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Protein

Fascin

Gene

Fscn1

Organism
Rattus norvegicus (Rat)
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.1 Publication

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fascin
Gene namesi
Name:Fscn1By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1583309. Fscn1.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Cytoplasmcytoskeleton By similarity
  • Cell projectiongrowth cone 1 Publication
  • Cell projectionfilopodium By similarity
  • Cell projectioninvadopodium By similarity
  • Cell projectionmicrovillus By similarity
  • Cell junction By similarity

  • 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. In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol.By similarity

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • cell projection membrane Source: UniProtKB
  • cytoplasm Source: RGD
  • cytosol Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • filamentous actin Source: GO_Central
  • filopodium Source: RGD
  • growth cone Source: RGD
  • invadopodium Source: UniProtKB
  • lamellipodium Source: RGD
  • microspike Source: UniProtKB
  • microvillus Source: RGD
  • plasma membrane Source: RGD
  • podosome Source: UniProtKB
  • ruffle Source: RGD
  • stress fiber Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 493492FascinPRO_0000343450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei39 – 391Phosphoserine; by PKCBy similarity
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei127 – 1271PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei239 – 2391PhosphothreonineBy similarity
Cross-linki399 – 399Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei403 – 4031PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylation on Ser-39 inhibits the actin-binding ability of fascin.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP85845.

2D gel databases

World-2DPAGE0004:P85845.

PTM databases

iPTMnetiP85845.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: GO_Central

Protein-protein interaction databases

BioGridi598682. 2 interactions.
IntActiP85845. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP85845.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Composed of four beta-trefoil domains.By similarity

Sequence similaritiesi

Belongs to the fascin family.Sequence analysis

Phylogenomic databases

HOVERGENiHBG000968.
InParanoidiP85845.
KOiK17455.
PhylomeDBiP85845.

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.

P85845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTANGTAEAV QIQFGLISCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ
60 70 80 90 100
PPDEAGSAAV CLRSHLGPYL AADKDGNVTC EREVPDGDCR FLVVAHDDGR
110 120 130 140 150
WSLQSEAHRR YFGGTEDRLS CFAQSVSPAE KWSVHIAMHP QVNIYSVTRK
160 170 180 190 200
RYAHLSARPA DEIAVDRDVP WGVDSLITLA FQDQRYSVQT SDHRFLRHDG
210 220 230 240 250
RLVARPEPAT GFTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
260 270 280 290 300
DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
310 320 330 340 350
DTRKCAFRTH TGKYWTLTAT GGVQSTASTK NASCYFDIEW CERRITLRAS
360 370 380 390 400
NGKFVTAKKN GQLAATVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV
410 420 430 440 450
TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSS VTSSSDTPVD
460 470 480 490
FFLEFCDYNK VALKVGGRYL KGDHAGVLKA CAETIDPATL WEY
Length:493
Mass (Da):54,491
Last modified:September 22, 2009 - v2
Checksum:i5680527FA91F7B10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC168678 mRNA. Translation: AAI68678.1.
RefSeqiNP_001094276.1. NM_001100806.1.
UniGeneiRn.199526.

Genome annotation databases

GeneIDi683788.
KEGGirno:683788.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC168678 mRNA. Translation: AAI68678.1.
RefSeqiNP_001094276.1. NM_001100806.1.
UniGeneiRn.199526.

3D structure databases

ProteinModelPortaliP85845.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi598682. 2 interactions.
IntActiP85845. 1 interaction.

PTM databases

iPTMnetiP85845.

2D gel databases

World-2DPAGE0004:P85845.

Proteomic databases

PRIDEiP85845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi683788.
KEGGirno:683788.

Organism-specific databases

CTDi6624.
RGDi1583309. Fscn1.

Phylogenomic databases

HOVERGENiHBG000968.
InParanoidiP85845.
KOiK17455.
PhylomeDBiP85845.

Miscellaneous databases

PROiP85845.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  2. "Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones."
    Sasaki Y., Hayashi K., Shirao T., Ishikawa R., Kohama K.
    J. Neurochem. 66:980-988(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIN-BINDING.
  3. "Proteome profile of the mature rat olfactory bulb."
    Maurya D.K., Sundaram C.S., Bhargava P.
    Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFSCN1_RAT
AccessioniPrimary (citable) accession number: P85845
Secondary accession number(s): B5DEI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: September 22, 2009
Last modified: July 6, 2016
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.