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Protein

Fascin

Gene

Fscn1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • drug binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fascin
Alternative name(s):
Singed-like protein
Gene namesi
Name:Fscn1
Synonyms:Fan1, Snl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1352745. Fscn1.

Subcellular locationi

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

  • Note: Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone (PubMed:24720729). Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). In glioma cells, partially colocalizes with F-actin stress fibers in the cytosol (By similarity).By similarity1 Publication

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell projection membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • 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: UniProtKB
  • podosome Source: UniProtKB
  • ruffle Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity1 Publication
Chaini2 – 493492FascinPRO_0000219380Add
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-acetyllysineCombined sources
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 – 4031PhosphothreonineBy similarity

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

EPDiQ61553.
MaxQBiQ61553.
PaxDbiQ61553.
PeptideAtlasiQ61553.
PRIDEiQ61553.

2D gel databases

REPRODUCTION-2DPAGEIPI00353563.

PTM databases

iPTMnetiQ61553.
PhosphoSiteiQ61553.
SwissPalmiQ61553.

Expressioni

Tissue specificityi

Most abundant in brain. Found in other tissues including uterus, small intestine and spleen.

Gene expression databases

BgeeiQ61553.
ExpressionAtlasiQ61553. baseline and differential.
GenevisibleiQ61553. MM.

Interactioni

Subunit structurei

Interacts with RUFY3 (via N-terminus); the interaction induces neuron axon development (PubMed:24720729). Associates with beta-catenin (PubMed:8794867). Interacts with PLXNB3 (PubMed:21706053).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Plxnb3Q9QY403EBI-2308857,EBI-6271317

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI

Protein-protein interaction databases

DIPiDIP-54657N.
IntActiQ61553. 4 interactions.
MINTiMINT-4095345.
STRINGi10090.ENSMUSP00000031565.

Structurei

3D structure databases

ProteinModelPortaliQ61553.
SMRiQ61553. Positions 8-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Composed of four beta-trefoil domains.By similarity

Sequence similaritiesi

Belongs to the fascin family.Curated

Phylogenomic databases

eggNOGiENOG410IF4E. Eukaryota.
ENOG410XPHV. LUCA.
GeneTreeiENSGT00530000063373.
HOGENOMiHOG000267034.
HOVERGENiHBG000968.
InParanoidiQ61553.
KOiK17455.
OMAiCFAQTIS.
OrthoDBiEOG7VQJCP.
PhylomeDBiQ61553.
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.

Q61553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTANGTAEAV QIQFGLISCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ
60 70 80 90 100
PPDEAGSAAV CLRSHLGRYL 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 CDRRITLRAS
360 370 380 390 400
NGKFVTAKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV
410 420 430 440 450
TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSS VTSSSDTPVD
460 470 480 490
FFLEFCDYNK VALKVGGRYL KGDHAGVLKA CAETIDPASL WEY
Length:493
Mass (Da):54,508
Last modified:May 1, 2007 - v4
Checksum:i1C6DCD5211B74969
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641S → T in AAB41126 (PubMed:7738015).Curated
Sequence conflicti64 – 641S → T in AAB58784 (PubMed:8794867).Curated
Sequence conflicti262 – 2621Q → E in AAB41126 (PubMed:7738015).Curated
Sequence conflicti262 – 2621Q → E in AAB58784 (PubMed:8794867).Curated
Sequence conflicti271 – 2711R → G in AAB41126 (PubMed:7738015).Curated
Sequence conflicti271 – 2711R → G in AAB58784 (PubMed:8794867).Curated
Sequence conflicti362 – 3632QL → HV in AAB41126 (PubMed:7738015).Curated
Sequence conflicti362 – 3632QL → HV in AAB58784 (PubMed:8794867).Curated
Sequence conflicti387 – 3871V → A in AAB41126 (PubMed:7738015).Curated
Sequence conflicti387 – 3871V → A in AAB58784 (PubMed:8794867).Curated
Sequence conflicti396 – 3961G → A in AAB41126 (PubMed:7738015).Curated
Sequence conflicti396 – 3961G → A in AAB58784 (PubMed:8794867).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33726 mRNA. Translation: AAB41126.1.
U90355 Genomic DNA. Translation: AAB58784.1.
AK167670 mRNA. Translation: BAE39719.1.
BC010338 mRNA. Translation: AAH10338.1.
BC037137 mRNA. Translation: AAH37137.2.
BC052408 mRNA. Translation: AAH52408.1.
CCDSiCCDS19834.1.
PIRiA56430.
RefSeqiNP_032010.2. NM_007984.2.
UniGeneiMm.289707.

Genome annotation databases

EnsembliENSMUST00000031565; ENSMUSP00000031565; ENSMUSG00000029581.
GeneIDi14086.
KEGGimmu:14086.
UCSCiuc009ajl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33726 mRNA. Translation: AAB41126.1.
U90355 Genomic DNA. Translation: AAB58784.1.
AK167670 mRNA. Translation: BAE39719.1.
BC010338 mRNA. Translation: AAH10338.1.
BC037137 mRNA. Translation: AAH37137.2.
BC052408 mRNA. Translation: AAH52408.1.
CCDSiCCDS19834.1.
PIRiA56430.
RefSeqiNP_032010.2. NM_007984.2.
UniGeneiMm.289707.

3D structure databases

ProteinModelPortaliQ61553.
SMRiQ61553. Positions 8-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-54657N.
IntActiQ61553. 4 interactions.
MINTiMINT-4095345.
STRINGi10090.ENSMUSP00000031565.

PTM databases

iPTMnetiQ61553.
PhosphoSiteiQ61553.
SwissPalmiQ61553.

2D gel databases

REPRODUCTION-2DPAGEIPI00353563.

Proteomic databases

EPDiQ61553.
MaxQBiQ61553.
PaxDbiQ61553.
PeptideAtlasiQ61553.
PRIDEiQ61553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031565; ENSMUSP00000031565; ENSMUSG00000029581.
GeneIDi14086.
KEGGimmu:14086.
UCSCiuc009ajl.1. mouse.

Organism-specific databases

CTDi6624.
MGIiMGI:1352745. Fscn1.

Phylogenomic databases

eggNOGiENOG410IF4E. Eukaryota.
ENOG410XPHV. LUCA.
GeneTreeiENSGT00530000063373.
HOGENOMiHOG000267034.
HOVERGENiHBG000968.
InParanoidiQ61553.
KOiK17455.
OMAiCFAQTIS.
OrthoDBiEOG7VQJCP.
PhylomeDBiQ61553.
TreeFamiTF323992.

Miscellaneous databases

ChiTaRSiFscn1. mouse.
PROiQ61553.
SOURCEiSearch...

Gene expression databases

BgeeiQ61553.
ExpressionAtlasiQ61553. baseline and differential.
GenevisibleiQ61553. MM.

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. "Cloning and expression of a murine fascin homolog from mouse brain."
    Edwards R.A., Herrera-Sosa H., Otto J., Bryan J.
    J. Biol. Chem. 270:10764-10770(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Beta-catenin associates with the actin-bundling protein fascin in a noncadherin complex."
    Tao Y.S., Edwards R.A., Tubb B., Wang S., Bryan J., McCrea P.D.
    J. Cell Biol. 134:1271-1281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ASSOCIATION WITH BETA-CATENIN.
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Placenta.
  4. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Embryonic brain and Mammary gland.
  5. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-32; 69-82; 132-149; 168-185; 202-217; 248-271; 380-389 AND 409-426, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Migrastatin analogues target fascin to block tumour metastasis."
    Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.
    Nature 464:1062-1066(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and morphology through Rac1 and the actin cytoskeleton."
    Li X., Law J.W., Lee A.Y.
    Oncogene 31:595-610(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXNB3.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Rufy3, a protein specifically expressed in neurons, interacts with actin-bundling protein Fascin to control the growth of axons."
    Wei Z., Sun M., Liu X., Zhang J., Jin Y.
    J. Neurochem. 130:678-692(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUFY3, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFSCN1_MOUSE
AccessioniPrimary (citable) accession number: Q61553
Secondary accession number(s): O09099
, O09156, Q05DK3, Q7TN32, Q80V75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: July 6, 2016
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.