publication1
Mutagenesisi471K → A: Decreased actin-bundling activity. 1 Publication1
Mutagenesisi488A → W: Decreased actin-bundling activity. 1 Publication1

Organism-specific databases

DisGeNETi6624.
OpenTargetsiENSG00000075618.
PharmGKBiPA128394534.

Polymorphism and mutation databases

BioMutaiFSCN1.
DMDMi2498357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002193792 – 493FascinAdd BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1 Publication1
Modified residuei38PhosphoserineCombined sources1
Modified residuei39Phosphoserine; by PKC1 Publication1
Modified residuei74N6-acetyllysineBy similarity1
Modified residuei127PhosphoserineCombined sources1
Modified residuei234PhosphoserineCombined sources1
Modified residuei239PhosphothreonineCombined sources1
Cross-linki399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei403PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16658.
MaxQBiQ16658.
PaxDbiQ16658.
PeptideAtlasiQ16658.
PRIDEiQ16658.

2D gel databases

REPRODUCTION-2DPAGEIPI00163187.
Q16658.
UCD-2DPAGEQ16658.

PTM databases

iPTMnetiQ16658.
PhosphoSitePlusiQ16658.
SwissPalmiQ16658.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000075618.
CleanExiHS_FSCN1.
ExpressionAtlasiQ16658. baseline and differential.
GenevisibleiQ16658. HS.

Organism-specific databases

HPAiCAB000121.
CAB035991.
HPA005723.

Interactioni

Subunit structurei

Interacts with RUFY3 (via N-terminus); the interaction induces neuron axon development. Associates with beta-catenin (By similarity). Interacts with PLXNB3 (PubMed:21706053).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FANCD2Q9BXW96EBI-351076,EBI-359343
MLH1P406927EBI-351076,EBI-744248
PLXNB3Q9ULL42EBI-351076,EBI-311073
YWHAZP631043EBI-351076,EBI-347088

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi112508. 41 interactors.
DIPiDIP-33171N.
IntActiQ16658. 31 interactors.
MINTiMINT-3033029.
STRINGi9606.ENSP00000371798.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Beta strandi23 – 26Combined sources4
Helixi29 – 31Combined sources3
Beta strandi33 – 39Combined sources7
Helixi42 – 44Combined sources3
Beta strandi46 – 49Combined sources4
Helixi53 – 55Combined sources3
Beta strandi60 – 63Combined sources4
Beta strandi69 – 72Combined sources4
Beta strandi78 – 84Combined sources7
Helixi87 – 89Combined sources3
Beta strandi91 – 95Combined sources5
Beta strandi97 – 99Combined sources3
Beta strandi101 – 105Combined sources5
Turni106 – 108Combined sources3
Beta strandi111 – 116Combined sources6
Beta strandi118 – 125Combined sources8
Helixi128 – 130Combined sources3
Beta strandi132 – 136Combined sources5
Beta strandi141 – 146Combined sources6
Turni147 – 150Combined sources4
Beta strandi151 – 156Combined sources6
Beta strandi162 – 169Combined sources8
Helixi173 – 175Combined sources3
Beta strandi177 – 181Combined sources5
Beta strandi183 – 189Combined sources7
Beta strandi202 – 205Combined sources4
Helixi208 – 210Combined sources3
Beta strandi212 – 216Combined sources5
Beta strandi221 – 224Combined sources4
Beta strandi230 – 234Combined sources5
Turni235 – 238Combined sources4
Beta strandi239 – 242Combined sources4
Helixi250 – 252Combined sources3
Beta strandi254 – 258Combined sources5
Beta strandi262 – 266Combined sources5
Beta strandi272 – 274Combined sources3
Beta strandi277 – 280Combined sources4
Beta strandi282 – 286Combined sources5
Helixi290 – 292Combined sources3
Beta strandi294 – 298Combined sources5
Turni300 – 302Combined sources3
Beta strandi305 – 308Combined sources4
Turni310 – 312Combined sources3
Beta strandi314 – 317Combined sources4
Beta strandi321 – 329Combined sources9
Helixi332 – 334Combined sources3
Beta strandi336 – 341Combined sources6
Beta strandi344 – 348Combined sources5
Beta strandi354 – 357Combined sources4
Beta strandi361 – 369Combined sources9
Helixi372 – 374Combined sources3
Beta strandi376 – 380Combined sources5
Beta strandi384 – 386Combined sources3
Beta strandi393 – 397Combined sources5
Turni399 – 401Combined sources3
Beta strandi403 – 410Combined sources8
Beta strandi414 – 419Combined sources6
Beta strandi422 – 426Combined sources5
Beta strandi432 – 435Combined sources4
Beta strandi439 – 447Combined sources9
Beta strandi451 – 456Combined sources6
Turni457 – 459Combined sources3
Beta strandi460 – 465Combined sources6
Beta strandi468 – 472Combined sources5
Beta strandi476 – 484Combined sources9
Helixi487 – 489Combined sources3
Beta strandi490 – 492Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DFCX-ray2.90A/B1-493[»]
3LLPX-ray1.80A/B1-493[»]
3P53X-ray2.00A/B1-493[»]
4GOVX-ray2.20A/B1-493[»]
4GOYX-ray2.30A/B1-493[»]
4GP0X-ray2.50A/B1-493[»]
4GP3X-ray2.25A/B1-493[»]
ProteinModelPortaliQ16658.
SMRiQ16658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16658.

Family & Domainsi

Domaini

Composed of four beta-trefoil domains.1 Publication

Sequence similaritiesi

Belongs to the fascin family.Curated

Phylogenomic databases

eggNOGiENOG410IF4E. Eukaryota.
ENOG410XPHV. LUCA.
GeneTreeiENSGT00530000063373.
HOGENOMiHOG000267034.
HOVERGENiHBG000968.
InParanoidiQ16658.
KOiK17455.
OMAiCFAQTIS.
OrthoDBiEOG091G0C6S.
PhylomeDBiQ16658.
TreeFamiTF323992.

Family and domain databases

InterProiIPR008999. Actin_cross-linking.
IPR010431. Fascin.
IPR022768. Fascin-domain.
IPR024703. Fascin_metazoans.
IPR030146. FSCN1.
[Graphical view]
PANTHERiPTHR10551. PTHR10551. 1 hit.
PTHR10551:SF8. PTHR10551:SF8. 1 hit.
PfamiPF06268. Fascin. 4 hits.
[Graphical view]
PIRSFiPIRSF005682. Fascin. 1 hit.
SUPFAMiSSF50405. SSF50405. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ
60 70 80 90 100
PPDEAGSAAV CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR
110 120 130 140 150
WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK
160 170 180 190 200
RYAHLSARPA DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG
210 220 230 240 250
RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
260 270 280 290 300
DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
310 320 330 340 350
DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS
360 370 380 390 400
NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV
410 420 430 440 450
TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD
460 470 480 490
FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY
Length:493
Mass (Da):54,530
Last modified:January 23, 2007 - v3
Checksum:iC1453714BED6109A
GO

Sequence cautioni

The sequence AAH07539 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti440A → V in AAH06304 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03057 mRNA. Translation: AAA86442.1.
U09873 mRNA. Translation: AAA62201.1.
AY044229 Genomic DNA. Translation: AAL01526.1.
AK316607 mRNA. Translation: BAG38194.1.
BT006636 mRNA. Translation: AAP35282.1.
AC006483 Genomic DNA. No translation available.
CH471144 Genomic DNA. Translation: EAW87346.1.
BC000521 mRNA. Translation: AAH00521.1.
BC006304 mRNA. Translation: AAH06304.1.
BC007539 mRNA. Translation: AAH07539.1. Different initiation.
BC007643 mRNA. Translation: AAH07643.1.
BC007948 mRNA. Translation: AAH07948.1.
BC007988 mRNA. Translation: AAH07988.1.
CCDSiCCDS5342.1.
PIRiI38621.
RefSeqiNP_003079.1. NM_003088.3.
UniGeneiHs.118400.

Genome annotation databases

EnsembliENST00000382361; ENSP00000371798; ENSG00000075618.
GeneIDi6624.
KEGGihsa:6624.
UCSCiuc003sou.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03057 mRNA. Translation: AAA86442.1.
U09873 mRNA. Translation: AAA62201.1.
AY044229 Genomic DNA. Translation: AAL01526.1.
AK316607 mRNA. Translation: BAG38194.1.
BT006636 mRNA. Translation: AAP35282.1.
AC006483 Genomic DNA. No translation available.
CH471144 Genomic DNA. Translation: EAW87346.1.
BC000521 mRNA. Translation: AAH00521.1.
BC006304 mRNA. Translation: AAH06304.1.
BC007539 mRNA. Translation: AAH07539.1. Different initiation.
BC007643 mRNA. Translation: AAH07643.1.
BC007948 mRNA. Translation: AAH07948.1.
BC007988 mRNA. Translation: AAH07988.1.
CCDSiCCDS5342.1.
PIRiI38621.
RefSeqiNP_003079.1. NM_003088.3.
UniGeneiHs.118400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DFCX-ray2.90A/B1-493[»]
3LLPX-ray1.80A/B1-493[»]
3P53X-ray2.00A/B1-493[»]
4GOVX-ray2.20A/B1-493[»]
4GOYX-ray2.30A/B1-493[»]
4GP0X-ray2.50A/B1-493[»]
4GP3X-ray2.25A/B1-493[»]
ProteinModelPortaliQ16658.
SMRiQ16658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112508. 41 interactors.
DIPiDIP-33171N.
IntActiQ16658. 31 interactors.
MINTiMINT-3033029.
STRINGi9606.ENSP00000371798.

PTM databases

iPTMnetiQ16658.
PhosphoSitePlusiQ16658.
SwissPalmiQ16658.

Polymorphism and mutation databases

BioMutaiFSCN1.
DMDMi2498357.

2D gel databases

REPRODUCTION-2DPAGEIPI00163187.
Q16658.
UCD-2DPAGEQ16658.

Proteomic databases

EPDiQ16658.
MaxQBiQ16658.
PaxDbiQ16658.
PeptideAtlasiQ16658.
PRIDEiQ16658.

Protocols and materials databases

DNASUi6624.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382361; ENSP00000371798; ENSG00000075618.
GeneIDi6624.
KEGGihsa:6624.
UCSCiuc003sou.4. human.

Organism-specific databases

CTDi6624.
DisGeNETi6624.
GeneCardsiFSCN1.
H-InvDBHIX0033686.
HGNCiHGNC:11148. FSCN1.
HPAiCAB000121.
CAB035991.
HPA005723.
MIMi602689. gene.
neXtProtiNX_Q16658.
OpenTargetsiENSG00000075618.
PharmGKBiPA128394534.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF4E. Eukaryota.
ENOG410XPHV. LUCA.
GeneTreeiENSGT00530000063373.
HOGENOMiHOG000267034.
HOVERGENiHBG000968.
InParanoidiQ16658.
KOiK17455.
OMAiCFAQTIS.
OrthoDBiEOG091G0C6S.
PhylomeDBiQ16658.
TreeFamiTF323992.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000075618-MONOMER.
SIGNORiQ16658.

Miscellaneous databases

ChiTaRSiFSCN1. human.
EvolutionaryTraceiQ16658.
GeneWikiiFSCN1.
GenomeRNAii6624.
PROiQ16658.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000075618.
CleanExiHS_FSCN1.
ExpressionAtlasiQ16658. baseline and differential.
GenevisibleiQ16658. HS.

Family and domain databases

InterProiIPR008999. Actin_cross-linking.
IPR010431. Fascin.
IPR022768. Fascin-domain.
IPR024703. Fascin_metazoans.
IPR030146. FSCN1.
[Graphical view]
PANTHERiPTHR10551. PTHR10551. 1 hit.
PTHR10551:SF8. PTHR10551:SF8. 1 hit.
PfamiPF06268. Fascin. 4 hits.
[Graphical view]
PIRSFiPIRSF005682. Fascin. 1 hit.
SUPFAMiSSF50405. SSF50405. 4 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFSCN1_HUMAN
AccessioniPrimary (citable) accession number: Q16658
Secondary accession number(s): A6NI89
, B2RE97, Q96IC5, Q96IH1, Q9BRF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.