Full text data of FSCN1
FSCN1
(FAN1, HSN, SNL)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Fascin (55 kDa actin-bundling protein; Singed-like protein; p55)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Fascin (55 kDa actin-bundling protein; Singed-like protein; p55)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00163187
IPI00163187 Fascin 55 kDa actin bundling protein, Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Probably involved in the assembly of actin filament bundles present in microspikes, membrane ruffles, and stress fibers, ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00163187 Fascin 55 kDa actin bundling protein, Organizes filamentous actin into bundles with a minimum of 4.1:1 actin/fascin ratio. Probably involved in the assembly of actin filament bundles present in microspikes, membrane ruffles, and stress fibers, ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q16658
ID FSCN1_HUMAN Reviewed; 493 AA.
AC Q16658; A6NI89; B2RE97; Q96IC5; Q9BRF1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Fascin;
DE AltName: Full=55 kDa actin-bundling protein;
DE AltName: Full=Singed-like protein;
DE AltName: Full=p55;
GN Name=FSCN1; Synonyms=FAN1, HSN, SNL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=8068206; DOI=10.1089/dna.1994.13.821;
RA Duh F.-M., Latif F., Weng Y., Geil L., Modi W., Stackhouse T.,
RA Matsumura F., Duan D.R., Linehan W.M., Lerman M.I., Gnarra J.R.;
RT "cDNA cloning and expression of the human homolog of the sea urchin
RT fascin and Drosophila singed genes which encodes an actin-bundling
RT protein.";
RL DNA Cell Biol. 13:821-827(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7933116;
RA Mosialos G., Yamashiro S., Baughman R.W., Matsudaira P., Vara L.,
RA Matsumura F., Kieff E., Birkenbach M.;
RT "Epstein-Barr virus infection induces expression in B lymphocytes of a
RT novel gene encoding an evolutionarily conserved 55-kilodalton actin-
RT bundling protein.";
RL J. Virol. 68:7320-7328(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bros M., Ross X.L., Reske-Kunz A.B., Ross R.;
RT "Human fascin gene sequence.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-32; 44-63; 69-82; 111-149; 159-185; 202-217;
RP 230-241; 248-271; 314-341; 409-426 AND 469-493, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 119-149; 202-217; 230-241; 314-330 AND 380-389,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=3525578; DOI=10.1083/jcb.103.2.631;
RA Yamashiro-Matsumura S., Matsumura F.;
RT "Intracellular localization of the 55-kD actin-bundling protein in
RT cultured cells: spatial relationships with actin, alpha-actinin,
RT tropomyosin, and fimbrin.";
RL J. Cell Biol. 103:631-640(1986).
RN [12]
RP PHOSPHORYLATION.
RX PubMed=8647875; DOI=10.1074/jbc.271.21.12632;
RA Yamakita Y., Ono S., Matsumura F., Yamashiro S.;
RT "Phosphorylation of human fascin inhibits its actin binding and
RT bundling activities.";
RL J. Biol. Chem. 271:12632-12638(1996).
RN [13]
RP FUNCTION.
RX PubMed=9362073; DOI=10.1091/mbc.8.11.2345;
RA Adams J.C.;
RT "Characterization of cell-matrix adhesion requirements for the
RT formation of fascin microspikes.";
RL Mol. Biol. Cell 8:2345-2363(1997).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9571235; DOI=10.1091/mbc.9.5.993;
RA Yamashiro S., Yamakita Y., Ono S., Matsumura F.;
RT "Fascin, an actin-bundling protein, induces membrane protrusions and
RT increases cell motility of epithelial cells.";
RL Mol. Biol. Cell 9:993-1006(1998).
RN [15]
RP PHOSPHORYLATION AT SER-39, AND MUTAGENESIS OF SER-39.
RX PubMed=8999969; DOI=10.1074/jbc.272.4.2527;
RA Ono S., Yamakita Y., Yamashiro S., Matsudaira P.T., Gnarra J.R.,
RA Obinata T., Matsumura F.;
RT "Identification of an actin binding region and a protein kinase C
RT phosphorylation site on human fascin.";
RL J. Biol. Chem. 272:2527-2533(1997).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20137952; DOI=10.1016/j.cub.2009.12.035;
RA Li A., Dawson J.C., Forero-Vargas M., Spence H.J., Yu X., Konig I.,
RA Anderson K., Machesky L.M.;
RT "The actin-bundling protein fascin stabilizes actin in invadopodia and
RT potentiates protrusive invasion.";
RL Curr. Biol. 20:339-345(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP INTERACTION WITH PLXNB3, AND SUBCELLULAR LOCATION.
RX PubMed=21706053; DOI=10.1038/onc.2011.256;
RA Li X., Law J.W., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and
RT morphology through Rac1 and the actin cytoskeleton.";
RL Oncogene 31:595-610(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND DOMAIN.
RX PubMed=20434460; DOI=10.1016/j.jmb.2010.04.043;
RA Sedeh R.S., Fedorov A.A., Fedorov E.V., Ono S., Matsumura F.,
RA Almo S.C., Bathe M.;
RT "Structure, evolutionary conservation, and conformational dynamics of
RT Homo sapiens fascin-1, an F-actin crosslinking protein.";
RL J. Mol. Biol. 400:589-604(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, MUTAGENESIS OF
RP HIS-392; LYS-471 AND ALA-488, AND DOMAIN.
RX PubMed=20393565; DOI=10.1038/nature08978;
RA Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.;
RT "Migrastatin analogues target fascin to block tumour metastasis.";
RL Nature 464:1062-1066(2010).
CC -!- FUNCTION: Organizes filamentous actin into bundles with a minimum
CC of 4.1:1 actin/fascin ratio. Plays a role in the organization of
CC actin filament bundles and the formation of microspikes, membrane
CC ruffles, and stress fibers. Important for the formation of a
CC diverse set of cell protrusions, such as filopodia, and for cell
CC motility and migration.
CC -!- SUBUNIT: Associates with beta-catenin. Interacts with PLXNB3.
CC -!- INTERACTION:
CC Q9BXW9:FANCD2; NbExp=6; IntAct=EBI-351076, EBI-359343;
CC P40692:MLH1; NbExp=7; IntAct=EBI-351076, EBI-744248;
CC Q9ULL4:PLXNB3; NbExp=2; IntAct=EBI-351076, EBI-311073;
CC P63104:YWHAZ; NbExp=3; IntAct=EBI-351076, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC filopodium. Cell projection, invadopodium. Cytoplasm, cytosol.
CC Note=In glioma cells, partially colocalizes with F-actin stress
CC fibers in the cytosol.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Composed of four beta-trefoil domains.
CC -!- PTM: Phosphorylation on Ser-39 inhibits the actin-binding ability
CC of fascin.
CC -!- SIMILARITY: Belongs to the fascin family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FSCN1ID44342ch7p22.html";
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DR EMBL; U03057; AAA86442.1; -; mRNA.
DR EMBL; U09873; AAA62201.1; -; mRNA.
DR EMBL; AY044229; AAL01526.1; -; Genomic_DNA.
DR EMBL; AK316607; BAG38194.1; -; mRNA.
DR EMBL; BT006636; AAP35282.1; -; mRNA.
DR EMBL; AC006483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87346.1; -; Genomic_DNA.
DR EMBL; BC000521; AAH00521.1; -; mRNA.
DR EMBL; BC006304; AAH06304.1; -; mRNA.
DR EMBL; BC007643; AAH07643.1; -; mRNA.
DR EMBL; BC007948; AAH07948.1; -; mRNA.
DR EMBL; BC007988; AAH07988.1; -; mRNA.
DR PIR; I38621; I38621.
DR RefSeq; NP_003079.1; NM_003088.3.
DR UniGene; Hs.118400; -.
DR PDB; 1DFC; X-ray; 2.90 A; A/B=1-493.
DR PDB; 3LLP; X-ray; 1.80 A; A/B=1-493.
DR PDB; 3O8K; X-ray; 2.70 A; A/B=1-493.
DR PDB; 3P53; X-ray; 2.00 A; A/B=1-493.
DR PDB; 4GOV; X-ray; 2.20 A; A/B=1-493.
DR PDB; 4GOY; X-ray; 2.30 A; A/B=1-493.
DR PDB; 4GP0; X-ray; 2.50 A; A/B=1-493.
DR PDB; 4GP3; X-ray; 2.25 A; A/B=1-493.
DR PDBsum; 1DFC; -.
DR PDBsum; 3LLP; -.
DR PDBsum; 3O8K; -.
DR PDBsum; 3P53; -.
DR PDBsum; 4GOV; -.
DR PDBsum; 4GOY; -.
DR PDBsum; 4GP0; -.
DR PDBsum; 4GP3; -.
DR ProteinModelPortal; Q16658; -.
DR SMR; Q16658; 8-493.
DR DIP; DIP-33171N; -.
DR IntAct; Q16658; 25.
DR MINT; MINT-3033029; -.
DR STRING; 9606.ENSP00000371798; -.
DR PhosphoSite; Q16658; -.
DR DMDM; 2498357; -.
DR REPRODUCTION-2DPAGE; IPI00163187; -.
DR REPRODUCTION-2DPAGE; Q16658; -.
DR UCD-2DPAGE; Q16658; -.
DR PaxDb; Q16658; -.
DR PRIDE; Q16658; -.
DR DNASU; 6624; -.
DR Ensembl; ENST00000382361; ENSP00000371798; ENSG00000075618.
DR GeneID; 6624; -.
DR KEGG; hsa:6624; -.
DR UCSC; uc003sou.3; human.
DR CTD; 6624; -.
DR GeneCards; GC07P005632; -.
DR H-InvDB; HIX0033686; -.
DR HGNC; HGNC:11148; FSCN1.
DR HPA; CAB000121; -.
DR HPA; CAB035991; -.
DR HPA; HPA005723; -.
DR MIM; 602689; gene.
DR neXtProt; NX_Q16658; -.
DR PharmGKB; PA128394534; -.
DR eggNOG; NOG85029; -.
DR HOGENOM; HOG000267034; -.
DR HOVERGEN; HBG000968; -.
DR InParanoid; Q16658; -.
DR KO; K17455; -.
DR OMA; PATLWEY; -.
DR OrthoDB; EOG7VQJCP; -.
DR PhylomeDB; Q16658; -.
DR ChiTaRS; FSCN1; human.
DR EvolutionaryTrace; Q16658; -.
DR GeneWiki; FSCN1; -.
DR GenomeRNAi; 6624; -.
DR NextBio; 25801; -.
DR PRO; PR:Q16658; -.
DR ArrayExpress; Q16658; -.
DR Bgee; Q16658; -.
DR CleanEx; HS_FSCN1; -.
DR Genevestigator; Q16658; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0071437; C:invadopodium; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR InterPro; IPR008999; Actin_cross-linking.
DR InterPro; IPR010431; Fascin.
DR InterPro; IPR022768; Fascin-domain.
DR InterPro; IPR024703; Fascin_metazoans.
DR PANTHER; PTHR10551; PTHR10551; 1.
DR Pfam; PF06268; Fascin; 4.
DR PIRSF; PIRSF005682; Fascin; 1.
DR SUPFAM; SSF50405; SSF50405; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell junction;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 493 Fascin.
FT /FTId=PRO_0000219379.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 38 38 Phosphoserine.
FT MOD_RES 39 39 Phosphoserine; by PKC.
FT MUTAGEN 39 39 S->A: Loss of phosphorylation.
FT MUTAGEN 392 392 H->A: Decreased actin-bundling activity.
FT MUTAGEN 471 471 K->A: Decreased actin-bundling activity.
FT MUTAGEN 488 488 A->W: Decreased actin-bundling activity.
FT CONFLICT 440 440 A -> V (in Ref. 8; AAH06304).
FT STRAND 13 17
FT STRAND 23 26
FT HELIX 29 31
FT STRAND 33 39
FT HELIX 42 44
FT STRAND 46 49
FT HELIX 53 55
FT STRAND 60 63
FT STRAND 69 72
FT STRAND 78 84
FT HELIX 87 89
FT STRAND 91 95
FT STRAND 97 99
FT STRAND 101 105
FT TURN 106 108
FT STRAND 111 116
FT STRAND 118 125
FT HELIX 128 130
FT STRAND 132 136
FT STRAND 141 146
FT TURN 147 150
FT STRAND 151 156
FT STRAND 162 169
FT HELIX 173 175
FT STRAND 177 181
FT STRAND 183 189
FT STRAND 202 205
FT HELIX 208 210
FT STRAND 212 216
FT STRAND 221 224
FT STRAND 230 234
FT TURN 235 238
FT STRAND 239 242
FT HELIX 250 252
FT STRAND 254 258
FT STRAND 262 266
FT STRAND 272 274
FT STRAND 277 280
FT STRAND 282 286
FT HELIX 290 292
FT STRAND 294 298
FT TURN 300 302
FT STRAND 305 308
FT TURN 310 312
FT STRAND 314 317
FT STRAND 321 329
FT HELIX 332 334
FT STRAND 336 341
FT STRAND 344 348
FT STRAND 354 357
FT STRAND 361 369
FT HELIX 372 374
FT STRAND 376 380
FT STRAND 384 386
FT STRAND 393 397
FT TURN 399 401
FT STRAND 403 410
FT STRAND 414 419
FT STRAND 422 426
FT STRAND 432 435
FT STRAND 439 447
FT STRAND 451 456
FT TURN 457 459
FT STRAND 460 465
FT STRAND 468 472
FT STRAND 476 484
FT HELIX 487 489
FT STRAND 490 492
SQ SEQUENCE 493 AA; 54530 MW; C1453714BED6109A CRC64;
MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV
CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS
CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA
FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL
KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS NGKFVTSKKN
GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND
GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA
SAETVDPASL WEY
//
ID FSCN1_HUMAN Reviewed; 493 AA.
AC Q16658; A6NI89; B2RE97; Q96IC5; Q9BRF1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Fascin;
DE AltName: Full=55 kDa actin-bundling protein;
DE AltName: Full=Singed-like protein;
DE AltName: Full=p55;
GN Name=FSCN1; Synonyms=FAN1, HSN, SNL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=8068206; DOI=10.1089/dna.1994.13.821;
RA Duh F.-M., Latif F., Weng Y., Geil L., Modi W., Stackhouse T.,
RA Matsumura F., Duan D.R., Linehan W.M., Lerman M.I., Gnarra J.R.;
RT "cDNA cloning and expression of the human homolog of the sea urchin
RT fascin and Drosophila singed genes which encodes an actin-bundling
RT protein.";
RL DNA Cell Biol. 13:821-827(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7933116;
RA Mosialos G., Yamashiro S., Baughman R.W., Matsudaira P., Vara L.,
RA Matsumura F., Kieff E., Birkenbach M.;
RT "Epstein-Barr virus infection induces expression in B lymphocytes of a
RT novel gene encoding an evolutionarily conserved 55-kilodalton actin-
RT bundling protein.";
RL J. Virol. 68:7320-7328(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bros M., Ross X.L., Reske-Kunz A.B., Ross R.;
RT "Human fascin gene sequence.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-32; 44-63; 69-82; 111-149; 159-185; 202-217;
RP 230-241; 248-271; 314-341; 409-426 AND 469-493, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 119-149; 202-217; 230-241; 314-330 AND 380-389,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=3525578; DOI=10.1083/jcb.103.2.631;
RA Yamashiro-Matsumura S., Matsumura F.;
RT "Intracellular localization of the 55-kD actin-bundling protein in
RT cultured cells: spatial relationships with actin, alpha-actinin,
RT tropomyosin, and fimbrin.";
RL J. Cell Biol. 103:631-640(1986).
RN [12]
RP PHOSPHORYLATION.
RX PubMed=8647875; DOI=10.1074/jbc.271.21.12632;
RA Yamakita Y., Ono S., Matsumura F., Yamashiro S.;
RT "Phosphorylation of human fascin inhibits its actin binding and
RT bundling activities.";
RL J. Biol. Chem. 271:12632-12638(1996).
RN [13]
RP FUNCTION.
RX PubMed=9362073; DOI=10.1091/mbc.8.11.2345;
RA Adams J.C.;
RT "Characterization of cell-matrix adhesion requirements for the
RT formation of fascin microspikes.";
RL Mol. Biol. Cell 8:2345-2363(1997).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9571235; DOI=10.1091/mbc.9.5.993;
RA Yamashiro S., Yamakita Y., Ono S., Matsumura F.;
RT "Fascin, an actin-bundling protein, induces membrane protrusions and
RT increases cell motility of epithelial cells.";
RL Mol. Biol. Cell 9:993-1006(1998).
RN [15]
RP PHOSPHORYLATION AT SER-39, AND MUTAGENESIS OF SER-39.
RX PubMed=8999969; DOI=10.1074/jbc.272.4.2527;
RA Ono S., Yamakita Y., Yamashiro S., Matsudaira P.T., Gnarra J.R.,
RA Obinata T., Matsumura F.;
RT "Identification of an actin binding region and a protein kinase C
RT phosphorylation site on human fascin.";
RL J. Biol. Chem. 272:2527-2533(1997).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20137952; DOI=10.1016/j.cub.2009.12.035;
RA Li A., Dawson J.C., Forero-Vargas M., Spence H.J., Yu X., Konig I.,
RA Anderson K., Machesky L.M.;
RT "The actin-bundling protein fascin stabilizes actin in invadopodia and
RT potentiates protrusive invasion.";
RL Curr. Biol. 20:339-345(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP INTERACTION WITH PLXNB3, AND SUBCELLULAR LOCATION.
RX PubMed=21706053; DOI=10.1038/onc.2011.256;
RA Li X., Law J.W., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and
RT morphology through Rac1 and the actin cytoskeleton.";
RL Oncogene 31:595-610(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND DOMAIN.
RX PubMed=20434460; DOI=10.1016/j.jmb.2010.04.043;
RA Sedeh R.S., Fedorov A.A., Fedorov E.V., Ono S., Matsumura F.,
RA Almo S.C., Bathe M.;
RT "Structure, evolutionary conservation, and conformational dynamics of
RT Homo sapiens fascin-1, an F-actin crosslinking protein.";
RL J. Mol. Biol. 400:589-604(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, MUTAGENESIS OF
RP HIS-392; LYS-471 AND ALA-488, AND DOMAIN.
RX PubMed=20393565; DOI=10.1038/nature08978;
RA Chen L., Yang S., Jakoncic J., Zhang J.J., Huang X.Y.;
RT "Migrastatin analogues target fascin to block tumour metastasis.";
RL Nature 464:1062-1066(2010).
CC -!- FUNCTION: Organizes filamentous actin into bundles with a minimum
CC of 4.1:1 actin/fascin ratio. Plays a role in the organization of
CC actin filament bundles and the formation of microspikes, membrane
CC ruffles, and stress fibers. Important for the formation of a
CC diverse set of cell protrusions, such as filopodia, and for cell
CC motility and migration.
CC -!- SUBUNIT: Associates with beta-catenin. Interacts with PLXNB3.
CC -!- INTERACTION:
CC Q9BXW9:FANCD2; NbExp=6; IntAct=EBI-351076, EBI-359343;
CC P40692:MLH1; NbExp=7; IntAct=EBI-351076, EBI-744248;
CC Q9ULL4:PLXNB3; NbExp=2; IntAct=EBI-351076, EBI-311073;
CC P63104:YWHAZ; NbExp=3; IntAct=EBI-351076, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC filopodium. Cell projection, invadopodium. Cytoplasm, cytosol.
CC Note=In glioma cells, partially colocalizes with F-actin stress
CC fibers in the cytosol.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Composed of four beta-trefoil domains.
CC -!- PTM: Phosphorylation on Ser-39 inhibits the actin-binding ability
CC of fascin.
CC -!- SIMILARITY: Belongs to the fascin family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FSCN1ID44342ch7p22.html";
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DR EMBL; U03057; AAA86442.1; -; mRNA.
DR EMBL; U09873; AAA62201.1; -; mRNA.
DR EMBL; AY044229; AAL01526.1; -; Genomic_DNA.
DR EMBL; AK316607; BAG38194.1; -; mRNA.
DR EMBL; BT006636; AAP35282.1; -; mRNA.
DR EMBL; AC006483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87346.1; -; Genomic_DNA.
DR EMBL; BC000521; AAH00521.1; -; mRNA.
DR EMBL; BC006304; AAH06304.1; -; mRNA.
DR EMBL; BC007643; AAH07643.1; -; mRNA.
DR EMBL; BC007948; AAH07948.1; -; mRNA.
DR EMBL; BC007988; AAH07988.1; -; mRNA.
DR PIR; I38621; I38621.
DR RefSeq; NP_003079.1; NM_003088.3.
DR UniGene; Hs.118400; -.
DR PDB; 1DFC; X-ray; 2.90 A; A/B=1-493.
DR PDB; 3LLP; X-ray; 1.80 A; A/B=1-493.
DR PDB; 3O8K; X-ray; 2.70 A; A/B=1-493.
DR PDB; 3P53; X-ray; 2.00 A; A/B=1-493.
DR PDB; 4GOV; X-ray; 2.20 A; A/B=1-493.
DR PDB; 4GOY; X-ray; 2.30 A; A/B=1-493.
DR PDB; 4GP0; X-ray; 2.50 A; A/B=1-493.
DR PDB; 4GP3; X-ray; 2.25 A; A/B=1-493.
DR PDBsum; 1DFC; -.
DR PDBsum; 3LLP; -.
DR PDBsum; 3O8K; -.
DR PDBsum; 3P53; -.
DR PDBsum; 4GOV; -.
DR PDBsum; 4GOY; -.
DR PDBsum; 4GP0; -.
DR PDBsum; 4GP3; -.
DR ProteinModelPortal; Q16658; -.
DR SMR; Q16658; 8-493.
DR DIP; DIP-33171N; -.
DR IntAct; Q16658; 25.
DR MINT; MINT-3033029; -.
DR STRING; 9606.ENSP00000371798; -.
DR PhosphoSite; Q16658; -.
DR DMDM; 2498357; -.
DR REPRODUCTION-2DPAGE; IPI00163187; -.
DR REPRODUCTION-2DPAGE; Q16658; -.
DR UCD-2DPAGE; Q16658; -.
DR PaxDb; Q16658; -.
DR PRIDE; Q16658; -.
DR DNASU; 6624; -.
DR Ensembl; ENST00000382361; ENSP00000371798; ENSG00000075618.
DR GeneID; 6624; -.
DR KEGG; hsa:6624; -.
DR UCSC; uc003sou.3; human.
DR CTD; 6624; -.
DR GeneCards; GC07P005632; -.
DR H-InvDB; HIX0033686; -.
DR HGNC; HGNC:11148; FSCN1.
DR HPA; CAB000121; -.
DR HPA; CAB035991; -.
DR HPA; HPA005723; -.
DR MIM; 602689; gene.
DR neXtProt; NX_Q16658; -.
DR PharmGKB; PA128394534; -.
DR eggNOG; NOG85029; -.
DR HOGENOM; HOG000267034; -.
DR HOVERGEN; HBG000968; -.
DR InParanoid; Q16658; -.
DR KO; K17455; -.
DR OMA; PATLWEY; -.
DR OrthoDB; EOG7VQJCP; -.
DR PhylomeDB; Q16658; -.
DR ChiTaRS; FSCN1; human.
DR EvolutionaryTrace; Q16658; -.
DR GeneWiki; FSCN1; -.
DR GenomeRNAi; 6624; -.
DR NextBio; 25801; -.
DR PRO; PR:Q16658; -.
DR ArrayExpress; Q16658; -.
DR Bgee; Q16658; -.
DR CleanEx; HS_FSCN1; -.
DR Genevestigator; Q16658; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0071437; C:invadopodium; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR InterPro; IPR008999; Actin_cross-linking.
DR InterPro; IPR010431; Fascin.
DR InterPro; IPR022768; Fascin-domain.
DR InterPro; IPR024703; Fascin_metazoans.
DR PANTHER; PTHR10551; PTHR10551; 1.
DR Pfam; PF06268; Fascin; 4.
DR PIRSF; PIRSF005682; Fascin; 1.
DR SUPFAM; SSF50405; SSF50405; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell junction;
KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 493 Fascin.
FT /FTId=PRO_0000219379.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 38 38 Phosphoserine.
FT MOD_RES 39 39 Phosphoserine; by PKC.
FT MUTAGEN 39 39 S->A: Loss of phosphorylation.
FT MUTAGEN 392 392 H->A: Decreased actin-bundling activity.
FT MUTAGEN 471 471 K->A: Decreased actin-bundling activity.
FT MUTAGEN 488 488 A->W: Decreased actin-bundling activity.
FT CONFLICT 440 440 A -> V (in Ref. 8; AAH06304).
FT STRAND 13 17
FT STRAND 23 26
FT HELIX 29 31
FT STRAND 33 39
FT HELIX 42 44
FT STRAND 46 49
FT HELIX 53 55
FT STRAND 60 63
FT STRAND 69 72
FT STRAND 78 84
FT HELIX 87 89
FT STRAND 91 95
FT STRAND 97 99
FT STRAND 101 105
FT TURN 106 108
FT STRAND 111 116
FT STRAND 118 125
FT HELIX 128 130
FT STRAND 132 136
FT STRAND 141 146
FT TURN 147 150
FT STRAND 151 156
FT STRAND 162 169
FT HELIX 173 175
FT STRAND 177 181
FT STRAND 183 189
FT STRAND 202 205
FT HELIX 208 210
FT STRAND 212 216
FT STRAND 221 224
FT STRAND 230 234
FT TURN 235 238
FT STRAND 239 242
FT HELIX 250 252
FT STRAND 254 258
FT STRAND 262 266
FT STRAND 272 274
FT STRAND 277 280
FT STRAND 282 286
FT HELIX 290 292
FT STRAND 294 298
FT TURN 300 302
FT STRAND 305 308
FT TURN 310 312
FT STRAND 314 317
FT STRAND 321 329
FT HELIX 332 334
FT STRAND 336 341
FT STRAND 344 348
FT STRAND 354 357
FT STRAND 361 369
FT HELIX 372 374
FT STRAND 376 380
FT STRAND 384 386
FT STRAND 393 397
FT TURN 399 401
FT STRAND 403 410
FT STRAND 414 419
FT STRAND 422 426
FT STRAND 432 435
FT STRAND 439 447
FT STRAND 451 456
FT TURN 457 459
FT STRAND 460 465
FT STRAND 468 472
FT STRAND 476 484
FT HELIX 487 489
FT STRAND 490 492
SQ SEQUENCE 493 AA; 54530 MW; C1453714BED6109A CRC64;
MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV
CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS
CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA
FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL
KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR
DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS NGKFVTSKKN
GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND
GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA
SAETVDPASL WEY
//
MIM
602689
*RECORD*
*FIELD* NO
602689
*FIELD* TI
*602689 FASCIN, SEA URCHIN, HOMOLOG OF, 1; FSCN1
;;SINGED, DROSOPHILA, HOMOLOG OF; SNL;;
read moreACTIN-BUNDLING PROTEIN, 55-KD;;
p55
*FIELD* TX
CLONING
Sea urchin fascin, one of the first actin-bundling proteins extensively
characterized, can crosslink actin filaments in vitro (Bryan and Kane,
1982). The cloning of a fascin cDNA by Bryan et al. (1993) showed that
fascin is homologous to the Drosophila singed gene product. Duh et al.
(1994) isolated cDNAs encoding the human homolog of sea urchin fascin
and Drosophila singed, called HSN by them, from a human teratocarcinoma
cDNA library. The HSN mRNA was expressed at various levels in all human
tissues analyzed and at high levels in actively growing renal carcinoma
cell lines and in activated but not in resting lymphocytes, suggesting a
functional role for HSN in proliferation. The HSN gene is predicted to
encode a 493-amino acid protein with a molecular mass of 55 kD. Based on
peptide sequence identity and immunocrossreactivity, Duh et al. (1994)
indicated that the HSN protein is the 55-kD actin-bundling protein
purified from HeLa cells (Yamashiro-Matsumura and Matsumura, 1985).
GENE FUNCTION
Yamashiro-Matsumura and Matsumura (1986) suggested that the 55-kD HSN
protein is involved in the assembly of actin filament bundles present in
microspikes, membrane ruffles, and stress fibers.
Yamakita et al. (1996) demonstrated that the actin-binding and -bundling
activities of SNL are inhibited by phosphorylation. SNL is
phosphorylated in vivo upon treatment with
12-O-tetradecanoylphorbol-13-acetate, a tumor promoter. The
phosphorylation gradually increases, concomitant with the disappearance
of SNL from stress fibers, microspikes, and membrane ruffles. Ono et al.
(1997) identified serine-39 as the major site of SNL phosphorylation.
This site is highly conserved among all fascin homologs. Substitution of
serine-39 with alanine eliminated the phosphorylation-dependent
regulation of the actin-binding activity of SNL, indicating that
phosphorylation at this site regulates the actin-binding ability of SNL.
Ono et al. (1997) found that the C-terminal half of SNL contains an
actin-binding domain.
Using immunofluorescence microscopy and Western blot analysis, Mosialos
et al. (1996) demonstrated that an anti-p55 antibody reacted with nearly
all purified dendritic cells but not with other blood leukocytes.
Expression of p55 colocalized with actin. Immunohistochemistry indicated
that p55 is expressed in dendritic cells in lymph node T-cell zones.
Sonderbye et al. (1997) used flow cytometric and immunohistochemical
analyses to show that expression of fascin is rare in CD34
(142230)-positive progenitor cells but that cytoplasmic expression
increases with differentiation in culture until nearly all dendritic
cells are fascin-positive.
Using immunohistochemistry, Pinkus et al. (1997) found that nearly all
Reed-Sternberg cells in Hodgkin disease (236000), except in the nodular
lymphocyte predominance type, express fascin. They proposed that fascin
expression may be helpful in distinguishing Hodgkin from non-Hodgkin
lymphoma and suggested that Reed-Sternberg cells may have a dendritic
cell derivation.
By in vivo selection, transcriptomic analysis, functional verification,
and clinical validation, Minn et al. (2005) identified a set of genes
that marks and mediates breast cancer metastasis to the lungs. Some of
these genes serve dual functions, providing growth advantages both in
the primary tumor and in the lung microenvironment. Others contribute to
aggressive growth selectivity in the lung. Two that were not
functionally validated but that achieved the highest statistical
significance (P less than 0.000001) were FSCN1 and angiopoietin-like-4
(ANGPTL4; 605910). Those subjects expressing the lung metastasis
signature had a significantly poorer lung metastasis-free survival, but
not bone metastasis-free survival, compared to subjects without the
signature.
Zhang et al. (2009) found that RAB35 (604199) regulates the assembly of
actin filaments during bristle development in Drosophila and filopodia
formation in cultured cells. These effects were mediated by the
actin-bundling protein fascin, which directly associated with active
Rab35. Targeting Rab35 to the outer mitochondrial membrane triggered
actin recruitment, demonstrating a role for an intracellular trafficking
protein in localized actin assembly.
MAPPING
Duh et al. (1994) mapped the SNL gene to 7p22 by fluorescence in situ
hybridization.
*FIELD* RF
1. Bryan, J.; Edwards, R.; Matsudaira, P.; Otto, J.; Wulfkuhle, J.
: Fascin, an echinoid actin-bundling protein, is a homolog of the
Drosophila singed gene product. Proc. Nat. Acad. Sci. 90: 9115-9119,
1993.
2. Bryan, J.; Kane, R. E.: Actin gelation in sea urchin egg extracts. Methods
Cell Biol. 25: 175-199, 1982.
3. Duh, F.-M.; Latif, F.; Weng, Y.; Geil, L.; Modi, W.; Stackhouse,
T.; Matsumura, F.; Duan, D. R.; Linehan, W. M.; Lerman, M. I.; Gnarra,
J. R.: cDNA cloning and expression of the human homolog of the sea
urchin fascin and Drosophila singed genes which encodes an actin-bundling
protein. DNA Cell Biol. 13: 821-827, 1994.
4. Minn, A. J.; Gupta, G. P.; Siegel, P. M.; Bos, P. D.; Shu, W.;
Giri, D. D.; Viale, A.; Olshen, A. B.; Gerald, W. L.; Massague, J.
: Genes that mediate breast cancer metastasis to lung. Nature 436:
518-524, 2005.
5. Mosialos, G.; Birkenbach, M.; Ayehunie, S.; Matsumura, F.; Pinkus,
G. S.; Kieff, E.; Langhoff, E.: Circulating human dendritic cells
differentially express high levels of a 55-kD actin-bundling protein. Am.
J. Path. 148: 593-600, 1996.
6. Ono, S.; Yamakita, Y.; Yamashiro, S.; Matsudaira, P. T.; Gnarra,
J. R.; Obinata, T.; Matsumura, F.: Identification of an actin binding
region and a protein kinase C phosphorylation site on human fascin. J.
Biol. Chem. 272: 2527-2533, 1997.
7. Pinkus, G. S.; Pinkus, J. L.; Langhoff, E.; Matsumura, F.; Yamashiro,
S.; Mosialos, G.; Said, J. W.: Fascin, a sensitive new marker for
Reed-Sternberg cells of Hodgkin's disease: evidence for a dendritic
or B cell derivation? Am. J. Path. 150: 543-562, 1997.
8. Sonderbye, L.; Magerstadt, R.; Blatman, R. N.; Preffer, F. I.;
Langhoff, E.: Selective expression of human fascin (p55) by dendritic
leukocytes. Adv. Exp. Med. Biol. 471: 41-46, 1997.
9. Yamakita, Y.; Ono, S.; Matsumura, F.; Yamashiro, S.: Phosphorylation
of human fascin inhibits its actin binding and bundling activities. J.
Biol. Chem. 271: 12632-12638, 1996.
10. Yamashiro-Matsumura, S.; Matsumura, F.: Purification and characterization
of an F-actin-bundling 55-kilodalton protein from HeLa cells. J.
Biol. Chem. 260: 5087-5097, 1985.
11. Yamashiro-Matsumura, S.; Matsumura, F.: Intracellular localization
of the 55-kD actin-bundling protein in cultured cells: spatial relationships
with actin, alpha-actinin, tropomyosin, and fimbrin. J. Cell Biol. 103:
631-640, 1986.
12. Zhang, J.; Fonovic, M.; Suyama, K.; Bogyo, M.; Scott, M. P.:
Rab35 controls actin bundling by recruiting fascin as an effector
protein. Science 325: 1250-1254, 2009.
*FIELD* CN
Ada Hamosh - updated: 10/13/2009
Ada Hamosh - updated: 8/15/2005
Paul J. Converse - updated: 2/21/2001
*FIELD* CD
Ethylin Wang Jabs: 6/5/1998
*FIELD* ED
alopez: 10/23/2009
terry: 10/13/2009
alopez: 8/18/2005
terry: 8/15/2005
tkritzer: 11/21/2003
carol: 6/25/2003
carol: 1/28/2003
mgross: 9/18/2002
mgross: 2/21/2001
terry: 2/21/2001
dholmes: 7/22/1998
psherman: 6/6/1998
psherman: 6/5/1998
*RECORD*
*FIELD* NO
602689
*FIELD* TI
*602689 FASCIN, SEA URCHIN, HOMOLOG OF, 1; FSCN1
;;SINGED, DROSOPHILA, HOMOLOG OF; SNL;;
read moreACTIN-BUNDLING PROTEIN, 55-KD;;
p55
*FIELD* TX
CLONING
Sea urchin fascin, one of the first actin-bundling proteins extensively
characterized, can crosslink actin filaments in vitro (Bryan and Kane,
1982). The cloning of a fascin cDNA by Bryan et al. (1993) showed that
fascin is homologous to the Drosophila singed gene product. Duh et al.
(1994) isolated cDNAs encoding the human homolog of sea urchin fascin
and Drosophila singed, called HSN by them, from a human teratocarcinoma
cDNA library. The HSN mRNA was expressed at various levels in all human
tissues analyzed and at high levels in actively growing renal carcinoma
cell lines and in activated but not in resting lymphocytes, suggesting a
functional role for HSN in proliferation. The HSN gene is predicted to
encode a 493-amino acid protein with a molecular mass of 55 kD. Based on
peptide sequence identity and immunocrossreactivity, Duh et al. (1994)
indicated that the HSN protein is the 55-kD actin-bundling protein
purified from HeLa cells (Yamashiro-Matsumura and Matsumura, 1985).
GENE FUNCTION
Yamashiro-Matsumura and Matsumura (1986) suggested that the 55-kD HSN
protein is involved in the assembly of actin filament bundles present in
microspikes, membrane ruffles, and stress fibers.
Yamakita et al. (1996) demonstrated that the actin-binding and -bundling
activities of SNL are inhibited by phosphorylation. SNL is
phosphorylated in vivo upon treatment with
12-O-tetradecanoylphorbol-13-acetate, a tumor promoter. The
phosphorylation gradually increases, concomitant with the disappearance
of SNL from stress fibers, microspikes, and membrane ruffles. Ono et al.
(1997) identified serine-39 as the major site of SNL phosphorylation.
This site is highly conserved among all fascin homologs. Substitution of
serine-39 with alanine eliminated the phosphorylation-dependent
regulation of the actin-binding activity of SNL, indicating that
phosphorylation at this site regulates the actin-binding ability of SNL.
Ono et al. (1997) found that the C-terminal half of SNL contains an
actin-binding domain.
Using immunofluorescence microscopy and Western blot analysis, Mosialos
et al. (1996) demonstrated that an anti-p55 antibody reacted with nearly
all purified dendritic cells but not with other blood leukocytes.
Expression of p55 colocalized with actin. Immunohistochemistry indicated
that p55 is expressed in dendritic cells in lymph node T-cell zones.
Sonderbye et al. (1997) used flow cytometric and immunohistochemical
analyses to show that expression of fascin is rare in CD34
(142230)-positive progenitor cells but that cytoplasmic expression
increases with differentiation in culture until nearly all dendritic
cells are fascin-positive.
Using immunohistochemistry, Pinkus et al. (1997) found that nearly all
Reed-Sternberg cells in Hodgkin disease (236000), except in the nodular
lymphocyte predominance type, express fascin. They proposed that fascin
expression may be helpful in distinguishing Hodgkin from non-Hodgkin
lymphoma and suggested that Reed-Sternberg cells may have a dendritic
cell derivation.
By in vivo selection, transcriptomic analysis, functional verification,
and clinical validation, Minn et al. (2005) identified a set of genes
that marks and mediates breast cancer metastasis to the lungs. Some of
these genes serve dual functions, providing growth advantages both in
the primary tumor and in the lung microenvironment. Others contribute to
aggressive growth selectivity in the lung. Two that were not
functionally validated but that achieved the highest statistical
significance (P less than 0.000001) were FSCN1 and angiopoietin-like-4
(ANGPTL4; 605910). Those subjects expressing the lung metastasis
signature had a significantly poorer lung metastasis-free survival, but
not bone metastasis-free survival, compared to subjects without the
signature.
Zhang et al. (2009) found that RAB35 (604199) regulates the assembly of
actin filaments during bristle development in Drosophila and filopodia
formation in cultured cells. These effects were mediated by the
actin-bundling protein fascin, which directly associated with active
Rab35. Targeting Rab35 to the outer mitochondrial membrane triggered
actin recruitment, demonstrating a role for an intracellular trafficking
protein in localized actin assembly.
MAPPING
Duh et al. (1994) mapped the SNL gene to 7p22 by fluorescence in situ
hybridization.
*FIELD* RF
1. Bryan, J.; Edwards, R.; Matsudaira, P.; Otto, J.; Wulfkuhle, J.
: Fascin, an echinoid actin-bundling protein, is a homolog of the
Drosophila singed gene product. Proc. Nat. Acad. Sci. 90: 9115-9119,
1993.
2. Bryan, J.; Kane, R. E.: Actin gelation in sea urchin egg extracts. Methods
Cell Biol. 25: 175-199, 1982.
3. Duh, F.-M.; Latif, F.; Weng, Y.; Geil, L.; Modi, W.; Stackhouse,
T.; Matsumura, F.; Duan, D. R.; Linehan, W. M.; Lerman, M. I.; Gnarra,
J. R.: cDNA cloning and expression of the human homolog of the sea
urchin fascin and Drosophila singed genes which encodes an actin-bundling
protein. DNA Cell Biol. 13: 821-827, 1994.
4. Minn, A. J.; Gupta, G. P.; Siegel, P. M.; Bos, P. D.; Shu, W.;
Giri, D. D.; Viale, A.; Olshen, A. B.; Gerald, W. L.; Massague, J.
: Genes that mediate breast cancer metastasis to lung. Nature 436:
518-524, 2005.
5. Mosialos, G.; Birkenbach, M.; Ayehunie, S.; Matsumura, F.; Pinkus,
G. S.; Kieff, E.; Langhoff, E.: Circulating human dendritic cells
differentially express high levels of a 55-kD actin-bundling protein. Am.
J. Path. 148: 593-600, 1996.
6. Ono, S.; Yamakita, Y.; Yamashiro, S.; Matsudaira, P. T.; Gnarra,
J. R.; Obinata, T.; Matsumura, F.: Identification of an actin binding
region and a protein kinase C phosphorylation site on human fascin. J.
Biol. Chem. 272: 2527-2533, 1997.
7. Pinkus, G. S.; Pinkus, J. L.; Langhoff, E.; Matsumura, F.; Yamashiro,
S.; Mosialos, G.; Said, J. W.: Fascin, a sensitive new marker for
Reed-Sternberg cells of Hodgkin's disease: evidence for a dendritic
or B cell derivation? Am. J. Path. 150: 543-562, 1997.
8. Sonderbye, L.; Magerstadt, R.; Blatman, R. N.; Preffer, F. I.;
Langhoff, E.: Selective expression of human fascin (p55) by dendritic
leukocytes. Adv. Exp. Med. Biol. 471: 41-46, 1997.
9. Yamakita, Y.; Ono, S.; Matsumura, F.; Yamashiro, S.: Phosphorylation
of human fascin inhibits its actin binding and bundling activities. J.
Biol. Chem. 271: 12632-12638, 1996.
10. Yamashiro-Matsumura, S.; Matsumura, F.: Purification and characterization
of an F-actin-bundling 55-kilodalton protein from HeLa cells. J.
Biol. Chem. 260: 5087-5097, 1985.
11. Yamashiro-Matsumura, S.; Matsumura, F.: Intracellular localization
of the 55-kD actin-bundling protein in cultured cells: spatial relationships
with actin, alpha-actinin, tropomyosin, and fimbrin. J. Cell Biol. 103:
631-640, 1986.
12. Zhang, J.; Fonovic, M.; Suyama, K.; Bogyo, M.; Scott, M. P.:
Rab35 controls actin bundling by recruiting fascin as an effector
protein. Science 325: 1250-1254, 2009.
*FIELD* CN
Ada Hamosh - updated: 10/13/2009
Ada Hamosh - updated: 8/15/2005
Paul J. Converse - updated: 2/21/2001
*FIELD* CD
Ethylin Wang Jabs: 6/5/1998
*FIELD* ED
alopez: 10/23/2009
terry: 10/13/2009
alopez: 8/18/2005
terry: 8/15/2005
tkritzer: 11/21/2003
carol: 6/25/2003
carol: 1/28/2003
mgross: 9/18/2002
mgross: 2/21/2001
terry: 2/21/2001
dholmes: 7/22/1998
psherman: 6/6/1998
psherman: 6/5/1998